Molecule_ID	Molecule_type	Molecule_name	Synonyms	Gene_Name	Gene_ID	Molecule_species	SpeciesID	Species	Genus	GenusID	Family	FamilyID	Order	OrderID	Class	ClassID	Phylum	PhylumID	Kingdom	KingdomID	Gene_Transcripts	Sequence	Chromosomal_location	Function	Structure	HGNC_ID	UniProt_ID	UniProt_ID_status	Ensembl ID	Precursor_Accession	Mature_Accession	Mature_Precursor miRNAs	circBase_ID	piRBase_ID
Mol00001	Protein	PP2A B subunit isoform R5-alpha (PPP2R5A)	PP2A B subunit isoform B'-alpha; PP2A B subunit isoform B56-alpha; PP2A B subunit isoform PR61-alpha; PR61alpha; PP2A B subunit isoform R5-alpha	PPP2R5A	5525	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261461.7, PPP2R5A-201, 3245; ENST00000537030.3, PPP2R5A-205, 1719; ENST00000498129.6, PPP2R5A-204, 745; ENST00000479259.1, PPP2R5A-202, 740; ENST00000498123.5, PPP2R5A-203, 399"	MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKDATSNEQQELFCQKLQQCCILFDFMDSVSDLKSKEIKRATLNELVEYVSTNRGVIVESAYSDIVKMISANIFRTLPPSDNPDFDPEEDEPTLEASWPHIQLVYEFFLRFLESPDFQPSIAKRYIDQKFVQQLLELFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNIFLRFIYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLMKVLIPMHTAKGLALFHAQLAYCVVQFLEKDTTLTEPVIRGLLKFWPKTCSQKEVMFLGEIEEILDVIEPTQFKKIEEPLFKQISKCVSSSHFQVAERALYFWNNEYILSLIEENIDKILPIMFASLYKISKEHWNPTIVALVYNVLKTLMEMNGKLFDDLTSSYKAERQREKKKELEREELWKKLEELKLKKALEKQNSAYNMHSILSNTSAE	chr1:212285410-212361853[+]	"The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment."	PDB: 6NTS	HGNC:9309	2A5A_HUMAN	Reviewed	ENSG00000066027	.	.	.	.	.
Mol00002	Protein	Lymphocyte activation antigen 4F2 (SLC3A2)	.	SLC3A2	6520	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000338663.12, SLC3A2-201, 1885; ENST00000377891.6, SLC3A2-204, 2222; ENST00000377890.6, SLC3A2-203, 2161; ENST00000544377.2, SLC3A2-221, 2041; ENST00000377889.6, SLC3A2-202, 1993; ENST00000681657.1, SLC3A2-240, 1905; ENST00000680631.1, SLC3A2-230, 1890; ENST00000538084.2, SLC3A2-211, 2334; ENST00000681569.1, SLC3A2-239, 2313; ENST00000680729.1, SLC3A2-233, 2265; ENST00000681467.1, SLC3A2-237, 2227; ENST00000680725.1, SLC3A2-232, 2197; ENST00000535296.5, SLC3A2-206, 2084; ENST00000680297.1, SLC3A2-228, 1975; ENST00000681232.1, SLC3A2-236, 1917; ENST00000539891.6, SLC3A2-215, 1554; ENST00000536981.6, SLC3A2-208, 1413; ENST00000539458.1, SLC3A2-213, 565; ENST00000539507.1, SLC3A2-214, 534; ENST00000541372.1, SLC3A2-216, 269; ENST00000680002.1, SLC3A2-226, 2491; ENST00000541425.6, SLC3A2-217, 2029; ENST00000679908.1, SLC3A2-225, 2029; ENST00000680610.1, SLC3A2-229, 1929; ENST00000681107.1, SLC3A2-234, 1908; ENST00000680134.1, SLC3A2-227, 1869; ENST00000457660.6, SLC3A2-205, 873; ENST00000546253.5, SLC3A2-222, 582; ENST00000537508.6, SLC3A2-209, 552; ENST00000681563.1, SLC3A2-238, 2843; ENST00000680654.1, SLC3A2-231, 2554; ENST00000542922.5, SLC3A2-220, 2174; ENST00000681215.1, SLC3A2-235, 2101; ENST00000541649.2, SLC3A2-218, 1926; ENST00000538682.6, SLC3A2-212, 1803; ENST00000679594.1, SLC3A2-224, 1512; ENST00000535768.2, SLC3A2-207, 1300; ENST00000537839.5, SLC3A2-210, 584; ENST00000546312.5, SLC3A2-223, 564; ENST00000542793.1, SLC3A2-219, 539"	MELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPSASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSFLAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLVTQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAALPGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHGDFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLSTQPGREEGSPLELERLKLEPHEGLLLRFPYAA	chr11:62856004-62888880[+]	"Component of several heterodimeric complexes involved in amino acid transport. The precise substrate specificity depends on the other subunit in the heterodimer. The complexes function as amino acid exchangers. The homodimer functions as sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as phenylalanine, tyrosine, L-DOPA, leucine, histidine, methionine and tryptophan. The heterodimer formed by SLC3A2 and SLC7A6 or SLC3A2 and SLC7A7 mediates the uptake of dibasic amino acids. The heterodimer with SLC7A5/LAT1 mediates the transport of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane. The heterodimer with SLC7A5/LAT1 is involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes. The heterodimer with SLC7A5/LAT1 is involved in the uptake of leucine. When associated with LAPTM4B, the heterodimer with SLC7A5/LAT1 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation. The heterodimer with SLC7A5/LAT1 may play a role in the transport of L-DOPA across the blood-brain barrier. The heterodimer formed by SLC3A2 and SLC7A5/LAT1 or SLC3A2 and SLC7A8/LAT2 is involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Together with ICAM1, regulates the transport activity of SLC7A8/LAT2 in polarized intestinal cells by generating and delivering intracellular signals. Required for targeting of SLC7A5/LAT1 and SLC7A8/LAT2 to the plasma membrane and for channel activity. Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. May mediate blood-to-retina L-leucine transport across the inner blood-retinal barrier."	PDB: 2DH2; PDB: 2DH3; PDB: 6IRS; PDB: 6IRT; PDB: 6JMQ; PDB: 6JMR; PDB: 6S8V; PDB: 7B00; PDB: 7CCS	HGNC:11026	4F2_HUMAN	Reviewed	ENSG00000168003	.	.	.	.	.
Mol00003	Protein	ATP-binding cassette sub-family B5 (ABCB5)	ABCB5 P-gp; P-glycoprotein ABCB5	ABCB5	340273	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000404938.7, ABCB5-202, 5350; ENST00000258738.10, ABCB5-201, 2906; ENST00000443026.6, ABCB5-205, 2247; ENST00000406935.5, ABCB5-203, 1483; ENST00000441315.1, ABCB5-204, 2204; ENST00000477094.5, ABCB5-206, 673"	MENSERAEEMQENYQRNGTAEEQPKLRKEAVGSIEIFRFADGLDITLMILGILASLVNGACLPLMPLVLGEMSDNLISGCLVQTNTTNYQNCTQSQEKLNEDMTLLTLYYVGIGVAALIFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCDIGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGLVKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSKAGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIKRTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEPGYTIGTVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHIFQVIDKKPSIDNFSTAGYKPESIEGTVEFKNVSFNYPSRPSIKILKGLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIMVDENDIRALNVRHYRDHIGVVSQEPVLFGTTISNNIKYGRDDVTDEEMERAAREANAYDFIMEFPNKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDSESKSAVQAALEKASKGRTTIVVAHRLSTIRSADLIVTLKDGMLAEKGAHAELMAKRGLYYSLVMSQDIKKADEQMESMTYSTERKTNSLPLHSVKSIKSDFIDKAEESTQSKEISLPEVSLLKILKLNKPEWPFVVLGTLASVLNGTVHPVFSIIFAKIITMFGNNDKTTLKHDAEIYSMIFVILGVICFVSYFMQGLFYGRAGEILTMRLRHLAFKAMLYQDIAWFDEKENSTGGLTTILAIDIAQIQGATGSRIGVLTQNATNMGLSVIISFIYGWEMTFLILSIAPVLAVTGMIETAAMTGFANKDKQELKHAGKIATEALENIRTIVSLTREKAFEQMYEEMLQTQHRNTSKKAQIIGSCYAFSHAFIYFAYAAGFRFGAYLIQAGRMTPEGMFIVFTAIAYGAMAIGETLVLAPEYSKAKSGAAHLFALLEKKPNIDSRSQEGKKPDTCEGNLEFREVSFFYPCRPDVFILRGLSLSIERGKTVAFVGSSGCGKSTSVQLLQRLYDPVQGQVLFDGVDAKELNVQWLRSQIAIVPQEPVLFNCSIAENIAYGDNSRVVPLDEIKEAANAANIHSFIEGLPEKYNTQVGLKGAQLSGGQKQRLAIARALLQKPKILLLDEATSALDNDSEKVVQHALDKARTGRTCLVVTHRLSAIQNADLIVVLHNGKIKEQGTHQELLRNRDIYFKLVNAQSVQ	chr7:20615667-20777038[+]	"Energy-dependent efflux transporter responsible for decreased drug accumulation in multidrug-resistant cells. Specifically present in limbal stem cells, where it plays a key role in corneal development and repair."	.	HGNC:46	ABCB5_HUMAN	Reviewed	ENSG00000004846	.	.	.	.	.
Mol00004	Protein	ABC-type oligopeptide transporter ABCB9 (ABCB9)	ATP-binding cassette sub-family B member 9; ATP-binding cassette transporter 9; ABC transporter 9 protein; hABCB9; TAP-like protein; TAPL; KIAA1520	ABCB9	23457	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000280560.13, ABCB9-201, 3484; ENST00000542678.5, ABCB9-215, 6051; ENST00000392439.7, ABCB9-204, 3791; ENST00000540285.5, ABCB9-210, 3330; ENST00000442833.6, ABCB9-206, 2587; ENST00000344275.11, ABCB9-202, 2394; ENST00000346530.9, ABCB9-203, 3399; ENST00000541424.1, ABCB9-212, 2108; ENST00000546077.1, ABCB9-218, 1419; ENST00000536976.5, ABCB9-207, 1168; ENST00000542448.5, ABCB9-214, 1104; ENST00000540971.5, ABCB9-211, 1066; ENST00000546289.5, ABCB9-219, 917; ENST00000543935.1, ABCB9-216, 568; ENST00000545373.1, ABCB9-217, 549; ENST00000537276.5, ABCB9-208, 2591; ENST00000426173.6, ABCB9-205, 2134; ENST00000541983.1, ABCB9-213, 546; ENST00000622723.1, ABCB9-220, 368; ENST00000538895.5, ABCB9-209, 2430"	MRLWKAVVVTLAFMSVDICVTTAIYVFSHLDRSLLEDIRHFNIFDSVLDLWAACLYRSCLLLGATIGVAKNSALGPRRLRASWLVITLVCLFVGIYAMVKLLLFSEVRRPIRDPWFWALFVWTYISLGASFLLWWLLSTVRPGTQALEPGAATEAEGFPGSGRPPPEQASGATLQKLLSYTKPDVAFLVAASFFLIVAALGETFLPYYTGRAIDGIVIQKSMDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLGLQPAADFTAGHNEPVANGSHKA	chr12:122920951-122981649[-]	"ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen for degradation. Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers. Binds and transports smaller and larger peptides with the same affinity. Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored."	.	HGNC:50	ABCB9_HUMAN	Reviewed	ENSG00000150967	.	.	.	.	.
Mol00005	Protein	ATP-binding cassette sub-family G2 (ABCG2)	.	ABCG2	9429	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000237612.8, ABCG2-201, 4206; ENST00000650821.1, ABCG2-205, 4844; ENST00000515655.5, ABCG2-204, 4276; ENST00000505480.6, ABCG2-203, 804; ENST00000503830.2, ABCG2-202, 475"	MSSSNVEVFIPVSQGNTNGFPATASNDLKAFTEGAVLSFHNICYRVKLKSGFLPCRKPVEKEILSNINGIMKPGLNAILGPTGGGKSSLLDVLAARKDPSGLSGDVLINGAPRPANFKCNSGYVVQDDVVMGTLTVRENLQFSAALRLATTMTNHEKNERINRVIQELGLDKVADSKVGTQFIRGVSGGERKRTSIGMELITDPSILFLDEPTTGLDSSTANAVLLLLKRMSKQGRTIIFSIHQPRYSIFKLFDSLTLLASGRLMFHGPAQEALGYFESAGYHCEAYNNPADFFLDIINGDSTAVALNREEDFKATEIIEPSKQDKPLIEKLAEIYVNSSFYKETKAELHQLSGGEKKKKITVFKEISYTTSFCHQLRWVSKRSFKNLLGNPQASIAQIIVTVVLGLVIGAIYFGLKNDSTGIQNRAGVLFFLTTNQCFSSVSAVELFVVEKKLFIHEYISGYYRVSSYFLGKLLSDLLPMRMLPSIIFTCIVYFMLGLKPKADAFFVMMFTLMMVAYSASSMALAIAAGQSVVSVATLLMTICFVFMMIFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNNPCNYATCTGEEYLVKQGIDLSPWGLWKNHVALACMIVIFLTIAYLKLLFLKKYS	chr4:88090150-88231628[-]	"Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells. Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a urate exporter functioning in both renal and extrarenal urate excretion. In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate. Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates. Mediates the secretion of the riboflavin and biotin vitamins into milk. Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability. Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux. In placenta, it limits the penetration of drugs from the maternal plasma into the fetus. May play a role in early stem cell self-renewal by blocking differentiation."	PDB: 5NJ3; PDB: 5NJG; PDB: 6ETI; PDB: 6FEQ; PDB: 6FFC; PDB: 6HBU; PDB: 6HCO; PDB: 6HIJ; PDB: 6HZM; PDB: 6VXF; PDB: 6VXH; PDB: 6VXI; PDB: 6VXJ; PDB: 7NEQ; PDB: 7NEZ; PDB: 7NFD; PDB: 7OJ8; PDB: 7OJH; PDB: 7OJI	HGNC:74	ABCG2_HUMAN	Reviewed	ENSG00000118777	.	.	.	.	.
Mol00006	Protein	Tyrosine-protein kinase ABL1 (ABL1)	Abelson murine leukemia viral oncogene homolog 1; Abelson tyrosine-protein kinase 1; Proto-oncogene c-Abl; p150; ABL; JTK7	ABL1	25	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000318560.6, ABL1-201, 5578; ENST00000372348.7, ABL1-202, 4754; ENST00000393293.4, ABL1-203, 532"	MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR	chr9:130713016-130887675[+]	"Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. In response to oxidative stress, phosphorylates serine/threonine kinase PRKD2 at 'Tyr-717'. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Regulates T-cell differentiation in a TBX21-dependent manner. Phosphorylates TBX21 on tyrosine residues leading to an enhancement of its transcriptional activator activity."	PDB: 1AB2; PDB: 1AWO; PDB: 1BBZ; PDB: 1JU5; PDB: 1OPL; PDB: 1ZZP; PDB: 2ABL; PDB: 2E2B; PDB: 2F4J; PDB: 2FO0; PDB: 2G1T; PDB: 2G2F; PDB: 2G2H; PDB: 2G2I; PDB: 2GQG; PDB: 2HIW; PDB: 2HYY; PDB: 2HZ0; PDB: 2HZ4; PDB: 2HZI; PDB: 2O88; PDB: 2V7A; PDB: 3CS9; PDB: 3EG0; PDB: 3EG1; PDB: 3EG2; PDB: 3EG3; PDB: 3EGU; PDB: 3K2M; PDB: 3PYY; PDB: 3QRI; PDB: 3QRJ; PDB: 3QRK; PDB: 3T04; PDB: 3UE4; PDB: 3UYO; PDB: 4J9B; PDB: 4J9C; PDB: 4J9D; PDB: 4J9E; PDB: 4J9F; PDB: 4J9G; PDB: 4J9H; PDB: 4J9I; PDB: 4JJB; PDB: 4JJC; PDB: 4JJD; PDB: 4TWP; PDB: 4WA9; PDB: 4XEY; PDB: 4YC8; PDB: 4ZOG; PDB: 5DC0; PDB: 5DC4; PDB: 5DC9; PDB: 5HU9; PDB: 5MO4; PDB: 5NP2; PDB: 5OAZ; PDB: 6AMV; PDB: 6AMW; PDB: 6BL8; PDB: 6NPE; PDB: 6NPU; PDB: 6NPV; PDB: 6XR6; PDB: 6XR7; PDB: 6XRG; PDB: 7CC2; PDB: 7DT2	HGNC:76	ABL1_HUMAN	Reviewed	ENSG00000097007	.	.	.	.	.
Mol00007	Protein	Mammalian disintegrin-metalloprotease (ADAM10)	.	ADAM10	102	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000260408.8, ADAM10-201, 11158; ENST00000461408.2, ADAM10-205, 1932; ENST00000402627.5, ADAM10-203, 861; ENST00000439637.5, ADAM10-204, 601; ENST00000558004.1, ADAM10-212, 587; ENST00000561288.1, ADAM10-217, 583; ENST00000559053.1, ADAM10-214, 541; ENST00000396136.6, ADAM10-202, 2418; ENST00000558733.5, ADAM10-213, 995; ENST00000475898.1, ADAM10-208, 674; ENST00000497846.5, ADAM10-211, 647; ENST00000560608.5, ADAM10-215, 587; ENST00000561149.1, ADAM10-216, 529; ENST00000482945.5, ADAM10-210, 2333; ENST00000470269.5, ADAM10-207, 1693; ENST00000481164.1, ADAM10-209, 750; ENST00000462061.1, ADAM10-206, 436"	MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR	chr15:58588809-58749791[-]	"Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA. Enhances the cleavage of CHL1 by BACE1. Cleaves NRCAM. Cleaves TREM2, resulting in shedding of the TREM2 ectodomain. Involved in the development and maturation of glomerular and coronary vasculature. During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions. May regulate the EFNA5-EPHA3 signaling."	PDB: 6BDZ; PDB: 6BE6	HGNC:188	ADA10_HUMAN	Reviewed	ENSG00000137845	.	.	.	.	.
Mol00008	Protein	Myeloma cell metalloproteinase (ADAM9)	ADAM 9; Cellular disintegrin-related protein; Meltrin-gamma; Metalloprotease/disintegrin/cysteine-rich protein 9; Myeloma cell metalloproteinase; KIAA0021; MCMP; MDC9; MLTNG	ADAM9	8754	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000487273.7, ADAM9-209, 4112; ENST00000676765.1, ADAM9-214, 4632; ENST00000677004.1, ADAM9-217, 4448; ENST00000676936.1, ADAM9-216, 4318; ENST00000677582.1, ADAM9-221, 3976; ENST00000676643.1, ADAM9-212, 3929; ENST00000481513.5, ADAM9-206, 2387; ENST00000466936.5, ADAM9-203, 2053; ENST00000676617.1, ADAM9-211, 5077; ENST00000678474.1, ADAM9-224, 4538; ENST00000677165.1, ADAM9-219, 4365; ENST00000679268.1, ADAM9-228, 4321; ENST00000678730.1, ADAM9-226, 4267; ENST00000676669.1, ADAM9-213, 4264; ENST00000677908.1, ADAM9-222, 4183; ENST00000678540.1, ADAM9-225, 4059; ENST00000677137.1, ADAM9-218, 3901; ENST00000677359.1, ADAM9-220, 3894; ENST00000379917.7, ADAM9-201, 3836; ENST00000481873.7, ADAM9-207, 3793; ENST00000468065.5, ADAM9-204, 3755; ENST00000678253.1, ADAM9-223, 3565; ENST00000678863.1, ADAM9-227, 3088; ENST00000484143.2, ADAM9-208, 5847; ENST00000481058.2, ADAM9-205, 7079; ENST00000676919.1, ADAM9-215, 5326; ENST00000676489.1, ADAM9-210, 4735; ENST00000463437.3, ADAM9-202, 2838"	MGSGARFPSGTLRVRWLLLLGLVGPVLGAARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGVCNSNKNCHCENGWAPPNCETKGYGGSVDSGPTYNEMNTALRDGLLVFFFLIVPLIVCAIFIFIKRDQLWRSYFRKKRSQTYESDGKNQANPSRQPGSVPRHVSPVTPPREVPIYANRFAVPTYAAKQPQQFPSRPPPPQPKVSSQGNLIPARPAPAPPLYSSLT	chr8:38996754-39105445[+]	"Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins."	.	HGNC:216	ADAM9_HUMAN	Reviewed	ENSG00000168615	.	.	.	.	.
Mol00009	Protein	Adhesion G-protein coupled receptor V1 (ADGRV1)	ADGRV1; G-protein coupled receptor 98; Monogenic audiogenic seizure susceptibility protein 1 homolog; Usher syndrome type-2C protein; Very large G-protein coupled receptor 1; GPR98; KIAA0686; KIAA1943; MASS1; VLGR1	ADGRV1	84059	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000405460.9, ADGRV1-201, 19557; ENST00000425867.3, ADGRV1-202, 8141; ENST00000640403.1, ADGRV1-232, 6723; ENST00000638975.1, ADGRV1-214, 2467; ENST00000640815.1, ADGRV1-237, 1522; ENST00000639821.1, ADGRV1-222, 893; ENST00000507314.2, ADGRV1-206, 698; ENST00000508842.5, ADGRV1-207, 582; ENST00000639707.1, ADGRV1-221, 564; ENST00000640369.1, ADGRV1-230, 500; ENST00000640407.1, ADGRV1-233, 5673; ENST00000640779.1, ADGRV1-236, 4680; ENST00000640012.1, ADGRV1-224, 3241; ENST00000638990.1, ADGRV1-215, 2433; ENST00000450321.2, ADGRV1-203, 879; ENST00000639431.1, ADGRV1-217, 611; ENST00000639212.1, ADGRV1-216, 1167; ENST00000639530.1, ADGRV1-219, 1101; ENST00000640256.1, ADGRV1-228, 904; ENST00000638585.1, ADGRV1-212, 631; ENST00000640061.1, ADGRV1-225, 584; ENST00000505845.2, ADGRV1-205, 559; ENST00000639473.1, ADGRV1-218, 6608; ENST00000638510.1, ADGRV1-211, 6503; ENST00000640374.1, ADGRV1-231, 5401; ENST00000509621.1, ADGRV1-208, 5211; ENST00000504142.2, ADGRV1-204, 5047; ENST00000640464.1, ADGRV1-234, 4505; ENST00000639676.1, ADGRV1-220, 3116; ENST00000640109.1, ADGRV1-227, 2906; ENST00000638316.1, ADGRV1-210, 2221; ENST00000640281.1, ADGRV1-229, 1466; ENST00000640083.1, ADGRV1-226, 1454; ENST00000640729.1, ADGRV1-235, 1360; ENST00000638638.1, ADGRV1-213, 1309; ENST00000639884.1, ADGRV1-223, 1177; ENST00000513828.1, ADGRV1-209, 596"	MSVFLGPGMPSASLLVNLLSALLILFVFGETEIRFTGQTEFVVNETSTTVIRLIIERIGEPANVTAIVSLYGEDAGDFFDTYAAAFIPAGETNRTVYIAVCDDDLPEPDETFIFHLTLQKPSANVKLGWPRTVTVTILSNDNAFGIISFNMLPSIAVSEPKGRNESMPLTLIREKGTYGMVMVTFEVEGGPNPPDEDLSPVKGNITFPPGRATVIYNLTVLDDEVPENDEIFLIQLKSVEGGAEINTSRNSIEIIIKKNDSPVRFLQSIYLVPEEDHILIIPVVRGKDNNGNLIGSDEYEVSISYAVTTGNSTAHAQQNLDFIDLQPNTTVVFPPFIHESHLKFQIVDDTIPEIAESFHIMLLKDTLQGDAVLISPSVVQVTIKPNDKPYGVLSFNSVLFERTVIIDEDRISRYEEITVVRNGGTHGNVSANWVLTRNSTDPSPVTADIRPSSGVLHFAQGQMLATIPLTVVDDDLPEEAEAYLLQILPHTIRGGAEVSEPAELLFYIQDSDDVYGLITFFPMENQKIESSPGERYLSLSFTRLGGTKGDVRLLYSVLYIPAGAVDPLQAKEGILNISRRNDLIFPEQKTQVTTKLPIRNDAFLQNGAHFLVQLETVELLNIIPLIPPISPRFGEICNISLLVTPAIANGEIGFLSNLPIILHEPEDFAAEVVYIPLHRDGTDGQATVYWSLKPSGFNSKAVTPDDIGPFNGSVLFLSGQSDTTINITIKGDDIPEMNETVTLSLDRVNVENQVLKSGYTSRDLIILENDDPGGVFEFSPASRGPYVIKEGESVELHIIRSRGSLVKQFLHYRVEPRDSNEFYGNTGVLEFKPGEREIVITLLARLDGIPELDEHYWVVLSSHGERESKLGSATIVNITILKNDDPHGIIEFVSDGLIVMINESKGDAIYSAVYDVVRNRGNFGDVSVSWVVSPDFTQDVFPVQGTVVFGDQEFSKNITIYSLPDEIPEEMEEFTVILLNGTGGAKVGNRTTATLRIRRNDDPIYFAEPRVVRVQEGETANFTVLRNGSVDVTCMVQYATKDGKATARERDFIPVEKGETLIFEVGSRQQSISIFVNEDGIPETDEPFYIILLNSTGDTVVYQYGVATVIIEANDDPNGIFSLEPIDKAVEEGKTNAFWILRHRGYFGSVSVSWQLFQNDSALQPGQEFYETSGTVNFMDGEEAKPIILHAFPDKIPEFNEFYFLKLVNISGGSPGPGGQLAETNLQVTVMVPFNDDPFGVFILDPECLEREVAEDVLSEDDMSYITNFTILRQQGVFGDVQLGWEILSSEFPAGLPPMIDFLLVGIFPTTVHLQQHMRRHHSGTDALYFTGLEGAFGTVNPKYHPSRNNTIANFTFSAWVMPNANTNGFIIAKDDGNGSIYYGVKIQTNESHVTLSLHYKTLGSNATYIAKTTVMKYLEESVWLHLLIILEDGIIEFYLDGNAMPRGIKSLKGEAITDGPGILRIGAGINGNDRFTGLMQDVRSYERKLTLEEIYELHAMPAKSDLHPISGYLEFRQGETNKSFIISARDDNDEEGEELFILKLVSVYGGARISEENTTARLTIQKSDNANGLFGFTGACIPEIAEEGSTISCVVERTRGALDYVHVFYTISQIETDGINYLVDDFANASGTITFLPWQRSEVLNIYVLDDDIPELNEYFRVTLVSAIPGDGKLGSTPTSGASIDPEKETTDITIKASDHPYGLLQFSTGLPPQPKDAMTLPASSVPHITVEEEDGEIRLLVIRAQGLLGRVTAEFRTVSLTAFSPEDYQNVAGTLEFQPGERYKYIFINITDNSIPELEKSFKVELLNLEGGVAELFRVDGSGSGDGDMEFFLPTIHKRASLGVASQILVTIAASDHAHGVFEFSPESLFVSGTEPEDGYSTVTLNVIRHHGTLSPVTLHWNIDSDPDGDLAFTSGNITFEIGQTSANITVEILPDEDPELDKAFSVSVLSVSSGSLGAHINATLTVLASDDPYGIFIFSEKNRPVKVEEATQNITLSIIRLKGLMGKVLVSYATLDDMEKPPYFPPNLARATQGRDYIPASGFALFGANQSEATIAISILDDDEPERSESVFIELLNSTLVAKVQSRSIPNSPRLGPKVETIAQLIIIANDDAFGTLQLSAPIVRVAENHVGPIINVTRTGGAFADVSVKFKAVPITAIAGEDYSIASSDVVLLEGETSKAVPIYVINDIYPELEESFLVQLMNETTGGARLGALTEAVIIIEASDDPYGLFGFQITKLIVEEPEFNSVKVNLPIIRNSGTLGNVTVQWVATINGQLATGDLRVVSGNVTFAPGETIQTLLLEVLADDVPEIEEVIQVQLTDASGGGTIGLDRIANIIIPANDDPYGTVAFAQMVYRVQEPLERSSCANITVRRSGGHFGRLLLFYSTSDIDVVALAMEEGQDLLSYYESPIQGVPDPLWRTWMNVSAVGEPLYTCATLCLKEQACSAFSFFSASEGPQCFWMTSWISPAVNNSDFWTYRKNMTRVASLFSGQAVAGSDYEPVTRQWAIMQEGDEFANLTVSILPDDFPEMDESFLISLLEVHLMNISASLKNQPTIGQPNISTVVIALNGDAFGVFVIYNISPNTSEDGLFVEVQEQPQTLVELMIHRTGGSLGQVAVEWRVVGGTATEGLDFIGAGEILTFAEGETKKTVILTILDDSEPEDDESIIVSLVYTEGGSRILPSSDTVRVNILANDNVAGIVSFQTASRSVIGHEGEILQFHVIRTFPGRGNVTVNWKIIGQNLELNFANFSGQLFFPEGSLNTTLFVHLLDDNIPEEKEVYQVILYDVRTQGVPPAGIALLDAQGYAAVLTVEASDEPHGVLNFALSSRFVLLQEANITIQLFINREFGSLGAINVTYTTVPGMLSLKNQTVGNLAEPEVDFVPIIGFLILEEGETAAAINITILEDDVPELEEYFLVNLTYVGLTMAASTSFPPRLDSEGLTAQVIIDANDGARGVIEWQQSRFEVNETHGSLTLVAQRSREPLGHVSLFVYAQNLEAQVGLDYIFTPMILHFADGERYKNVNIMILDDDIPEGDEKFQLILTNPSPGLELGKNTIALIIVLANDDGPGVLSFNNSEHFFLREPTALYVQESVAVLYIVREPAQGLFGTVTVQFIVTEVNSSNESKDLTPSKGYIVLEEGVRFKALQISAILDTEPEMDEYFVCTLFNPTGGARLGVHVQTLITVLQNQAPLGLFSISAVENRATSIDIEEANRTVYLNVSRTNGIDLAVSVQWETVSETAFGMRGMDVVFSVFQSFLDESASGWCFFTLENLIYGIMLRKSSVTVYRWQGIFIPVEDLNIENPKTCEAFNIGFSPYFVITHEERNEEKPSLNSVFTFTSGFKLFLVQTIIILESSQVRYFTSDSQDYLIIASQRDDSELTQVFRWNGGSFVLHQKLPVRGVLTVALFNKGGSVFLAISQANARLNSLLFRWSGSGFINFQEVPVSGTTEVEALSSANDIYLIFAENVFLGDQNSIDIFIWEMGQSSFRYFQSVDFAAVNRIHSFTPASGIAHILLIGQDMSALYCWNSERNQFSFVLEVPSAYDVASVTVKSLNSSKNLIALVGAHSHIYELAYISSHSDFIPSSGELIFEPGEREATIAVNILDDTVPEKEESFKVQLKNPKGGAEIGINDSVTITILSNDDAYGIVAFAQNSLYKQVEEMEQDSLVTLNVERLKGTYGRITIAWEADGSISDIFPTSGVILFTEGQVLSTITLTILADNIPELSEVVIVTLTRITTEGVEDSYKGATIDQDRSKSVITTLPNDSPFGLVGWRAASVFIRVAEPKENTTTLQLQIARDKGLLGDIAIHLRAQPNFLLHVDNQATENEDYVLQETIIIMKENIKEAHAEVSILPDDLPELEEGFIVTITEVNLVNSDFSTGQPSVRRPGMEIAEIMIEENDDPRGIFMFHVTRGAGEVITAYEVPPPLNVLQVPVVRLAGSFGAVNVYWKASPDSAGLEDFKPSHGILEFADKQVTAMIEITIIDDAEFELTETFNISLISVAGGGRLGDDVVVTVVIPQNDSPFGVFGFEEKTVMIDESLSSDDPDSYVTLTVVRSPGGKGTVRLEWTIDEKAKHNLSPLNGTLHFDETESQKTIVLHTLQDTVLEEDRRFTIQLISIDEVEISPVKGSASIIIRGDKRASGEVGIAPSSRHILIGEPSAKYNGTAIISLVRGPGILGEVTVFWRIFPPSVGEFAETSGKLTMRDEQSAVIVVIQALNDDIPEEKSFYEFQLTAVSEGGVLSESSSTANITVVASDSPYGRFAFSHEQLRVSEAQRVNITIIRSSGDFGHVRLWYKTMSGTAEAGLDFVPAAGELLFEAGEMRKSLHVEILDDDYPEGPEEFSLTITKVELQGRGYDFTIQENGLQIDQPPEIGNISIVRIIIMKNDNAEGIIEFDPKYTAFEVEEDVGLIMIPVVRLHGTYGYVTADFISQSSSASPGGVDYILHGSTVTFQHGQNLSFINISIIDDNESEFEEPIEILLTGATGGAVLGRHLVSRIIIAKSDSPFGVIRFLNQSKISIANPNSTMILSLVLERTGGLLGEIQVNWETVGPNSQEALLPQNRDIADPVSGLFYFGEGEGGVRTIILTIYPHEEIEVEETFIIKLHLVKGEAKLDSRAKDVTLTIQEFGDPNGVVQFAPETLSKKTYSEPLALEGPLLITFFVRRVKGTFGEIMVYWELSSEFDITEDFLSTSGFFTIADGESEASFDVHLLPDEVPEIEEDYVIQLVSVEGGAELDLEKSITWFSVYANDDPHGVFALYSDRQSILIGQNLIRSIQINITRLAGTFGDVAVGLRISSDHKEQPIVTENAERQLVVKDGATYKVDVVPIKNQVFLSLGSNFTLQLVTVMLVGGRFYGMPTILQEAKSAVLPVSEKAANSQVGFESTAFQLMNITAGTSHVMISRRGTYGALSVAWTTGYAPGLEIPEFIVVGNMTPTLGSLSFSHGEQRKGVFLWTFPSPGWPEAFVLHLSGVQSSAPGGAQLRSGFIVAEIEPMGVFQFSTSSRNIIVSEDTQMIRLHVQRLFGFHSDLIKVSYQTTAGSAKPLEDFEPVQNGELFFQKFQTEVDFEITIINDQLSEIEEFFYINLTSVEIRGLQKFDVNWSPRLNLDFSVAVITILDNDDLAGMDISFPETTVAVAVDTTLIPVETESTTYLSTSKTTTILQPTNVVAIVTEATGVSAIPEKLVTLHGTPAVSEKPDVATVTANVSIHGTFSLGPSIVYIEEEMKNGTFNTAEVLIRRTGGFTGNVSITVKTFGERCAQMEPNALPFRGIYGISNLTWAVEEEDFEEQTLTLIFLDGERERKVSVQILDDDEPEGQEFFYVFLTNPQGGAQIVEEKDDTGFAAFAMVIITGSDLHNGIIGFSEESQSGLELREGAVMRRLHLIVTRQPNRAFEDVKVFWRVTLNKTVVVLQKDGVNLVEELQSVSGTTTCTMGQTKCFISIELKPEKVPQVEVYFFVELYEATAGAAINNSARFAQIKILESDESQSLVYFSVGSRLAVAHKKATLISLQVARDSGTGLMMSVNFSTQELRSAETIGRTIISPAISGKDFVITEGTLVFEPGQRSTVLDVILTPETGSLNSFPKRFQIVLFDPKGGARIDKVYGTANITLVSDADSQAIWGLADQLHQPVNDDILNRVLHTISMKVATENTDEQLSAMMHLIEKITTEGKIQAFSVASRTLFYEILCSLINPKRKDTRGFSHFAEVTENFAFSLLTNVTCGSPGEKSKTILDSCPYLSILALHWYPQQINGHKFEGKEGDYIRIPERLLDVQDAEIMAGKSTCKLVQFTEYSSQQWFISGNNLPTLKNKVLSLSVKGQSSQLLTNDNEVLYRIYAAEPRIIPQTSLCLLWNQAAASWLSDSQFCKVVEETADYVECACSHMSVYAVYARTDNLSSYNEAFFTSGFICISGLCLAVLSHIFCARYSMFAAKLLTHMMAASLGTQILFLASAYASPQLAEESCSAMAAVTHYLYLCQFSWMLIQSVNFWYVLVMNDEHTERRYLLFFLLSWGLPAFVVILLIVILKGIYHQSMSQIYGLIHGDLCFIPNVYAALFTAALVPLTCLVVVFVVFIHAYQVKPQWKAYDDVFRGRTNAAEIPLILYLFALISVTWLWGGLHMAYRHFWMLVLFVIFNSLQGLYVFMVYFILHNQMCCPMKASYTVEMNGHPGPSTAFFTPGSGMPPAGGEISKSTQNLIGAMEEVPPDWERASFQQGSQASPDLKPSPQNGATFPSSGGYGQGSLIADEESQEFDDLIFALKTGAGLSVSDNESGQGSQEGGTLTDSQIVELRRIPIADTHL	chr5:90529344-91164437[+]	"G-protein coupled receptor which has an essential role in the development of hearing and vision. Couples to G-alpha(i)-proteins, GNAI1/2/3, G-alpha(q)-proteins, GNAQ, as well as G-alpha(s)-proteins, GNAS, inhibiting adenylate cyclase (AC) activity and cAMP production. Required for the hair bundle ankle formation, which connects growing stereocilia in developing cochlear hair cells of the inner ear. In response to extracellular calcium, activates kinases PKA and PKC to regulate myelination by inhibiting the ubiquitination of MAG, thus enhancing the stability of this protein in myelin-forming cells of the auditory pathway. In retina photoreceptors, the USH2 complex is required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport. Involved in the regulation of bone metabolism."	.	HGNC:17416	AGRV1_HUMAN	Reviewed	ENSG00000164199	.	.	.	.	.
Mol00010	Protein	A-kinase anchor protein 1 (AKAP1)	A-kinase anchor protein 149 kDa; AKAP 149; Dual specificity A-kinase-anchoring protein 1; D-AKAP-1; Protein kinase A-anchoring protein 1; PRKA1; Spermatid A-kinase anchor protein 84; S-AKAP84; AKAP149; PRKA1	AKAP1	8165	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000337714.8, AKAP1-202, 3909; ENST00000621116.4, AKAP1-219, 4285; ENST00000539273.5, AKAP1-204, 3153; ENST00000571629.5, AKAP1-206, 3105; ENST00000572557.5, AKAP1-208, 3098; ENST00000314126.4, AKAP1-201, 2380; ENST00000572156.1, AKAP1-207, 710; ENST00000575322.1, AKAP1-216, 650; ENST00000576295.5, AKAP1-217, 614; ENST00000574683.1, AKAP1-213, 588; ENST00000575186.5, AKAP1-215, 578; ENST00000575032.5, AKAP1-214, 570; ENST00000570423.5, AKAP1-205, 568; ENST00000576591.1, AKAP1-218, 565; ENST00000572814.1, AKAP1-210, 532; ENST00000573085.1, AKAP1-211, 484; ENST00000572560.1, AKAP1-209, 442; ENST00000481416.5, AKAP1-203, 4089; ENST00000573326.1, AKAP1-212, 1580"	MAIQFRSLFPLALPGMLALLGWWWFFSRKKGHVSSHDEQQVEAGAVQLRADPAIKEPLPVEDVCPKVVSTPPSVTEPPEKELSTVSKLPAEPPALLQTHPPCRRSESSGILPNTTDMRLRPGTRRDDSTKLELALTGGEAKSIPLECPLSSPKGVLFSSKSAEVCKQDSPFSRVPRKVQPGYPVVPAEKRSSGERARETGGAEGTGDAVLGEKVLEEALLSREHVLELENSKGPSLASLEGEEDKGKSSSSQVVGPVQEEEYVAEKLPSRFIESAHTELAKDDAAPAPPVADAKAQDRGVEGELGNEESLDRNEEGLDRNEEGLDRNEESLDRNEEGLDRNEEIKRAAFQIISQVISEATEQVLATTVGKVAGRVCQASQLQGQKEESCVPVHQKTVLGPDTAEPATAEAAVAPPDAGLPLPGLPAEGSPPPKTYVSCLKSLLSSPTKDSKPNISAHHISLASCLALTTPSEELPDRAGILVEDATCVTCMSDSSQSVPLVASPGHCSDSFSTSGLEDSCTETSSSPRDKAITPPLPESTVPFSNGVLKGELSDLGAEDGWTMDAEADHSGGSDRNSMDSVDSCCSLKKTESFQNAQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMPLSDDDQFSPEADAAMSEMTGNTALLAQVTSYSPTGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYYTSL	chr17:57085092-57121346[+]	Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. Involved in mitochondrial-mediated antiviral innate immunity. Promotes translocation of NDUFS1 into mitochondria to regulate mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) activity.	.	HGNC:367	AKAP1_HUMAN	Reviewed	ENSG00000121057	.	.	.	.	.
Mol00011	Protein	RAC-beta serine/threonine-protein kinase (AKT2)	Protein kinase Akt-2; Protein kinase B beta; PKB beta; RAC-PK-beta	AKT2	208	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000392038.7, AKT2-206, 5250; ENST00000424901.5, AKT2-210, 5170; ENST00000311278.10, AKT2-201, 1393; ENST00000579047.5, AKT2-234, 2029; ENST00000578615.6, AKT2-232, 1188; ENST00000672890.1, AKT2-244, 1148; ENST00000441941.6, AKT2-212, 974; ENST00000416362.5, AKT2-207, 974; ENST00000416994.6, AKT2-208, 904; ENST00000423127.5, AKT2-209, 798; ENST00000392037.5, AKT2-205, 681; ENST00000486368.6, AKT2-219, 606; ENST00000596634.5, AKT2-241, 583; ENST00000456441.5, AKT2-214, 582; ENST00000452077.5, AKT2-213, 577; ENST00000583859.5, AKT2-239, 567; ENST00000578123.5, AKT2-229, 564; ENST00000427375.1, AKT2-211, 554; ENST00000358335.9, AKT2-202, 546; ENST00000580747.5, AKT2-236, 525; ENST00000476247.6, AKT2-215, 488; ENST00000497948.5, AKT2-226, 456; ENST00000578310.1, AKT2-231, 158; ENST00000391844.8, AKT2-203, 1795; ENST00000584288.5, AKT2-240, 1706; ENST00000492463.6, AKT2-224, 737; ENST00000489375.5, AKT2-222, 734; ENST00000491778.6, AKT2-223, 573; ENST00000601166.5, AKT2-242, 554; ENST00000581582.1, AKT2-238, 655; ENST00000391845.6, AKT2-204, 636; ENST00000672879.1, AKT2-243, 618; ENST00000498350.1, AKT2-227, 562; ENST00000480878.6, AKT2-217, 506; ENST00000486647.5, AKT2-220, 457; ENST00000483166.5, AKT2-218, 4454; ENST00000578975.1, AKT2-233, 3337; ENST00000476266.5, AKT2-216, 3309; ENST00000487537.3, AKT2-221, 1669; ENST00000537834.5, AKT2-228, 1402; ENST00000496089.6, AKT2-225, 982; ENST00000580878.1, AKT2-237, 709; ENST00000579345.5, AKT2-235, 561; ENST00000578282.5, AKT2-230, 305"	MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE	chr19:40230317-40285536[-]	"AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.; FUNCTION: One of the few specific substrates of AKT2 identified recently is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'."	PDB: 1GZK; PDB: 1GZN; PDB: 1GZO; PDB: 1MRV; PDB: 1MRY; PDB: 1O6K; PDB: 1O6L; PDB: 1P6S; PDB: 2JDO; PDB: 2JDR; PDB: 2UW9; PDB: 2X39; PDB: 2XH5; PDB: 3D0E; PDB: 3E87; PDB: 3E88; PDB: 3E8D	HGNC:392	AKT2_HUMAN	Reviewed	ENSG00000105221	.	.	.	.	.
Mol00012	Protein	Annexin A2 (ANXA2)	Annexin II; Annexin-2; Calpactin I heavy chain; Calpactin-1 heavy chain; Chromobindin-8; Lipocortin II; Placental anticoagulant protein IV; PAP-IV; Protein I; p36; ANX2; ANX2L4; CAL1H; LPC2D	ANXA2	302	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000451270.7, ANXA2-204, 1554; ENST00000678450.1, ANXA2-243, 2069; ENST00000678061.1, ANXA2-242, 1989; ENST00000560468.6, ANXA2-233, 1838; ENST00000557906.6, ANXA2-207, 1790; ENST00000677968.1, ANXA2-241, 1761; ENST00000678870.1, ANXA2-245, 1747; ENST00000559956.6, ANXA2-227, 1709; ENST00000396024.7, ANXA2-202, 1676; ENST00000558558.6, ANXA2-213, 1616; ENST00000559818.6, ANXA2-226, 1615; ENST00000679109.1, ANXA2-246, 1560; ENST00000332680.8, ANXA2-201, 1444; ENST00000421017.6, ANXA2-203, 1444; ENST00000559780.6, ANXA2-225, 1964; ENST00000559113.6, ANXA2-217, 1542; ENST00000558985.6, ANXA2-214, 1445; ENST00000560367.6, ANXA2-230, 777; ENST00000559467.5, ANXA2-221, 755; ENST00000559176.5, ANXA2-218, 744; ENST00000557986.5, ANXA2-209, 733; ENST00000560165.5, ANXA2-229, 718; ENST00000559350.5, ANXA2-219, 669; ENST00000560466.5, ANXA2-232, 665; ENST00000560389.5, ANXA2-231, 594; ENST00000558132.5, ANXA2-210, 580; ENST00000559725.5, ANXA2-224, 561; ENST00000558986.5, ANXA2-215, 560; ENST00000558998.5, ANXA2-216, 543; ENST00000559370.5, ANXA2-220, 521; ENST00000557904.5, ANXA2-206, 369; ENST00000560014.5, ANXA2-228, 2339; ENST00000558169.6, ANXA2-211, 1920; ENST00000676687.1, ANXA2-239, 1659; ENST00000561022.5, ANXA2-237, 834; ENST00000558503.6, ANXA2-212, 827; ENST00000560936.2, ANXA2-236, 908; ENST00000557937.5, ANXA2-208, 694; ENST00000560495.1, ANXA2-234, 567; ENST00000561445.5, ANXA2-238, 514; ENST00000504475.6, ANXA2-205, 3528; ENST00000677258.1, ANXA2-240, 2946; ENST00000678796.1, ANXA2-244, 1938; ENST00000559647.2, ANXA2-223, 1747; ENST00000559559.5, ANXA2-222, 1076; ENST00000560546.5, ANXA2-235, 574"	MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD	chr15:60347134-60402883[-]	"Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9."	PDB: 1W7B; PDB: 1XJL; PDB: 2HYU; PDB: 2HYV; PDB: 2HYW; PDB: 4DRW; PDB: 4FTG; PDB: 4HRH; PDB: 5LPU; PDB: 5LPX; PDB: 5LQ0; PDB: 5LQ2; PDB: 5N7D; PDB: 5N7F; PDB: 5N7G; PDB: 6TWQ; PDB: 6TWU; PDB: 6TWX; PDB: 6TWY	HGNC:537	ANXA2_HUMAN	Reviewed	ENSG00000182718	.	.	.	.	.
Mol00013	Protein	Apoptotic protease-activating factor 1 (APAF1)	APAF-1; KIAA0413	APAF1	317	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000551964.6, APAF1-210, 7201; ENST00000357310.5, APAF1-202, 7055; ENST00000359972.6, APAF1-203, 7029; ENST00000550527.5, APAF1-209, 6581; ENST00000333991.5, APAF1-201, 4539; ENST00000547045.5, APAF1-205, 3744; ENST00000552268.5, APAF1-211, 1143; ENST00000549007.1, APAF1-208, 3492; ENST00000547743.1, APAF1-207, 651; ENST00000547666.1, APAF1-206, 1596; ENST00000552929.1, APAF1-212, 993; ENST00000546491.1, APAF1-204, 892; ENST00000555047.1, APAF1-213, 389"	MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE	chr12:98645290-98735433[+]	"Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis."	PDB: 1C15; PDB: 1CWW; PDB: 1CY5; PDB: 1Z6T; PDB: 2P1H; PDB: 2YGS; PDB: 3J2T; PDB: 3JBT; PDB: 3YGS; PDB: 4RHW; PDB: 5JUY; PDB: 5WVC; PDB: 5WVE	HGNC:576	APAF_HUMAN	Reviewed	ENSG00000120868	.	.	.	.	.
Mol00014	Protein	Adenomatous polyposis coli protein (APC)	Protein APC; Deleted in polyposis 2.5; DP2.5	APC	324	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000257430.9, APC-201, 10704; ENST00000508376.6, APC-207, 10619; ENST00000512211.6, APC-210, 4061; ENST00000507379.5, APC-206, 3602; ENST00000504915.2, APC-203, 817; ENST00000509732.5, APC-209, 524; ENST00000508624.5, APC-208, 7406; ENST00000502371.2, APC-202, 2630; ENST00000505350.1, APC-205, 573; ENST00000505084.1, APC-204, 1212"	MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQIAEIKEKIGTRSAEDPVSEVPAVSQHPRTKSSRLQGSSLSSESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTAQTKREVPKNKAPTAEKRESGPKQAAVNAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPKESNENQEKEAEKTIDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKPAQTASKLPPPVARKPSQLPVYKLLPSQNRLQPQKHVSFTPGDDMPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGEGVRGGAQSGEFEKRDTIPTEGRSTDEAQGGKTSSVTIPELDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASASSSAPNKNQLDGKKKKPTSPVKPIPQNTEYRTRVRKNADSKNNLNAERVFSDNKDSKKQNLKNNSKVFNDKLPNNEDRVRGSFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKAKENKESEAKVTSHTELTSNQQSANKTQAIAKQPINRGQPKPILQKQSTFPQSSKDIPDRGAATDEKLQNFAIENTPVCFSHNSSLSSLSDIDQENNNKENEPIKETEPPDSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKKPSRLKGDNEKHSPRNMGGILGEDLTLDLKDIQRPDSEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLETKKIESESKGIKGGKKVYKSLITGKVRSNSEISGQMKQPLQANMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGQTATTSPRGAKPSVKSELSPVARQTSQIGGSSKAPSRSGSRDSTPSRPAQQPLSRPIQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQMSQQNLTKQTGLSKNASSIPRSESASKGLNQMNNGNGANKKVELSRMSSTKSSGSESDRSERPVLVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPASPTRSQAQTPVLSPSLPDMSLSTHSSVQAGGWRKLPPNLSPTIEYNDGRPAKRHDIARSHSESPSRLPINRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSISGTKQSKENQVSAKGTWRKIKENEFSPTNSTSQTVSSGATNGAESKTLIYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKANPNIKDSKDNQAKQNVGNGSVPMRTVGLENRLNSFIQVDAPDQKGTEIKPGQNNPVPVSETNESSIVERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVNNNTKKRDSKTDSTESSGTQSPKRHSGSYLVTSV	chr5:112707498-112846239[+]	Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.	PDB: 1DEB; PDB: 1EMU; PDB: 1JPP; PDB: 1M5I; PDB: 1T08; PDB: 1TH1; PDB: 1V18; PDB: 2RQU; PDB: 3AU3; PDB: 3NMW; PDB: 3NMX; PDB: 3NMZ; PDB: 3QHE; PDB: 3RL7; PDB: 3RL8; PDB: 3T7U; PDB: 4G69; PDB: 4YJE; PDB: 4YJL; PDB: 4YK6; PDB: 5B6G; PDB: 5IZ6; PDB: 5IZ8; PDB: 5IZ9; PDB: 5IZA; PDB: 5Z8H	HGNC:583	APC_HUMAN	Reviewed	ENSG00000134982	.	.	.	.	.
Mol00015	Protein	Amphiregulin (AREG)	AR; Colorectum cell-derived growth factor; CRDGF; AREGB; SDGF	AREG	374	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000395748.8, AREG-201, 1234; ENST00000502307.1, AREG-202, 956; ENST00000511560.1, AREG-203, 763"	MRAPLLPPAPVVLSLLILGSGHYAAGLDLNDTYSGKREPFSGDHSADGFEVTSRSEMSSGSEISPVSEMPSSSEPSSGADYDYSEEYDNEPQIPGYIVDDSVRVEQVVKPPQNKTESENTSDKPKRKKKGGKNGKNRRNRKKKNPCNAEFQNFCIHGECKYIEHLEAVTCKCQQEYFGERCGEKSMKTHSMIDSSLSKIALAAIAAFMSAVILTAVAVITVQLRRQYVRKYEGEAEERKKLRQENGNVHAIA	chr4:74445136-74455005[+]	"Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts."	PDB: 2RNL	HGNC:651	AREG_HUMAN	Reviewed	ENSG00000109321	.	.	.	.	.
Mol00016	Protein	Cyclic AMP-dependent transcription factor ATF-2 (ATF2)	cAMP-dependent transcription factor ATF-2; Activating transcription factor 2; Cyclic AMP-responsive element-binding protein 2; CREB-2; cAMP-responsive element-binding protein 2; HB16; cAMP response element-binding protein CRE-BP1; CREB2; CREBP1	ATF2	1386	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264110.7, ATF2-201, 4164; ENST00000426833.7, ATF2-212, 4132; ENST00000345739.9, ATF2-202, 4079; ENST00000409635.5, ATF2-206, 2109; ENST00000392544.5, ATF2-203, 1919; ENST00000409833.5, ATF2-207, 1335; ENST00000409437.5, ATF2-204, 3697; ENST00000435004.6, ATF2-215, 1115; ENST00000437522.5, ATF2-217, 883; ENST00000409499.5, ATF2-205, 801; ENST00000417080.5, ATF2-210, 2113; ENST00000429579.5, ATF2-214, 2081; ENST00000428760.5, ATF2-213, 1989; ENST00000421438.5, ATF2-211, 1966; ENST00000415955.5, ATF2-209, 1896; ENST00000456655.5, ATF2-219, 1861; ENST00000435231.6, ATF2-216, 784; ENST00000413123.5, ATF2-208, 681; ENST00000445349.1, ATF2-218, 483; ENST00000478905.1, ATF2-220, 697"	MKFKLHVNSARQYKDLWNMSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPATSTTETPASPAHTTPQTQSTSGRRRRAANEDPDEKRRKFLERNRAAASRCRQKRKVWVQSLEKKAEDLSSLNGQLQSEVTLLRNEVAQLKQLLLAHKDCPVTAMQKKSGYHTADKDDSSEDISVPSSPHTEAIQHSSVSTSNGVSSTSKAEAVATSVLTQMADQSTEPALSQIVMAPSSQSQPSGS	chr2:175072250-175168382[-]	"Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus sequences (5'-TGACTCA-3'). In the nucleus, contributes to global transcription and the DNA damage response, in addition to specific transcriptional activities that are related to cell development, proliferation and death. In the cytoplasm, interacts with and perturbs HK1- and VDAC1-containing complexes at the mitochondrial outer membrane, thereby impairing mitochondrial membrane potential, inducing mitochondrial leakage and promoting cell death. The phosphorylated form (mediated by ATM) plays a role in the DNA damage response and is involved in the ionizing radiation (IR)-induced S phase checkpoint control and in the recruitment of the MRN complex into the IR-induced foci (IRIF). Exhibits histone acetyltransferase (HAT) activity which specifically acetylates histones H2B and H4 in vitro. In concert with CUL3 and RBX1, promotes the degradation of KAT5 thereby attenuating its ability to acetylate and activate ATM. Can elicit oncogenic or tumor suppressor activities depending on the tissue or cell type."	PDB: 1BHI; PDB: 1T2K; PDB: 4H36; PDB: 6ZQS; PDB: 6ZR5	HGNC:784	ATF2_HUMAN	Reviewed	ENSG00000115966	.	.	.	.	.
Mol00017	Protein	Ubiquitin-like protein ATG12 (ATG12)	Autophagy-related protein 12; APG12-like; APG12; APG12L	ATG12	9140	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000509910.2, ATG12-208, 4040; ENST00000500945.2, ATG12-202, 1430; ENST00000513322.5, ATG12-212, 1558; ENST00000379594.7, ATG12-201, 1082; ENST00000505993.5, ATG12-204, 773; ENST00000513167.1, ATG12-210, 732; ENST00000509598.5, ATG12-207, 2106; ENST00000513292.5, ATG12-211, 692; ENST00000514775.1, ATG12-213, 553; ENST00000505252.1, ATG12-203, 3274; ENST00000508464.5, ATG12-206, 1211; ENST00000507793.5, ATG12-205, 807; ENST00000511984.5, ATG12-209, 567"	MAEEPQSVLQLPTSIAAGGEGLTDVSPETTTPEPPSSAAVSPGTEEPAGDTKKKIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHYCKSQAWG	chr5:115828200-115841837[-]	"Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes."	PDB: 4GDK; PDB: 4GDL; PDB: 4NAW	HGNC:588	ATG12_HUMAN	Reviewed	ENSG00000145782	.	.	.	.	.
Mol00018	Protein	Autophagy protein 5 (ATG5)	APG5-like; Apoptosis-specific protein; APG5L; ASP	ATG5	9474	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369076.8, ATG5-204, 3185; ENST00000343245.7, ATG5-201, 3092; ENST00000635758.2, ATG5-208, 3035; ENST00000360666.6, ATG5-202, 2712; ENST00000636437.1, ATG5-210, 2261; ENST00000613993.1, ATG5-207, 733; ENST00000369070.5, ATG5-203, 3088; ENST00000646025.1, ATG5-211, 1888; ENST00000636335.1, ATG5-209, 1219; ENST00000475645.1, ATG5-205, 2659; ENST00000476518.1, ATG5-206, 602"	MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVMRQEDISEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPSKDAIEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEYPAEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLKEVCPSAIDPEDGEKKNQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIIPQPTD	chr6:106045423-106325791[-]	"Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway."	PDB: 4GDK; PDB: 4GDL; PDB: 4NAW; PDB: 4TQ0; PDB: 4TQ1; PDB: 5D7G; PDB: 5NPV; PDB: 5NPW	HGNC:589	ATG5_HUMAN	Reviewed	ENSG00000057663	.	.	.	.	.
Mol00019	Protein	Ubiquitin-like modifier-activating enzyme ATG7 (ATG7)	ATG12-activating enzyme E1 ATG7; Autophagy-related protein 7; APG7-like; hAGP7; Ubiquitin-activating enzyme E1-like protein; APG7L	ATG7	10533	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000693202.1, ATG7-226, 5333; ENST00000354449.7, ATG7-201, 4959; ENST00000685771.1, ATG7-225, 2436; ENST00000354956.9, ATG7-202, 2296; ENST00000446450.6, ATG7-213, 2042; ENST00000451513.5, ATG7-214, 972; ENST00000414717.5, ATG7-203, 710; ENST00000423116.1, ATG7-206, 589; ENST00000444619.5, ATG7-211, 565; ENST00000419112.5, ATG7-205, 565; ENST00000451830.5, ATG7-215, 549; ENST00000427759.5, ATG7-208, 455; ENST00000446110.1, ATG7-212, 435; ENST00000435760.6, ATG7-210, 2618; ENST00000424071.5, ATG7-207, 758; ENST00000418682.5, ATG7-204, 584; ENST00000434066.6, ATG7-209, 553; ENST00000469654.2, ATG7-221, 739; ENST00000488924.5, ATG7-224, 570; ENST00000464282.1, ATG7-219, 558; ENST00000460444.5, ATG7-217, 540; ENST00000478638.5, ATG7-223, 520; ENST00000460291.1, ATG7-216, 951; ENST00000461278.1, ATG7-218, 545; ENST00000470474.1, ATG7-222, 534; ENST00000467121.1, ATG7-220, 488"	MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDMSAPTPARCCPAIGTLYNTNTLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGLDQRFSLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVSLLKHYSDFFQGQRTKITIGVYDPCNLAQYPGWPLRNFLVLAAHRWSSSFQSVEVVCFRDRTMQGARDVAHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVNFSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPKQQGAGDLCPNHPVASADLLGSSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHSFLEDLTGLTLLHQETQAAEIWDMSDDETI	chr3:11272309-11557665[+]	"E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner (By similarity)."	.	HGNC:16935	ATG7_HUMAN	Reviewed	ENSG00000197548	.	.	.	.	.
Mol00020	Protein	Copper-transporting ATPase 1 (ATP7A)	Copper pump 1; Menkes disease-associated protein; MC1; MNK	ATP7A	538	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000341514.11, ATP7A-201, 8492; ENST00000687086.1, ATP7A-229, 5092; ENST00000686133.1, ATP7A-217, 5003; ENST00000685264.1, ATP7A-212, 4984; ENST00000692908.1, ATP7A-253, 4908; ENST00000686543.1, ATP7A-223, 4716; ENST00000689767.1, ATP7A-246, 8569; ENST00000343533.10, ATP7A-202, 8548; ENST00000685033.1, ATP7A-210, 5592; ENST00000686033.1, ATP7A-215, 4755; ENST00000689649.1, ATP7A-244, 3268; ENST00000689530.1, ATP7A-242, 3250; ENST00000688338.1, ATP7A-237, 3180; ENST00000686480.1, ATP7A-221, 3115; ENST00000686688.1, ATP7A-225, 3050; ENST00000693398.1, ATP7A-257, 3000; ENST00000693167.1, ATP7A-255, 2839; ENST00000691152.1, ATP7A-249, 2460; ENST00000689891.1, ATP7A-248, 2313; ENST00000692110.1, ATP7A-251, 2202; ENST00000693051.1, ATP7A-254, 2198; ENST00000688249.1, ATP7A-236, 2183; ENST00000687416.1, ATP7A-231, 2137; ENST00000687984.1, ATP7A-234, 1994; ENST00000687599.1, ATP7A-232, 1978; ENST00000686464.1, ATP7A-220, 1818; ENST00000685885.1, ATP7A-214, 1644; ENST00000645454.1, ATP7A-206, 978; ENST00000686560.1, ATP7A-224, 930; ENST00000689731.1, ATP7A-245, 913; ENST00000688165.1, ATP7A-235, 868; ENST00000684798.1, ATP7A-209, 782; ENST00000692729.1, ATP7A-252, 743; ENST00000686896.1, ATP7A-226, 721; ENST00000686050.1, ATP7A-216, 706; ENST00000642651.1, ATP7A-204, 571; ENST00000689872.1, ATP7A-247, 5842; ENST00000645094.1, ATP7A-205, 4019; ENST00000688889.1, ATP7A-239, 2524; ENST00000693387.1, ATP7A-256, 2211; ENST00000686515.1, ATP7A-222, 2605; ENST00000642523.1, ATP7A-203, 1793; ENST00000686255.1, ATP7A-218, 7359; ENST00000682475.1, ATP7A-207, 6274; ENST00000687628.1, ATP7A-233, 5297; ENST00000688746.1, ATP7A-238, 5087; ENST00000689083.1, ATP7A-240, 4730; ENST00000691456.1, ATP7A-250, 3075; ENST00000686999.1, ATP7A-227, 2834; ENST00000689541.1, ATP7A-243, 2573; ENST00000686416.1, ATP7A-219, 2474; ENST00000689514.1, ATP7A-241, 2388; ENST00000685208.1, ATP7A-211, 2316; ENST00000682742.2, ATP7A-208, 2121; ENST00000685434.1, ATP7A-213, 1992; ENST00000687325.1, ATP7A-230, 1279; ENST00000687082.1, ATP7A-228, 1094"	MDPSMGVNSVTISVEGMTCNSCVWTIEQQIGKVNGVHHIKVSLEEKNATIIYDPKLQTPKTLQEAIDDMGFDAVIHNPDPLPVLTDTLFLTVTASLTLPWDHIQSTLLKTKGVTDIKIYPQKRTVAVTIIPSIVNANQIKELVPELSLDTGTLEKKSGACEDHSMAQAGEVVLKMKVEGMTCHSCTSTIEGKIGKLQGVQRIKVSLDNQEATIVYQPHLISVEEMKKQIEAMGFPAFVKKQPKYLKLGAIDVERLKNTPVKSSEGSQQRSPSYTNDSTATFIIDGMHCKSCVSNIESTLSALQYVSSIVVSLENRSAIVKYNASSVTPESLRKAIEAVSPGLYRVSITSEVESTSNSPSSSSLQKIPLNVVSQPLTQETVINIDGMTCNSCVQSIEGVISKKPGVKSIRVSLANSNGTVEYDPLLTSPETLRGAIEDMGFDATLSDTNEPLVVIAQPSSEMPLLTSTNEFYTKGMTPVQDKEEGKNSSKCYIQVTGMTCASCVANIERNLRREEGIYSILVALMAGKAEVRYNPAVIQPPMIAEFIRELGFGATVIENADEGDGVLELVVRGMTCASCVHKIESSLTKHRGILYCSVALATNKAHIKYDPEIIGPRDIIHTIESLGFEASLVKKDRSASHLDHKREIRQWRRSFLVSLFFCIPVMGLMIYMMVMDHHFATLHHNQNMSKEEMINLHSSMFLERQILPGLSVMNLLSFLLCVPVQFFGGWYFYIQAYKALKHKTANMDVLIVLATTIAFAYSLIILLVAMYERAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLDSDNILLSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVFVSIATLLVWIVIGFLNFEIVETYFPGYNRSISRTETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLTESNRISHHKILAIVGTAESNSEHPLGTAITKYCKQELDTETLGTCIDFQVVPGCGISCKVTNIEGLLHKNNWNIEDNNIKNASLVQIDASNEQSSTSSSMIIDAQISNALNAQQYKVLIGNREWMIRNGLVINNDVNDFMTEHERKGRTAVLVAVDDELCGLIAIADTVKPEAELAIHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMANVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLVGIPIAAGVFMPIGLVLQPWMGSAAMAASSVSVVLSSLFLKLYRKPTYESYELPARSQIGQKSPSEISVHVGIDDTSRNSPKLGLLDRIVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTAL	chrX:77910690-78050395[+]	"ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis. Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state. Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway. Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions. May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3. In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis."	PDB: 1AW0; PDB: 1KVI; PDB: 1KVJ; PDB: 1Q8L; PDB: 1S6O; PDB: 1S6U; PDB: 1Y3J; PDB: 1Y3K; PDB: 1YJR; PDB: 1YJT; PDB: 1YJU; PDB: 1YJV; PDB: 2AW0; PDB: 2G9O; PDB: 2GA7; PDB: 2K1R; PDB: 2KIJ; PDB: 2KMV; PDB: 2KMX; PDB: 3CJK; PDB: 5T7L; PDB: 7LU8	HGNC:869	ATP7A_HUMAN	Reviewed	ENSG00000165240	.	.	.	.	.
Mol00021	Protein	Copper-transporting ATPase 2 (ATP7B)	Copper pump 2; Wilson disease-associated protein; PWD; WC1; WND	ATP7B	540	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000242839.10, ATP7B-201, 6598; ENST00000344297.9, ATP7B-202, 6016; ENST00000673772.1, ATP7B-218, 4308; ENST00000400366.6, ATP7B-203, 4065; ENST00000448424.7, ATP7B-206, 6451; ENST00000674147.1, ATP7B-226, 5415; ENST00000634844.1, ATP7B-215, 4398; ENST00000418097.7, ATP7B-205, 4340; ENST00000400370.8, ATP7B-204, 3252; ENST00000634308.1, ATP7B-211, 4321; ENST00000634296.1, ATP7B-210, 2328; ENST00000673864.1, ATP7B-221, 1011; ENST00000482841.6, ATP7B-208, 1845; ENST00000673789.1, ATP7B-219, 1083; ENST00000634519.1, ATP7B-212, 727; ENST00000673844.1, ATP7B-220, 536; ENST00000635406.1, ATP7B-216, 506; ENST00000673867.1, ATP7B-222, 6613; ENST00000634810.1, ATP7B-214, 5825; ENST00000634620.1, ATP7B-213, 5653; ENST00000674126.1, ATP7B-225, 4954; ENST00000673923.1, ATP7B-223, 3336; ENST00000674078.1, ATP7B-224, 2966; ENST00000673696.1, ATP7B-217, 2800; ENST00000483772.2, ATP7B-209, 717; ENST00000466629.1, ATP7B-207, 463"	MPEQERQITAREGASRKILSKLSLPTRAWEPAMKKSFAFDNVGYEGGLDGLGPSSQVATSTVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEASIAEGKAASWPSRSLPAQEAVVKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAAIKSKVAPLSLGPIDIERLQSTNPKRPLSSANQNFNNSETLGHQGSHVVTLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEALPPGNFKVSLPDGAEGSGTDHRSSSSHSPGSPPRNQVQGTCSTTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSESCSTNPLGNHSAGNSMVQTTDGTPTSVQEVAPHTGRLPANHAPDILAKSPQSTRAVAPQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVMEDYAGSDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQRNPNAHHLDHKMEIKQWKKSFLCSLVFGIPVMALMIYMLIPSNEPHQSMVLDHNIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEKAERSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFIDFGVVQRYFPNPNKHISQTEVIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCTDFQAVPGCGIGCKVSNVEGILAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIVLQPWMGSAAMAASSVSVVLSSLQLKCYKKPDLERYEAQAHGHMKPLTASQVSVHIGMDDRWRDSPRATPWDQVSYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQYI	chr13:51930436-52012125[-]	"Copper ion transmembrane transporter involved in the export of copper out of the cells. It is involved in copper homeostasis in the liver, where it ensures the efflux of copper from hepatocytes into the bile in response to copper overload."	PDB: 2ARF; PDB: 2EW9; PDB: 2KOY; PDB: 2LQB; PDB: 2N7Y; PDB: 2ROP; PDB: 6A71; PDB: 6A72	HGNC:870	ATP7B_HUMAN	Reviewed	ENSG00000123191	.	.	.	.	.
Mol00022	Protein	Aurora kinase A (AURKA)	Aurora 2; Aurora/IPL1-related kinase 1; ARK-1; Aurora-related kinase 1; hARK1; Breast tumor-amplified kinase; Serine/threonine-protein kinase 15; Serine/threonine-protein kinase 6; Serine/threonine-protein kinase aurora-A; AIK; AIRK1; ARK1; AURA; AYK1; BTAK; IAK1; STK15; STK6	AURKA	6790	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000395915.8, AURKA-208, 2033; ENST00000347343.6, AURKA-202, 2248; ENST00000395914.5, AURKA-207, 2238; ENST00000312783.10, AURKA-201, 2223; ENST00000395913.7, AURKA-206, 2169; ENST00000395911.5, AURKA-205, 2145; ENST00000371356.6, AURKA-203, 2112; ENST00000395907.5, AURKA-204, 1902; ENST00000441357.5, AURKA-211, 991; ENST00000420474.5, AURKA-209, 879; ENST00000456249.5, AURKA-213, 810; ENST00000422322.5, AURKA-210, 744; ENST00000451915.1, AURKA-212, 584"	MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS	chr20:56369389-56392337[-]	"Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Important for microtubule formation and/or stabilization. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1."	PDB: 1MQ4; PDB: 1MUO; PDB: 1OL5; PDB: 1OL6; PDB: 1OL7; PDB: 2BMC; PDB: 2C6D; PDB: 2C6E; PDB: 2DWB; PDB: 2J4Z; PDB: 2J50; PDB: 2NP8; PDB: 2W1C; PDB: 2W1D; PDB: 2W1E; PDB: 2W1F; PDB: 2W1G; PDB: 2WQE; PDB: 2WTV; PDB: 2WTW; PDB: 2X6D; PDB: 2X6E; PDB: 2X81; PDB: 2XNE; PDB: 2XNG; PDB: 2XRU; PDB: 3COH; PDB: 3E5A; PDB: 3EFW; PDB: 3FDN; PDB: 3H0Y; PDB: 3H0Z; PDB: 3H10; PDB: 3HA6; PDB: 3K5U; PDB: 3LAU; PDB: 3M11; PDB: 3MYG; PDB: 3NRM; PDB: 3O50; PDB: 3O51; PDB: 3P9J; PDB: 3QBN; PDB: 3R21; PDB: 3R22; PDB: 3UNZ; PDB: 3UO4; PDB: 3UO5; PDB: 3UO6; PDB: 3UOD; PDB: 3UOH; PDB: 3UOJ; PDB: 3UOK; PDB: 3UOL; PDB: 3UP2; PDB: 3UP7; PDB: 3VAP; PDB: 3W10; PDB: 3W16; PDB: 3W18; PDB: 3W2C; PDB: 4B0G; PDB: 4BN1; PDB: 4BYI; PDB: 4BYJ; PDB: 4C3P; PDB: 4C3R; PDB: 4CEG; PDB: 4DEA; PDB: 4DEB; PDB: 4DED; PDB: 4DEE; PDB: 4DHF; PDB: 4J8M; PDB: 4J8N; PDB: 4JAI; PDB: 4JAJ; PDB: 4JBO; PDB: 4JBP; PDB: 4JBQ; PDB: 4O0S; PDB: 4O0U; PDB: 4O0W; PDB: 4PRJ; PDB: 4UYN; PDB: 4UZD; PDB: 4UZH; PDB: 4ZS0; PDB: 4ZTQ; PDB: 4ZTR; PDB: 4ZTS; PDB: 5AAD; PDB: 5AAE; PDB: 5AAF; PDB: 5AAG; PDB: 5DN3; PDB: 5DNR; PDB: 5DOS; PDB: 5DPV; PDB: 5DR2; PDB: 5DR6; PDB: 5DR9; PDB: 5DRD; PDB: 5DT0; PDB: 5DT3; PDB: 5DT4; PDB: 5EW9; PDB: 5G15; PDB: 5G1X; PDB: 5L8J; PDB: 5L8K; PDB: 5L8L; PDB: 5LXM; PDB: 5OBJ; PDB: 5OBR; PDB: 5ODT; PDB: 5ONE; PDB: 5ORL; PDB: 5ORN; PDB: 5ORO; PDB: 5ORP; PDB: 5ORR; PDB: 5ORS; PDB: 5ORT; PDB: 5ORV; PDB: 5ORW; PDB: 5ORX; PDB: 5ORY; PDB: 5ORZ; PDB: 5OS0; PDB: 5OS1; PDB: 5OS2; PDB: 5OS3; PDB: 5OS4; PDB: 5OS5; PDB: 5OS6; PDB: 5OSD; PDB: 5OSE; PDB: 5OSF; PDB: 5ZAN; PDB: 6C2R; PDB: 6C2T; PDB: 6C83; PDB: 6CPE; PDB: 6CPF; PDB: 6CPG; PDB: 6GRA; PDB: 6HJJ; PDB: 6HJK; PDB: 6I2U; PDB: 6R49; PDB: 6R4A; PDB: 6R4B; PDB: 6R4C; PDB: 6R4D; PDB: 6VPG; PDB: 6VPH; PDB: 6VPI; PDB: 6VPJ; PDB: 6VPL; PDB: 6VPM; PDB: 6XKA; PDB: 6Z4Y; PDB: 7AYH; PDB: 7AYI; PDB: 7O2V	HGNC:11393	AURKA_HUMAN	Reviewed	ENSG00000087586	.	.	.	.	.
Mol00023	Protein	Bcl-2-like protein 2 (BCL2L2)	Bcl2-L-2; Apoptosis regulator Bcl-W; BCLW; KIAA0271	BCL2L2	599	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000250405.10, BCL2L2-201, 3526; ENST00000678311.1, BCL2L2-208, 3568; ENST00000679219.1, BCL2L2-210, 3557; ENST00000679000.1, BCL2L2-209, 3539; ENST00000557236.6, BCL2L2-206, 1245; ENST00000557579.2, BCL2L2-207, 762; ENST00000553824.5, BCL2L2-202, 548; ENST00000556599.1, BCL2L2-205, 548; ENST00000554635.1, BCL2L2-203, 545; ENST00000556100.3, BCL2L2-204, 1368"	MATPASAPDTRALVADFVGYKLRQKGYVCGAGPGEGPAADPLHQAMRAAGDEFETRFRRTFSDLAAQLHVTPGSAQQRFTQVSDELFQGGPNWGRLVAFFVFGAALCAESVNKEMEPLVGQVQEWMVAYLETQLADWIHSSGGWAEFTALYGDGALEEARRLREGNWASVRTVLTGAVALGALVTVGAFFASK	chr14:23298790-23311751[+]	Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.	PDB: 1MK3; PDB: 1O0L; PDB: 1ZY3; PDB: 2Y6W; PDB: 4CIM	HGNC:995	B2CL2_HUMAN	Reviewed	ENSG00000129473	.	.	.	.	.
Mol00024	Protein	Bcl-2-like protein 11 (BCL2L11)	Bcl2-L-11; Bcl2-interacting mediator of cell death; BIM	BCL2L11	10018	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393256.8, BCL2L11-206, 5098; ENST00000622509.4, BCL2L11-222, 5231; ENST00000621302.4, BCL2L11-221, 5224; ENST00000619294.4, BCL2L11-219, 5132; ENST00000610735.4, BCL2L11-217, 5120; ENST00000615946.4, BCL2L11-218, 5026; ENST00000622612.4, BCL2L11-223, 4995; ENST00000308659.12, BCL2L11-201, 1522; ENST00000357757.6, BCL2L11-203, 947; ENST00000337565.9, BCL2L11-202, 720; ENST00000405953.5, BCL2L11-207, 425; ENST00000620862.4, BCL2L11-220, 5044; ENST00000438054.1, BCL2L11-214, 656; ENST00000432179.1, BCL2L11-210, 572; ENST00000393252.3, BCL2L11-205, 482; ENST00000439718.1, BCL2L11-215, 936; ENST00000431217.1, BCL2L11-209, 883; ENST00000437029.5, BCL2L11-213, 729; ENST00000436733.5, BCL2L11-212, 618; ENST00000452231.5, BCL2L11-216, 459; ENST00000415458.5, BCL2L11-208, 438; ENST00000433098.5, BCL2L11-211, 1197; ENST00000361493.10, BCL2L11-204, 443"	MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH	chr2:111119378-111168445[+]	"Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis."	PDB: 1F95; PDB: 2K7W; PDB: 2NL9; PDB: 2V6Q; PDB: 2VM6; PDB: 2WH6; PDB: 2YQ6; PDB: 2YQ7; PDB: 3D7V; PDB: 3FDL; PDB: 3IO8; PDB: 3IO9; PDB: 3KJ0; PDB: 3KJ1; PDB: 3KJ2; PDB: 4A1U; PDB: 4A1W; PDB: 4B4S; PDB: 4D2M; PDB: 4QVF; PDB: 4UF3; PDB: 4YJ4; PDB: 4ZIE; PDB: 4ZIF; PDB: 4ZIH; PDB: 5AGW; PDB: 5AGX; PDB: 5C3G; PDB: 5VWV; PDB: 5VWW; PDB: 5VWX; PDB: 5VWY; PDB: 5VWZ; PDB: 5VX0; PDB: 5VX2; PDB: 5VX3; PDB: 5WOS; PDB: 6QFI; PDB: 6RJP; PDB: 6TQQ; PDB: 6UA3; PDB: 6UAB; PDB: 6VBX; PDB: 6X8O	HGNC:994	B2L11_HUMAN	Reviewed	ENSG00000153094	.	.	.	.	.
Mol00025	Protein	Apoptosis regulator BAX (BAX)	Bcl-2-like protein 4; Bcl2-L-4; BCL2L4	BAX	581	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000345358.12, BAX-202, 795; ENST00000293288.12, BAX-201, 1358; ENST00000415969.6, BAX-205, 540; ENST00000539787.2, BAX-212, 458; ENST00000354470.7, BAX-203, 433; ENST00000506183.5, BAX-208, 383; ENST00000356483.8, BAX-204, 677; ENST00000515540.5, BAX-211, 300; ENST00000502487.5, BAX-206, 1346; ENST00000513217.1, BAX-209, 869; ENST00000513545.5, BAX-210, 775; ENST00000503726.2, BAX-207, 488"	MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG	chr19:48954815-48961798[+]	"Plays a role in the mitochondrial apoptotic process. Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis."	PDB: 1F16; PDB: 2G5B; PDB: 2K7W; PDB: 2LR1; PDB: 3PK1; PDB: 3PL7; PDB: 4BD2; PDB: 4BD6; PDB: 4BD7; PDB: 4BD8; PDB: 4BDU; PDB: 4S0O; PDB: 4S0P; PDB: 4UF2; PDB: 4ZIE; PDB: 4ZIF; PDB: 4ZIG; PDB: 4ZIH; PDB: 4ZII; PDB: 5W5X; PDB: 5W5Z; PDB: 5W60; PDB: 5W61; PDB: 6EB6; PDB: 6L8V; PDB: 6L95; PDB: 6TRR; PDB: 6XY6; PDB: 7ADT	HGNC:959	BAX_HUMAN	Reviewed	ENSG00000087088	.	.	.	.	.
Mol00026	Protein	Bcl-2-binding component 3 (BBC3)	JFY-1; p53 up-regulated modulator of apoptosis; PUMA	BBC3	27113	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000439096.3, BBC3-203, 1846; ENST00000449228.5, BBC3-204, 1827; ENST00000341983.8, BBC3-202, 1538; ENST00000300880.11, BBC3-201, 1347; ENST00000601438.2, BBC3-206, 1747; ENST00000598636.1, BBC3-205, 900"	MARARQEGSSPEPVEGLARDGPRPFPLGRLVPSAVSCGLCEPGLAAAPAAPTLLPAAYLCAPTAPPAVTAALGGSRWPGGPRSRPRGPRPDGPQPSLSLAEQHLESPVPSAPGALAGGPTQAAPGVRGEEEQWAREIGAQLRRMADDLNAQYERRRQEEQQRHRPSPWRVLYNLIMGLLPLPRGHRAPEMEPN	chr19:47220822-47232766[-]	"Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis. Promotes partial unfolding of BCL2L1 and dissociation of BCL2L1 from p53/TP53, releasing the bound p53/TP53 to induce apoptosis. Regulates ER stress-induced neuronal apoptosis."	PDB: 2M04; PDB: 4BPI; PDB: 4BPJ; PDB: 4BPK; PDB: 4HNJ; PDB: 5UUL; PDB: 6QFM; PDB: 6QG8; PDB: 6TQP; PDB: 7DVD	HGNC:17868	BBC3_HUMAN	Reviewed	ENSG00000105327	.	.	.	.	.
Mol00027	Protein	B-cell lymphoma/leukemia 11A (BCL11A)	BCL-11A; B-cell CLL/lymphoma 11A; COUP-TF-interacting protein 1; Ecotropic viral integration site 9 protein homolog; EVI-9; Zinc finger protein 856; CTIP1; EVI9; KIAA1809; ZNF856	BCL11A	53335	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000642384.2, BCL11A-213, 6102; ENST00000356842.9, BCL11A-202, 4052; ENST00000358510.6, BCL11A-203, 2664; ENST00000359629.10, BCL11A-204, 2494; ENST00000642180.1, BCL11A-212, 6003; ENST00000335712.11, BCL11A-201, 5519; ENST00000643716.1, BCL11A-219, 4874; ENST00000646249.1, BCL11A-224, 3388; ENST00000489516.7, BCL11A-209, 1519; ENST00000643004.1, BCL11A-216, 1379; ENST00000642439.1, BCL11A-214, 1325; ENST00000643459.1, BCL11A-218, 993; ENST00000643222.1, BCL11A-217, 866; ENST00000409351.5, BCL11A-205, 758; ENST00000479026.2, BCL11A-207, 564; ENST00000489183.1, BCL11A-208, 372; ENST00000647469.1, BCL11A-226, 369; ENST00000631857.1, BCL11A-211, 2316; ENST00000647472.1, BCL11A-227, 1329; ENST00000477659.1, BCL11A-206, 2775; ENST00000642824.1, BCL11A-215, 726; ENST00000645405.1, BCL11A-222, 634; ENST00000492272.6, BCL11A-210, 619; ENST00000647038.1, BCL11A-225, 522; ENST00000645224.1, BCL11A-221, 3727; ENST00000645455.1, BCL11A-223, 819; ENST00000644606.1, BCL11A-220, 518"	MSRRKQGKPQHLSKREFSPEPLEAILTDDEPDHGPLGAPEGDHDLLTCGQCQMNFPLGDILIFIEHKRKQCNGSLCLEKAVDKPPSPSPIEMKKASNPVEVGIQVTPEDDDCLSTSSRGICPKQEHIADKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGICKDEPSSYTCTTCKQPFTSAWFLLQHAQNTHGLRIYLESEHGSPLTPRVGIPSGLGAECPSQPPLHGIHIADNNPFNLLRIPGSVSREASGLAEGRFPPTPPLFSPPPRHHLDPHRIERLGAEEMALATHHPSAFDRVLRLNPMAMEPPAMDFSRRLRELAGNTSSPPLSPGRPSPMQRLLQPFQPGSKPPFLATPPLPPLQSAPPPSQPPVKSKSCEFCGKTFKFQSNLVVHRRSHTGEKPYKCNLCDHACTQASKLKRHMKTHMHKSSPMTVKSDDGLSTASSPEPGTSDLVGSASSALKSVVAKFKSENDPNLIPENGDEEEEEDDEEEEEEEEEEEEELTESERVDYGFGLSLEAARHHENSSRGAVVGVGDESRALPDVMQGMVLSSMQHFSEAFHQVLGEKHKRGHLAEAEGHRDTCDEDSVAGESDRIDDGTVNGRGCSPGESASGGLSKKLLLGSPSSLSPFSKRIKLEKEFDLPPAAMPNTENVYSQWLAGYAASRQLKDPFLSFGDSRQSPFASSSEHSSENGSLRFSTPPGELDGGISGRSGTGSGGSTPHISGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKTE	chr2:60450520-60554467[-]	"Transcription factor. Associated with the BAF SWI/SNF chromatin remodeling complex. Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes, including a distal promoter of the HBG1 hemoglobin subunit gamma-1 gene. Involved in regulation of the developmental switch from gamma- to beta-globin, probably via direct repression of HBG1; hence indirectly repressing fetal hemoglobin (HbF) level. Involved in brain development. May play a role in hematopoiesis. Essential factor in lymphopoiesis required for B-cell formation in fetal liver. May function as a modulator of the transcriptional repression activity of NR2F2."	PDB: 5VTB; PDB: 6KI6; PDB: 6U9Q	HGNC:13221	BC11A_HUMAN	Reviewed	ENSG00000119866	.	.	.	.	.
Mol00028	Protein	Branched-chain-amino-acid aminotransferase (BCAT1)	BCAT(c); Protein ECA39; BCT1; ECA39	BCAT1	586	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261192.12, BCAT1-201, 9314; ENST00000538118.5, BCAT1-204, 4694; ENST00000342945.9, BCAT1-202, 4319; ENST00000539282.5, BCAT1-205, 1811; ENST00000539780.5, BCAT1-206, 1360; ENST00000546285.1, BCAT1-209, 549; ENST00000612790.1, BCAT1-210, 675; ENST00000544418.1, BCAT1-208, 2320; ENST00000543099.1, BCAT1-207, 568; ENST00000355164.3, BCAT1-203, 521"	MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS	chr12:24810024-24949101[-]	"Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine."	PDB: 2ABJ; PDB: 2COG; PDB: 2COI; PDB: 2COJ	HGNC:976	BCAT1_HUMAN	Reviewed	ENSG00000060982	.	.	.	.	.
Mol00029	Protein	Apoptosis regulator Bcl-2 (BCL2)	.	BCL2	596	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000333681.5, BCL2-201, 6881; ENST00000398117.1, BCL2-202, 7461; ENST00000589955.2, BCL2-203, 5011; ENST00000678301.1, BCL2-208, 5580; ENST00000590515.1, BCL2-204, 572; ENST00000678349.1, BCL2-209, 6551; ENST00000678134.1, BCL2-207, 6203; ENST00000677227.1, BCL2-205, 1896; ENST00000677635.1, BCL2-206, 5563"	MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK	chr18:63123346-63320128[-]	"Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release."	PDB: 1G5M; PDB: 1GJH; PDB: 1YSW; PDB: 2O21; PDB: 2O22; PDB: 2O2F; PDB: 2W3L; PDB: 2XA0; PDB: 4AQ3; PDB: 4IEH; PDB: 4LVT; PDB: 4LXD; PDB: 4MAN; PDB: 5AGW; PDB: 5AGX; PDB: 5FCG; PDB: 5JSN; PDB: 5VAU; PDB: 5VAX; PDB: 5VAY; PDB: 6GL8; PDB: 6IWB; PDB: 6O0K; PDB: 6O0L; PDB: 6O0M; PDB: 6O0O; PDB: 6O0P; PDB: 7LHB	HGNC:990	BCL2_HUMAN	Reviewed	ENSG00000171791	.	.	.	.	.
Mol00030	Protein	B-cell CLL/lymphoma 9 protein (BCL9)	B-cell lymphoma 9 protein; Bcl-9; Protein legless homolog	BCL9	607	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000234739.8, BCL9-201, 6189; ENST00000683836.1, BCL9-203, 6117; ENST00000684121.1, BCL9-204, 5639; ENST00000497938.1, BCL9-202, 476"	MHSSNPKVRSSPSGNTQSSPKSKQEVMVRPPTVMSPSGNPQLDSKFSNQGKQGGSASQSQPSPCDSKSGGHTPKALPGPGGSMGLKNGAGNGAKGKGKRERSISADSFDQRDPGTPNDDSDIKECNSADHIKSQDSQHTPHSMTPSNATAPRSSTPSHGQTTATEPTPAQKTPAKVVYVFSTEMANKAAEAVLKGQVETIVSFHIQNISNNKTERSTAPLNTQISALRNDPKPLPQQPPAPANQDQNSSQNTRLQPTPPIPAPAPKPAAPPRPLDRESPGVENKLIPSVGSPASSTPLPPDGTGPNSTPNNRAVTPVSQGSNSSSADPKAPPPPPVSSGEPPTLGENPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTGAQSGGPQQNPGVLDGPQKKPEGPIQAMMAQSQSLGKGPGPRTDVGAPFGPQGHRDVPFSPDEMVPPSMNSQSGTIGPDHLDHMTPEQIAWLKLQQEFYEEKRRKQEQVVVQQCSLQDMMVHQHGPRGVVRGPPPPYQMTPSEGWAPGGTEPFSDGINMPHSLPPRGMAPHPNMPGSQMRLPGFAGMINSEMEGPNVPNPASRPGLSGVSWPDDVPKIPDGRNFPPGQGIFSGPGRGERFPNPQGLSEEMFQQQLAEKQLGLPPGMAMEGIRPSMEMNRMIPGSQRHMEPGNNPIFPRIPVEGPLSPSRGDFPKGIPPQMGPGRELEFGMVPSGMKGDVNLNVNMGSNSQMIPQKMREAGAGPEEMLKLRPGGSDMLPAQQKMVPLPFGEHPQQEYGMGPRPFLPMSQGPGSNSGLRNLREPIGPDQRTNSRLSHMPPLPLNPSSNPTSLNTAPPVQRGLGRKPLDISVAGSQVHSPGINPLKSPTMHQVQSPMLGSPSGNLKSPQTPSQLAGMLAGPAAAASIKSPPVLGSAAASPVHLKSPSLPAPSPGWTSSPKPPLQSPGIPPNHKAPLTMASPAMLGNVESGGPPPPTASQPASVNIPGSLPSSTPYTMPPEPTLSQNPLSIMMSRMSKFAMPSSTPLYHDAIKTVASSDDDSPPARSPNLPSMNNMPGMGINTQNPRISGPNPVVPMPTLSPMGMTQPLSHSNQMPSPNAVGPNIPPHGVPMGPGLMSHNPIMGHGSQEPPMVPQGRMGFPQGFPPVQSPPQQVPFPHNGPSGGQGSFPGGMGFPGEGPLGRPSNLPQSSADAALCKPGGPGGPDSFTVLGNSMPSVFTDPDLQEVIRPGATGIPEFDLSRIIPSEKPSQTLQYFPRGEVPGRKQPQGPGPGFSHMQGMMGEQAPRMGLALPGMGGPGPVGTPDIPLGTAPSMPGHNPMRPPAFLQQGMMGPHHRMMSPAQSTMPGQPTLMSNPAAAVGMIPGKDRGPAGLYTHPGPVGSPGMMMSMQGMMGPQQNIMIPPQMRPRGMAADVGMGGFSQGPGNPGNMMF	chr1:147541501-147626216[+]	Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity).	PDB: 2GL7; PDB: 2VP7; PDB: 2VPB; PDB: 2VPD; PDB: 2VPE; PDB: 2VPG; PDB: 3SL9	HGNC:1008	BCL9_HUMAN	Reviewed	ENSG00000116128	.	.	.	.	.
Mol00031	Protein	Beclin-1 (BECN1)	Coiled-coil myosin-like BCL2-interacting protein; Protein GT197; GT197	BECN1	8678	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000590099.6, BECN1-213, 2109; ENST00000361523.8, BECN1-201, 2112; ENST00000438274.7, BECN1-202, 1569; ENST00000590764.1, BECN1-215, 854; ENST00000588276.5, BECN1-208, 769; ENST00000586589.5, BECN1-205, 731; ENST00000593205.5, BECN1-220, 629; ENST00000590852.1, BECN1-216, 570; ENST00000589636.5, BECN1-211, 561; ENST00000612631.1, BECN1-221, 559; ENST00000589663.5, BECN1-212, 489; ENST00000591085.1, BECN1-217, 559; ENST00000587880.1, BECN1-207, 524; ENST00000586754.2, BECN1-206, 475; ENST00000617806.4, BECN1-222, 4865; ENST00000543382.6, BECN1-203, 2504; ENST00000591307.5, BECN1-218, 744; ENST00000589493.1, BECN1-210, 719; ENST00000585515.5, BECN1-204, 636; ENST00000589492.1, BECN1-209, 597; ENST00000590185.1, BECN1-214, 581; ENST00000593112.1, BECN1-219, 557"	MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK	chr17:42810134-42833350[-]	"Plays a central role in autophagy. Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. Protects against infection by a neurovirulent strain of Sindbis virus. May play a role in antiviral host defense."	PDB: 2P1L; PDB: 2PON; PDB: 3DVU; PDB: 4DDP; PDB: 4MI8; PDB: 5EFM; PDB: 5HHE; PDB: 5VAU; PDB: 5VAX; PDB: 5VAY; PDB: 6DCN; PDB: 6DCO; PDB: 6HOI; PDB: 6HOJ; PDB: 6HOK; PDB: 7BL1	HGNC:1034	BECN1_HUMAN	Reviewed	ENSG00000126581	.	.	.	.	.
Mol00032	Protein	Bcl-2-interacting killer (BIK)	Apoptosis inducer NBK; BIP1; BP4; NBK	BIK	638	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000216115.3, BIK-201, 951"	MSEVRPLSRDILMETLLYEQLLEPPTMEVLGMTDSEEDLDPMEDFDSLECMEGSDALALRLACIGDEMDVSLRAPRLAQLSEVAMHSLGLAFIYDQTEDIRDVLRSFMDGFTTLKENIMRFWRSPNPGSWVSCEQVLLALLLLLALLLPLLSGGLHLLLK	chr22:43110750-43129712[+]	"Accelerates programmed cell death. Association to the apoptosis repressors Bcl-X(L), BHRF1, Bcl-2 or its adenovirus homolog E1B 19k protein suppresses this death-promoting activity. Does not interact with BAX."	.	HGNC:1051	BIK_HUMAN	Reviewed	ENSG00000100290	.	.	.	.	.
Mol00033	Protein	Baculoviral IAP repeat-containing protein 5 (BIRC5)	Apoptosis inhibitor 4; Apoptosis inhibitor survivin; API4; IAP4	BIRC5	332	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000350051.8, BIRC5-202, 2574; ENST00000301633.8, BIRC5-201, 2711; ENST00000374948.6, BIRC5-203, 2446; ENST00000590449.1, BIRC5-207, 568; ENST00000587746.5, BIRC5-205, 492; ENST00000592734.5, BIRC5-211, 386; ENST00000590925.6, BIRC5-208, 648; ENST00000586192.5, BIRC5-204, 524; ENST00000591800.1, BIRC5-209, 496; ENST00000589892.1, BIRC5-206, 747; ENST00000592115.5, BIRC5-210, 1141"	MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD	chr17:78214186-78225636[+]	Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Essential for the maintenance of mitochondrial integrity and function. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.	PDB: 1E31; PDB: 1F3H; PDB: 1XOX; PDB: 2QFA; PDB: 2RAW; PDB: 2RAX; PDB: 3UEC; PDB: 3UED; PDB: 3UEE; PDB: 3UEF; PDB: 3UEG; PDB: 3UEH; PDB: 3UEI; PDB: 3UIG; PDB: 3UIH; PDB: 3UII; PDB: 3UIJ; PDB: 3UIK; PDB: 4A0I; PDB: 4A0J; PDB: 4A0N; PDB: 6SHO; PDB: 6YIE; PDB: 6YIF; PDB: 6YIH	HGNC:593	BIRC5_HUMAN	Reviewed	ENSG00000089685	.	.	.	.	.
Mol00034	Protein	Serine/threonine-protein kinase B-raf (BRAF)	Proto-oncogene B-Raf; p94; v-Raf murine sarcoma viral oncogene homolog B1; BRAF1; RAFB1	BRAF	673	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000644969.2, BRAF-215, 9807; ENST00000496384.7, BRAF-204, 9578; ENST00000646891.1, BRAF-220, 6458; ENST00000288602.11, BRAF-201, 2561; ENST00000469930.2, BRAF-202, 1180; ENST00000646730.1, BRAF-219, 2829; ENST00000642228.1, BRAF-206, 2574; ENST00000497784.2, BRAF-205, 2387; ENST00000644650.1, BRAF-213, 1639; ENST00000647434.1, BRAF-221, 1217; ENST00000479537.6, BRAF-203, 1129; ENST00000644120.1, BRAF-212, 3889; ENST00000643790.1, BRAF-211, 575; ENST00000642808.1, BRAF-208, 439; ENST00000644905.1, BRAF-214, 5217; ENST00000642875.1, BRAF-209, 2871; ENST00000642272.1, BRAF-207, 2320; ENST00000646427.1, BRAF-218, 2265; ENST00000645443.1, BRAF-216, 2190; ENST00000646334.1, BRAF-217, 1779; ENST00000643356.1, BRAF-210, 853"	MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH	chr7:140719327-140924929[-]	"Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus (Probable). Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway. May play a role in the postsynaptic responses of hippocampal neurons."	PDB: 1UWH; PDB: 1UWJ; PDB: 2FB8; PDB: 2L05; PDB: 3C4C; PDB: 3D4Q; PDB: 3IDP; PDB: 3II5; PDB: 3NY5; PDB: 3OG7; PDB: 3PPJ; PDB: 3PPK; PDB: 3PRF; PDB: 3PRI; PDB: 3PSB; PDB: 3PSD; PDB: 3Q4C; PDB: 3Q96; PDB: 3SKC; PDB: 3TV4; PDB: 3TV6; PDB: 4CQE; PDB: 4DBN; PDB: 4E26; PDB: 4E4X; PDB: 4EHE; PDB: 4EHG; PDB: 4FC0; PDB: 4FK3; PDB: 4G9C; PDB: 4G9R; PDB: 4H58; PDB: 4JVG; PDB: 4KSP; PDB: 4KSQ; PDB: 4MBJ; PDB: 4MNE; PDB: 4MNF; PDB: 4PP7; PDB: 4R5Y; PDB: 4RZV; PDB: 4RZW; PDB: 4WO5; PDB: 4XV1; PDB: 4XV2; PDB: 4XV3; PDB: 4XV9; PDB: 4YHT; PDB: 5C9C; PDB: 5CSW; PDB: 5CSX; PDB: 5CT7; PDB: 5FD2; PDB: 5HI2; PDB: 5HID; PDB: 5HIE; PDB: 5ITA; PDB: 5J17; PDB: 5J18; PDB: 5J2R; PDB: 5JRQ; PDB: 5JSM; PDB: 5JT2; PDB: 5VAL; PDB: 5VAM; PDB: 5VR3; PDB: 5VYK; PDB: 6B8U; PDB: 6CAD; PDB: 6N0P; PDB: 6N0Q; PDB: 6NSQ; PDB: 6NYB; PDB: 6P3D; PDB: 6P7G; PDB: 6PP9; PDB: 6Q0J; PDB: 6Q0K; PDB: 6Q0T; PDB: 6U2G; PDB: 6U2H; PDB: 6UAN; PDB: 6UUO; PDB: 6V2U; PDB: 6V2W; PDB: 6XAG; PDB: 6XLO; PDB: 7M0T; PDB: 7M0U; PDB: 7M0V; PDB: 7M0W; PDB: 7M0X; PDB: 7M0Y; PDB: 7M0Z	HGNC:1097	BRAF_HUMAN	Reviewed	ENSG00000157764	.	.	.	.	.
Mol00035	Protein	Breast cancer type 1 susceptibility protein (BRCA1)	RING finger protein 53; RING-type E3 ubiquitin transferase BRCA1; RNF53	BRCA1	672	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357654.9, BRCA1-203, 7088; ENST00000471181.7, BRCA1-210, 7270; ENST00000493795.5, BRCA1-221, 5732; ENST00000468300.5, BRCA1-208, 3273; ENST00000491747.6, BRCA1-219, 2379; ENST00000354071.7, BRCA1-202, 4497; ENST00000352993.7, BRCA1-201, 3668; ENST00000644379.1, BRCA1-232, 2571; ENST00000634433.1, BRCA1-230, 2534; ENST00000652672.1, BRCA1-234, 2291; ENST00000470026.5, BRCA1-209, 2108; ENST00000477152.5, BRCA1-214, 1980; ENST00000478531.5, BRCA1-215, 1972; ENST00000493919.5, BRCA1-222, 1948; ENST00000494123.5, BRCA1-223, 1612; ENST00000484087.5, BRCA1-216, 1495; ENST00000591534.5, BRCA1-226, 1282; ENST00000473961.5, BRCA1-212, 958; ENST00000487825.5, BRCA1-217, 800; ENST00000586385.5, BRCA1-225, 781; ENST00000497488.1, BRCA1-224, 779; ENST00000476777.5, BRCA1-213, 769; ENST00000461574.1, BRCA1-206, 726; ENST00000618469.1, BRCA1-228, 718; ENST00000591849.5, BRCA1-227, 563; ENST00000644555.1, BRCA1-233, 558; ENST00000489037.1, BRCA1-218, 455; ENST00000412061.3, BRCA1-204, 1312; ENST00000461221.5, BRCA1-205, 5693; ENST00000492859.5, BRCA1-220, 1584; ENST00000642945.1, BRCA1-231, 1255; ENST00000461798.5, BRCA1-207, 582; ENST00000621897.1, BRCA1-229, 375; ENST00000472490.1, BRCA1-211, 561"	MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY	chr17:43044295-43170245[-]	"E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator."	PDB: 1JM7; PDB: 1JNX; PDB: 1N5O; PDB: 1OQA; PDB: 1T15; PDB: 1T29; PDB: 1T2U; PDB: 1T2V; PDB: 1Y98; PDB: 2ING; PDB: 3COJ; PDB: 3K0H; PDB: 3K0K; PDB: 3K15; PDB: 3K16; PDB: 3PXA; PDB: 3PXB; PDB: 3PXC; PDB: 3PXD; PDB: 3PXE; PDB: 4IFI; PDB: 4IGK; PDB: 4JLU; PDB: 4OFB; PDB: 4U4A; PDB: 4Y18; PDB: 4Y2G; PDB: 6G2I; PDB: 7LYB	HGNC:1100	BRCA1_HUMAN	Reviewed	ENSG00000012048	.	.	.	.	.
Mol00036	Protein	Cadherin-1 (CDH1)	.	CDH1	999	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261769.10, CDH1-201, 4811; ENST00000422392.6, CDH1-202, 2567; ENST00000566612.5, CDH1-210, 4138; ENST00000566510.5, CDH1-209, 2661; ENST00000561751.1, CDH1-203, 736; ENST00000562836.5, CDH1-205, 2759; ENST00000564676.5, CDH1-206, 969; ENST00000564745.1, CDH1-207, 581; ENST00000562118.1, CDH1-204, 952; ENST00000567320.1, CDH1-211, 352; ENST00000565810.1, CDH1-208, 282"	MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD	chr16:68737292-68835537[+]	"Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7."	.	HGNC:1748	CADH1_HUMAN	Reviewed	ENSG00000039068	.	.	.	.	.
Mol00037	Protein	Caspase-9 (CASP9)	CASP-9; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3; ICE-like apoptotic protease 6; ICE-LAP6; MCH6	CASP9	842	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000333868.10, CASP9-201, 2808; ENST00000348549.9, CASP9-202, 1621; ENST00000375890.8, CASP9-203, 1351; ENST00000546424.5, CASP9-210, 4463; ENST00000447522.5, CASP9-207, 954; ENST00000440484.1, CASP9-206, 781; ENST00000424908.5, CASP9-205, 740; ENST00000469637.1, CASP9-208, 725; ENST00000400777.7, CASP9-204, 1878; ENST00000474305.2, CASP9-209, 1111; ENST00000546969.1, CASP9-211, 569"	MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAKLSKPTLENLTPVVLRPEIRKPEVLRPETPRPVDIGSGGFGDVGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATPFQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTS	chr1:15490832-15526534[-]	Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP).; FUNCTION: Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.	PDB: 1JXQ; PDB: 1NW9; PDB: 2AR9; PDB: 3D9T; PDB: 3V3K; PDB: 3YGS; PDB: 4RHW; PDB: 5JUY; PDB: 5WVC; PDB: 5WVE	HGNC:1511	CASP9_HUMAN	Reviewed	ENSG00000132906	.	.	.	.	.
Mol00038	Protein	Procathepsin L (CTSL)	Cathepsin L1; Major excreted protein; MEP; CTSL1	CTSL	1514	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000343150.10, CTSL-203, 1654; ENST00000677761.1, CTSL-223, 2397; ENST00000676480.1, CTSL-208, 2392; ENST00000679149.1, CTSL-241, 2129; ENST00000679157.1, CTSL-242, 1981; ENST00000676531.1, CTSL-209, 1813; ENST00000677821.1, CTSL-224, 1719; ENST00000677262.1, CTSL-217, 1613; ENST00000676881.1, CTSL-212, 1593; ENST00000340342.11, CTSL-201, 1536; ENST00000676946.1, CTSL-214, 1420; ENST00000678442.1, CTSL-230, 1394; ENST00000678596.1, CTSL-231, 1963; ENST00000678649.1, CTSL-233, 1897; ENST00000677864.1, CTSL-225, 1373; ENST00000676769.1, CTSL-211, 1329; ENST00000342020.6, CTSL-202, 1315; ENST00000678599.1, CTSL-232, 1196; ENST00000677019.1, CTSL-216, 1100; ENST00000679030.1, CTSL-239, 1010; ENST00000677638.1, CTSL-222, 2682; ENST00000679028.1, CTSL-238, 2037; ENST00000679025.1, CTSL-237, 1650; ENST00000678367.1, CTSL-229, 1578; ENST00000677955.1, CTSL-227, 1555; ENST00000678259.1, CTSL-228, 1369; ENST00000677523.1, CTSL-220, 1221; ENST00000676961.1, CTSL-215, 4588; ENST00000677345.1, CTSL-218, 3930; ENST00000679252.1, CTSL-243, 3848; ENST00000676909.1, CTSL-213, 3663; ENST00000482054.2, CTSL-205, 2786; ENST00000676576.1, CTSL-210, 2765; ENST00000678965.1, CTSL-236, 2678; ENST00000676466.1, CTSL-207, 2650; ENST00000678752.1, CTSL-235, 2585; ENST00000679141.1, CTSL-240, 2517; ENST00000677935.1, CTSL-226, 2204; ENST00000677349.1, CTSL-219, 2092; ENST00000677615.1, CTSL-221, 2058; ENST00000375894.10, CTSL-204, 1541; ENST00000495822.2, CTSL-206, 1345; ENST00000678654.1, CTSL-234, 1345"	MNPTLILAAFCLGIASATLTFDHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYREGKHSFTMAMNAFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPTV	chr9:87724051-87731469[+]	"Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter. In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation. Secreted form generates endostatin from COL18A1. Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation. Required for maximal stimulation of steroidogenesis by TIMP1."	PDB: 1CJL; PDB: 1CS8; PDB: 1ICF; PDB: 1MHW; PDB: 2NQD; PDB: 2VHS; PDB: 2XU1; PDB: 2XU3; PDB: 2XU4; PDB: 2XU5; PDB: 2YJ2; PDB: 2YJ8; PDB: 2YJ9; PDB: 2YJB; PDB: 2YJC; PDB: 3BC3; PDB: 3H89; PDB: 3H8B; PDB: 3H8C; PDB: 3HHA; PDB: 3HWN; PDB: 3IV2; PDB: 3K24; PDB: 3KSE; PDB: 3OF8; PDB: 3OF9; PDB: 4AXL; PDB: 4AXM; PDB: 5F02; PDB: 5I4H; PDB: 5MAE; PDB: 5MAJ; PDB: 5MQY; PDB: 6EZP; PDB: 6EZX; PDB: 6F06; PDB: 6JD0; PDB: 6JD8	HGNC:2537	CATL1_HUMAN	Reviewed	ENSG00000135047	.	.	.	.	.
Mol00039	Protein	G1/S-specific cyclin-D2 (CCND2)	.	CCND2	894	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261254.8, CCND2-201, 6493; ENST00000676411.1, CCND2-208, 6849; ENST00000676279.1, CCND2-207, 6352; ENST00000675880.1, CCND2-206, 6532; ENST00000675468.1, CCND2-205, 6135; ENST00000536537.2, CCND2-202, 1062; ENST00000536795.1, CCND2-203, 572; ENST00000541542.1, CCND2-204, 322"	MELLCHEVDPVRRAVRDRNLLRDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAGVPTPKSHLQLLGAVCMFLASKLKETSPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQQREKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEEVSSLTCDALTELLAKITNTDVDCLKACQEQIEAVLLNSLQQYRQDQRDGSKSEDELDQASTPTDVRDIDL	chr12:4269771-4305353[+]	Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals.	PDB: 6EI2	HGNC:1583	CCND2_HUMAN	Reviewed	ENSG00000118971	.	.	.	.	.
Mol00040	Protein	Cyclin-J (CCNJ)	.	CCNJ	54619	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000465148.3, CCNJ-203, 3959; ENST00000265992.9, CCNJ-201, 4115; ENST00000403870.7, CCNJ-202, 2830"	MELEGQWWRGQLAADIHQALRYKELKLPSYKGQSPQLSLRRYFADLIAIVSNRFTLCPSARHLAVYLLDLFMDRYDISIQQLHLVALSCLLLASKFEEKEDSVPKLEQLNSLGCMTNMNLVLTKQNLLHMELLLLETFQWNLCLPTAAHFIEYYLSEAVHETDLHDGWPMICLEKTKLYMAKYADYFLEVSLQVAAACVASSRIILRLSPTWPTRLHRLTAYSWDFLVQCIERLLIAHDNDVKEANKQRGQAGPQSAQLSVFQTASQPSRPVHFQQPQYLHQTHQTSLQYRHPTSEQPSCQQIVSTTHTSSYTLQTCPAGFQTSVQGLGHMQTGVGMSLAIPVEVKPCLSVSYNRSYQINEHYPCITPCFER	chr10:96043394-96060870[+]	.	.	HGNC:23434	CCNJ_HUMAN	Reviewed	ENSG00000107443	.	.	.	.	.
Mol00041	Protein	CUB domain-containing protein 1 (CDCP1)	.	CDCP1	64866	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000296129.6, CDCP1-201, 5963; ENST00000425231.2, CDCP1-202, 1416; ENST00000490471.1, CDCP1-203, 563"	MAGLNCGVSIALLGVLLLGAARLPRGAEAFEIALPRESNITVLIKLGTPTLLAKPCYIVISKRHITMLSIKSGERIVFTFSCQSPENHFVIEIQKNIDCMSGPCPFGEVQLQPSTSLLPTLNRTFIWDVKAHKSIGLELQFSIPRLRQIGPGESCPDGVTHSISGRIDATVVRIGTFCSNGTVSRIKMQEGVKMALHLPWFHPRNVSGFSIANRSSIKRLCIIESVFEGEGSATLMSANYPEGFPEDELMTWQFVVPAHLRASVSFLNFNLSNCERKEERVEYYIPGSTTNPEVFKLEDKQPGNMAGNFNLSLQGCDQDAQSPGILRLQFQVLVQHPQNESNKIYVVDLSNERAMSLTIEPRPVKQSRKFVPGCFVCLESRTCSSNLTLTSGSKHKISFLCDDLTRLWMNVEKTISCTDHRYCQRKSYSLQVPSDILHLPVELHDFSWKLLVPKDRLSLVLVPAQKLQQHTHEKPCNTSFSYLVASAIPSQDLYFGSFCPGGSIKQIQVKQNISVTLRTFAPSFQQEASRQGLTVSFIPYFKEEGVFTVTPDTKSKVYLRTPNWDRGLPSLTSVSWNISVPRDQVACLTFFKERSGVVCQTGRAFMIIQEQRTRAEEIFSLDEDVLPKPSFHHHSFWVNISNCSPTSGKQLDLLFSVTLTPRTVDLTVILIAAVGGGVLLLSALGLIICCVKKKKKKTNKGPAVGIYNDNINTEMPRQPKKFQKGRKDNDSHVYAVIEDTMVYGHLLQDSSGSFLQPEVDTYRPFQGTMGVCPPSPPTICSRAPTAKLATEEPPPRSPPESESEPYTFSHPNNGDVSSKDTDIPLLNTQEPMEPAE	chr3:45082277-45146422[-]	May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis.	.	HGNC:24357	CDCP1_HUMAN	Reviewed	ENSG00000163814	.	.	.	.	.
Mol00042	Protein	Cyclin-dependent kinase 4 (CDK4)	Cell division protein kinase 4; PSK-J3	CDK4	1019	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000257904.11, CDK4-201, 1865; ENST00000312990.10, CDK4-202, 1650; ENST00000547281.5, CDK4-204, 825; ENST00000546489.5, CDK4-203, 776; ENST00000551800.5, CDK4-209, 773; ENST00000552254.5, CDK4-211, 769; ENST00000552388.1, CDK4-212, 694; ENST00000549606.5, CDK4-206, 558; ENST00000552862.1, CDK4-214, 447; ENST00000547853.1, CDK4-205, 228; ENST00000553237.5, CDK4-215, 952; ENST00000550419.5, CDK4-207, 919; ENST00000551888.5, CDK4-210, 636; ENST00000551706.1, CDK4-208, 984; ENST00000552713.5, CDK4-213, 685"	MATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGGGGGGGLPISTVREVALLRRLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRDVSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGNPE	chr12:57747727-57756013[-]	"Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex."	PDB: 2W96; PDB: 2W99; PDB: 2W9F; PDB: 2W9Z; PDB: 3G33; PDB: 5FWK; PDB: 5FWL; PDB: 5FWM; PDB: 5FWP; PDB: 6P8E; PDB: 6P8F; PDB: 6P8G; PDB: 6P8H	HGNC:1773	CDK4_HUMAN	Reviewed	ENSG00000135446	.	.	.	.	.
Mol00043	Protein	Cyclin-dependent kinase 6 (CDK6)	Cell division protein kinase 6; Serine/threonine-protein kinase PLSTIRE; CDKN6	CDK6	1021	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000424848.3, CDK6-202, 11663; ENST00000265734.8, CDK6-201, 11612; ENST00000491250.1, CDK6-205, 558; ENST00000467166.1, CDK6-203, 779; ENST00000473078.1, CDK6-204, 386"	MEKDGLCRADQQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLFDVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYFQDLERCKENLDSHLPPSQNTSELNTA	chr7:92604921-92836573[-]	"Serine/threonine-protein kinase involved in the control of the cell cycle and differentiation; promotes G1/S transition. Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins during interphase at G1 to form a pRB/RB1 kinase and controls the entrance into the cell cycle. Involved in initiation and maintenance of cell cycle exit during cell differentiation; prevents cell proliferation and regulates negatively cell differentiation, but is required for the proliferation of specific cell types (e.g. erythroid and hematopoietic cells). Essential for cell proliferation within the dentate gyrus of the hippocampus and the subventricular zone of the lateral ventricles. Required during thymocyte development. Promotes the production of newborn neurons, probably by modulating G1 length. Promotes, at least in astrocytes, changes in patterns of gene expression, changes in the actin cytoskeleton including loss of stress fibers, and enhanced motility during cell differentiation. Prevents myeloid differentiation by interfering with RUNX1 and reducing its transcription transactivation activity, but promotes proliferation of normal myeloid progenitors. Delays senescence. Promotes the proliferation of beta-cells in pancreatic islets of Langerhans. May play a role in the centrosome organization during the cell cycle phases."	PDB: 1BI7; PDB: 1BI8; PDB: 1BLX; PDB: 1G3N; PDB: 1JOW; PDB: 1XO2; PDB: 2EUF; PDB: 2F2C; PDB: 3NUP; PDB: 3NUX; PDB: 4AUA; PDB: 4EZ5; PDB: 4TTH; PDB: 5L2I; PDB: 5L2S; PDB: 5L2T; PDB: 6OQL; PDB: 6OQO	HGNC:1777	CDK6_HUMAN	Reviewed	ENSG00000105810	.	.	.	.	.
Mol00044	Protein	Cyclin-dependent kinase inhibitor 1A (CDKN1A)	CDK-interacting protein 1; Melanoma differentiation-associated protein 6; MDA-6; p21; CAP20; CDKN1; CIP1; MDA6; PIC1; SDI1; WAF1	CDKN1A	1026	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000244741.10, CDKN1A-201, 2117; ENST00000405375.5, CDKN1A-203, 2267; ENST00000448526.6, CDKN1A-204, 2104; ENST00000615513.4, CDKN1A-208, 2102; ENST00000373711.3, CDKN1A-202, 793; ENST00000478800.1, CDKN1A-207, 616; ENST00000459970.1, CDKN1A-205, 604; ENST00000462537.3, CDKN1A-206, 553"	MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP	chr6:36676460-36687337[+]	"May be involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding. Plays an important role in controlling cell cycle progression and DNA damage-induced G2 arrest."	PDB: 1AXC; PDB: 2ZVV; PDB: 2ZVW; PDB: 4RJF; PDB: 5E0U; PDB: 6CBI; PDB: 6CEJ; PDB: 6CIV; PDB: 6CIX; PDB: 6P8H; PDB: 7KQ0; PDB: 7KQ1	HGNC:1784	CDN1A_HUMAN	Reviewed	ENSG00000124762	.	.	.	.	.
Mol00045	Protein	Cyclin-dependent kinase inhibitor 1B (CDKN1B)	Cyclin-dependent kinase inhibitor p27; p27Kip1; KIP1	CDKN1B	1027	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000228872.9, CDKN1B-201, 2411; ENST00000614874.2, CDKN1B-205, 4335; ENST00000396340.1, CDKN1B-202, 897; ENST00000442489.1, CDKN1B-203, 577; ENST00000682620.1, CDKN1B-207, 3094; ENST00000682080.1, CDKN1B-206, 2465; ENST00000684771.1, CDKN1B-209, 2004; ENST00000477087.1, CDKN1B-204, 453; ENST00000683707.1, CDKN1B-208, 2467"	MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT	chr12:12685498-12722369[+]	"Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA. Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry."	PDB: 1H27; PDB: 1JSU; PDB: 2AST; PDB: 5UQ3; PDB: 6ATH; PDB: 6P8E; PDB: 6P8F; PDB: 6P8G; PDB: 7B5L; PDB: 7B5M; PDB: 7B5R	HGNC:1785	CDN1B_HUMAN	Reviewed	ENSG00000111276	.	.	.	.	.
Mol00046	Protein	Ceramide synthase 2 (CERS2)	CerS2; LAG1 longevity assurance homolog 2; SP260; Sphingosine N-acyltransferase CERS2; Tumor metastasis-suppressor gene 1 protein; Very-long-chain ceramide synthase CERS2; LASS2; TMSG1	CERS2	29956	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368954.10, CERS2-205, 2323; ENST00000271688.10, CERS2-201, 2544; ENST00000561294.5, CERS2-214, 1803; ENST00000560793.6, CERS2-213, 1661; ENST00000368949.8, CERS2-204, 1002; ENST00000361419.9, CERS2-203, 997; ENST00000558062.5, CERS2-210, 896; ENST00000421609.5, CERS2-206, 738; ENST00000457392.1, CERS2-207, 545; ENST00000345896.8, CERS2-202, 2170; ENST00000482825.7, CERS2-209, 1618; ENST00000460664.5, CERS2-208, 850; ENST00000559020.1, CERS2-211, 594; ENST00000559660.1, CERS2-212, 242"	MLQTLYDYFWWERLWLPVNLTWADLEDRDGRVYAKASDLYITLPLALLFLIVRYFFELYVATPLAALLNIKEKTRLRAPPNATLEHFYLTSGKQPKQVEVELLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTFYLIAFIAGMAVIVDKPWFYDMKKVWEGYPIQSTIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILISFSWFANYIRAGTLIMALHDSSDYLLESAKMFNYAGWKNTCNNIFIVFAIVFIITRLVILPFWILHCTLVYPLELYPAFFGYYFFNSMMGVLQLLHIFWAYLILRMAHKFITGKLVEDERSDREETESSEGEEAAAGGGAKSRPLANGHPILNNNHRKND	chr1:150960583-150975003[-]	"Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very-long-chain fatty acyl-CoA (chain length C22-C27). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively. Plays a non-redundant role in the synthesis of ceramides with very-long-chain fatty acids in kidney, liver and brain. Regulates the abundance of myelin-specific sphingolipids galactosylceramide and sulfatide that affects myelin sheath architecture and motor neuron functions."	.	HGNC:14076	CERS2_HUMAN	Reviewed	ENSG00000143418	.	.	.	.	.
Mol00047	Protein	CASP8 and FADD-like apoptosis regulator (CFLAR)	Caspase homolog; CASH; Caspase-eight-related protein; Casper; Caspase-like apoptosis regulatory protein; CLARP; Cellular FLICE-like inhibitory protein; c-FLIP; FADD-like antiapoptotic molecule 1; FLAME-1; Inhibitor of FLICE; I-FLICE; MACH-related inducer of toxicity; MRIT; Usurpin; CASH; CASP8AP1; CLARP; MRIT	CFLAR	8837	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000309955.8, CFLAR-201, 14612; ENST00000395148.6, CFLAR-205, 4415; ENST00000423241.6, CFLAR-207, 2128; ENST00000341582.10, CFLAR-203, 2056; ENST00000457277.5, CFLAR-214, 1868; ENST00000443227.5, CFLAR-213, 1679; ENST00000341222.10, CFLAR-202, 1283; ENST00000479953.6, CFLAR-222, 1230; ENST00000440180.5, CFLAR-211, 1198; ENST00000342795.9, CFLAR-204, 1613; ENST00000494258.5, CFLAR-224, 693; ENST00000417748.1, CFLAR-206, 684; ENST00000441224.5, CFLAR-212, 655; ENST00000425030.1, CFLAR-208, 596; ENST00000462763.5, CFLAR-218, 588; ENST00000470178.6, CFLAR-219, 516; ENST00000433445.1, CFLAR-209, 435; ENST00000439154.6, CFLAR-210, 1310; ENST00000490965.1, CFLAR-223, 529; ENST00000474842.1, CFLAR-221, 1091; ENST00000461820.5, CFLAR-217, 830; ENST00000461422.1, CFLAR-216, 717; ENST00000470664.1, CFLAR-220, 704; ENST00000460961.1, CFLAR-215, 548"	MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQSVYGVDQTHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMKNVEFKAQKRGLCTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRKKLILSYT	chr2:201116154-201176687[+]	Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.	PDB: 2N5R; PDB: 3H11; PDB: 3H13; PDB: 6M6O	HGNC:1876	CFLAR_HUMAN	Reviewed	ENSG00000003402	.	.	.	.	.
Mol00048	Protein	Collagen alpha-1(III) chain (COL3A1)	.	COL3A1	1281	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000304636.9, COL3A1-201, 5490; ENST00000317840.9, COL3A1-202, 3873; ENST00000450867.1, COL3A1-203, 268; ENST00000487010.1, COL3A1-206, 2054; ENST00000470167.1, COL3A1-205, 628; ENST00000467886.1, COL3A1-204, 226"	MMSFVQKGSWLLLALLHPTIILAQQEAVEGGCSHLGQSYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPFGECCAVCPQPPTAPTRPPNGQGPQGPKGDPGPPGIPGRNGDPGIPGQPGSPGSPGPPGICESCPTGPQNYSPQYDSYDVKSGVAVGGLAGYPGPAGPPGPPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPGGKGEMGPAGIPGAPGLMGARGPPGPAGANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAGIPGVPGAKGEDGKDGSPGEPGANGLPGAAGERGAPGFRGPAGPNGIPGEKGPAGERGAPGPAGPRGAAGEPGRDGVPGGPGMRGMPGSPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGPQGPPGKNGETGPQGPPGPTGPGGDKGDTGPPGPQGLQGLPGTGGPPGENGKPGEPGPKGDAGAPGAPGGKGDAGAPGERGPPGLAGAPGLRGGAGPPGPEGGKGAAGPPGPPGAAGTPGLQGMPGERGGLGSPGPKGDKGEPGGPGADGVPGKDGPRGPTGPIGPPGPAGQPGDKGEGGAPGLPGIAGPRGSPGERGETGPPGPAGFPGAPGQNGEPGGKGERGAPGEKGEGGPPGVAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAGFPGARGLPGPPGSNGNPGPPGPSGSPGKDGPPGPAGNTGAPGSPGVSGPKGDAGQPGEKGSPGAQGPPGAPGPLGIAGITGARGLAGPPGMPGPRGSPGPQGVKGESGKPGANGLSGERGPPGPQGLPGLAGTAGEPGRDGNPGSDGLPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPAGKSGDRGESGPAGPAGAPGPAGSRGAPGPQGPRGDKGETGERGAAGIKGHRGFPGNPGAPGSPGPAGQQGAIGSPGPAGPRGPVGPSGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGVGAAAIAGIGGEKAGGFAPYYGDEPMDFKINTDEIMTSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVFCNMETGETCISANPLNVPRKHWWTDSSAEKKHVWFGESMDGGFQFSYGNPELPEDVLDVHLAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKALKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYRTRKAVRLPIVDIAPYDIGGPDQEFGVDVGPVCFL	chr2:188974373-189012746[+]	Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.	PDB: 2V53; PDB: 3DMW; PDB: 4AE2; PDB: 4AEJ; PDB: 4AK3; PDB: 4GYX; PDB: 6FZV; PDB: 6FZW	HGNC:2201	CO3A1_HUMAN	Reviewed	ENSG00000168542	.	.	.	.	.
Mol00049	Protein	E3 ubiquitin-protein ligase COP1 (COP1)	Constitutive photomorphogenesis protein 1 homolog; hCOP1; RING finger and WD repeat domain protein 2; RING finger protein 200; RING-type E3 ubiquitin transferase RFWD2; RFWD2; RNF200	COP1	64326	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367669.8, COP1-204, 2826; ENST00000308769.12, COP1-201, 2124; ENST00000367666.5, COP1-202, 2022; ENST00000459744.5, COP1-205, 741; ENST00000498306.5, COP1-210, 617; ENST00000649803.1, COP1-211, 2336; ENST00000367667.5, COP1-203, 2034; ENST00000474194.1, COP1-207, 975; ENST00000491600.5, COP1-209, 773; ENST00000461830.6, COP1-206, 2131; ENST00000482305.1, COP1-208, 450"	MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAVSAAALVSGGVAQAAGSGGLGGPVRPVLVAPAVSGSGGGAVSTGLSRHSCAARPSAGVGGSSSSLGSGSRKRPLLAPLCNGLINSYEDKSNDFVCPICFDMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDWLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGSSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYDTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALPDGESNVLIAANSQGTIKVLELV	chr1:175944831-176207286[-]	"E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable)."	PDB: 5HQG; PDB: 5IGQ	HGNC:17440	COP1_HUMAN	Reviewed	ENSG00000143207	.	.	.	.	.
Mol00050	Protein	Cellular tumor antigen p53 (TP53)	Antigen NY-CO-13; Phosphoprotein p53; Tumor suppressor p53; P53	TP53	7157	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000269305.9, TP53-201, 2512; ENST00000420246.6, TP53-204, 2653; ENST00000622645.4, TP53-226, 2653; ENST00000610292.4, TP53-219, 2639; ENST00000455263.6, TP53-206, 2580; ENST00000610538.4, TP53-220, 2580; ENST00000620739.4, TP53-225, 2579; ENST00000445888.6, TP53-205, 2506; ENST00000619485.4, TP53-224, 2506; ENST00000510385.5, TP53-213, 2404; ENST00000618944.4, TP53-222, 2404; ENST00000504290.5, TP53-208, 2331; ENST00000610623.4, TP53-221, 2331; ENST00000504937.5, TP53-209, 2271; ENST00000619186.4, TP53-223, 2271; ENST00000359597.8, TP53-202, 1152; ENST00000413465.6, TP53-203, 1018; ENST00000509690.5, TP53-212, 729; ENST00000508793.5, TP53-211, 634; ENST00000604348.5, TP53-218, 568; ENST00000503591.1, TP53-207, 565; ENST00000514944.5, TP53-214, 546; ENST00000576024.1, TP53-217, 175; ENST00000635293.1, TP53-227, 1883; ENST00000574684.1, TP53-216, 104; ENST00000505014.5, TP53-210, 1261; ENST00000571370.1, TP53-215, 1112"	MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD	chr17:7661779-7687538[-]	"Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2. However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2."	PDB: 1A1U; PDB: 1AIE; PDB: 1C26; PDB: 1DT7; PDB: 1GZH; PDB: 1H26; PDB: 1HS5; PDB: 1JSP; PDB: 1KZY; PDB: 1MA3; PDB: 1OLG; PDB: 1OLH; PDB: 1PES; PDB: 1PET; PDB: 1SAE; PDB: 1SAF; PDB: 1SAK; PDB: 1SAL; PDB: 1TSR; PDB: 1TUP; PDB: 1UOL; PDB: 1XQH; PDB: 1YC5; PDB: 1YCQ; PDB: 1YCR; PDB: 1YCS; PDB: 2AC0; PDB: 2ADY; PDB: 2AHI; PDB: 2ATA; PDB: 2B3G; PDB: 2BIM; PDB: 2BIN; PDB: 2BIO; PDB: 2BIP; PDB: 2BIQ; PDB: 2F1X; PDB: 2FEJ; PDB: 2FOJ; PDB: 2FOO; PDB: 2GS0; PDB: 2H1L; PDB: 2H2D; PDB: 2H2F; PDB: 2H4F; PDB: 2H4H; PDB: 2H4J; PDB: 2H59; PDB: 2J0Z; PDB: 2J10; PDB: 2J11; PDB: 2J1W; PDB: 2J1X; PDB: 2J1Y; PDB: 2J1Z; PDB: 2J20; PDB: 2J21; PDB: 2K8F; PDB: 2L14; PDB: 2LY4; PDB: 2MEJ; PDB: 2MWO; PDB: 2MWP; PDB: 2MWY; PDB: 2MZD; PDB: 2OCJ; PDB: 2PCX; PDB: 2RUK; PDB: 2VUK; PDB: 2WGX; PDB: 2X0U; PDB: 2X0V; PDB: 2X0W; PDB: 2XWR; PDB: 2YBG; PDB: 2YDR; PDB: 2Z5S; PDB: 2Z5T; PDB: 3D05; PDB: 3D06; PDB: 3D07; PDB: 3D08; PDB: 3D09; PDB: 3D0A; PDB: 3DAB; PDB: 3DAC; PDB: 3IGK; PDB: 3IGL; PDB: 3KMD; PDB: 3KZ8; PDB: 3LW1; PDB: 3OQ5; PDB: 3PDH; PDB: 3Q01; PDB: 3Q05; PDB: 3Q06; PDB: 3SAK; PDB: 3TG5; PDB: 3TS8; PDB: 3ZME; PDB: 4AGL; PDB: 4AGM; PDB: 4AGN; PDB: 4AGO; PDB: 4AGP; PDB: 4AGQ; PDB: 4BUZ; PDB: 4BV2; PDB: 4HFZ; PDB: 4HJE; PDB: 4IBQ; PDB: 4IBS; PDB: 4IBT; PDB: 4IBU; PDB: 4IBV; PDB: 4IBW; PDB: 4IBY; PDB: 4IBZ; PDB: 4IJT; PDB: 4KVP; PDB: 4LO9; PDB: 4LOE; PDB: 4LOF; PDB: 4MZI; PDB: 4MZR; PDB: 4QO1; PDB: 4RP6; PDB: 4RP7; PDB: 4X34; PDB: 4XR8; PDB: 4ZZJ; PDB: 5A7B; PDB: 5AB9; PDB: 5ABA; PDB: 5AOI; PDB: 5AOJ; PDB: 5AOK; PDB: 5AOL; PDB: 5AOM; PDB: 5BUA; PDB: 5ECG; PDB: 5G4M; PDB: 5G4N; PDB: 5G4O; PDB: 5HOU; PDB: 5HP0; PDB: 5HPD; PDB: 5LAP; PDB: 5LGY; PDB: 5MCT; PDB: 5MCU; PDB: 5MCV; PDB: 5MCW; PDB: 5MF7; PDB: 5MG7; PDB: 5MHC; PDB: 5MOC; PDB: 5O1A; PDB: 5O1B; PDB: 5O1C; PDB: 5O1D; PDB: 5O1E; PDB: 5O1F; PDB: 5O1G; PDB: 5O1H; PDB: 5O1I; PDB: 5OL0; PDB: 5UN8; PDB: 5XZC; PDB: 6FF9; PDB: 6FJ5; PDB: 6GGA; PDB: 6GGB; PDB: 6GGC; PDB: 6GGD; PDB: 6GGE; PDB: 6GGF; PDB: 6LHD; PDB: 6R5L; PDB: 6RJZ; PDB: 6RK8; PDB: 6RKI; PDB: 6RKK; PDB: 6RKM; PDB: 6RL3; PDB: 6RL4; PDB: 6RL6; PDB: 6RM5; PDB: 6RM7; PDB: 6RWH; PDB: 6RWI; PDB: 6RWS; PDB: 6RWU; PDB: 6RX2; PDB: 6RZ3; PDB: 6S39; PDB: 6S3C; PDB: 6S40; PDB: 6S9Q; PDB: 6SHZ; PDB: 6SI0; PDB: 6SI1; PDB: 6SI2; PDB: 6SI3; PDB: 6SI4; PDB: 6SIN; PDB: 6SIO; PDB: 6SIP; PDB: 6SIQ; PDB: 6SL6; PDB: 6SLV; PDB: 6T58; PDB: 6V4F; PDB: 6V4H; PDB: 6VQO; PDB: 6VR1; PDB: 6VR5; PDB: 6VRM; PDB: 6VRN; PDB: 6W51; PDB: 6XRE; PDB: 7BWN; PDB: 7DHY; PDB: 7DHZ; PDB: 7DVD; PDB: 7EL4	HGNC:11998	P53_HUMAN	Reviewed	ENSG00000141510	.	.	.	.	.
Mol00051	Protein	Anamorsin (CIAPIN1)	Cytokine-induced apoptosis inhibitor 1; Fe-S cluster assembly protein DRE2 homolog; CUA001; PRO0915	CIAPIN1	57019	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000394391.9, CIAPIN1-201, 2021; ENST00000567518.5, CIAPIN1-209, 2016; ENST00000569370.5, CIAPIN1-213, 1559; ENST00000568940.5, CIAPIN1-211, 1137; ENST00000565961.5, CIAPIN1-207, 1814; ENST00000569979.5, CIAPIN1-214, 896; ENST00000565786.5, CIAPIN1-206, 641; ENST00000563341.1, CIAPIN1-202, 505; ENST00000567751.5, CIAPIN1-210, 328; ENST00000570000.5, CIAPIN1-215, 994; ENST00000569246.5, CIAPIN1-212, 910; ENST00000565368.5, CIAPIN1-205, 851; ENST00000566284.1, CIAPIN1-208, 1165; ENST00000563561.1, CIAPIN1-203, 597; ENST00000564885.1, CIAPIN1-204, 493"	MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKELQREPLTPEEVQSVREHLGHESDNLLFVQITGKKPNFEVGSSRQLKLSITKKSSPSVKPAVDPAAAKLWTLSANDMEDDSMDLIDSDELLDPEDLKKPDPASLRAASCGEGKKRKACKNCTCGLAEELEKEKSREQMSSQPKSACGNCYLGDAFRCASCPYLGMPAFKPGEKVLLSDSNLHDA	chr16:57428187-57447420[-]	"Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells."	PDB: 2LD4; PDB: 2YUI; PDB: 4M7R	HGNC:28050	CPIN1_HUMAN	Reviewed	ENSG00000005194	.	.	.	.	.
Mol00052	Protein	Alpha-crystallin B chain (CRYAB)	Alpha(B)-crystallin; Heat shock protein beta-5; HspB5; Renal carcinoma antigen NY-REN-27; Rosenthal fiber component; CRYA2; HSPB5	CRYAB	1410	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650687.2, CRYAB-217, 774; ENST00000533475.6, CRYAB-213, 1117; ENST00000527899.6, CRYAB-206, 1107; ENST00000533879.2, CRYAB-214, 1057; ENST00000531198.5, CRYAB-211, 1013; ENST00000526180.6, CRYAB-205, 977; ENST00000616970.5, CRYAB-216, 941; ENST00000525823.1, CRYAB-203, 915; ENST00000527950.5, CRYAB-207, 887; ENST00000227251.7, CRYAB-201, 848; ENST00000651164.1, CRYAB-218, 836; ENST00000651650.1, CRYAB-219, 623; ENST00000533280.6, CRYAB-212, 589; ENST00000528961.6, CRYAB-209, 540; ENST00000533971.2, CRYAB-215, 2271; ENST00000529647.5, CRYAB-210, 695; ENST00000526167.5, CRYAB-204, 668; ENST00000528628.5, CRYAB-208, 624; ENST00000524660.1, CRYAB-202, 464; ENST00000652223.1, CRYAB-220, 3414; ENST00000652606.1, CRYAB-221, 1960"	MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK	chr11:111908564-111923722[-]	"May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity)."	PDB: 2KLR; PDB: 2N0K; PDB: 2WJ7; PDB: 2Y1Y; PDB: 2Y1Z; PDB: 2Y22; PDB: 2YGD; PDB: 3J07; PDB: 3L1G; PDB: 3SGM; PDB: 3SGN; PDB: 3SGO; PDB: 3SGP; PDB: 3SGR; PDB: 3SGS; PDB: 4M5S; PDB: 4M5T; PDB: 5VVV; PDB: 6BP9	HGNC:2389	CRYAB_HUMAN	Reviewed	ENSG00000109846	.	.	.	.	.
Mol00053	Protein	Catenin beta-1 (CTNNB1)	Beta-catenin; CTNNB; OK/SW-cl.35; PRO2286	CTNNB1	1499	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000349496.11, CTNNB1-201, 3661; ENST00000645320.1, CTNNB1-241, 4735; ENST00000441708.2, CTNNB1-208, 3906; ENST00000396185.8, CTNNB1-203, 3472; ENST00000433400.6, CTNNB1-207, 3431; ENST00000644524.1, CTNNB1-233, 3388; ENST00000644678.1, CTNNB1-234, 3321; ENST00000645900.1, CTNNB1-244, 3284; ENST00000643297.1, CTNNB1-225, 3283; ENST00000643541.1, CTNNB1-226, 3278; ENST00000396183.7, CTNNB1-202, 3268; ENST00000643031.1, CTNNB1-223, 3267; ENST00000646381.1, CTNNB1-251, 3249; ENST00000642836.1, CTNNB1-219, 3232; ENST00000645493.1, CTNNB1-242, 3196; ENST00000645210.1, CTNNB1-238, 3195; ENST00000642992.1, CTNNB1-222, 3134; ENST00000644867.1, CTNNB1-235, 3087; ENST00000453024.6, CTNNB1-210, 3052; ENST00000643977.1, CTNNB1-228, 3036; ENST00000646174.1, CTNNB1-249, 2933; ENST00000642315.1, CTNNB1-217, 2890; ENST00000643992.1, CTNNB1-229, 2858; ENST00000647390.1, CTNNB1-255, 2784; ENST00000645982.1, CTNNB1-246, 2778; ENST00000642248.1, CTNNB1-216, 2775; ENST00000646116.1, CTNNB1-248, 2770; ENST00000450969.6, CTNNB1-209, 2764; ENST00000431914.6, CTNNB1-206, 2749; ENST00000646725.1, CTNNB1-252, 2744; ENST00000642426.1, CTNNB1-218, 2720; ENST00000405570.6, CTNNB1-204, 2642; ENST00000646369.1, CTNNB1-250, 2607; ENST00000642986.1, CTNNB1-221, 3298; ENST00000645276.1, CTNNB1-239, 3127; ENST00000644873.1, CTNNB1-236, 3086; ENST00000642886.1, CTNNB1-220, 3039; ENST00000647264.1, CTNNB1-254, 2994; ENST00000644138.1, CTNNB1-230, 2777; ENST00000647413.1, CTNNB1-256, 2458; ENST00000645927.1, CTNNB1-245, 1100; ENST00000426215.5, CTNNB1-205, 563; ENST00000644906.1, CTNNB1-237, 560; ENST00000646074.1, CTNNB1-247, 3197; ENST00000471014.2, CTNNB1-212, 836; ENST00000488914.2, CTNNB1-215, 558; ENST00000643052.1, CTNNB1-224, 4888; ENST00000645763.1, CTNNB1-243, 4159; ENST00000643865.1, CTNNB1-227, 4145; ENST00000485265.2, CTNNB1-214, 4058; ENST00000647021.1, CTNNB1-253, 3472; ENST00000645305.1, CTNNB1-240, 3312; ENST00000482042.1, CTNNB1-213, 1366; ENST00000644501.1, CTNNB1-232, 1149; ENST00000465552.2, CTNNB1-211, 883; ENST00000644395.1, CTNNB1-231, 475"	MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL	chr3:41194741-41260096[+]	"Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle. Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling."	PDB: 1G3J; PDB: 1JDH; PDB: 1JPW; PDB: 1LUJ; PDB: 1P22; PDB: 1QZ7; PDB: 1T08; PDB: 1TH1; PDB: 2G57; PDB: 2GL7; PDB: 2Z6H; PDB: 3DIW; PDB: 3FQN; PDB: 3FQR; PDB: 3SL9; PDB: 3SLA; PDB: 3TX7; PDB: 4DJS; PDB: 6M90; PDB: 6M91; PDB: 6M92; PDB: 6M93; PDB: 6M94; PDB: 6O9B; PDB: 6O9C; PDB: 6WLX; PDB: 6WNX; PDB: 7AFW; PDB: 7AR4	HGNC:2514	CTNB1_HUMAN	Reviewed	ENSG00000168036	.	.	.	.	.
Mol00054	Protein	Cullin-5 (CUL5)	CUL-5; Vasopressin-activated calcium-mobilizing receptor 1; VACM-1; VACM1	CUL5	8065	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393094.7, CUL5-201, 6171; ENST00000532782.1, CUL5-206, 388; ENST00000531427.5, CUL5-203, 3596; ENST00000532064.5, CUL5-205, 1109; ENST00000531843.1, CUL5-204, 375; ENST00000526303.1, CUL5-202, 751"	MATSNLLKNKGSLQFEDKWDFMRPIVLKLLRQESVTKQQWFDLFSDVHAVCLWDDKGPAKIHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEWRKFFTQCDILPKPFCQLEITLMGKQGSNKKSNVEDSIVRKLMLDTWNESIFSNIKNRLQDSAMKLVHAERLGEAFDSQLVIGVRESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQAPSYLQQNGVQNYMKYADAKLKEEEKRALRYLETRRECNSVEALMECCVNALVTSFKETILAECQGMIKRNETEKLHLMFSLMDKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDSEKYVEQLLTLFNRFSKLVKEAFQDDPRFLTARDKAYKAVVNDATIFKLELPLKQKGVGLKTQPESKCPELLANYCDMLLRKTPLSKKLTSEEIEAKLKEVLLVLKYVQNKDVFMRYHKAHLTRRLILDISADSEIEENMVEWLREVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNKLALPADSVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFYKKNHSGRKLHWHHLMSNGIITFKNEVGQYDLEVTTFQLAVLFAWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPKLKRQVLLYEPQVNSPKDFTEGTLFSVNQEFSLIKNAKVQKRGKINLIGRLQLTTERMREEENEGIVQLRILRTQEAIIQIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQIEWLIEHKYIRRDESDINTFIYMA	chr11:108008898-108107761[+]	"Core component of multiple SCF-like ECS (Elongin-Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. ECS(SOCS1) seems to direct ubiquitination of JAK2. ECS(KLHDC1) complex is part of the DesCEND (destruction via C-end degrons) pathway and mediates ubiquitination and degradation of truncated SELENOS selenoprotein produced by failed UGA/Sec decoding, which ends with a glycine. May form a cell surface vasopressin receptor."	PDB: 3DPL; PDB: 3DQV; PDB: 4JGH; PDB: 4N9F; PDB: 6V9I; PDB: 7ONI	HGNC:2556	CUL5_HUMAN	Reviewed	ENSG00000166266	.	.	.	.	.
Mol00055	Protein	Deoxycytidylate deaminase (DCTD)	dCMP deaminase	DCTD	1635	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000438320.7, DCTD-202, 1928; ENST00000357067.7, DCTD-201, 1931; ENST00000510370.5, DCTD-213, 794; ENST00000503988.1, DCTD-206, 1027; ENST00000503820.5, DCTD-205, 896; ENST00000512766.5, DCTD-214, 683; ENST00000514754.5, DCTD-217, 645; ENST00000510307.5, DCTD-212, 592; ENST00000503182.5, DCTD-204, 578; ENST00000508994.1, DCTD-209, 332; ENST00000507543.5, DCTD-207, 1874; ENST00000500813.6, DCTD-203, 1829; ENST00000507631.5, DCTD-208, 879; ENST00000513348.5, DCTD-215, 615; ENST00000509218.5, DCTD-210, 568; ENST00000509757.5, DCTD-211, 564; ENST00000513383.5, DCTD-216, 517"	MSEVSCKKRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMPNGCSDDVLPWRRTAENKLDTKYPYVCHAELNAIMNKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEATAARLLFNMAGVTFRKFIPKCSKIVIDFDSINSRPSQKLQ	chr4:182890060-182917936[-]	Supplies the nucleotide substrate for thymidylate synthetase.	PDB: 2W4L	HGNC:2710	DCTD_HUMAN	Reviewed	ENSG00000129187	.	.	.	.	.
Mol00056	Protein	Protein delta homolog 1 (DLK1)	DLK-1; pG2; FA1; DLK	DLK1	8788	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000341267.9, DLK1-202, 4657; ENST00000331224.10, DLK1-201, 1324; ENST00000392848.9, DLK1-203, 555; ENST00000556051.1, DLK1-205, 469; ENST00000555747.1, DLK1-204, 538"	MTATEALLRVLLLLLAFGHSTYGAECFPACNPQNGFCEDDNVCRCQPGWQGPLCDQCVTSPGCLHGLCGEPGQCICTDGWDGELCDRDVRACSSAPCANNRTCVSLDDGLYECSCAPGYSGKDCQKKDGPCVINGSPCQHGGTCVDDEGRASHASCLCPPGFSGNFCEIVANSCTPNPCENDGVCTDIGGDFRCRCPAGFIDKTCSRPVTNCASSPCQNGGTCLQHTQVSYECLCKPEFTGLTCVKKRALSPQQVTRLPSGYGLAYRLTPGVHELPVQQPEHRILKVSMKELNKKTPLLTEGQAICFTILGVLTSLVVLGTVGIVFLNKCETWVSNLRYNHMLRKKKNLLLQYNSGEDLAVNIIFPEKIDMTTFSKEAGDEEI	chr14:100725705-100738224[+]	May have a role in neuroendocrine differentiation.	.	HGNC:2907	DLK1_HUMAN	Reviewed	ENSG00000185559	.	.	.	.	.
Mol00057	Protein	Delta-like protein 1 (DLL1)	Drosophila Delta homolog 1; Delta1; H-Delta-1; UNQ146/PRO172	DLL1	28514	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000366756.4, DLL1-201, 3779; ENST00000630500.1, DLL1-202, 548"	MGSRCALALAVLSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGAGPPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGGGADSAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLATQRHLTVGEEWSQDLHSSGRTDLKYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGERGEKVCNPGWKGPYCTEPICLPGCDEQHGFCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCKNGATCTNTGQGSYTCSCRPGYTGATCELGIDECDPSPCKNGGSCTDLENSYSCTCPPGFYGKICELSAMTCADGPCFNGGRCSDSPDGGYSCRCPVGYSGFNCEKKIDYCSSSPCSNGAKCVDLGDAYLCRCQAGFSGRHCDDNVDDCASSPCANGGTCRDGVNDFSCTCPPGYTGRNCSAPVSRCEHAPCHNGATCHERGHRYVCECARGYGGPNCQFLLPELPPGPAVVDLTEKLEGQGGPFPWVAVCAGVILVLMLLLGCAAVVVCVRLRLQKHRPPADPCRGETETMNNLANCQREKDISVSIIGATQIKNTNKKADFHGDHSADKNGFKARYPAVDYNLVQDLKGDDTAVRDAHSKRDTKCQPQGSSGEEKGTPTTLRGGEASERKRPDSGCSTSKDTKYQSVYVISEEKDECVIATEV	chr6:170282206-170306565[-]	"Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner. Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD). Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation. Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner. During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries. During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway. At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway. Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis. Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell. Plays a role in immune systeme development, namely the development of all T-cells and marginal zone (MZ) B-cells. Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor. Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation. Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression. During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-derived progenitors, is neither required for satellite cell homing nor for PAX7 expression. Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium. Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels. During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression. Controls sprouting angiogenesis and subsequent vertical branch formation througth regulation on tip cell differentiation. Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine. Plays a role during inner ear development; negatively regulates auditory hair cell differentiation. Plays a role during nephron development through Notch signaling pathway. Regulates growth, blood pressure and energy homeostasis."	PDB: 4XBM	HGNC:2908	DLL1_HUMAN	Reviewed	ENSG00000198719	.	.	.	.	.
Mol00058	Protein	DNA (cytosine-5)-methyltransferase 1 (DNMT1)	Dnmt1; CXXC-type zinc finger protein 9; DNA methyltransferase HsaI; DNA MTase HsaI; M.HsaI; MCMT; AIM; CXXC9; DNMT	DNMT1	1786	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359526.9, DNMT1-202, 5274; ENST00000340748.8, DNMT1-201, 5408; ENST00000676610.1, DNMT1-230, 7157; ENST00000678804.1, DNMT1-247, 5728; ENST00000677946.1, DNMT1-241, 5665; ENST00000679103.1, DNMT1-251, 5126; ENST00000679313.1, DNMT1-252, 5122; ENST00000588118.5, DNMT1-213, 973; ENST00000588952.5, DNMT1-215, 841; ENST00000592342.5, DNMT1-226, 636; ENST00000592054.5, DNMT1-225, 591; ENST00000586800.5, DNMT1-209, 583; ENST00000590619.1, DNMT1-221, 231; ENST00000592705.5, DNMT1-227, 5215; ENST00000677013.1, DNMT1-233, 5175; ENST00000677634.1, DNMT1-238, 5165; ENST00000677250.1, DNMT1-236, 5127; ENST00000677616.1, DNMT1-237, 5101; ENST00000677685.1, DNMT1-239, 4974; ENST00000588913.5, DNMT1-214, 1775; ENST00000586988.5, DNMT1-210, 711; ENST00000586799.1, DNMT1-208, 672; ENST00000676604.1, DNMT1-229, 4821; ENST00000677038.1, DNMT1-234, 1756; ENST00000589538.5, DNMT1-220, 559; ENST00000593049.5, DNMT1-228, 534; ENST00000591798.5, DNMT1-224, 521; ENST00000586086.1, DNMT1-205, 489; ENST00000677783.1, DNMT1-240, 6469; ENST00000678024.1, DNMT1-242, 6142; ENST00000676820.1, DNMT1-231, 6055; ENST00000676868.1, DNMT1-232, 5845; ENST00000678694.1, DNMT1-246, 4482; ENST00000589351.6, DNMT1-219, 4395; ENST00000679100.1, DNMT1-250, 3348; ENST00000678647.1, DNMT1-245, 3302; ENST00000586667.2, DNMT1-207, 3259; ENST00000678851.1, DNMT1-248, 3143; ENST00000586588.5, DNMT1-206, 3094; ENST00000678957.1, DNMT1-249, 2873; ENST00000678107.1, DNMT1-243, 2204; ENST00000678239.1, DNMT1-244, 2117; ENST00000585843.1, DNMT1-203, 911; ENST00000587197.1, DNMT1-211, 809; ENST00000677135.1, DNMT1-235, 653; ENST00000589349.5, DNMT1-218, 603; ENST00000589294.1, DNMT1-217, 575; ENST00000589091.1, DNMT1-216, 563; ENST00000591239.1, DNMT1-222, 550; ENST00000585920.1, DNMT1-204, 529; ENST00000587604.1, DNMT1-212, 513; ENST00000591764.1, DNMT1-223, 341"	MPARTAPARVPTLAVPAISLPDDVRRRLKDLERDSLTEKECVKEKLNLLHEFLQTEIKNQLCDLETKLRKEELSEEGYLAKVKSLLNKDLSLENGAHAYNREVNGRLENGNQARSEARRVGMADANSPPKPLSKPRTPRRSKSDGEAKPEPSPSPRITRKSTRQTTITSHFAKGPAKRKPQEESERAKSDESIKEEDKDQDEKRRRVTSRERVARPLPAEEPERAKSGTRTEKEEERDEKEEKRLRSQTKEPTPKQKLKEEPDREARAGVQADEDEDGDEKDEKKHRSQPKDLAAKRRPEEKEPEKVNPQISDEKDEDEKEEKRRKTTPKEPTEKKMARAKTVMNSKTHPPKCIQCGQYLDDPDLKYGQHPPDAVDEPQMLTNEKLSIFDANESGFESYEALPQHKLTCFSVYCKHGHLCPIDTGLIEKNIELFFSGSAKPIYDDDPSLEGGVNGKNLGPINEWWITGFDGGEKALIGFSTSFAEYILMDPSPEYAPIFGLMQEKIYISKIVVEFLQSNSDSTYEDLINKIETTVPPSGLNLNRFTEDSLLRHAQFVVEQVESYDEAGDSDEQPIFLTPCMRDLIKLAGVTLGQRRAQARRQTIRHSTREKDRGPTKATTTKLVYQIFDTFFAEQIEKDDREDKENAFKRRRCGVCEVCQQPECGKCKACKDMVKFGGSGRSKQACQERRCPNMAMKEADDDEEVDDNIPEMPSPKKMHQGKKKKQNKNRISWVGEAVKTDGKKSYYKKVCIDAETLEVGDCVSVIPDDSSKPLYLARVTALWEDSSNGQMFHAHWFCAGTDTVLGATSDPLELFLVDECEDMQLSYIHSKVKVIYKAPSENWAMEGGMDPESLLEGDDGKTYFYQLWYDQDYARFESPPKTQPTEDNKFKFCVSCARLAEMRQKEIPRVLEQLEDLDSRVLYYSATKNGILYRVGDGVYLPPEAFTFNIKLSSPVKRPRKEPVDEDLYPEHYRKYSDYIKGSNLDAPEPYRIGRIKEIFCPKKSNGRPNETDIKIRVNKFYRPENTHKSTPASYHADINLLYWSDEEAVVDFKAVQGRCTVEYGEDLPECVQVYSMGGPNRFYFLEAYNAKSKSFEDPPNHARSPGNKGKGKGKGKGKPKSQACEPSEPEIEIKLPKLRTLDVFSGCGGLSEGFHQAGISDTLWAIEMWDPAAQAFRLNNPGSTVFTEDCNILLKLVMAGETTNSRGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFLLENVRNFVSFKRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITVRDTMSDLPEVRNGASALEISYNGEPQSWFQRQLRGAQYQPILRDHICKDMSALVAARMRHIPLAPGSDWRDLPNIEVRLSDGTMARKLRYTHHDRKNGRSSSGALRGVCSCVEAGKACDPAARQFNTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDTYRLFGNILDKHRQVGNAVPPPLAKAIGLEIKLCMLAKARESASAKIKEEEAAKD	chr19:10133342-10231286[-]	"Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. Promotes tumor growth."	PDB: 3EPZ; PDB: 3PTA; PDB: 3SWR; PDB: 4WXX; PDB: 4YOC; PDB: 4Z96; PDB: 4Z97; PDB: 5WVO; PDB: 5YDR; PDB: 6K3A; PDB: 6X9I; PDB: 6X9J; PDB: 6X9K	HGNC:2976	DNMT1_HUMAN	Reviewed	ENSG00000130816	.	.	.	.	.
Mol00059	Protein	Dual specificity protein phosphatase 6 (DUSP6)	Dual specificity protein phosphatase PYST1; Mitogen-activated protein kinase phosphatase 3; MAP kinase phosphatase 3; MKP-3; MKP3; PYST1	DUSP6	1848	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000279488.8, DUSP6-201, 3627; ENST00000308385.6, DUSP6-202, 1959; ENST00000547291.1, DUSP6-204, 1074; ENST00000548755.1, DUSP6-205, 567; ENST00000547140.1, DUSP6-203, 604"	MIDTLRPVPFASEMAISKTVAWLNEQLELGNERLLLMDCRPQELYESSHIESAINVAIPGIMLRRLQKGNLPVRALFTRGEDRDRFTRRCGTDTVVLYDESSSDWNENTGGESVLGLLLKKLKDEGCRAFYLEGGFSKFQAEFSLHCETNLDGSCSSSSPPLPVLGLGGLRISSDSSSDIESDLDRDPNSATDSDGSPLSNSQPSFPVEILPFLYLGCAKDSTNLDVLEEFGIKYILNVTPNLPNLFENAGEFKYKQIPISDHWSQNLSQFFPEAISFIDEARGKNCGVLVHCLAGISRSVTVTVAYLMQKLNLSMNDAYDIVKMKKSNISPNFNFMGQLLDFERTLGLSSPCDNRVPAQQLYFTTPSNQNVYQVDSLQST	chr12:89347235-89352501[-]	"Inactivates MAP kinases. Has a specificity for the ERK family. Plays an important role in alleviating chronic postoperative pain. Necessary for the normal dephosphorylation of the long-lasting phosphorylated forms of spinal MAPK1/3 and MAP kinase p38 induced by peripheral surgery, which drives the resolution of acute postoperative allodynia. Also important for dephosphorylation of MAPK1/3 in local wound tissue, which further contributes to resolution of acute pain. Promotes cell differentiation by regulating MAPK1/MAPK3 activity and regulating the expression of AP1 transcription factors."	PDB: 1HZM; PDB: 1MKP	HGNC:3072	DUS6_HUMAN	Reviewed	ENSG00000139318	.	.	.	.	.
Mol00060	Protein	Endothelin-1 receptor (EDNRA)	Endothelin receptor type A; ET-A; ETA-R; hET-AR; ETA; ETRA	EDNRA	1909	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000651419.1, EDNRA-209, 3970; ENST00000324300.10, EDNRA-201, 4150; ENST00000358556.8, EDNRA-202, 3823; ENST00000506066.1, EDNRA-204, 1032; ENST00000648866.1, EDNRA-208, 4135; ENST00000511804.5, EDNRA-206, 1569; ENST00000510697.5, EDNRA-205, 1160; ENST00000503721.1, EDNRA-203, 2186; ENST00000514245.1, EDNRA-207, 422"	METLCLRASFWLALVGCVISDNPERYSTNLSNHVDDFTTFRGTELSFLVTTHQPTNLVLPSNGSMHNYCPQQTKITSAFKYINTVISCTIFIVGMVGNATLLRIIYQNKCMRNGPNALIASLALGDLIYVVIDLPINVFKLLAGRWPFDHNDFGVFLCKLFPFLQKSSVGITVLNLCALSVDRYRAVASWSRVQGIGIPLVTAIEIVSIWILSFILAIPEAIGFVMVPFEYRGEQHKTCMLNATSKFMEFYQDVKDWWLFGFYFCMPLVCTAIFYTLMTCEMLNRRNGSLRIALSEHLKQRREVAKTVFCLVVIFALCWFPLHLSRILKKTVYNEMDKNRCELLSFLLLMDYIGINLATMNSCINPIALYFVSKKFKNCFQSCLCCCCYQSKSLMTSVPMNGTSIQWKNHDQNNHNTDRSSHKDSMN	chr4:147480917-147544954[+]	Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3.	.	HGNC:3179	EDNRA_HUMAN	Reviewed	ENSG00000151617	.	.	.	.	.
Mol00061	Protein	Epidermal growth factor receptor (EGFR)	Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1; ERBB; ERBB1; HER1	EGFR	1956	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000275493.7, EGFR-201, 9905; ENST00000454757.6, EGFR-206, 5464; ENST00000455089.5, EGFR-207, 3844; ENST00000344576.7, EGFR-203, 2872; ENST00000342916.7, EGFR-202, 2239; ENST00000420316.6, EGFR-204, 1570; ENST00000450046.1, EGFR-205, 691; ENST00000463948.1, EGFR-209, 561; ENST00000459688.1, EGFR-208, 452; ENST00000485503.1, EGFR-210, 665"	MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA	chr7:55019017-55211628[+]	"Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration. Plays a role in enhancing learning and memory performance."	PDB: 1IVO; PDB: 1M14; PDB: 1M17; PDB: 1MOX; PDB: 1NQL; PDB: 1XKK; PDB: 1YY9; PDB: 1Z9I; PDB: 2EB2; PDB: 2EB3; PDB: 2GS2; PDB: 2GS6; PDB: 2GS7; PDB: 2ITN; PDB: 2ITO; PDB: 2ITP; PDB: 2ITQ; PDB: 2ITT; PDB: 2ITU; PDB: 2ITV; PDB: 2ITW; PDB: 2ITX; PDB: 2ITY; PDB: 2ITZ; PDB: 2J5E; PDB: 2J5F; PDB: 2J6M; PDB: 2JIT; PDB: 2JIU; PDB: 2JIV; PDB: 2KS1; PDB: 2M0B; PDB: 2M20; PDB: 2N5S; PDB: 2RF9; PDB: 2RFD; PDB: 2RFE; PDB: 2RGP; PDB: 3B2U; PDB: 3B2V; PDB: 3BEL; PDB: 3BUO; PDB: 3C09; PDB: 3G5V; PDB: 3G5Y; PDB: 3GOP; PDB: 3GT8; PDB: 3IKA; PDB: 3LZB; PDB: 3NJP; PDB: 3OB2; PDB: 3OP0; PDB: 3P0Y; PDB: 3PFV; PDB: 3POZ; PDB: 3QWQ; PDB: 3UG1; PDB: 3UG2; PDB: 3VJN; PDB: 3VJO; PDB: 3VRP; PDB: 3VRR; PDB: 3W2O; PDB: 3W2P; PDB: 3W2Q; PDB: 3W2R; PDB: 3W2S; PDB: 3W32; PDB: 3W33; PDB: 4G5J; PDB: 4G5P; PDB: 4HJO; PDB: 4I1Z; PDB: 4I20; PDB: 4I21; PDB: 4I22; PDB: 4I23; PDB: 4I24; PDB: 4JQ7; PDB: 4JQ8; PDB: 4JR3; PDB: 4JRV; PDB: 4KRL; PDB: 4KRM; PDB: 4KRO; PDB: 4KRP; PDB: 4LI5; PDB: 4LL0; PDB: 4LQM; PDB: 4LRM; PDB: 4R3P; PDB: 4R3R; PDB: 4R5S; PDB: 4RIW; PDB: 4RIX; PDB: 4RIY; PDB: 4RJ4; PDB: 4RJ5; PDB: 4RJ6; PDB: 4RJ7; PDB: 4RJ8; PDB: 4TKS; PDB: 4UIP; PDB: 4UV7; PDB: 4WD5; PDB: 4WKQ; PDB: 4WRG; PDB: 4ZAU; PDB: 4ZJV; PDB: 4ZSE; PDB: 5C8K; PDB: 5C8M; PDB: 5C8N; PDB: 5CAL; PDB: 5CAN; PDB: 5CAO; PDB: 5CAP; PDB: 5CAQ; PDB: 5CAS; PDB: 5CAU; PDB: 5CAV; PDB: 5CNN; PDB: 5CNO; PDB: 5CZH; PDB: 5CZI; PDB: 5D41; PDB: 5EDP; PDB: 5EDQ; PDB: 5EDR; PDB: 5EM5; PDB: 5EM6; PDB: 5EM7; PDB: 5EM8; PDB: 5FED; PDB: 5FEE; PDB: 5FEQ; PDB: 5GMP; PDB: 5GNK; PDB: 5GTY; PDB: 5GTZ; PDB: 5HCX; PDB: 5HCY; PDB: 5HCZ; PDB: 5HG5; PDB: 5HG7; PDB: 5HG8; PDB: 5HG9; PDB: 5HIB; PDB: 5HIC; PDB: 5J9Y; PDB: 5J9Z; PDB: 5JEB; PDB: 5LV6; PDB: 5SX4; PDB: 5SX5; PDB: 5U8L; PDB: 5UG8; PDB: 5UG9; PDB: 5UGA; PDB: 5UGB; PDB: 5UGC; PDB: 5UWD; PDB: 5WB7; PDB: 5WB8; PDB: 5X26; PDB: 5X27; PDB: 5X28; PDB: 5X2A; PDB: 5X2C; PDB: 5X2F; PDB: 5X2K; PDB: 5XDK; PDB: 5XDL; PDB: 5XGM; PDB: 5XGN; PDB: 5XWD; PDB: 5Y25; PDB: 5Y9T; PDB: 5YU9; PDB: 5ZTO; PDB: 5ZWJ; PDB: 6ARU; PDB: 6B3S; PDB: 6D8E; PDB: 6DUK; PDB: 6JRJ; PDB: 6JRK; PDB: 6JRX; PDB: 6JWL; PDB: 6JX0; PDB: 6JX4; PDB: 6JXT; PDB: 6JZ0; PDB: 6LUB; PDB: 6LUD; PDB: 6P1D; PDB: 6P1L; PDB: 6P8Q; PDB: 6S89; PDB: 6S8A; PDB: 6S9B; PDB: 6S9C; PDB: 6S9D; PDB: 6TFU; PDB: 6TFV; PDB: 6TFW; PDB: 6TFY; PDB: 6TFZ; PDB: 6TG0; PDB: 6TG1; PDB: 6V5N; PDB: 6V5P; PDB: 6V66; PDB: 6V6K; PDB: 6V6O; PDB: 6VH4; PDB: 6VHN; PDB: 6VHP; PDB: 6WA2; PDB: 6WAK; PDB: 6WXN; PDB: 6XL4; PDB: 6Z4B; PDB: 6Z4D; PDB: 7A2A; PDB: 7AEI; PDB: 7AEM; PDB: 7JXI; PDB: 7JXK; PDB: 7JXL; PDB: 7JXM; PDB: 7JXP; PDB: 7JXQ; PDB: 7JXW; PDB: 7K1H; PDB: 7K1I; PDB: 7LGS; PDB: 7OXB	HGNC:3236	EGFR_HUMAN	Reviewed	ENSG00000146648	.	.	.	.	.
Mol00062	Protein	Hypoxia-inducible factor 2-alpha (EPAS1)	EPAS-1; Basic-helix-loop-helix-PAS protein MOP2; Class E basic helix-loop-helix protein 73; bHLHe73; HIF-1-alpha-like factor; HLF; Hypoxia-inducible factor 2-alpha; HIF-2-alpha; HIF2-alpha; Member of PAS protein 2; PAS domain-containing protein 2; BHLHE73; HIF2A; MOP2; PASD2	EPAS1	2034	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263734.5, EPAS1-201, 5155; ENST00000449347.5, EPAS1-202, 1067; ENST00000467888.5, EPAS1-207, 665; ENST00000460015.1, EPAS1-203, 558; ENST00000475822.1, EPAS1-209, 551; ENST00000468530.1, EPAS1-208, 452; ENST00000466465.5, EPAS1-206, 3622; ENST00000465318.5, EPAS1-205, 741; ENST00000483692.1, EPAS1-210, 657; ENST00000463191.1, EPAS1-204, 559"	MTADKEKKRSSSERRKEKSRDAARCRRSKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLSLKNGSGFGKKSKDMSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVKVYNNCPPHNSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRITELIGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVIYNPRNLQPQCIMCVNYVLSEIEKNDVVFSMDQTESLFKPHLMAMNSIFDSSGKGAVSEKSNFLFTKLKEEPEELAQLAPTPGDAIISLDFGNQNFEESSAYGKAILPPSQPWATELRSHSTQSEAGSLPAFTVPQAAAPGSTTPSATSSSSSCSTPNSPEDYYTSLDNDLKIEVIEKLFAMDTEAKDQCSTQTDFNELDLETLAPYIPMDGEDFQLSPICPEERLLAENPQSTPQHCFSAMTNIFQPLAPVAPHSPFLLDKFQQQLESKKTEPEHRPMSSIFFDAGSKASLPPCCGQASTPLSSMGGRSNTQWPPDPPLHFGPTKWAVGDQRTEFLGAAPLGPPVSPPHVSTFKTRSAKGFGARGPDVLSPAMVALSNKLKLKRQLEYEEQAFQDLSGGDPPGGSTSHLMWKRMKNLRGGSCPLMPDKPLSANVPNDKFTQNPMRGLGHPLRHLPLPQPPSAISPGENSKSRFPPQCYATQYQDYSLSSAHKVSGMASRLLGPSFESYLLPELTRYDCEVNVPVLGSSTLLQGGDLLRALDQAT	chr2:46293667-46386697[+]	Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX1 seems to activate CTAD (By similarity).	PDB: 1P97; PDB: 2A24; PDB: 3F1N; PDB: 3F1O; PDB: 3F1P; PDB: 3H7W; PDB: 3H82; PDB: 4GHI; PDB: 4GS9; PDB: 4PKY; PDB: 4XT2; PDB: 5KIZ; PDB: 5TBM; PDB: 5UFP; PDB: 6BVB; PDB: 6CZW; PDB: 6D09; PDB: 6D0B; PDB: 6D0C; PDB: 6I7Q; PDB: 6I7R; PDB: 6X21; PDB: 6X28; PDB: 6X2H; PDB: 6X37; PDB: 6X3D	HGNC:3374	EPAS1_HUMAN	Reviewed	ENSG00000116016	.	.	.	.	.
Mol00063	Protein	Ephrin type-A receptor 3 (EPHA3)	EPH-like kinase 4; EK4; hEK4; HEK; Human embryo kinase; Tyrosine-protein kinase TYRO4; Tyrosine-protein kinase receptor ETK1; Eph-like tyrosine kinase 1; ETK; ETK1; HEK; TYRO4	EPHA3	2042	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000336596.7, EPHA3-201, 5712; ENST00000452448.6, EPHA3-202, 2546; ENST00000494014.1, EPHA3-203, 3085"	MDCQLSILLLLSCSVLDSFGELIPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFREHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCSCNAGYEERGFMCQACRPGFYKALDGNMKCAKCPPHSSTQEDGSMNCRCENNYFRADKDPPSMACTRPPSSPRNVISNINETSVILDWSWPLDTGGRKDVTFNIICKKCGWNIKQCEPCSPNVRFLPRQFGLTNTTVTVTDLLAHTNYTFEIDAVNGVSELSSPPRQFAAVSITTNQAAPSPVLTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTIYVFQIRARTAAGYGTNSRKFEFETSPDSFSISGESSQVVMIAISAAVAIILLTVVIYVLIGRFCGYKSKHGADEKRLHFGNGHLKLPGLRTYVDPHTYEDPTQAVHEFAKELDATNISIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPIRWTSPEAIAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPPPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDITTFRTTGDWLNGVWTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV	chr3:89107621-89482134[+]	"Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development."	PDB: 2GSF; PDB: 2QO2; PDB: 2QO7; PDB: 2QO9; PDB: 2QOB; PDB: 2QOC; PDB: 2QOD; PDB: 2QOF; PDB: 2QOI; PDB: 2QOK; PDB: 2QOL; PDB: 2QON; PDB: 2QOO; PDB: 2QOQ; PDB: 3DZQ; PDB: 3FXX; PDB: 3FY2; PDB: 4G2F; PDB: 4GK2; PDB: 4GK3; PDB: 4GK4; PDB: 4L0P; PDB: 4P4C; PDB: 4P5Q; PDB: 4P5Z; PDB: 4TWN; PDB: 4TWO; PDB: 6IN0	HGNC:3387	EPHA3_HUMAN	Reviewed	ENSG00000044524	.	.	.	.	.
Mol00064	Protein	Cytoplasmic tyrosine-protein kinase BMX (BMX)	Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38	BMX	660	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000348343.11, BMX-202, 2543; ENST00000357607.6, BMX-203, 2598; ENST00000342014.6, BMX-201, 2499; ENST00000463891.1, BMX-204, 554; ENST00000489983.1, BMX-205, 514"	MDTKSILEELLLKRSQQKKKMSPNNYKERLFVLTKTNLSYYEYDKMKRGSRKGSIEIKKIRCVEKVNLEEQTPVERQYPFQIVYKDGLLYVYASNEESRSQWLKALQKEIRGNPHLLVKYHSGFFVDGKFLCCQQSCKAAPGCTLWEAYANLHTAVNEEKHRVPTFPDRVLKIPRAVPVLKMDAPSSSTTLAQYDNESKKNYGSQPPSSSTSLAQYDSNSKKIYGSQPNFNMQYIPREDFPDWWQVRKLKSSSSSEDVASSNQKERNVNHTTSKISWEFPESSSSEEEENLDDYDWFAGNISRSQSEQLLRQKGKEGAFMVRNSSQVGMYTVSLFSKAVNDKKGTVKHYHVHTNAENKLYLAENYCFDSIPKLIHYHQHNSAGMITRLRHPVSTKANKVPDSVSLGNGIWELKREEITLLKELGSGQFGVVQLGKWKGQYDVAVKMIKEGSMSEDEFFQEAQTMMKLSHPKLVKFYGVCSKEYPIYIVTEYISNGCLLNYLRSHGKGLEPSQLLEMCYDVCEGMAFLESHQFIHRDLAARNCLVDRDLCVKVSDFGMTRYVLDDQYVSSVGTKFPVKWSAPEVFHYFKYSSKSDVWAFGILMWEVFSLGKQPYDLYDNSQVVLKVSQGHRLYRPHLASDTIYQIMYSCWHELPEKRPTFQQLLSSIEPLREKDKH	chrX:15464246-15556529[+]	"Non-receptor tyrosine kinase that plays central but diverse modulatory roles in various signaling processes involved in the regulation of actin reorganization, cell migration, cell proliferation and survival, cell adhesion, and apoptosis. Participates in signal transduction stimulated by growth factor receptors, cytokine receptors, G-protein coupled receptors, antigen receptors and integrins. Induces tyrosine phosphorylation of BCAR1 in response to integrin regulation. Activation of BMX by integrins is mediated by PTK2/FAK1, a key mediator of integrin signaling events leading to the regulation of actin cytoskeleton and cell motility. Plays a critical role in TNF-induced angiogenesis, and implicated in the signaling of TEK and FLT1 receptors, 2 important receptor families essential for angiogenesis. Required for the phosphorylation and activation of STAT3, a transcription factor involved in cell differentiation. Also involved in interleukin-6 (IL6) induced differentiation. Plays also a role in programming adaptive cytoprotection against extracellular stress in different cell systems, salivary epithelial cells, brain endothelial cells, and dermal fibroblasts. May be involved in regulation of endocytosis through its interaction with an endosomal protein RUFY1. May also play a role in the growth and differentiation of hematopoietic cells; as well as in signal transduction in endocardial and arterial endothelial cells."	.	HGNC:1079	BMX_HUMAN	Reviewed	ENSG00000102010	.	.	.	.	.
Mol00065	Protein	Receptor tyrosine-protein kinase erbB-2 (ERBB2)	.	ERBB2	2064	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000269571.10, ERBB2-201, 4557; ENST00000584601.5, ERBB2-219, 4792; ENST00000406381.6, ERBB2-202, 4564; ENST00000541774.5, ERBB2-204, 4341; ENST00000584450.5, ERBB2-218, 3730; ENST00000578199.5, ERBB2-205, 2526; ENST00000445658.6, ERBB2-203, 3238; ENST00000580074.1, ERBB2-210, 754; ENST00000578709.5, ERBB2-209, 559; ENST00000582818.5, ERBB2-213, 529; ENST00000578502.1, ERBB2-207, 497; ENST00000578373.5, ERBB2-206, 4523; ENST00000582648.5, ERBB2-211, 1013; ENST00000584099.1, ERBB2-217, 583; ENST00000584888.1, ERBB2-221, 500; ENST00000583038.5, ERBB2-214, 4930; ENST00000582788.5, ERBB2-212, 2004; ENST00000584908.5, ERBB2-222, 1316; ENST00000578630.1, ERBB2-208, 874; ENST00000584014.5, ERBB2-216, 849; ENST00000584684.1, ERBB2-220, 649; ENST00000583391.1, ERBB2-215, 465"	MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV	chr17:39687914-39730426[+]	"Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization."	PDB: 1MFG; PDB: 1MFL; PDB: 1MW4; PDB: 1N8Z; PDB: 1QR1; PDB: 1S78; PDB: 2A91; PDB: 2JWA; PDB: 2KS1; PDB: 2L4K; PDB: 2N2A; PDB: 3BE1; PDB: 3H3B; PDB: 3MZW; PDB: 3N85; PDB: 3PP0; PDB: 3RCD; PDB: 3WLW; PDB: 3WSQ; PDB: 4GFU; PDB: 4HRL; PDB: 4HRM; PDB: 4HRN; PDB: 5K33; PDB: 5KWG; PDB: 5MY6; PDB: 5O4G; PDB: 5OB4; PDB: 5TQS; PDB: 6ATT; PDB: 6BGT; PDB: 6J71; PDB: 6LBX; PDB: 6OGE; PDB: 7JXH; PDB: 7MN5; PDB: 7MN6	HGNC:3430	ERBB2_HUMAN	Reviewed	ENSG00000141736	.	.	.	.	.
Mol00066	Protein	General transcription and DNA repair factor IIH helicase subunit XPB (ERCC3)	TFIIH subunit XPB; Basic transcription factor 2 89 kDa subunit; BTF2 p89; DNA excision repair protein ERCC-3; DNA repair protein complementing XP-B cells; TFIIH basal transcription factor complex 89 kDa subunit; TFIIH 89 kDa subunit; TFIIH p89; Xeroderma pigmentosum group B-complementing protein; XPB; XPBC	ERCC3	2071	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000285398.7, ERCC3-201, 2718; ENST00000647169.1, ERCC3-220, 2787; ENST00000647496.1, ERCC3-221, 701; ENST00000456257.1, ERCC3-204, 563; ENST00000645233.1, ERCC3-214, 3398; ENST00000445889.5, ERCC3-203, 2920; ENST00000426778.5, ERCC3-202, 2916; ENST00000645467.1, ERCC3-215, 2807; ENST00000646654.1, ERCC3-219, 2656; ENST00000644317.1, ERCC3-213, 2345; ENST00000645736.1, ERCC3-217, 2297; ENST00000642308.1, ERCC3-210, 1285; ENST00000645504.1, ERCC3-216, 720; ENST00000491292.5, ERCC3-208, 4018; ENST00000646042.1, ERCC3-218, 3390; ENST00000494464.5, ERCC3-209, 1367; ENST00000462306.5, ERCC3-206, 963; ENST00000642972.1, ERCC3-211, 886; ENST00000460485.1, ERCC3-205, 815; ENST00000643982.1, ERCC3-212, 590; ENST00000490062.1, ERCC3-207, 576"	MGKRDRADRDKKKSRKRHYEDEEDDEEDAPGNDPQEAVPSAAGKQVDESGTKVDEYGAKDYRLQMPLKDDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPTHVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIMQFIKLCTVSYGKVKLVLKHNRYFVESCHPDVIQHLLQDPVIRECRLRNSEGEATELITETFTSKSAISKTAESSGGPSTSRVTDPQGKSDIPMDLFDFYEQMDKDEEEEEETQTVSFEVKQEMIEELQKRCIHLEYPLLAEYDFRNDSVNPDINIDLKPTAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTAACTVRKRCLVLGNSAVSVEQWKAQFKMWSTIDDSQICRFTSDAKDKPIGCSVAISTYSMLGHTTKRSWEAERVMEWLKTQEWGLMILDEVHTIPAKMFRRVLTIVQAHCKLGLTATLVREDDKIVDLNFLIGPKLYEANWMELQNNGYIAKVQCAEVWCPMSPEFYREYVAIKTKKRILLYTMNPNKFRACQFLIKFHERRNDKIIVFADNVFALKEYAIRLNKPYIYGPTSQGERMQILQNFKHNPKINTIFISKVGDTSFDLPEANVLIQISSHGGSRRQEAQRLGRVLRAKKGMVAEEYNAFFYSLVSQDTQEMAYSTKRQRFLVDQGYSFKVITKLAGMEEEDLAFSTKEEQQQLLQKVLAATDLDAEEEVVAGEFGSRSSQASRRFGTMSSMSGADDTVYMEYHSSRSKAPSKHVHPLFKRFRK	chr2:127257290-127294166[-]	"ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATPase activity of XPB/ERCC3, but not its helicase activity, is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. The ATP-dependent helicase activity of XPB/ERCC3 is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription."	PDB: 4ERN; PDB: 5IVW; PDB: 5IY6; PDB: 5IY7; PDB: 5IY8; PDB: 5IY9; PDB: 5OF4; PDB: 6NMI; PDB: 6O9L; PDB: 6O9M; PDB: 6RO4; PDB: 7AD8; PDB: 7EGB; PDB: 7EGC; PDB: 7ENA; PDB: 7ENC; PDB: 7LBM; PDB: 7NVR; PDB: 7NVV; PDB: 7NVW; PDB: 7NVX; PDB: 7NVY; PDB: 7NVZ; PDB: 7NW0	HGNC:3435	ERCC3_HUMAN	Reviewed	ENSG00000163161	.	.	.	.	.
Mol00067	Protein	Protein FAM168A (TCRP1)	Tongue cancer chemotherapy resistance-associated protein 1; KIAA0280; TCRP1	FAM168A	23201	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356467.5, FAM168A-202, 7192; ENST00000064778.8, FAM168A-201, 7296; ENST00000450446.6, FAM168A-204, 1364; ENST00000632101.1, FAM168A-205, 473; ENST00000432223.2, FAM168A-203, 696"	MNPVYSPVQPGAPYGNPKNMAYTGYPTAYPAAAPAYNPSLYPTNSPSYAPEFQFLHSAYATLLMKQAWPQNSSSCGTEGTFHLPVDTGTENRTYQASSAAFRYTAGTPYKVPPTQSNTAPPPYSPSPNPYQTAMYPIRSAYPQQNLYAQGAYYTQPVYAAQPHVIHHTTVVQPNSIPSAIYPAPVAAPRTNGVAMGMVAGTTMAMSAGTLLTTPQHTAIGAHPVSMPTYRAQGTPAYSYVPPHW	chr11:73400487-73598189[-]	"In cancer context, protects cells from induced-DNA damage and apoptosis. Acts, at least in part, through PI3K/AKT/NFKB signaling pathway and by preventing POLB degradation. Decreases POLB ubiquitation and stabilizes its protein levels."	.	HGNC:28999	F168A_HUMAN	Reviewed	ENSG00000054965	.	.	.	.	.
Mol00068	Protein	FAS-associated death domain protein (FADD)	FAS-associating death domain-containing protein; Growth-inhibiting gene 3 protein; Mediator of receptor induced toxicity; MORT1; GIG3	FADD	8772	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000301838.5, FADD-201, 1708"	MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS	chr11:70203296-70207390[+]	"Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling."	PDB: 1A1W; PDB: 1A1Z; PDB: 1E3Y; PDB: 1E41; PDB: 2GF5; PDB: 3EZQ; PDB: 3OQ9; PDB: 6ACI	HGNC:3573	FADD_HUMAN	Reviewed	ENSG00000168040	.	.	.	.	.
Mol00069	Protein	F-box/WD repeat-containing protein 7 (FBXW7)	Archipelago homolog; hAgo; F-box and WD-40 domain-containing protein 7; F-box protein FBX30; SEL-10; hCdc4; FBW7; FBX30; SEL10	FBXW7	55294	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000281708.10, FBXW7-201, 5639; ENST00000603548.6, FBXW7-204, 5653; ENST00000393956.9, FBXW7-203, 4317; ENST00000296555.11, FBXW7-202, 4301; ENST00000603841.1, FBXW7-206, 2261; ENST00000604872.6, FBXW7-211, 921; ENST00000605042.1, FBXW7-212, 671; ENST00000647166.1, FBXW7-215, 655; ENST00000643834.1, FBXW7-214, 445; ENST00000642901.1, FBXW7-213, 395; ENST00000647183.1, FBXW7-216, 1735; ENST00000604095.1, FBXW7-208, 755; ENST00000603821.1, FBXW7-205, 4279; ENST00000604069.1, FBXW7-207, 615; ENST00000604822.1, FBXW7-210, 570; ENST00000604316.1, FBXW7-209, 528"	MNQELLSVGSKRRRTGGSLRGNPSSSQVDEEQMNRVVEEEQQQQLRQQEEEHTARNGEVVGVEPRPGGQNDSQQGQLEENNNRFISVDEDSSGNQEEQEEDEEHAGEQDEEDEEEEEMDQESDDFDQSDDSSREDEHTHTNSVTNSSSIVDLPVHQLSSPFYTKTTKMKRKLDHGSEVRSFSLGKKPCKVSEYTSTTGLVPCSATPTTFGDLRAANGQGQQRRRITSVQPPTGLQEWLKMFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPKELALYVLSFLEPKDLLQAAQTCRYWRILAEDNLLWREKCKEEGIDEPLHIKRRKVIKPGFIHSPWKSAYIRQHRIDTNWRRGELKSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPNKHQSAVTCLQFNKNFVITSSDDGTVKLWDLKTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK	chr4:152320544-152536092[-]	"Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bring them to the SCF complex for ubiquitination. Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NFE2L1, NOTCH2, MCL1, and probably PSEN1. Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation. Involved in bone homeostasis and negative regulation of osteoclast differentiation. Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1; CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination. Also able to promote 'Lys-63'-linked ubiquitination in response to DNA damage. The SCF(FBXW7) complex facilitates double-strand break repair following phosphorylation by ATM: phosphorylation promotes localization to sites of double-strand breaks and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4, enhancing DNA non-homologous end joining."	PDB: 2OVP; PDB: 2OVQ; PDB: 2OVR; PDB: 5IBK; PDB: 5V4B	HGNC:16712	FBXW7_HUMAN	Reviewed	ENSG00000109670	.	.	.	.	.
Mol00070	Protein	Fibroblast growth factor 9 (FGF9)	FGF-9; Glia-activating factor; GAF; Heparin-binding growth factor 9; HBGF-9	FGF9	2254	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000382353.6, FGF9-201, 4530; ENST00000478546.1, FGF9-203, 784; ENST00000461657.1, FGF9-202, 424"	MAPLGEVGNYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAVTDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELYKDILSQS	chr13:21671073-21704498[+]	"Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors."	.	HGNC:3687	FGF9_HUMAN	Reviewed	ENSG00000102678	.	.	.	.	.
Mol00071	Protein	Forkhead box protein C2 (FOXC2)	Forkhead-related protein FKHL14; Mesenchyme fork head protein 1; MFH-1 protein; Transcription factor FKH-14; FKHL14; MFH1	FOXC2	2303	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649859.1, FOXC2-201, 2900"	MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYSAGMGRSYAPYHHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKEKEERAHLKEPPPAASKGAPATPHLADAPKEAEKKVVIKSEAASPALPVITKVETLSPESALQGSPRSAASTPAGSPDGSLPEHHAAAPNGLPGFSVENIMTLRTSPPGGELSPGAGRAGLVVPPLALPYAAAPPAAYGQPCAQGLEAGAAGGYQCSMRAMSLYTGAERPAHMCVPPALDEALSDHPSGPTSPLSALNLAAGQEGALAATGHHHQHHGHHHPQAPPPPPAPQPQPTPQPGAAAAQAASWYLNHSGDLNHLPGHTFAAQQQTFPNVREMFNSHRLGIENSTLGESQVSGNASCQLPYRSTPPLYRHAAPYSYDCTKY	chr16:86566829-86569728[+]	Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.	PDB: 1D5V; PDB: 6AKO; PDB: 6AKP; PDB: 6LBM; PDB: 6O3T	HGNC:3801	FOXC2_HUMAN	Reviewed	ENSG00000176692	.	.	.	.	.
Mol00072	Protein	Fascin (FSCN1)	55 kDa actin-bundling protein; Singed-like protein; p55; FAN1; HSN; SNL	FSCN1	6624	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000382361.8, FSCN1-201, 2784; ENST00000447103.5, FSCN1-204, 713; ENST00000444748.5, FSCN1-203, 580; ENST00000405801.2, FSCN1-202, 550; ENST00000473330.1, FSCN1-205, 2215"	MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRDRRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKASAETVDPASLWEY	chr7:5592816-5606655[+]	"Actin-binding protein that contains 2 major actin binding sites. Organizes filamentous actin into parallel bundles. Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF."	PDB: 1DFC; PDB: 3LLP; PDB: 3P53; PDB: 4GOV; PDB: 4GOY; PDB: 4GP0; PDB: 4GP3; PDB: 6B0T; PDB: 6I0Z; PDB: 6I10; PDB: 6I11; PDB: 6I12; PDB: 6I13; PDB: 6I14; PDB: 6I15; PDB: 6I16; PDB: 6I17; PDB: 6I18	HGNC:11148	FSCN1_HUMAN	Reviewed	ENSG00000075618	.	.	.	.	.
Mol00073	Protein	Far upstream element-binding protein 1 (FUBP1)	FBP; FUSE-binding protein 1; DNA helicase V; hDH V	FUBP1	8880	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000370768.7, FUBP1-203, 6714; ENST00000370767.5, FUBP1-202, 2524; ENST00000421641.1, FUBP1-204, 802; ENST00000294623.8, FUBP1-201, 2201; ENST00000489495.5, FUBP1-211, 2156; ENST00000470287.1, FUBP1-205, 726; ENST00000492405.5, FUBP1-212, 668; ENST00000474632.5, FUBP1-206, 639; ENST00000488814.5, FUBP1-210, 612; ENST00000483894.5, FUBP1-208, 605; ENST00000492724.1, FUBP1-213, 583; ENST00000487684.1, FUBP1-209, 535; ENST00000480673.5, FUBP1-207, 262"	MADYSTVPPPSSGSAGGGGGGGGGGGVNDAFKDALQRARQIAAKIGGDAGTSLNSNDYGYGGQKRPLEDGDQPDAKKVAPQNDSFGTQLPPMHQQQSRSVMTEEYKVPDGMVGFIIGRGGEQISRIQQESGCKIQIAPDSGGLPERSCMLTGTPESVQSAKRLLDQIVEKGRPAPGFHHGDGPGNAVQEIMIPASKAGLVIGKGGETIKQLQERAGVKMVMIQDGPQNTGADKPLRITGDPYKVQQAKEMVLELIRDQGGFREVRNEYGSRIGGNEGIDVPIPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGTTPERIAQITGPPDRCQHAAEIITDLLRSVQAGNPGGPGPGGRGRGRGQGNWNMGPPGGLQEFNFIVPTGKTGLIIGKGGETIKSISQQSGARIELQRNPPPNADPNMKLFTIRGTPQQIDYARQLIEEKIGGPVNPLGPPVPHGPHGVPGPHGPPGPPGPGTPMGPYNPAPYNPGPPGPAPHGPPAPYAPQGWGNAYPHWQQQAPPDPAKAGTDPNSAAWAAYYAHYYQQQAQPPPAAPAGAPTTTQTNGQGDQQNPAPAGQVDYTKAWEEYYKKMGQAVPAPTGAPPGGQPDYSAAWAEYYRQQAAYYAQTSPQGMPQHPPAPQGQ	chr1:77944055-77979110[-]	Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription.	PDB: 1J4W; PDB: 2KXH; PDB: 4LIJ; PDB: 6Y24; PDB: 6Y2C; PDB: 6Y2D	HGNC:4004	FUBP1_HUMAN	Reviewed	ENSG00000162613	.	.	.	.	.
Mol00074	Protein	Growth arrest-specific protein 7 (GAS7)	GAS-7; KIAA0394	GAS7	8522	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000432992.7, GAS7-203, 8269; ENST00000437099.6, GAS7-204, 8003; ENST00000585266.5, GAS7-219, 3535; ENST00000580865.5, GAS7-213, 2417; ENST00000542249.5, GAS7-205, 1799; ENST00000579158.5, GAS7-210, 1528; ENST00000323816.8, GAS7-201, 8033; ENST00000396115.6, GAS7-202, 929; ENST00000584146.6, GAS7-217, 732; ENST00000578599.5, GAS7-207, 556; ENST00000584389.5, GAS7-218, 554; ENST00000583882.5, GAS7-216, 553; ENST00000580043.1, GAS7-211, 544; ENST00000578655.1, GAS7-208, 603; ENST00000580811.5, GAS7-212, 567; ENST00000581112.5, GAS7-214, 554; ENST00000581871.5, GAS7-215, 538; ENST00000579140.5, GAS7-209, 474; ENST00000578456.1, GAS7-206, 831"	MSGARCRTLYPFSGERHGQGLRFAAGELITLLQVPDGGWWEGEKEDGLRGWFPASYVQLLEKPGMVPPPPGEESQTVILPPGWQSYLSPQGRRYYVNTTTNETTWERPSSSPGIPASPGSHRSSLPPTVNGYHASGTPAHPPETAHMSVRKSTGDSQNLGSSSPSKKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEDYAKNLAKLSQNSLASQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQRDLEMKTQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQLLRKVDPAKDRELWVREHKTGNIRPVDMEI	chr17:9910606-10198606[-]	May play a role in promoting maturation and morphological differentiation of cerebellar neurons.	PDB: 2LX7; PDB: 2YSH	HGNC:4169	GAS7_HUMAN	Reviewed	ENSG00000007237	.	.	.	.	.
Mol00075	Protein	L-glutamine amidohydrolase (GLS)	GLS; K-glutaminase; L-glutamine amidohydrolase; GLS1; KIAA0838	GLS	2744	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000320717.8, GLS-201, 4840; ENST00000338435.8, GLS-202, 4475; ENST00000409626.5, GLS-205, 997; ENST00000457316.5, GLS-208, 821; ENST00000409428.5, GLS-204, 816; ENST00000412247.1, GLS-206, 693; ENST00000409215.5, GLS-203, 632; ENST00000417154.5, GLS-207, 837; ENST00000471443.1, GLS-212, 524; ENST00000479552.1, GLS-213, 2016; ENST00000496170.1, GLS-215, 673; ENST00000461965.5, GLS-209, 575; ENST00000469774.1, GLS-211, 557; ENST00000468352.5, GLS-210, 413; ENST00000495444.1, GLS-214, 394"	MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL	chr2:190880821-190965552[+]	"Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain."	PDB: 3CZD; PDB: 3UNW; PDB: 3UO9; PDB: 3VOY; PDB: 3VOZ; PDB: 3VP0; PDB: 3VP1; PDB: 3VP2; PDB: 3VP3; PDB: 3VP4; PDB: 4O7D; PDB: 5D3O; PDB: 5FI2; PDB: 5FI6; PDB: 5FI7; PDB: 5HL1; PDB: 5I94; PDB: 5JYO; PDB: 5JYP; PDB: 5U0I; PDB: 5U0J; PDB: 5UQE; PDB: 5WJ6; PDB: 6LOX; PDB: 6UJG; PDB: 6UJM; PDB: 6UK6; PDB: 6UKB; PDB: 6UL9; PDB: 6ULA; PDB: 6ULJ; PDB: 6UMC; PDB: 6UMD; PDB: 6UME; PDB: 6UMF	HGNC:4331	GLSK_HUMAN	Reviewed	ENSG00000115419	.	.	.	.	.
Mol00076	Protein	GRB2-related adapter protein (GRAP)	.	GRAP	10750	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000284154.10, GRAP-201, 1988; ENST00000573099.5, GRAP-204, 846; ENST00000395635.5, GRAP-202, 834; ENST00000583020.1, GRAP-205, 776; ENST00000571380.1, GRAP-203, 610"	MESVALYSFQATESDELAFNKGDTLKILNMEDDQNWYKAELRGVEGFIPKNYIRVKPHPWYSGRISRQLAEEILMKRNHLGAFLIRESESSPGEFSVSVNYGDQVQHFKVLREASGKYFLWEEKFNSLNELVDFYRTTTIAKKRQIFLRDEEPLLKSPGACFAQAQFDFSAQDPSQLSFRRGDIIEVLERPDPHWWRGRSCGRVGFFPRSYVQPVHL	chr17:19020656-19047011[-]	Couples signals from receptor and cytoplasmic tyrosine kinases to the Ras signaling pathway. Plays a role in the inner ear and in hearing.	.	HGNC:4562	GRAP_HUMAN	Reviewed	ENSG00000154016	.	.	.	.	.
Mol00077	Protein	Glycogen synthase kinase-3 beta (GSK3B)	GSK-3 beta; Serine/threonine-protein kinase GSK3B	GSK3B	2932	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264235.13, GSK3B-201, 7743; ENST00000316626.6, GSK3B-202, 7000; ENST00000678439.1, GSK3B-253, 6714; ENST00000650344.2, GSK3B-205, 1731; ENST00000677034.1, GSK3B-218, 1343; ENST00000678561.1, GSK3B-255, 673; ENST00000678013.1, GSK3B-242, 647; ENST00000676910.1, GSK3B-216, 645; ENST00000677423.1, GSK3B-227, 591; ENST00000679201.1, GSK3B-268, 546; ENST00000678159.1, GSK3B-245, 335; ENST00000677878.1, GSK3B-237, 305; ENST00000678787.1, GSK3B-259, 290; ENST00000679206.1, GSK3B-269, 280; ENST00000677903.1, GSK3B-239, 276; ENST00000677338.1, GSK3B-224, 276; ENST00000678181.1, GSK3B-246, 271; ENST00000677885.1, GSK3B-238, 215; ENST00000679188.1, GSK3B-266, 207; ENST00000677362.1, GSK3B-225, 206; ENST00000677875.1, GSK3B-236, 195; ENST00000679066.1, GSK3B-261, 180; ENST00000677400.1, GSK3B-226, 178; ENST00000677046.1, GSK3B-219, 137; ENST00000677169.1, GSK3B-223, 646; ENST00000677128.1, GSK3B-222, 599; ENST00000678350.1, GSK3B-251, 558; ENST00000677483.1, GSK3B-228, 502; ENST00000679194.1, GSK3B-267, 489; ENST00000677648.1, GSK3B-231, 460; ENST00000676775.1, GSK3B-212, 450; ENST00000678608.1, GSK3B-256, 450; ENST00000677069.1, GSK3B-221, 448; ENST00000676948.1, GSK3B-217, 437; ENST00000677995.1, GSK3B-241, 422; ENST00000677716.1, GSK3B-232, 417; ENST00000676887.1, GSK3B-214, 414; ENST00000679068.1, GSK3B-262, 408; ENST00000678509.1, GSK3B-254, 392; ENST00000678064.1, GSK3B-243, 389; ENST00000678286.1, GSK3B-249, 384; ENST00000676733.1, GSK3B-210, 340; ENST00000678678.1, GSK3B-257, 330; ENST00000678377.1, GSK3B-252, 325; ENST00000676844.1, GSK3B-213, 241; ENST00000676722.1, GSK3B-208, 4361; ENST00000677788.1, GSK3B-233, 2556; ENST00000676650.1, GSK3B-207, 1311; ENST00000676566.1, GSK3B-206, 1200; ENST00000677502.1, GSK3B-229, 1157; ENST00000676743.1, GSK3B-211, 355; ENST00000676890.1, GSK3B-215, 284; ENST00000679131.1, GSK3B-264, 224; ENST00000678342.1, GSK3B-250, 216; ENST00000473886.2, GSK3B-203, 215; ENST00000677804.1, GSK3B-234, 141; ENST00000676723.1, GSK3B-209, 140; ENST00000679164.1, GSK3B-265, 140; ENST00000677067.1, GSK3B-220, 136; ENST00000677959.1, GSK3B-240, 128; ENST00000678754.1, GSK3B-258, 128; ENST00000679085.1, GSK3B-263, 127; ENST00000678210.1, GSK3B-247, 126; ENST00000677870.1, GSK3B-235, 118; ENST00000678967.1, GSK3B-260, 114; ENST00000677530.1, GSK3B-230, 1826; ENST00000678245.1, GSK3B-248, 1561; ENST00000678121.1, GSK3B-244, 1018; ENST00000474830.1, GSK3B-204, 518"	MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST	chr3:119821321-120094994[-]	"Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1. Requires primed phosphorylation of the majority of its substrates. In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. May also mediate the development of insulin resistance by regulating activation of transcription factors. Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase. In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes. Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA. Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin. Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules. MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease. Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair. Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes. Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation. Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin. Is necessary for the establishment of neuronal polarity and axon outgrowth. Phosphorylates MARK2, leading to inhibit its activity. Phosphorylates SIK1 at 'Thr-182', leading to sustain its activity. Phosphorylates ZC3HAV1 which enhances its antiviral activity. Phosphorylates SNAI1, leading to its BTRC-triggered ubiquitination and proteasomal degradation. Phosphorylates SFPQ at 'Thr-687' upon T-cell activation. Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including ARNTL/BMAL1, CLOCK and PER2. Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation. Phosphorylates ARNTL/BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation. Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation. Regulates the circadian rhythmicity of hippocampal long-term potentiation and ARNTL/BMLA1 and PER2 expression. Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, leading to activate KAT5/TIP60 acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer. Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation. Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, leading to stabilize E2F1 and promote its activity."	PDB: 1GNG; PDB: 1H8F; PDB: 1I09; PDB: 1J1B; PDB: 1J1C; PDB: 1O6K; PDB: 1O6L; PDB: 1O9U; PDB: 1PYX; PDB: 1Q3D; PDB: 1Q3W; PDB: 1Q41; PDB: 1Q4L; PDB: 1Q5K; PDB: 1R0E; PDB: 1UV5; PDB: 2JDO; PDB: 2JDR; PDB: 2JLD; PDB: 2O5K; PDB: 2OW3; PDB: 2UW9; PDB: 2X39; PDB: 2XH5; PDB: 3CQU; PDB: 3CQW; PDB: 3DU8; PDB: 3E87; PDB: 3E88; PDB: 3E8D; PDB: 3F7Z; PDB: 3F88; PDB: 3GB2; PDB: 3I4B; PDB: 3L1S; PDB: 3M1S; PDB: 3MV5; PDB: 3OW4; PDB: 3PUP; PDB: 3Q3B; PDB: 3QKK; PDB: 3SAY; PDB: 3SD0; PDB: 3ZDI; PDB: 3ZRK; PDB: 3ZRL; PDB: 3ZRM; PDB: 4ACC; PDB: 4ACD; PDB: 4ACG; PDB: 4ACH; PDB: 4AFJ; PDB: 4B7T; PDB: 4DIT; PDB: 4EKK; PDB: 4IQ6; PDB: 4J1R; PDB: 4J71; PDB: 4NM0; PDB: 4NM3; PDB: 4NM5; PDB: 4NM7; PDB: 4PTC; PDB: 4PTE; PDB: 4PTG; PDB: 5F94; PDB: 5F95; PDB: 5HLN; PDB: 5HLP; PDB: 5K5N; PDB: 5KPK; PDB: 5KPL; PDB: 5KPM; PDB: 5OY4; PDB: 5T31; PDB: 6B8J; PDB: 6BUU; PDB: 6GJO; PDB: 6GN1; PDB: 6H0U; PDB: 6HK3; PDB: 6HK4; PDB: 6HK7; PDB: 6NPZ; PDB: 6TCU; PDB: 6V6L; PDB: 6Y9R; PDB: 6Y9S; PDB: 7B6F	HGNC:4617	GSK3B_HUMAN	Reviewed	ENSG00000082701	.	.	.	.	.
Mol00078	Protein	Glutathione S-transferase P (GSTP1)	GST class-pi; GSTP1-1; FAEES3; GST3	GSTP1	2950	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000398606.10, GSTP1-202, 741; ENST00000398603.6, GSTP1-201, 706; ENST00000495996.1, GSTP1-206, 221; ENST00000498765.5, GSTP1-207, 723; ENST00000646888.1, GSTP1-208, 471; ENST00000494593.1, GSTP1-205, 1681; ENST00000467591.1, GSTP1-203, 736; ENST00000489040.1, GSTP1-204, 523"	MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ	chr11:67583742-67586656[+]	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.	PDB: 10GS; PDB: 11GS; PDB: 12GS; PDB: 13GS; PDB: 14GS; PDB: 16GS; PDB: 17GS; PDB: 18GS; PDB: 19GS; PDB: 1AQV; PDB: 1AQW; PDB: 1AQX; PDB: 1EOG; PDB: 1EOH; PDB: 1GSS; PDB: 1KBN; PDB: 1LBK; PDB: 1MD3; PDB: 1MD4; PDB: 1PGT; PDB: 1PX6; PDB: 1PX7; PDB: 1ZGN; PDB: 20GS; PDB: 22GS; PDB: 2A2R; PDB: 2A2S; PDB: 2GSS; PDB: 2J9H; PDB: 2PGT; PDB: 3CSH; PDB: 3CSI; PDB: 3CSJ; PDB: 3DD3; PDB: 3DGQ; PDB: 3GSS; PDB: 3GUS; PDB: 3HJM; PDB: 3HJO; PDB: 3HKR; PDB: 3IE3; PDB: 3KM6; PDB: 3KMN; PDB: 3KMO; PDB: 3N9J; PDB: 3PGT; PDB: 4GSS; PDB: 4PGT; PDB: 5DAK; PDB: 5DAL; PDB: 5DCG; PDB: 5DDL; PDB: 5DJL; PDB: 5DJM; PDB: 5GSS; PDB: 5J41; PDB: 5JCW; PDB: 5L6X; PDB: 5X79; PDB: 6AP9; PDB: 6GSS; PDB: 6LLX; PDB: 6Y1E; PDB: 7GSS; PDB: 8GSS; PDB: 9GSS	HGNC:4638	GSTP1_HUMAN	Reviewed	ENSG00000084207	.	.	.	.	.
Mol00079	Protein	Solute carrier family 2 member 1 (SLC2A1)	Glucose transporter type 1; erythrocyte/brain; GLUT-1; HepG2 glucose transporter; GLUT1	SLC2A1	6513	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000426263.10, SLC2A1-203, 3384; ENST00000674765.1, SLC2A1-212, 1851; ENST00000475162.3, SLC2A1-205, 598; ENST00000460369.3, SLC2A1-204, 541; ENST00000372500.4, SLC2A1-201, 533; ENST00000630287.2, SLC2A1-208, 2398; ENST00000669445.1, SLC2A1-210, 150; ENST00000676097.1, SLC2A1-214, 271; ENST00000674545.1, SLC2A1-211, 2888; ENST00000676254.1, SLC2A1-215, 2795; ENST00000675112.1, SLC2A1-213, 2652; ENST00000625233.2, SLC2A1-206, 1031; ENST00000630821.1, SLC2A1-209, 591; ENST00000415851.6, SLC2A1-202, 578; ENST00000629908.1, SLC2A1-207, 401"	MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV	chr1:42925353-42958893[-]	"Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. Most important energy carrier of the brain: present at the blood-brain barrier and assures the energy-independent, facilitative transport of glucose into the brain. In association with BSG and NXNL1, promotes retinal cone survival by increasing glucose uptake into photoreceptors."	PDB: 4PYP; PDB: 5EQG; PDB: 5EQH; PDB: 5EQI; PDB: 6THA	HGNC:11005	GTR1_HUMAN	Reviewed	ENSG00000117394	.	.	.	.	.
Mol00080	Protein	Core histone macro-H2A.1 (H2AFY)	Histone macroH2A1; mH2A1; Histone H2A.y; H2A/y; Medulloblastoma antigen MU-MB-50.205; H2AFY	H2AFY	9555	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000511689.6, MACROH2A1-217, 1917; ENST00000304332.8, MACROH2A1-201, 1881; ENST00000312469.8, MACROH2A1-202, 1859; ENST00000510038.1, MACROH2A1-215, 1314; ENST00000423969.6, MACROH2A1-204, 924; ENST00000687629.1, MACROH2A1-221, 2039; ENST00000506671.5, MACROH2A1-210, 1905; ENST00000688649.1, MACROH2A1-222, 1772; ENST00000512507.5, MACROH2A1-218, 10982; ENST00000360597.8, MACROH2A1-203, 1772; ENST00000451949.6, MACROH2A1-205, 1744; ENST00000508785.5, MACROH2A1-213, 966; ENST00000513210.5, MACROH2A1-219, 775; ENST00000506532.5, MACROH2A1-209, 677; ENST00000508120.5, MACROH2A1-212, 536; ENST00000508962.1, MACROH2A1-214, 293; ENST00000505827.1, MACROH2A1-207, 2769; ENST00000511494.5, MACROH2A1-216, 2521; ENST00000507868.5, MACROH2A1-211, 861; ENST00000506218.1, MACROH2A1-208, 758; ENST00000513268.1, MACROH2A1-220, 501; ENST00000504197.5, MACROH2A1-206, 498"	MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLNLIHSEISNLAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN	chr5:135334381-135399914[-]	"Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin."	PDB: 1U35; PDB: 1ZR3; PDB: 1ZR5; PDB: 2F8N; PDB: 2FXK; PDB: 3HQH; PDB: 3HSV; PDB: 3IID; PDB: 3IIF; PDB: 3IVB; PDB: 5IIT; PDB: 5LNC; PDB: 7D3Y	HGNC:4740	H2AY_HUMAN	Reviewed	ENSG00000113648	.	.	.	.	.
Mol00081	Protein	Hairy/enhancer-of-split related with YRPW motif protein 1 (HEY1)	Cardiovascular helix-loop-helix factor 2; CHF-2; Class B basic helix-loop-helix protein 31; bHLHb31; HES-related repressor protein 1; Hairy and enhancer of split-related protein 1; HESR-1; Hairy-related transcription factor 1; HRT-1; hHRT1; BHLHB31; CHF2; HERP2; HESR1; HRT1	HEY1	23462	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354724.8, HEY1-202, 2197; ENST00000337919.9, HEY1-201, 2296; ENST00000523976.2, HEY1-208, 2034; ENST00000674418.1, HEY1-214, 3767; ENST00000674295.1, HEY1-212, 3715; ENST00000674358.1, HEY1-213, 2190; ENST00000518733.1, HEY1-204, 761; ENST00000674177.1, HEY1-210, 3878; ENST00000674160.1, HEY1-209, 2272; ENST00000435063.3, HEY1-203, 1854; ENST00000674192.1, HEY1-211, 1325; ENST00000519075.2, HEY1-205, 3667; ENST00000521111.2, HEY1-206, 3394; ENST00000523531.2, HEY1-207, 2320; ENST00000674439.1, HEY1-215, 2298"	MKRAHPEYSSSDSELDETIEVEKESADENGNLSSALGSMSPTTSSQILARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHTAGGKGYFDAHALAMDYRSLGFRECLAEVARYLSIIEGLDASDPLRVRLVSHLNNYASQREAASGAHAGLGHIPWGTVFGHHPHIAHPLLLPQNGHGNAGTTASPTEPHHQGRLGSAHPEAPALRAPPSGSLGPVLPVVTSASKLSPPLLSSVASLSAFPFSFGSFHLLSPNALSPSAPTQAANLGKPYRPWGTEIGAF	chr8:79762371-79767857[-]	"Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY2 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3. Involved in the regulation of liver cancer cells self-renewal."	PDB: 2DB7	HGNC:4880	HEY1_HUMAN	Reviewed	ENSG00000164683	.	.	.	.	.
Mol00082	Protein	Hypoxia-inducible factor 1-alpha (HIF1A)	HIF-1-alpha; HIF1-alpha; ARNT-interacting protein; Basic-helix-loop-helix-PAS protein MOP1; Class E basic helix-loop-helix protein 78; bHLHe78; Member of PAS protein 1; PAS domain-containing protein 8; BHLHE78; MOP1; PASD8	HIF1A	3091	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000337138.9, HIF1A-202, 3946; ENST00000539097.2, HIF1A-204, 3956; ENST00000323441.10, HIF1A-201, 3555; ENST00000394997.5, HIF1A-203, 3922; ENST00000557538.5, HIF1A-212, 3468; ENST00000557206.1, HIF1A-210, 767; ENST00000555014.1, HIF1A-207, 739; ENST00000553999.5, HIF1A-206, 616; ENST00000556237.1, HIF1A-208, 595; ENST00000557446.5, HIF1A-211, 559; ENST00000556827.1, HIF1A-209, 752; ENST00000547430.2, HIF1A-205, 711"	MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN	chr14:61695513-61748259[+]	"Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with NCOA1 and/or NCOA2. Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia."	PDB: 1H2K; PDB: 1H2L; PDB: 1H2M; PDB: 1L3E; PDB: 1L8C; PDB: 1LM8; PDB: 1LQB; PDB: 2ILM; PDB: 3HQR; PDB: 3HQU; PDB: 4AJY; PDB: 4H6J; PDB: 5JWP; PDB: 5L9B; PDB: 5L9V; PDB: 5LA9; PDB: 5LAS; PDB: 6GFX; PDB: 6GMR; PDB: 6YW3; PDB: 7LVS	HGNC:4910	HIF1A_HUMAN	Reviewed	ENSG00000100644	.	.	.	.	.
Mol00083	Protein	Hypoxia-inducible factor 1-alpha inhibitor (HIF1AN)	Factor inhibiting HIF-1; FIH-1; Hypoxia-inducible factor asparagine hydroxylase; FIH1	HIF1AN	55662	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000299163.7, HIF1AN-201, 12927; ENST00000533589.6, HIF1AN-205, 1042; ENST00000526476.5, HIF1AN-203, 708; ENST00000528044.1, HIF1AN-204, 559; ENST00000478787.1, HIF1AN-202, 888"	MAATAAEAVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN	chr10:100529072-100559998[+]	"Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation."	PDB: 1H2K; PDB: 1H2L; PDB: 1H2M; PDB: 1H2N; PDB: 1IZ3; PDB: 1MZE; PDB: 1MZF; PDB: 1YCI; PDB: 2CGN; PDB: 2CGO; PDB: 2ILM; PDB: 2W0X; PDB: 2WA3; PDB: 2WA4; PDB: 2XUM; PDB: 2Y0I; PDB: 2YC0; PDB: 2YDE; PDB: 3D8C; PDB: 3KCX; PDB: 3KCY; PDB: 3OD4; PDB: 3P3N; PDB: 3P3P; PDB: 4AI8; PDB: 4B7E; PDB: 4B7K; PDB: 4BIO; PDB: 4JAA; PDB: 4NR1; PDB: 4Z1V; PDB: 4Z2W; PDB: 5JWK; PDB: 5JWL; PDB: 5JWP; PDB: 5OP6; PDB: 5OP8; PDB: 5OPC; PDB: 6H9J; PDB: 6HA6; PDB: 6HC8; PDB: 6HKP; PDB: 6HL5; PDB: 6HL6; PDB: 6RUJ; PDB: 7A1J; PDB: 7A1K; PDB: 7A1L; PDB: 7A1M; PDB: 7A1N; PDB: 7A1O; PDB: 7A1P; PDB: 7A1Q; PDB: 7A1S	HGNC:17113	HIF1N_HUMAN	Reviewed	ENSG00000166135	.	.	.	.	.
Mol00084	Protein	High mobility group protein HMG-I/HMG-Y (HMGA1)	HMG-I(Y); High mobility group AT-hook protein 1; High mobility group protein A1; High mobility group protein R; HMGIY	HMGA1	3159	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000311487.9, HMGA1-201, 1920; ENST00000447654.5, HMGA1-205, 2159; ENST00000401473.7, HMGA1-204, 1887; ENST00000374116.3, HMGA1-203, 1848; ENST00000347617.10, HMGA1-202, 1773; ENST00000674029.1, HMGA1-207, 579; ENST00000478214.1, HMGA1-206, 716"	MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ	chr6:34236873-34246231[+]	"HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions."	PDB: 2EZD; PDB: 2EZE; PDB: 2EZF; PDB: 2EZG	HGNC:5010	HMGA1_HUMAN	Reviewed	ENSG00000137309	.	.	.	.	.
Mol00085	Protein	High mobility group protein HMGI-C (HMGA2)	High mobility group AT-hook protein 2; HMGIC	HMGA2	8091	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000403681.7, HMGA2-204, 4117; ENST00000393578.7, HMGA2-203, 1993; ENST00000536545.5, HMGA2-206, 1788; ENST00000354636.7, HMGA2-201, 1529; ENST00000393577.7, HMGA2-202, 611; ENST00000541363.5, HMGA2-210, 8094; ENST00000425208.6, HMGA2-205, 1444; ENST00000537429.5, HMGA2-208, 1527; ENST00000537275.5, HMGA2-207, 1508; ENST00000539662.1, HMGA2-209, 485; ENST00000545998.1, HMGA2-211, 1584"	MSARGEGAGQPSTSAQGQPAAPAPQKRGRGRPRKQQQEPTGEPSPKRPRGRPKGSKNKSPSKAAQKKAEATGEKRPRGRPRKWPQQVVQKKPAQEETEETSSQESAEED	chr12:65824460-65966291[+]	"Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Plays a role in postnatal myogenesis, is involved in satellite cell activation. Positively regulates IGF2 expression through PLAG1 and in a PLAG1-independent manner."	.	HGNC:5009	HMGA2_HUMAN	Reviewed	ENSG00000149948	.	.	.	.	.
Mol00086	Protein	High mobility group protein B1 (HMGB1)	High mobility group protein 1; HMG-1; HMG1	HMGB1	3146	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000341423.10, HMGB1-203, 5456; ENST00000405805.5, HMGB1-206, 4199; ENST00000339872.8, HMGB1-202, 2319; ENST00000399489.5, HMGB1-204, 1727; ENST00000399494.5, HMGB1-205, 1282; ENST00000326004.4, HMGB1-201, 821; ENST00000468384.1, HMGB1-207, 503; ENST00000490788.1, HMGB1-208, 425"	MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE	chr13:30456704-30617597[-]	"Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability (Ref.71). Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogdenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP."	PDB: 2LY4; PDB: 2RTU; PDB: 2YRQ; PDB: 6CG0; PDB: 6CIJ; PDB: 6CIK; PDB: 6CIL; PDB: 6CIM; PDB: 6OEM; PDB: 6OEN; PDB: 6OEO	HGNC:4983	HMGB1_HUMAN	Reviewed	ENSG00000189403	.	.	.	.	.
Mol00087	Protein	Heme oxygenase 1 (HMOX1)	HO-1; HO; HO1	HMOX1	3162	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000216117.9, HMOX1-201, 1554; ENST00000679074.1, HMOX1-207, 1454; ENST00000678411.1, HMOX1-206, 1088; ENST00000677931.1, HMOX1-205, 1062; ENST00000412893.5, HMOX1-202, 921; ENST00000481190.2, HMOX1-203, 1697; ENST00000494998.1, HMOX1-204, 567"	MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM	chr22:35380361-35394214[+]	"Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis."	PDB: 1N3U; PDB: 1N45; PDB: 1NI6; PDB: 1OYK; PDB: 1OYL; PDB: 1OZE; PDB: 1OZL; PDB: 1OZR; PDB: 1OZW; PDB: 1S13; PDB: 1S8C; PDB: 1T5P; PDB: 1TWN; PDB: 1TWR; PDB: 1XJZ; PDB: 1XK0; PDB: 1XK1; PDB: 1XK2; PDB: 1XK3; PDB: 3CZY; PDB: 3HOK; PDB: 3K4F; PDB: 3TGM; PDB: 4WD4; PDB: 5BTQ; PDB: 6EHA	HGNC:5013	HMOX1_HUMAN	Reviewed	ENSG00000100292	.	.	.	.	.
Mol00088	Protein	Heat shock 70 kDa protein 1A (HSP70)	Heat shock 70 kDa protein 1; HSP70-1; HSP70.1; HSP72; HSPA1; HSX70	HSPA1A	3303	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375651.7, HSPA1A-201, 2400; ENST00000608703.1, HSPA1A-202, 1909"	MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD	chr6:31815543-31817946[+]	"Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation."	PDB: 1HJO; PDB: 1S3X; PDB: 1XQS; PDB: 2E88; PDB: 2E8A; PDB: 2LMG; PDB: 3A8Y; PDB: 3ATU; PDB: 3ATV; PDB: 3AY9; PDB: 3D2E; PDB: 3D2F; PDB: 3JXU; PDB: 3LOF; PDB: 3Q49; PDB: 4IO8; PDB: 4J8F; PDB: 4PO2; PDB: 4WV5; PDB: 4WV7; PDB: 5AQW; PDB: 5AQX; PDB: 5AQY; PDB: 5AQZ; PDB: 5AR0; PDB: 5BN8; PDB: 5BN9; PDB: 5BPL; PDB: 5BPM; PDB: 5BPN; PDB: 5GJJ; PDB: 5MKR; PDB: 5MKS; PDB: 5XI9; PDB: 5XIR; PDB: 6FHK; PDB: 6G3R; PDB: 6G3S; PDB: 6JPV; PDB: 6K39	HGNC:5232	HS71A_HUMAN	Reviewed	ENSG00000204389	.	.	.	.	.
Mol00089	Protein	Homeobox protein Hox-A13 (HOXA13)	Homeobox protein Hox-1J; HOX1J	HOXA13	3209	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649031.1, HOXA13-202, 5015; ENST00000518136.3, HOXA13-201, 871"	MTASVLLHPRWIEPTVMFLYDNGGGLVADELNKNMEGAAAAAAAAAAAAAAGAGGGGFPHPAAAAAGGNFSVAAAAAAAAAAAANQCRNLMAHPAPLAPGAASAYSSAPGEAPPSAAAAAAAAAAAAAAAAAASSSGGPGPAGPAGAEAAKQCSPCSAAAQSSSGPAALPYGYFGSGYYPCARMGPHPNAIKSCAQPASAAAAAAFADKYMDTAGPAAEEFSSRAKEFAFYHQGYAAGPYHHHQPMPGYLDMPVVPGLGGPGESRHEPLGLPMESYQPWALPNGWNGQMYCPKEQAQPPHLWKSTLPDVVSHPSDASSYRRGRKKRVPYTKVQLKELEREYATNKFITKDKRRRISATTNLSERQVTIWFQNRRVKEKKVINKLKTTS	chr7:27193503-27200091[-]	"Sequence-specific, AT-rich binding transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.; FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis."	PDB: 2L7Z	HGNC:5102	HXA13_HUMAN	Reviewed	ENSG00000106031	.	.	.	.	.
Mol00090	Protein	Homeobox protein Hox-B3 (HOXB3)	Homeobox protein Hox-2.7; Homeobox protein Hox-2G; HOX2G	HOXB3	3213	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000498678.6, HOXB3-212, 3301; ENST00000470495.1, HOXB3-205, 4208; ENST00000311626.8, HOXB3-201, 2642; ENST00000472863.5, HOXB3-207, 1909; ENST00000489475.5, HOXB3-210, 1845; ENST00000460160.5, HOXB3-202, 1525; ENST00000476342.1, HOXB3-208, 1420; ENST00000490677.1, HOXB3-211, 1109; ENST00000465120.3, HOXB3-204, 943; ENST00000471459.1, HOXB3-206, 565; ENST00000552000.2, HOXB3-213, 466; ENST00000464266.1, HOXB3-203, 595; ENST00000478644.1, HOXB3-209, 398"	MQKATYYDNAAAALFGGYSSYPGSNGFGFDVPPQPPFQAATHLEGDYQRSACSLQSLGNAAPHAKSKELNGSCMRPGLAPEPLSAPPGSPPPSAAPTSATSNSSNGGGPSKSGPPKCGPGTNSTLTKQIFPWMKESRQTSKLKNNSPGTAEGCGGGGGGGGGGGSGGSGGGGGGGGGGDKSPPGSAASKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLSERQIKIWFQNRRMKYKKDQKAKGLASSSGGPSPAGSPPQPMQSTAGFMNALHSMTPSYESPSPPAFGKAHQNAYALPSNYQPPLKGCGAPQKYPPTPAPEYEPHVLQANGGAYGTPTMQGSPVYVGGGGYADPLPPPAGPSLYGLNHLSHHPSGNLDYNGAPPMAPSQHHGPCEPHPTYTDLSSHHAPPPQGRIQEAPKLTHL	chr17:48548870-48604912[-]	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	.	HGNC:5114	HXB3_HUMAN	Reviewed	ENSG00000120093	.	.	.	.	.
Mol00091	Protein	DNA-binding protein inhibitor ID-1 (ID1)	Class B basic helix-loop-helix protein 24; bHLHb24; Inhibitor of DNA binding 1; Inhibitor of differentiation 1; BHLHB24; ID	ID1	3397	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000376112.4, ID1-202, 983; ENST00000376105.4, ID1-201, 1233"	MKVASGSTATAAAGPSCALKAGKTASGAGEVVRCLSEQSVAISRCAGGAGARLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTPGGRGLPVRAPLSTLNGEISALTAEAACVPADDRILCR	chr20:31605283-31606515[+]	"Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer (By similarity)."	.	HGNC:5360	ID1_HUMAN	Reviewed	ENSG00000125968	.	.	.	.	.
Mol00092	Protein	Isocitrate dehydrogenase NADP 2 (IDH2)	IDH; ICD-M; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase	IDH2	3418	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000330062.8, IDH2-201, 2658; ENST00000540499.2, IDH2-202, 1453; ENST00000559482.5, IDH2-203, 1278; ENST00000560061.1, IDH2-204, 1449"	MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPVVEMDGDEMTRIIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKSSGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQ	chr15:90083045-90102477[-]	Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.	.	HGNC:5383	IDHP_HUMAN	Reviewed	ENSG00000182054	.	.	.	.	.
Mol00093	Protein	Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1)	IGF2 mRNA-binding protein 1; IMP-1; IMP1; Coding region determinant-binding protein; CRD-BP; IGF-II mRNA-binding protein 1; VICKZ family member 1; Zipcode-binding protein 1; ZBP-1; CRDBP; VICKZ1; ZBP1	IGF2BP1	10642	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000290341.8, IGF2BP1-201, 8796; ENST00000431824.2, IGF2BP1-202, 1317; ENST00000515586.5, IGF2BP1-206, 768; ENST00000510023.5, IGF2BP1-205, 754; ENST00000499130.6, IGF2BP1-203, 568; ENST00000505562.1, IGF2BP1-204, 461"	MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK	chr17:48997385-49056145[+]	"RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts."	PDB: 3KRM; PDB: 6QEY	HGNC:28866	IF2B1_HUMAN	Reviewed	ENSG00000159217	.	.	.	.	.
Mol00094	Protein	Eukaryotic translation initiation factor 4 gamma 1 (EIF4G1)	eIF-4-gamma 1; eIF-4G 1; eIF-4G1; p220; EIF4F; EIF4G; EIF4GI	EIF4G1	1981	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000346169.7, EIF4G1-202, 5405; ENST00000342981.8, EIF4G1-201, 5667; ENST00000424196.5, EIF4G1-212, 5653; ENST00000414031.5, EIF4G1-209, 5569; ENST00000352767.7, EIF4G1-204, 5484; ENST00000392537.6, EIF4G1-206, 5229; ENST00000382330.7, EIF4G1-205, 5129; ENST00000434061.6, EIF4G1-218, 5026; ENST00000350481.9, EIF4G1-203, 4990; ENST00000435046.7, EIF4G1-219, 5042; ENST00000427845.5, EIF4G1-216, 5038; ENST00000411531.5, EIF4G1-207, 4683; ENST00000441154.5, EIF4G1-221, 4311; ENST00000426123.5, EIF4G1-213, 2907; ENST00000421110.5, EIF4G1-210, 2755; ENST00000450424.5, EIF4G1-226, 2658; ENST00000444861.5, EIF4G1-224, 2384; ENST00000457456.5, EIF4G1-229, 983; ENST00000427141.6, EIF4G1-214, 730; ENST00000456033.5, EIF4G1-228, 694; ENST00000448284.1, EIF4G1-225, 677; ENST00000427607.5, EIF4G1-215, 596; ENST00000440448.5, EIF4G1-220, 578; ENST00000444134.5, EIF4G1-223, 558; ENST00000455679.5, EIF4G1-227, 542; ENST00000428387.5, EIF4G1-217, 524; ENST00000442406.5, EIF4G1-222, 5129; ENST00000676453.1, EIF4G1-240, 4590; ENST00000413967.5, EIF4G1-208, 2808; ENST00000422614.5, EIF4G1-211, 750; ENST00000676206.1, EIF4G1-239, 702; ENST00000460829.5, EIF4G1-230, 1804; ENST00000475721.5, EIF4G1-233, 1271; ENST00000464548.1, EIF4G1-231, 637; ENST00000484862.5, EIF4G1-236, 590; ENST00000466311.1, EIF4G1-232, 573; ENST00000478291.1, EIF4G1-234, 564; ENST00000493299.1, EIF4G1-238, 559; ENST00000482303.1, EIF4G1-235, 493; ENST00000485712.5, EIF4G1-237, 474"	MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN	chr3:184314495-184335358[+]	"Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation."	PDB: 1LJ2; PDB: 1UG3; PDB: 2W97; PDB: 4AZA; PDB: 4F02; PDB: 5EHC; PDB: 5EI3; PDB: 5EIR; PDB: 5T46; PDB: 6ZMW	HGNC:3296	IF4G1_HUMAN	Reviewed	ENSG00000114867	.	.	.	.	.
Mol00095	Protein	Eukaryotic translation initiation factor 4 gamma 2 (EIF4G2)	eIF-4-gamma 2; eIF-4G 2; eIF4G 2; Death-associated protein 5; DAP-5; p97; DAP5; OK/SW-cl.75	EIF4G2	1982	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000339995.11, EIF4G2-201, 3794; ENST00000526148.6, EIF4G2-208, 4001; ENST00000525681.6, EIF4G2-205, 3654; ENST00000396525.7, EIF4G2-202, 3346; ENST00000531416.6, EIF4G2-218, 1969; ENST00000524932.6, EIF4G2-203, 1286; ENST00000532082.6, EIF4G2-221, 1069; ENST00000528839.1, EIF4G2-213, 702; ENST00000530211.6, EIF4G2-214, 591; ENST00000532570.6, EIF4G2-226, 573; ENST00000527419.6, EIF4G2-210, 571; ENST00000530702.2, EIF4G2-216, 563; ENST00000531180.1, EIF4G2-217, 557; ENST00000527526.6, EIF4G2-211, 555; ENST00000528562.6, EIF4G2-212, 601; ENST00000531647.6, EIF4G2-220, 579; ENST00000534605.1, EIF4G2-231, 198; ENST00000525995.1, EIF4G2-207, 592; ENST00000534272.1, EIF4G2-229, 591; ENST00000531507.5, EIF4G2-219, 591; ENST00000525972.5, EIF4G2-206, 584; ENST00000532120.1, EIF4G2-222, 223; ENST00000532383.5, EIF4G2-225, 6769; ENST00000530564.1, EIF4G2-215, 849; ENST00000533485.1, EIF4G2-227, 806; ENST00000525606.5, EIF4G2-204, 690; ENST00000532152.5, EIF4G2-223, 587; ENST00000527015.1, EIF4G2-209, 582; ENST00000532349.1, EIF4G2-224, 550; ENST00000534246.1, EIF4G2-228, 523; ENST00000534470.1, EIF4G2-230, 520"	MESAIAEGGASRFSASSGGGGSRGAPQHYPKTAGNSEFLGKTPGQNAQKWIPARSTRRDDNSAANNSANEKERHDAIFRKVRGILNKLTPEKFDKLCLELLNVGVESKLILKGVILLIVDKALEEPKYSSLYAQLCLRLAEDAPNFDGPAAEGQPGQKQSTTFRRLLISKLQDEFENRTRNVDVYDKRENPLLPEEEEQRAIAKIKMLGNIKFIGELGKLDLIHESILHKCIKTLLEKKKRVQLKDMGEDLECLCQIMRTVGPRLDHERAKSLMDQYFARMCSLMLSKELPARIRFLLQDTVELREHHWVPRKAFLDNGPKTINQIRQDAVKDLGVFIPAPMAQGMRSDFFLEGPFMPPRMKMDRDPLGGLADMFGQMPGSGIGTGPGVIQDRFSPTMGRHRSNQLFNGHGGHIMPPTQSQFGEMGGKFMKSQGLSQLYHNQSQGLLSQLQGQSKDMPPRFSKKGQLNADEISLRPAQSFLMNKNQVPKLQPQITMIPPSAQPPRTQTPPLGQTPQLGLKTNPPLIQEKPAKTSKKPPPSKEELLKLTETVVTEYLNSGNANEAVNGVREMRAPKHFLPEMLSKVIILSLDRSDEDKEKASSLISLLKQEGIATSDNFMQAFLNVLDQCPKLEVDIPLVKSYLAQFAARAIISELVSISELAQPLESGTHFPLFLLCLQQLAKLQDREWLTELFQQSKVNMQKMLPEIDQNKDRMLEILEGKGLSFLFPLLKLEKELLKQIKLDPSPQTIYKWIKDNISPKLHVDKGFVNILMTSFLQYISSEVNPPSDETDSSSAPSKEQLEQEKQLLLSFKPVMQKFLHDHVDLQVSALYALQVHCYNSNFPKGMLLRFFVHFYDMEIIEEEAFLAWKEDITQEFPGKGKALFQVNQWLTWLETAEEEESEEEAD	chr11:10797050-10808940[-]	"Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases."	PDB: 3D3M; PDB: 3L6A; PDB: 4IUL	HGNC:3297	IF4G2_HUMAN	Reviewed	ENSG00000110321	.	.	.	.	.
Mol00096	Protein	Interferon alpha-inducible protein 27 (IFI27)	p27; Interferon alpha-induced 11.5 kDa protein; Interferon-stimulated gene 12a protein; ISG12(a); ISG12A	IFI27	3429	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000612813.4, IFI27-205, 725; ENST00000616764.5, IFI27-209, 714; ENST00000621160.5, IFI27-213, 652; ENST00000614204.4, IFI27-206, 692; ENST00000620396.4, IFI27-212, 599; ENST00000618863.1, IFI27-211, 505; ENST00000618200.4, IFI27-210, 364; ENST00000611954.4, IFI27-203, 227; ENST00000614288.1, IFI27-207, 666; ENST00000612499.1, IFI27-204, 2439; ENST00000614648.1, IFI27-208, 681; ENST00000557700.1, IFI27-202, 598; ENST00000555081.5, IFI27-201, 571"	MEASALTSSAVTSVAKVVRVASGSAVVLPLARIATVVIGGVVAMAAVPMVLSAMGFTAAGIASSSIAAKMMSAAAIANGGGVASGSLVATLQSLGATGLSGLTKFILGSIGSAIAAVIARFY	chr14:94104836-94116695[+]	"Probable adapter protein involved in different biological processes. Part of the signaling pathways that lead to apoptosis. Involved in type-I interferon-induced apoptosis characterized by a rapid and robust release of cytochrome C from the mitochondria and activation of BAX and caspases ,  and 9. Also functions in TNFSF10-induced apoptosis. May also have a function in the nucleus, where it may be involved in the interferon-induced negative regulation of the transcriptional activity of NR4A1, NR4A2 and NR4A3 through the enhancement of XPO1-mediated nuclear export of these nuclear receptors. May thereby play a role in the vascular response to injury. In the innate immune response, has an antiviral activity towards hepatitis C virus/HCV. May prevent the replication of the virus by recruiting both the hepatitis C virus non-structural protein 5A/NS5A and the ubiquitination machinery via SKP2, promoting the ubiquitin-mediated proteasomal degradation of NS5A."	.	HGNC:5397	IFI27_HUMAN	Reviewed	ENSG00000165949	.	.	.	.	.
Mol00097	Protein	Insulin-like growth factor 1 receptor (IGF1R)	.	IGF1R	3480	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650285.1, IGF1R-217, 12235; ENST00000649865.1, IGF1R-216, 12232; ENST00000558898.1, IGF1R-205, 1034; ENST00000558355.1, IGF1R-203, 572; ENST00000560144.1, IGF1R-209, 525; ENST00000560432.1, IGF1R-213, 657; ENST00000557873.5, IGF1R-201, 583; ENST00000557938.5, IGF1R-202, 574; ENST00000559582.1, IGF1R-207, 567; ENST00000560186.5, IGF1R-210, 551; ENST00000558751.1, IGF1R-204, 548; ENST00000560277.5, IGF1R-211, 526; ENST00000560972.1, IGF1R-214, 310; ENST00000558947.1, IGF1R-206, 303; ENST00000559925.5, IGF1R-208, 2280; ENST00000561049.1, IGF1R-215, 682; ENST00000560343.1, IGF1R-212, 343"	MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLHFTSTTTSKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKDVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDIEEVTENPKTEVCGGEKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTAADTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC	chr15:98648539-98964530[+]	"Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R.; FUNCTION: When present in a hybrid receptor with INSR, binds IGF1. 12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, 16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin."	PDB: 1IGR; PDB: 1JQH; PDB: 1K3A; PDB: 1M7N; PDB: 1P4O; PDB: 2OJ9; PDB: 2ZM3; PDB: 3D94; PDB: 3F5P; PDB: 3I81; PDB: 3LVP; PDB: 3LW0; PDB: 3NW5; PDB: 3NW6; PDB: 3NW7; PDB: 3O23; PDB: 3QQU; PDB: 4D2R; PDB: 4XSS; PDB: 5FXQ; PDB: 5FXR; PDB: 5FXS; PDB: 5HZN; PDB: 5U8Q; PDB: 5U8R; PDB: 6JK8; PDB: 6VWG; PDB: 6VWH; PDB: 6VWI; PDB: 6VWJ	HGNC:5465	IGF1R_HUMAN	Reviewed	ENSG00000140443	.	.	.	.	.
Mol00098	Protein	Nuclear factor kappa-B kinase subunit alpha inhibitor (IKKalpha)	I-kappa-B kinase alpha; IKK-A; IKK-alpha; IkBKA; IkappaB kinase; Conserved helix-loop-helix ubiquitous kinase; I-kappa-B kinase 1; IKK1; Nuclear factor NF-kappa-B inhibitor kinase alpha; NFKBIKA; Transcription factor 16; TCF-16; IKKA; TCF16	CHUK	1147	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000370397.8, CHUK-201, 3600; ENST00000590930.5, CHUK-204, 4845; ENST00000588656.1, CHUK-203, 675; ENST00000585551.1, CHUK-202, 424"	MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTSAKIISFLLPPDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPIIQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFHKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYAEVGVIGYLEDQIMSLHAEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPSDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGAVTPQTSAWLPPTSAEHDHSLSCVVTPQDGETSAQMIEENLNCLGHLSTIIHEANEEQGNSMMNLDWSWLTE	chr10:100188300-100229596[-]	"Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities. Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor. Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death. Phosphorylates AMBRA1 following mitophagy induction, promoting AMBRA1 interaction with ATG8 family proteins and its mitophagic activity."	PDB: 3BRT; PDB: 5EBZ; PDB: 5TQW; PDB: 5TQX; PDB: 5TQY	HGNC:1974	IKKA_HUMAN	Reviewed	ENSG00000213341	.	.	.	.	.
Mol00099	Protein	Interleukin-6 (IL6)	IL-6; B-cell stimulatory factor 2; BSF-2; CTL differentiation factor; CDF; Hybridoma growth factor; Interferon beta-2; IFN-beta-2; IFNB2	IL6	3569	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000258743.10, IL6-201, 1127; ENST00000404625.5, IL6-204, 1527; ENST00000407492.5, IL6-206, 926; ENST00000485300.1, IL6-209, 985; ENST00000401630.7, IL6-202, 765; ENST00000406575.1, IL6-205, 649; ENST00000426291.5, IL6-207, 574; ENST00000401651.5, IL6-203, 539; ENST00000464710.2, IL6-208, 3319"	MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM	chr7:22725884-22732002[+]	"Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (Probable). The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable)."	PDB: 1ALU; PDB: 1IL6; PDB: 1P9M; PDB: 2IL6; PDB: 4CNI; PDB: 4J4L; PDB: 4NI7; PDB: 4NI9; PDB: 4O9H; PDB: 4ZS7; PDB: 5FUC; PDB: 7NXZ	HGNC:6018	IL6_HUMAN	Reviewed	ENSG00000136244	.	.	.	.	.
Mol00100	Protein	Insulin receptor substrate 1 (IRS1)	IRS-1	IRS1	3667	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305123.6, IRS1-201, 9771; ENST00000498335.1, IRS1-202, 506"	MASPPESDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKGHHDGAAALGAGGGGGSCSGSSGLGEAGEDLSYGDVPPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSNCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSARLHPPLNHSRSIPMPASRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGPSTLTAPNGHYILSRGGNGHRCTPGTGLGTSPALAGDEAASAADLDNRFRKRTHSAGTSPTITHQKTPSQSSVASIEEYTEMMPAYPPGGGSGGRLPGHRHSAFVPTRSYPEEGLEMHPLERRGGHHRPDSSTLHTDDGYMPMSPGVAPVPSGRKGSGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGGCSPDIGGGPSSSSSSSNAVPSGTSYGKLWTNGVGGHHSHVLPHPKPPVESSGGKLLPCTGDYMNMSPVGDSNTSSPSDCYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSTSSGRLLYAATADDSSSSTSSDSLGGGYCGARLEPSLPHPHHQVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRAREQQQQQQPLLHPPEPKSPGEYVNIEFGSDQSGYLSGPVAFHSSPSVRCPSQLQPAPREEETGTEEYMKMDLGPGRRAAWQESTGVEMGRLGPAPPGAASICRPTRAVPSSRGDYMTMQMSCPRQSYVDTSPAAPVSYADMRTGIAAEEVSLPRATMAAASSSSAASASPTGPQGAAELAAHSSLLGGPQGPGGMSAFTRVNLSPNRNQSAKVIRADPQGCRRRHSSETFSSTPSATRVGNTVPFGAGAAVGGGGGSSSSSEDVKRHSSASFENVWLRPGELGGAPKEPAKLCGAAGGLENGLNYIDLDLVKDFKQCPQECTPEPQPPPPPPPHQPLGSGESSSTRRSSEDLSAYASISFQKQPEDRQ	chr2:226731312-226799820[-]	May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity).	PDB: 1IRS; PDB: 1K3A; PDB: 1QQG; PDB: 2Z8C; PDB: 5U1M; PDB: 6BNT	HGNC:6125	IRS1_HUMAN	Reviewed	ENSG00000169047	.	.	.	.	.
Mol00101	Protein	Ubiquitin-like protein ISG15 (ISG15)	Interferon-induced 15 kDa protein; Interferon-induced 17 kDa protein; IP17; Ubiquitin cross-reactive protein; hUCRP; G1P2; UCRP	ISG15	9636	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649529.1, ISG15-203, 637; ENST00000624697.4, ISG15-202, 787; ENST00000624652.1, ISG15-201, 657"	MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS	chr1:1001138-1014540[+]	"Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include IFIT1, MX1/MxA, PPM1B, UBE2L6, UBA7, CHMP5, CHMP2A, CHMP4B and CHMP6. Isgylation of the viral sensor IFIH1/MDA5 promotes IFIH1/MDA5 oligomerization and triggers activation of innate immunity against a range of viruses, including coronaviruses, flaviviruses and picornaviruses. Can also isgylate: EIF2AK2/PKR which results in its activation, DDX58/RIG-I which inhibits its function in antiviral signaling response, EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity, UBE2N and UBE2E1 which negatively regulates their activity, IRF3 which inhibits its ubiquitination and degradation and FLNB which prevents its ability to interact with the upstream activators of the JNK cascade thereby inhibiting IFNA-induced JNK signaling. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A, HIV-1 and Ebola virus. Restricts HIV-1 and ebola virus via disruption of viral budding. Inhibits the ubiquitination of HIV-1 Gag and host TSG101 and disrupts their interaction, thereby preventing assembly and release of virions from infected cells. Inhibits Ebola virus budding mediated by the VP40 protein by disrupting ubiquitin ligase activity of NEDD4 and its ability to ubiquitinate VP40. ISGylates influenza A virus NS1 protein which causes a loss of function of the protein and the inhibition of virus replication. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity. The secreted form acts through the integrin ITGAL/ITGB2 receptor to initiate activation of SRC family tyrosine kinases including LYN, HCK and FGR which leads to secretion of IFNG and IL10; the interaction is mediated by ITGAL."	PDB: 1Z2M; PDB: 2HJ8; PDB: 3PHX; PDB: 3PSE; PDB: 3R66; PDB: 3RT3; PDB: 3SDL; PDB: 5TL6; PDB: 5W8T; PDB: 5W8U; PDB: 6BI8; PDB: 6FFA; PDB: 6XA9; PDB: 7RBS; PDB: 7S6P	HGNC:4053	ISG15_HUMAN	Reviewed	ENSG00000187608	.	.	.	.	.
Mol00102	Protein	Tyrosine-protein kinase JAK2 (JAK3)	Janus kinase 2; JAK-2	JAK2	3717	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000381652.4, JAK2-201, 7023; ENST00000636127.1, JAK2-204, 2615; ENST00000476574.5, JAK2-202, 327; ENST00000487310.1, JAK2-203, 773"	MGMACLTMTEMEGTSTSSIYQNGDISGNANSMKQIDPVLQVYLYHSLGKSEADYLTFPSGEYVAEEICIAASKACGITPVYHNMFALMSETERIWYPPNHVFHIDESTRHNVLYRIRFYFPRWYCSGSNRAYRHGISRGAEAPLLDDFVMSYLFAQWRHDFVHGWIKVPVTHETQEECLGMAVLDMMRIAKENDQTPLAIYNSISYKTFLPKCIRAKIQDYHILTRKRIRYRFRRFIQQFSQCKATARNLKLKYLINLETLQSAFYTEKFEVKEPGSGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPNIIDVSIKQANQEGSNESRVVTIHKQDGKNLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPAVLENIQSNCHGPISMDFAISKLKKAGNQTGLYVLRCSPKDFNKYFLTFAVERENVIEYKHCLITKNENEEYNLSGTKKNFSSLKDLLNCYQMETVRSDNIIFQFTKCCPPKPKDKSNLLVFRTNGVSDVPTSPTLQRPTHMNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSKLSHKHLVLNYGVCVCGDENILVQEFVKFGSLDTYLKKNKNCINILWKLEVAKQLAWAMHFLEENTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG	chr9:4984390-5129948[+]	"Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin."	.	HGNC:6192	JAK2_HUMAN	Reviewed	ENSG00000096968	.	.	.	.	.
Mol00103	Protein	Transcription factor Jun (JUN)	Activator protein 1; AP1; Proto-oncogene c-Jun; Transcription factor AP-1 subunit Jun; V-jun avian sarcoma virus 17 oncogene homolog; p39	JUN	3725	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371222.4, JUN-201, 3257; ENST00000678696.1, JUN-202, 2852"	MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF	chr1:58776845-58784048[-]	"Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity. Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells."	PDB: 1A02; PDB: 1FOS; PDB: 1JNM; PDB: 1JUN; PDB: 1S9K; PDB: 1T2K; PDB: 5FV8; PDB: 5T01; PDB: 6Y3V	HGNC:6204	JUN_HUMAN	Reviewed	ENSG00000177606	.	.	.	.	.
Mol00104	Protein	Protein kinase C epsilon type (PRKCE)	nPKC-epsilon; PKCE	PRKCE	5581	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000306156.8, PRKCE-201, 5749; ENST00000394874.1, PRKCE-202, 996; ENST00000421201.1, PRKCE-203, 939; ENST00000467135.5, PRKCE-205, 1000; ENST00000469753.5, PRKCE-206, 979; ENST00000489067.1, PRKCE-212, 798; ENST00000497602.1, PRKCE-214, 755; ENST00000480633.1, PRKCE-210, 621; ENST00000494472.1, PRKCE-213, 583; ENST00000480453.5, PRKCE-209, 582; ENST00000476675.5, PRKCE-208, 570; ENST00000498388.1, PRKCE-215, 474; ENST00000472021.1, PRKCE-207, 434; ENST00000485176.1, PRKCE-211, 372; ENST00000462720.6, PRKCE-204, 305"	MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGRVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDQVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLIAGAESPQPASGSSPSEEDRSKSAPTSPCDQEIKELENNIRKALSFDNRGEEHRAASSPDGQLMSPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVASQNGEDAIKQHPFFKEIDWVLLEQKKIKPPFKPRIKTKRDVNNFDQDFTREEPVLTLVDEAIVKQINQEEFKGFSYFGEDLMP	chr2:45651345-46187990[+]	"Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. In HeLa cells, contributes to hepatocyte growth factor (HGF)-induced cell migration, and in human corneal epithelial cells, plays a critical role in wound healing after activation by HGF. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). In prostate cancer cells, interacts with and phosphorylates STAT3, which increases DNA-binding and transcriptional activity of STAT3 and seems to be essential for prostate cancer cell invasion. Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells."	PDB: 2WH0; PDB: 5LIH	HGNC:9401	KPCE_HUMAN	Reviewed	ENSG00000171132	.	.	.	.	.
Mol00105	Protein	Pyruvate kinase M2 (PKM)	Cytosolic thyroid hormone-binding protein; CTHBP; Opa-interacting protein 3; OIP-3; Pyruvate kinase 2/3; Pyruvate kinase muscle isozyme; Thyroid hormone-binding protein 1; THBP1; Tumor M2-PK; p58; OIP3; PK2; PK3; PKM2	PKM	5315	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000335181.10, PKM-202, 2305; ENST00000319622.10, PKM-201, 2717; ENST00000389093.7, PKM-203, 2279; ENST00000568459.5, PKM-219, 1806; ENST00000565184.6, PKM-215, 2503; ENST00000565154.6, PKM-214, 2004; ENST00000561609.5, PKM-204, 1568; ENST00000562997.5, PKM-206, 582; ENST00000566809.1, PKM-216, 560; ENST00000564178.5, PKM-209, 554; ENST00000567087.5, PKM-217, 550; ENST00000569050.1, PKM-221, 457; ENST00000567118.5, PKM-218, 2254; ENST00000569857.5, PKM-222, 1355; ENST00000564440.5, PKM-211, 3016; ENST00000565143.1, PKM-213, 2301; ENST00000563986.1, PKM-208, 825; ENST00000564276.1, PKM-210, 753; ENST00000563275.1, PKM-207, 699; ENST00000564993.1, PKM-212, 663; ENST00000570166.1, PKM-223, 626; ENST00000568743.1, PKM-220, 580; ENST00000562784.1, PKM-205, 529"	MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP	chr15:72199029-72231819[-]	"Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. In addition to its role in glycolysis, also regulates transcription. Stimulates POU5F1-mediated transcriptional activation. Promotes in a STAT1-dependent manner, the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages. Also acts as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs. Plays a general role in caspase independent cell death of tumor cells."	PDB: 1T5A; PDB: 1ZJH; PDB: 3BJF; PDB: 3BJT; PDB: 3G2G; PDB: 3GQY; PDB: 3GR4; PDB: 3H6O; PDB: 3ME3; PDB: 3SRD; PDB: 3SRF; PDB: 3SRH; PDB: 3U2Z; PDB: 4B2D; PDB: 4FXF; PDB: 4FXJ; PDB: 4G1N; PDB: 4JPG; PDB: 4QG6; PDB: 4QG8; PDB: 4QG9; PDB: 4QGC; PDB: 4RPP; PDB: 4WJ8; PDB: 4YJ5; PDB: 5X0I; PDB: 5X1V; PDB: 5X1W; PDB: 6B6U; PDB: 6GG3; PDB: 6GG4; PDB: 6GG5; PDB: 6GG6; PDB: 6JFB; PDB: 6NU1; PDB: 6NU5; PDB: 6NUB; PDB: 6TTF; PDB: 6TTH; PDB: 6TTI; PDB: 6TTQ; PDB: 6V74; PDB: 6V75; PDB: 6V76; PDB: 6WP3; PDB: 6WP4; PDB: 6WP5; PDB: 6WP6	HGNC:9021	KPYM_HUMAN	Reviewed	ENSG00000067225	.	.	.	.	.
Mol00106	Protein	Ribosomal protein S6 kinase alpha-5 (RPS6KA5)	S6K-alpha-5; 90 kDa ribosomal protein S6 kinase 5; Nuclear mitogen- and stress-activated protein kinase 1; RSK-like protein kinase; RSKL; MSK1	RPS6KA5	9252	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000614987.5, RPS6KA5-207, 26829; ENST00000536315.6, RPS6KA5-202, 2993; ENST00000418736.6, RPS6KA5-201, 2249; ENST00000648062.1, RPS6KA5-208, 4065; ENST00000556178.5, RPS6KA5-204, 2118; ENST00000554206.1, RPS6KA5-203, 1420; ENST00000556594.1, RPS6KA5-206, 596; ENST00000556304.1, RPS6KA5-205, 278"	MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMGVERPGVTNVARSAMMKDSPFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDENDNLEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNQNGYDESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFHAFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTLQPSNPADSNNPETLFQFSDSVA	chr14:90847861-91060641[-]	"Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury. Phosphorylates TRIM7 at 'Ser-107' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity."	PDB: 1VZO; PDB: 3KN5; PDB: 3KN6	HGNC:10434	KS6A5_HUMAN	Reviewed	ENSG00000100784	.	.	.	.	.
Mol00107	Protein	Prelamin-A/C (LMNA)	70 kDa lamin; Renal carcinoma antigen NY-REN-32; LMN1	LMNA	4000	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368300.9, LMNA-205, 3178; ENST00000361308.9, LMNA-201, 2465; ENST00000368301.6, LMNA-206, 2461; ENST00000675939.1, LMNA-232, 2401; ENST00000683032.1, LMNA-240, 2329; ENST00000368299.7, LMNA-204, 2253; ENST00000677389.1, LMNA-238, 2029; ENST00000448611.6, LMNA-207, 1943; ENST00000368297.5, LMNA-202, 1679; ENST00000675667.1, LMNA-229, 2826; ENST00000676385.2, LMNA-236, 2811; ENST00000682650.1, LMNA-239, 2288; ENST00000473598.6, LMNA-212, 2015; ENST00000504687.6, LMNA-219, 546; ENST00000675881.1, LMNA-231, 3218; ENST00000676434.1, LMNA-237, 3212; ENST00000684195.1, LMNA-242, 3081; ENST00000674720.1, LMNA-226, 3016; ENST00000674600.1, LMNA-225, 2576; ENST00000676208.1, LMNA-234, 2528; ENST00000674518.1, LMNA-224, 2391; ENST00000675455.1, LMNA-228, 2297; ENST00000675874.1, LMNA-230, 2239; ENST00000515459.5, LMNA-221, 757; ENST00000469565.6, LMNA-209, 591; ENST00000502751.5, LMNA-218, 570; ENST00000515711.1, LMNA-222, 569; ENST00000470199.2, LMNA-210, 551; ENST00000502357.5, LMNA-217, 537; ENST00000470835.1, LMNA-211, 472; ENST00000495341.5, LMNA-214, 394; ENST00000683773.1, LMNA-241, 288; ENST00000478063.2, LMNA-213, 285; ENST00000675989.1, LMNA-233, 3616; ENST00000676283.1, LMNA-235, 3342; ENST00000496738.6, LMNA-215, 2987; ENST00000675431.1, LMNA-227, 1514; ENST00000368298.2, LMNA-203, 1475; ENST00000498722.3, LMNA-216, 1031; ENST00000459904.2, LMNA-208, 919; ENST00000506981.1, LMNA-220, 576; ENST00000515824.1, LMNA-223, 393"	METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM	chr1:156082573-156140081[+]	"Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis."	PDB: 1IFR; PDB: 1IVT; PDB: 1X8Y; PDB: 2XV5; PDB: 2YPT; PDB: 3GEF; PDB: 3V4Q; PDB: 3V4W; PDB: 3V5B; PDB: 6GHD; PDB: 6JLB; PDB: 6RPR; PDB: 6SNZ; PDB: 6YF5; PDB: 6YJD; PDB: 7CRG	HGNC:6636	LMNA_HUMAN	Reviewed	ENSG00000160789	.	.	.	.	.
Mol00108	Protein	Melanoma-associated antigen 6 (MAGEA6)	Cancer/testis antigen 1.6; CT1.6; MAGE-6 antigen; MAGE3B antigen; MAGE6	MAGEA6	4105	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000329342.10, MAGEA6-201, 1682; ENST00000616035.4, MAGEA6-204, 1762; ENST00000457643.1, MAGEA6-203, 921; ENST00000412733.1, MAGEA6-202, 862"	MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQEAASSSSTLVEVTLGEVPAAESPDPPQSPQGASSLPTTMNYPLWSQSYEDSSNQEEEGPSTFPDLESEFQAALSRKVAKLVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASDSLQLVFGIELMEVDPIGHVYIFATCLGLSYDGLLGDNQIMPKTGFLIIILAIIAKEGDCAPEEKIWEELSVLEVFEGREDSIFGDPKKLLTQYFVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHMVKISGGPRISYPLLHEWALREGEE	chrX:152766136-152769716[-]	Activator of ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases that acts as a as repressor of autophagy. May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines.	.	HGNC:6804	MAGA6_HUMAN	Reviewed	ENSG00000197172	.	.	.	.	.
Mol00109	Protein	Melanoma-associated antigen 12 (MAGEA12)	Cancer/testis antigen 1.12; CT1.12; MAGE-12 antigen; MAGE12F antigen; MAGE12	MAGEA12	4111	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393869.8, MAGEA12-202, 1792; ENST00000357916.8, MAGEA12-201, 1664; ENST00000393900.4, MAGEA12-203, 1299"	MPLEQRSQHCKPEEGLEAQGEALGLVGAQAPATEEQETASSSSTLVEVTLREVPAAESPSPPHSPQGASTLPTTINYTLWSQSDEGSSNEEQEGPSTFPDLETSFQVALSRKMAELVHFLLLKYRAREPFTKAEMLGSVIRNFQDFFPVIFSKASEYLQLVFGIEVVEVVRIGHLYILVTCLGLSYDGLLGDNQIVPKTGLLIIVLAIIAKEGDCAPEEKIWEELSVLEASDGREDSVFAHPRKLLTQDLVQENYLEYRQVPGSDPACYEFLWGPRALVETSYVKVLHHLLKISGGPHISYPPLHEWAFREGEE	chrX:152733757-152737669[+]	"Not known, though may play a role tumor transformation or progression. In vitro promotes cell viability in melanoma cell lines."	.	HGNC:6799	MAGAC_HUMAN	Reviewed	ENSG00000213401	.	.	.	.	.
Mol00110	Protein	Induced myeloid leukemia cell differentiation protein Mcl-1 (MCL1)	Bcl-2-like protein 3; Bcl2-L-3; Bcl-2-related protein EAT/mcl1; mcl1/EAT; BCL2L3	MCL1	4170	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369026.3, MCL1-202, 3950; ENST00000620947.4, MCL1-205, 3626; ENST00000678770.1, MCL1-208, 1256; ENST00000307940.3, MCL1-201, 1110; ENST00000678610.1, MCL1-207, 3801; ENST00000617352.1, MCL1-204, 1036; ENST00000464132.2, MCL1-203, 4550; ENST00000676522.1, MCL1-206, 4524"	MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR	chr1:150560895-150579738[-]	"Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis."	PDB: 2KBW; PDB: 2MHS; PDB: 2NL9; PDB: 2NLA; PDB: 2PQK; PDB: 3D7V; PDB: 3IO9; PDB: 3KJ0; PDB: 3KJ1; PDB: 3KJ2; PDB: 3KZ0; PDB: 3MK8; PDB: 3PK1; PDB: 3TWU; PDB: 3WIX; PDB: 3WIY; PDB: 4BPI; PDB: 4BPJ; PDB: 4HW2; PDB: 4HW3; PDB: 4HW4; PDB: 4OQ5; PDB: 4OQ6; PDB: 4WGI; PDB: 4WMR; PDB: 4WMS; PDB: 4WMT; PDB: 4WMU; PDB: 4WMV; PDB: 4WMW; PDB: 4WMX; PDB: 4ZBF; PDB: 4ZBI; PDB: 5C3F; PDB: 5C6H; PDB: 5FC4; PDB: 5FDO; PDB: 5FDR; PDB: 5IEZ; PDB: 5IF4; PDB: 5JSB; PDB: 5KU9; PDB: 5LOF; PDB: 5MES; PDB: 5MEV; PDB: 5UUM; PDB: 5VKC; PDB: 5VX2; PDB: 5W89; PDB: 5W8F; PDB: 6B4L; PDB: 6B4U; PDB: 6BW2; PDB: 6BW8; PDB: 6FS0; PDB: 6FS1; PDB: 6FS2; PDB: 6MBD; PDB: 6MBE; PDB: 6NE5; PDB: 6O4U; PDB: 6O6F; PDB: 6O6G; PDB: 6OQB; PDB: 6OQC; PDB: 6OQD; PDB: 6OQN; PDB: 6OVC; PDB: 6P3P; PDB: 6QB3; PDB: 6QB4; PDB: 6QB6; PDB: 6QFC; PDB: 6QFI; PDB: 6QFM; PDB: 6QFQ; PDB: 6QGD; PDB: 6QXJ; PDB: 6QYK; PDB: 6QYL; PDB: 6QYN; PDB: 6QYO; PDB: 6QYP; PDB: 6QZ5; PDB: 6QZ6; PDB: 6QZ7; PDB: 6QZ8; PDB: 6QZB; PDB: 6STJ; PDB: 6U63; PDB: 6U64; PDB: 6U65; PDB: 6U67; PDB: 6U6F; PDB: 6UA3; PDB: 6UAB; PDB: 6UD2; PDB: 6UDI; PDB: 6UDT; PDB: 6UDU; PDB: 6UDV; PDB: 6UDX; PDB: 6UDY; PDB: 6VBX; PDB: 6YBG; PDB: 6YBJ; PDB: 6YBK; PDB: 6YBL; PDB: 6ZIE; PDB: 7NB4; PDB: 7NB7	HGNC:6943	MCL1_HUMAN	Reviewed	ENSG00000143384	.	.	.	.	.
Mol00111	Protein	Multidrug resistance protein 1 (ABCB1)	.	ABCB1	5243	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000622132.5, ABCB1-211, 5205; ENST00000265724.8, ABCB1-201, 4720; ENST00000543898.5, ABCB1-210, 4524; ENST00000416177.1, ABCB1-202, 461; ENST00000488737.6, ABCB1-207, 1864; ENST00000496821.5, ABCB1-209, 913; ENST00000475929.5, ABCB1-203, 787; ENST00000476862.1, ABCB1-204, 582; ENST00000483831.1, ABCB1-206, 642; ENST00000482527.1, ABCB1-205, 555; ENST00000491360.1, ABCB1-208, 539"	MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRSSLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTKRQ	chr7:87503017-87713323[-]	"Translocates drugs and phospholipids across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins. Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells."	PDB: 6C0V; PDB: 6FN1; PDB: 6FN4; PDB: 6QEX; PDB: 7A65; PDB: 7A69; PDB: 7A6C; PDB: 7A6E; PDB: 7A6F	HGNC:40	MDR1_HUMAN	Reviewed	ENSG00000085563	.	.	.	.	.
Mol00112	Protein	Myocyte-specific enhancer factor 2D (MEF2D)	.	MEF2D	4209	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000348159.9, MEF2D-201, 5912; ENST00000360595.7, MEF2D-202, 3194; ENST00000464356.6, MEF2D-203, 5598; ENST00000489057.1, MEF2D-205, 593; ENST00000475587.2, MEF2D-204, 1627; ENST00000493077.1, MEF2D-206, 526"	MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSTVPAPNFAMPVTVPVSNQSSLQFSNPSGSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGGDLNSANGACPSPVGNGYVSARASPGLLPVANGNSLNKVIPAKSPPPPTHSTQLGAPSRKPDLRVITSQAGKGLMHHLTEDHLDLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFSSMPTAYNTDYQLTSAELSSLPAFSSPGGLSLGNVTAWQQPQQPQQPQQPQPPQQQPPQPQQPQPQQPQQPQQPPQQQSHLVPVSLSNLIPGSPLPHVGAALTVTTHPHISIKSEPVSPSRERSPAPPPPAVFPAARPEPGDGLSSPAGGSYETGDRDDGRGDFGPTLGLLRPAPEPEAEGSAVKRMRLDTWTLK	chr1:156463727-156500779[-]	"Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. Plays a critical role in the regulation of neuronal apoptosis (By similarity)."	.	HGNC:6997	MEF2D_HUMAN	Reviewed	ENSG00000116604	.	.	.	.	.
Mol00113	Protein	Hepatocyte growth factor receptor (MET)	HGF receptor; HGF/SF receptor; Proto-oncogene c-Met; Scatter factor receptor; SF receptor; Tyrosine-protein kinase Met	MET	4233	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000397752.8, MET-202, 6822; ENST00000318493.11, MET-201, 6876; ENST00000436117.2, MET-204, 2295; ENST00000456159.1, MET-206, 767; ENST00000422097.1, MET-203, 688; ENST00000454623.1, MET-205, 475; ENST00000495962.1, MET-207, 741"	MKAPAVLAPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETPIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPDHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYVHAFESNNFIYFLTVQRETLDAQTFHTRIIRFCSINSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAAYVSKPGAQLARQIGASLNDDILFGVFAQSKPDSAEPMDRSAMCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARRDEYRTEFTTALQRVDLFMGQFSEVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHTLNQNGYTLVITGKKITKIPLNGLGCRHFQSCSQCLSAPPFVQCGWCHDKCVRSEECLSGTWTQQICLPAIYKVFPNSAPLEGGTRLTICGWDFGFRRNNKFDLKKTRVLLGNESCTLTLSESTMNTLKCTVGPAMNKHFNMSIIISNGHGTTQYSTFSYVDPVITSISPKYGPMAGGTLLTLTGNYLNSGNSRHISIGGKTCTLKSVSNSILECYTPAQTISTEFAVKLKIDLANRETSIFSYREDPIVYEIHPTKSFISGGSTITGVGKNLNSVSVPRMVINVHEAGRNFTVACQHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGILSKYFDLIYVHNPVFKPFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHLHSEAVLCTVPNDLLKLNSELNIEWKQAISSTVLGKVIVQPDQNFTGLIAGVVSISTALLLLLGFFLWLKKRKQIKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLTDMSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSEDNADDEVDTRPASFWETS	chr7:116672196-116798377[+]	"Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis (By similarity)."	PDB: 1FYR; PDB: 1R0P; PDB: 1R1W; PDB: 1SHY; PDB: 1SSL; PDB: 2G15; PDB: 2RFN; PDB: 2RFS; PDB: 2UZX; PDB: 2UZY; PDB: 2WD1; PDB: 2WGJ; PDB: 2WKM; PDB: 3A4P; PDB: 3BUX; PDB: 3C1X; PDB: 3CCN; PDB: 3CD8; PDB: 3CE3; PDB: 3CTH; PDB: 3CTJ; PDB: 3DKC; PDB: 3DKF; PDB: 3DKG; PDB: 3EFJ; PDB: 3EFK; PDB: 3F66; PDB: 3F82; PDB: 3I5N; PDB: 3L8V; PDB: 3LQ8; PDB: 3Q6U; PDB: 3Q6W; PDB: 3QTI; PDB: 3R7O; PDB: 3RHK; PDB: 3U6H; PDB: 3U6I; PDB: 3VW8; PDB: 3ZBX; PDB: 3ZC5; PDB: 3ZCL; PDB: 3ZXZ; PDB: 3ZZE; PDB: 4AOI; PDB: 4AP7; PDB: 4DEG; PDB: 4DEH; PDB: 4DEI; PDB: 4EEV; PDB: 4GG5; PDB: 4GG7; PDB: 4IWD; PDB: 4K3J; PDB: 4KNB; PDB: 4MXC; PDB: 4O3T; PDB: 4O3U; PDB: 4R1V; PDB: 4R1Y; PDB: 4XMO; PDB: 4XYF; PDB: 5DG5; PDB: 5EOB; PDB: 5EYC; PDB: 5EYD; PDB: 5HLW; PDB: 5HNI; PDB: 5HO6; PDB: 5HOA; PDB: 5HOR; PDB: 5HTI; PDB: 5LSP; PDB: 5T3Q; PDB: 5UAB; PDB: 5UAD; PDB: 5YA5; PDB: 6GCU; PDB: 6I04; PDB: 6SD9; PDB: 6SDC; PDB: 6SDD; PDB: 6SDE; PDB: 6UBW; PDB: 6WVZ; PDB: 7B3Q; PDB: 7B3T; PDB: 7B3V; PDB: 7B3W; PDB: 7B3Z; PDB: 7B40; PDB: 7B41; PDB: 7B42; PDB: 7B43; PDB: 7B44; PDB: 7MO7; PDB: 7MO8; PDB: 7MO9; PDB: 7MOA; PDB: 7MOB	HGNC:7029	MET_HUMAN	Reviewed	ENSG00000105976	.	.	.	.	.
Mol00114	Protein	Mitogen-activated protein kinase 1 (MAPK1)	MAP kinase 1; MAPK 1; ERT1; Extracellular signal-regulated kinase 2; ERK-2; MAP kinase isoform p42; p42-MAPK; Mitogen-activated protein kinase 2; MAP kinase 2; MAPK 2; ERK2; PRKM1; PRKM2	MAPK1	5594	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000215832.11, MAPK1-201, 5881; ENST00000398822.7, MAPK1-202, 1487; ENST00000544786.1, MAPK1-204, 951; ENST00000491588.1, MAPK1-203, 491"	MAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS	chr22:21759657-21867680[-]	"Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in response to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2 (By similarity)."	PDB: 1PME; PDB: 1TVO; PDB: 1WZY; PDB: 2OJG; PDB: 2OJI; PDB: 2OJJ; PDB: 2Y9Q; PDB: 3D42; PDB: 3D44; PDB: 3I5Z; PDB: 3I60; PDB: 3SA0; PDB: 3TEI; PDB: 3W55; PDB: 4FMQ; PDB: 4FUX; PDB: 4FUY; PDB: 4FV0; PDB: 4FV1; PDB: 4FV2; PDB: 4FV3; PDB: 4FV4; PDB: 4FV5; PDB: 4FV6; PDB: 4FV7; PDB: 4FV8; PDB: 4FV9; PDB: 4G6N; PDB: 4G6O; PDB: 4H3P; PDB: 4H3Q; PDB: 4IZ5; PDB: 4IZ7; PDB: 4IZA; PDB: 4N0S; PDB: 4NIF; PDB: 4O6E; PDB: 4QP1; PDB: 4QP2; PDB: 4QP3; PDB: 4QP4; PDB: 4QP6; PDB: 4QP7; PDB: 4QP8; PDB: 4QP9; PDB: 4QPA; PDB: 4QTA; PDB: 4QTE; PDB: 4XJ0; PDB: 4ZXT; PDB: 4ZZM; PDB: 4ZZN; PDB: 4ZZO; PDB: 5AX3; PDB: 5BUE; PDB: 5BUI; PDB: 5BUJ; PDB: 5BVD; PDB: 5BVE; PDB: 5BVF; PDB: 5K4I; PDB: 5LCJ; PDB: 5LCK; PDB: 5NGU; PDB: 5NHF; PDB: 5NHH; PDB: 5NHJ; PDB: 5NHL; PDB: 5NHO; PDB: 5NHP; PDB: 5NHV; PDB: 5V60; PDB: 5V61; PDB: 5V62; PDB: 5WP1; PDB: 6D5Y; PDB: 6DMG; PDB: 6G54; PDB: 6G8X; PDB: 6G91; PDB: 6G92; PDB: 6G93; PDB: 6G97; PDB: 6G9A; PDB: 6G9D; PDB: 6G9H; PDB: 6G9J; PDB: 6G9K; PDB: 6G9M; PDB: 6G9N; PDB: 6GDM; PDB: 6GDQ; PDB: 6GE0; PDB: 6GJB; PDB: 6GJD; PDB: 6NBS; PDB: 6OPG; PDB: 6OPH; PDB: 6OPI; PDB: 6Q7K; PDB: 6Q7S; PDB: 6Q7T; PDB: 6QA1; PDB: 6QA3; PDB: 6QA4; PDB: 6QAG; PDB: 6QAH; PDB: 6QAL; PDB: 6QAQ; PDB: 6QAW; PDB: 6RQ4; PDB: 6SLG; PDB: 7AUV; PDB: 7NQQ; PDB: 7NQW; PDB: 7NR3; PDB: 7NR5; PDB: 7NR8; PDB: 7NR9	HGNC:6871	MK01_HUMAN	Reviewed	ENSG00000100030	.	.	.	.	.
Mol00115	Protein	Autophagy-related protein LC3 B (MAP1LC3B)	Autophagy-related protein LC3 B; Autophagy-related ubiquitin-like modifier LC3 B; MAP1 light chain 3-like protein 2; MAP1A/MAP1B light chain 3 B; MAP1A/MAP1B LC3 B; Microtubule-associated protein 1 light chain 3 beta; MAP1ALC3	MAP1LC3B	81631	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000268607.10, MAP1LC3B-201, 2147; ENST00000650688.1, MAP1LC3B-206, 3134; ENST00000565788.1, MAP1LC3B-204, 625; ENST00000564844.1, MAP1LC3B-203, 3085; ENST00000570189.5, MAP1LC3B-205, 1259; ENST00000564638.1, MAP1LC3B-202, 735"	MPSEKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETFGMKLSV	chr16:87383953-87404779[+]	"Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria. While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. Upon nutrient stress, directly recruits cofactor JMY to the phagophore membrane surfaces and promotes JMY's actin nucleation activity and autophagosome biogenesis during autophagy."	PDB: 1V49; PDB: 2LUE; PDB: 2N9X; PDB: 2ZJD; PDB: 3VTU; PDB: 3VTV; PDB: 3VTW; PDB: 3WAO; PDB: 3X0W; PDB: 4WAA; PDB: 5D94; PDB: 5DCN; PDB: 5GMV; PDB: 5MS2; PDB: 5MS5; PDB: 5MS6; PDB: 5V4K; PDB: 5W9A; PDB: 5XAC; PDB: 5XAD; PDB: 5XAE; PDB: 6J04; PDB: 6LAN; PDB: 7ELG	HGNC:13352	MLP3B_HUMAN	Reviewed	ENSG00000140941	.	.	.	.	.
Mol00116	Protein	Macrophage metalloelastase (MMP12)	MME; Macrophage elastase; ME; hME; Matrix metalloproteinase-12; MMP-12; HME	MMP12	4321	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000571244.3, MMP12-201, 1822"	MKFLLILLLQATASGALPLNSSTSLEKNNVLFGERYLEKFYGLEINKLPVTKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMMHAPRCGVPDVHHFREMPGGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYGDPKENQRLPNPDNSEPALCDPNLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNLRPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNKYYYFFQGSNQFEYDFLLQRITKTLKSNSWFGC	chr11:102862736-102874982[-]	"May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3."	PDB: 1JIZ; PDB: 1JK3; PDB: 1OS2; PDB: 1OS9; PDB: 1RMZ; PDB: 1ROS; PDB: 1UTT; PDB: 1UTZ; PDB: 1Y93; PDB: 1YCM; PDB: 1Z3J; PDB: 2HU6; PDB: 2JXY; PDB: 2K2G; PDB: 2K9C; PDB: 2KRJ; PDB: 2MLR; PDB: 2MLS; PDB: 2N8R; PDB: 2OXU; PDB: 2OXW; PDB: 2OXZ; PDB: 2POJ; PDB: 2W0D; PDB: 2WO8; PDB: 2WO9; PDB: 2WOA; PDB: 2Z2D; PDB: 3BA0; PDB: 3EHX; PDB: 3EHY; PDB: 3F15; PDB: 3F16; PDB: 3F17; PDB: 3F18; PDB: 3F19; PDB: 3F1A; PDB: 3LIK; PDB: 3LIL; PDB: 3LIR; PDB: 3LJG; PDB: 3LK8; PDB: 3LKA; PDB: 3N2U; PDB: 3N2V; PDB: 3NX7; PDB: 3RTS; PDB: 3RTT; PDB: 3TS4; PDB: 3TSK; PDB: 3UVC; PDB: 4EFS; PDB: 4GQL; PDB: 4GR0; PDB: 4GR3; PDB: 4GR8; PDB: 4GUY; PDB: 4H30; PDB: 4H49; PDB: 4H76; PDB: 4H84; PDB: 4I03; PDB: 4IJO; PDB: 5CXA; PDB: 5CZM; PDB: 5D2B; PDB: 5D3C; PDB: 5I0L; PDB: 5I2Z; PDB: 5I3M; PDB: 5I43; PDB: 5I4O; PDB: 5L79; PDB: 5L7F; PDB: 5LAB; PDB: 5N5J; PDB: 5N5K; PDB: 6EKN; PDB: 6ELA; PDB: 6ENM; PDB: 6EOX; PDB: 6RD0; PDB: 6RLY; PDB: 7OVY	HGNC:7158	MMP12_HUMAN	Reviewed	ENSG00000262406	.	.	.	.	.
Mol00117	Protein	Collagenase 72 kDa type IV collagenase (MMP2)	72 kDa gelatinase; Gelatinase A; Matrix metalloproteinase-2; MMP-2; TBE-1; CLG4A	MMP2	4313	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000219070.9, MMP2-201, 3514; ENST00000570308.5, MMP2-208, 3235; ENST00000437642.6, MMP2-202, 2469; ENST00000543485.5, MMP2-203, 1978; ENST00000570283.1, MMP2-207, 755; ENST00000564864.5, MMP2-204, 736; ENST00000568715.5, MMP2-206, 566; ENST00000566564.1, MMP2-205, 443"	MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC	chr16:55389700-55506691[+]	"Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.; FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.; FUNCTION: [Isoform 2]: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways."	PDB: 1CK7; PDB: 1CXW; PDB: 1EAK; PDB: 1GEN; PDB: 1GXD; PDB: 1HOV; PDB: 1J7M; PDB: 1KS0; PDB: 1QIB; PDB: 1RTG; PDB: 3AYU	HGNC:7166	MMP2_HUMAN	Reviewed	ENSG00000087245	.	.	.	.	.
Mol00118	Protein	Matrix metalloproteinase-9 (MMP9)	MMP-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB; CLG4B	MMP9	4318	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000372330.3, MMP9-201, 2336"	MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED	chr20:46008908-46016561[+]	Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves NINJ1 to generate the Secreted ninjurin-1 form. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.	PDB: 1GKC; PDB: 1GKD; PDB: 1ITV; PDB: 1L6J; PDB: 2OVX; PDB: 2OVZ; PDB: 2OW0; PDB: 2OW1; PDB: 2OW2; PDB: 4H1Q; PDB: 4H2E; PDB: 4H3X; PDB: 4H82; PDB: 4HMA; PDB: 4JIJ; PDB: 4JQG; PDB: 4WZV; PDB: 4XCT; PDB: 5CUH; PDB: 5I12; PDB: 5TH6; PDB: 5TH9; PDB: 5UE3; PDB: 5UE4; PDB: 6ESM	HGNC:7176	MMP9_HUMAN	Reviewed	ENSG00000100985	.	.	.	.	.
Mol00119	Protein	Multidrug resistance-associated protein 1 (MRP1)	ATP-binding cassette sub-family C member 1; Glutathione-S-conjugate-translocating ATPase ABCC1; Leukotriene C(4) transporter; LTC4 transporter; MRP; MRP1	ABCC1	4363	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000399410.8, ABCC1-202, 6504; ENST00000399408.7, ABCC1-201, 6594; ENST00000572882.3, ABCC1-203, 6387; ENST00000677164.1, ABCC1-209, 6276; ENST00000678422.1, ABCC1-210, 6445; ENST00000676806.1, ABCC1-208, 3077; ENST00000679043.1, ABCC1-211, 1770; ENST00000576557.1, ABCC1-207, 542; ENST00000574224.2, ABCC1-204, 2616; ENST00000575422.5, ABCC1-206, 1198; ENST00000574761.1, ABCC1-205, 996"	MALRGFCSADGSDPLWDWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFYSFWERSRGIFLAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQVDLFRDITFYVYFSLLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPVLVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEALIVKSPQKEWNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLVALCTFAVYVTIDENNILDAQTAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGCQLEEPYYRSVIQACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGVSGPGKEAKQMENGMLVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEADKAQTGQVKLSVYWDYMKAIGLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMAKDAGLV	chr16:15949138-16143257[+]	"Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs by decreasing accumulation of drug in cells, and by mediating ATP- and GSH-dependent drug export. Hydrolyzes ATP with low efficiency. Catalyzes the export of sphingosine 1-phosphate from mast cells independently of their degranulation. Participates in inflammatory response by allowing export of leukotriene C4 from leukotriene C4-synthezing cells."	PDB: 2CBZ; PDB: 4C3Z	HGNC:51	MRP1_HUMAN	Reviewed	ENSG00000103222	.	.	.	.	.
Mol00120	Protein	ATP-binding cassette sub-family C2 (ABCC2)	Canalicular multidrug resistance protein; Canalicular multispecific organic anion transporter 1; Multidrug resistance-associated protein 2; CMOAT; CMOAT1; CMRP; MRP2	ABCC2	1244	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000647814.1, ABCC2-203, 5806; ENST00000648689.1, ABCC2-207, 1130; ENST00000648324.1, ABCC2-205, 1503; ENST00000649493.1, ABCC2-209, 1386; ENST00000649932.1, ABCC2-210, 1131; ENST00000648523.1, ABCC2-206, 1121; ENST00000647836.1, ABCC2-204, 1021; ENST00000496621.1, ABCC2-202, 525; ENST00000370434.1, ABCC2-201, 1714; ENST00000649459.1, ABCC2-208, 773"	MLEKFCNSTFWNSSFLDSPEADLPLCFEQTVLVWIPLGYLWLLAPWQLLHVYKSRTKRSSTTKLYLAKQVFVGFLLILAAIELALVLTEDSGQATVPAVRYTNPSLYLGTWLLVLLIQYSRQWCVQKNSWFLSLFWILSILCGTFQFQTLIRTLLQGDNSNLAYSCLFFISYGFQILILIFSAFSENNESSNNPSSIASFLSSITYSWYDSIILKGYKRPLTLEDVWEVDEEMKTKTLVSKFETHMKRELQKARRALQRRQEKSSQQNSGARLPGLNKNQSQSQDALVLEDVEKKKKKSGTKKDVPKSWLMKALFKTFYMVLLKSFLLKLVNDIFTFVSPQLLKLLISFASDRDTYLWIGYLCAILLFTAALIQSFCLQCYFQLCFKLGVKVRTAIMASVYKKALTLSNLARKEYTVGETVNLMSVDAQKLMDVTNFMHMLWSSVLQIVLSIFFLWRELGPSVLAGVGVMVLVIPINAILSTKSKTIQVKNMKNKDKRLKIMNEILSGIKILKYFAWEPSFRDQVQNLRKKELKNLLAFSQLQCVVIFVFQLTPVLVSVVTFSVYVLVDSNNILDAQKAFTSITLFNILRFPLSMLPMMISSMLQASVSTERLEKYLGGDDLDTSAIRHDCNFDKAMQFSEASFTWEHDSEATVRDVNLDIMAGQLVAVIGPVGSGKSSLISAMLGEMENVHGHITIKGTTAYVPQQSWIQNGTIKDNILFGTEFNEKRYQQVLEACALLPDLEMLPGGDLAEIGEKGINLSGGQKQRISLARATYQNLDIYLLDDPLSAVDAHVGKHIFNKVLGPNGLLKGKTRLLVTHSMHFLPQVDEIVVLGNGTIVEKGSYSALLAKKGEFAKNLKTFLRHTGPEEEATVHDGSEEEDDDYGLISSVEEIPEDAASITMRRENSFRRTLSRSSRSNGRHLKSLRNSLKTRNVNSLKEDEELVKGQKLIKKEFIETGKVKFSIYLEYLQAIGLFSIFFIILAFVMNSVAFIGSNLWLSAWTSDSKIFNSTDYPASQRDMRVGVYGALGLAQGIFVFIAHFWSAFGFVHASNILHKQLLNNILRAPMRFFDTTPTGRIVNRFAGDISTVDDTLPQSLRSWITCFLGIISTLVMICMATPVFTIIVIPLGIIYVSVQMFYVSTSRQLRRLDSVTRSPIYSHFSETVSGLPVIRAFEHQQRFLKHNEVRIDTNQKCVFSWITSNRWLAIRLELVGNLTVFFSALMMVIYRDTLSGDTVGFVLSNALNITQTLNWLVRMTSEIETNIVAVERITEYTKVENEAPWVTDKRPPPDWPSKGKIQFNNYQVRYRPELDLVLRGITCDIGSMEKIGVVGRTGAGKSSLTNCLFRILEAAGGQIIIDGVDIASIGLHDLREKLTIIPQDPILFSGSLRMNLDPFNNYSDEEIWKALELAHLKSFVASLQLGLSHEVTEAGGNLSIGQRQLLCLGRALLRKSKILVLDEATAAVDLETDNLIQTTIQNEFAHCTVITIAHRLHTIMDSDKVMVLDNGKIIECGSPEELLQIPGPFYFMAKEAGIENVNSTKF	chr10:99782640-99852594[+]	"ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports a wide variety of conjugated organic anions such as sulfate-, glucuronide- and glutathione (GSH)-conjugates of endo- and xenobiotics substrates. Mediates hepatobiliary excretion of mono- and bis-glucuronidated bilirubin molecules and therefore play an important role in bilirubin detoxification. Mediates also hepatobiliary excretion of others glucuronide conjugates such as 17beta-estradiol 17-glucosiduronic acid and leukotriene C4. Transports sulfated bile salt such as taurolithocholate sulfate. Transport various anticancer drugs, such as anthracycline, vinca alkaloid and methotrexate and HIV-drugs such as protease inhibitors. Confers resistance to several anti-cancer drugs including cisplatin, doxorubicin, epirubicin, methotrexate, etoposide and vincristine."	.	HGNC:53	MRP2_HUMAN	Reviewed	ENSG00000023839	.	.	.	.	.
Mol00121	Protein	Metastasis-associated protein MTA1 (MTA1)	.	MTA1	9112	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331320.12, MTA1-201, 2871; ENST00000435036.6, MTA1-207, 2888; ENST00000406191.5, MTA1-203, 2770; ENST00000405646.5, MTA1-202, 2709; ENST00000434050.5, MTA1-206, 2050; ENST00000438610.5, MTA1-208, 2144; ENST00000424723.5, MTA1-204, 904; ENST00000551236.5, MTA1-219, 461; ENST00000494981.1, MTA1-215, 509; ENST00000550551.5, MTA1-217, 416; ENST00000552286.5, MTA1-220, 1943; ENST00000469140.2, MTA1-209, 1666; ENST00000481012.5, MTA1-210, 987; ENST00000498644.5, MTA1-216, 871; ENST00000494026.1, MTA1-214, 852; ENST00000481206.1, MTA1-211, 842; ENST00000490198.5, MTA1-213, 814; ENST00000481635.1, MTA1-212, 700; ENST00000426567.5, MTA1-205, 568; ENST00000550808.5, MTA1-218, 561"	MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEEGEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED	chr14:105419820-105470729[+]	"Transcriptional coregulator which can act as both a transcriptional corepressor and coactivator. As a part of the histone-deacetylase multiprotein complex (NuRD), regulates transcription of its targets by modifying the acetylation status of the target chromatin and cofactor accessibility to the target DNA. In conjunction with other components of NuRD, acts as a transcriptional corepressor of BRCA1, ESR1, TFF1 and CDKN1A. Acts as a transcriptional coactivator of BCAS3, PAX5 and SUMO2, independent of the NuRD complex. Stimulates the expression of WNT1 by inhibiting the expression of its transcriptional corepressor SIX3. Regulates p53-dependent and -independent DNA repair processes following genotoxic stress. Regulates the stability and function of p53/TP53 by inhibiting its ubiquitination by COP1 and MDM2 thereby regulating the p53-dependent DNA repair. Plays an important role in tumorigenesis, tumor invasion, and metastasis. Involved in the epigenetic regulation of ESR1 expression in breast cancer in a TFAP2C, IFI16 and HDAC4/5/6-dependent manner. Plays a role in the regulation of the circadian clock and is essential for the generation and maintenance of circadian rhythms under constant light and for normal entrainment of behavior to light-dark (LD) cycles. Positively regulates the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of its own transcription and the transcription of CRY1. Regulates deacetylation of ARNTL/BMAL1 by regulating SIRT1 expression, resulting in derepressing CRY1-mediated transcription repression. Isoform Short binds to ESR1 and sequesters it in the cytoplasm and enhances its non-genomic responses. With TFCP2L1, promotes establishment and maintenance of pluripotency in embryonic stem cells (ESCs) and inhibits endoderm differentiation (By similarity)."	PDB: 4BKX; PDB: 4PBY; PDB: 4PBZ; PDB: 4PC0; PDB: 5FXY; PDB: 5ICN; PDB: 6G16; PDB: 6ZRC; PDB: 6ZRD; PDB: 7AO8; PDB: 7AO9; PDB: 7AOA	HGNC:7410	MTA1_HUMAN	Reviewed	ENSG00000182979	.	.	.	.	.
Mol00122	Protein	Serine/threonine-protein kinase mTOR (mTOR)	FK506-binding protein 12-rapamycin complex-associated protein 1; FKBP12-rapamycin complex-associated protein; Mammalian target of rapamycin; mTOR; Mechanistic target of rapamycin; Rapamycin and FKBP12 target 1; Rapamycin target protein 1; FRAP; FRAP1; FRAP2; RAFT1; RAPT1	MTOR	2475	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361445.9, MTOR-201, 8721; ENST00000376838.5, MTOR-202, 4017; ENST00000455339.1, MTOR-203, 694; ENST00000495435.1, MTOR-207, 2356; ENST00000490931.1, MTOR-206, 1111; ENST00000473471.5, MTOR-204, 862; ENST00000476768.1, MTOR-205, 610"	MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW	chr1:11106535-11262551[-]	"Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4. This also includes mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3: in the presence of nutrients, mediates phosphorylation of TFEB and TFE3, promoting their cytosolic retention and inactivation. Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. mTORC1 also negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions. Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1. mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422'. Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms. Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks. Phosphorylates SQSTM1, promoting interaction between SQSTM1 and KEAP1 and subsequent inactivation of the BCR(KEAP1) complex."	PDB: 1AUE; PDB: 1FAP; PDB: 1NSG; PDB: 2FAP; PDB: 2GAQ; PDB: 2NPU; PDB: 2RSE; PDB: 3FAP; PDB: 3JBZ; PDB: 4DRH; PDB: 4DRI; PDB: 4DRJ; PDB: 4FAP; PDB: 4JSN; PDB: 4JSP; PDB: 4JSV; PDB: 4JSX; PDB: 4JT5; PDB: 4JT6; PDB: 5FLC; PDB: 5GPG; PDB: 5H64; PDB: 5WBH; PDB: 5WBU; PDB: 5WBY; PDB: 5ZCS; PDB: 6BCU; PDB: 6BCX; PDB: 6M4U; PDB: 6M4W; PDB: 6SB0; PDB: 6SB2; PDB: 6ZWM; PDB: 6ZWO; PDB: 7OWG; PDB: 7PE7; PDB: 7PE8; PDB: 7PE9; PDB: 7PEA; PDB: 7PEB; PDB: 7PEC	HGNC:3942	MTOR_HUMAN	Reviewed	ENSG00000198793	.	.	.	.	.
Mol00123	Protein	Mucin-1 (MUC1)	.	MUC1	4582	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000620103.4, MUC1-225, 1811; ENST00000338684.9, MUC1-202, 1107; ENST00000610359.4, MUC1-221, 1101; ENST00000368392.7, MUC1-207, 1032; ENST00000615517.4, MUC1-224, 951; ENST00000368393.7, MUC1-208, 937; ENST00000337604.6, MUC1-201, 859; ENST00000368390.7, MUC1-206, 804; ENST00000368398.7, MUC1-210, 729; ENST00000343256.9, MUC1-204, 648; ENST00000368396.8, MUC1-209, 516; ENST00000457295.6, MUC1-212, 1161; ENST00000462317.5, MUC1-214, 1112; ENST00000438413.5, MUC1-211, 927; ENST00000485118.5, MUC1-219, 666; ENST00000471283.5, MUC1-218, 635; ENST00000368389.6, MUC1-205, 543; ENST00000342482.8, MUC1-203, 537; ENST00000462215.5, MUC1-213, 1189; ENST00000610468.4, MUC1-222, 1162; ENST00000614519.4, MUC1-223, 1093; ENST00000498431.5, MUC1-220, 667; ENST00000467134.5, MUC1-216, 619; ENST00000466913.1, MUC1-215, 177; ENST00000468978.2, MUC1-217, 899; ENST00000620770.1, MUC1-226, 572"	MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHSSVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL	chr1:155185824-155192916[-]	"The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack.; FUNCTION: The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. Modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, influences directly or indirectly the Ras/MAPK pathway. Promotes tumor progression. Regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity."	PDB: 1SM3; PDB: 2ACM; PDB: 2FO4; PDB: 5T6P; PDB: 5T78; PDB: 6FZQ; PDB: 6FZR; PDB: 6KX1; PDB: 6TGG	HGNC:7508	MUC1_HUMAN	Reviewed	ENSG00000185499	.	.	.	.	.
Mol00124	Protein	Myc proto-oncogene protein (MYC)	Class E basic helix-loop-helix protein 39; bHLHe39; Proto-oncogene c-Myc; Transcription factor p64; BHLHE39	MYC	4609	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000621592.8, MYC-206, 3721; ENST00000524013.2, MYC-205, 2150; ENST00000377970.6, MYC-202, 2351; ENST00000259523.10, MYC-201, 2042; ENST00000651626.1, MYC-209, 1957; ENST00000652288.1, MYC-210, 1877; ENST00000517291.2, MYC-203, 1023; ENST00000641036.1, MYC-207, 567; ENST00000641252.1, MYC-208, 345; ENST00000520751.1, MYC-204, 577"	MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA	chr8:127735434-127742951[+]	"Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release. Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform."	PDB: 1A93; PDB: 1EE4; PDB: 1MV0; PDB: 1NKP; PDB: 2A93; PDB: 2OR9; PDB: 4Y7R; PDB: 5I4Z; PDB: 5I50; PDB: 6C4U; PDB: 6E16; PDB: 6E24; PDB: 6G6J; PDB: 6G6K; PDB: 6G6L	HGNC:7553	MYC_HUMAN	Reviewed	ENSG00000136997	.	.	.	.	.
Mol00125	Protein	Netrin-1 (NTN1)	Epididymis tissue protein Li 131P; NTN1L	NTN1	9423	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000173229.7, NTN1-201, 5986; ENST00000436734.1, NTN1-202, 700"	MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGYYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKINMKKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA	chr17:9021510-9244000[+]	"Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Involved in dorsal root ganglion axon projection towards the spinal cord. It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in tumorigenesis by regulating apoptosis."	PDB: 4URT; PDB: 6FKQ; PDB: 7NDG; PDB: 7NE0; PDB: 7NE1	HGNC:8029	NET1_HUMAN	Reviewed	ENSG00000065320	.	.	.	.	.
Mol00126	Protein	NFE2-related factor 2 (NRF2)	NF-E2-related factor 2; NFE2-related factor 2; Nrf-2; HEBP1; Nuclear factor; erythroid derived 2; like 2; NRF2	NFE2L2	4780	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000397062.8, NFE2L2-201, 2446; ENST00000464747.5, NFE2L2-211, 2749; ENST00000397063.8, NFE2L2-202, 2651; ENST00000446151.6, NFE2L2-206, 2399; ENST00000423513.5, NFE2L2-204, 1382; ENST00000421929.5, NFE2L2-203, 979; ENST00000448782.5, NFE2L2-207, 975; ENST00000586532.5, NFE2L2-213, 942; ENST00000449627.1, NFE2L2-208, 909; ENST00000588123.1, NFE2L2-214, 814; ENST00000458603.1, NFE2L2-209, 455; ENST00000430047.1, NFE2L2-205, 451; ENST00000477534.1, NFE2L2-212, 930; ENST00000462023.1, NFE2L2-210, 521"	MMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN	chr2:177227595-177392697[-]	"Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles. In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex. In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the small Maf proteins and binding to ARE elements of cytoprotective target genes. The NFE2L2/NRF2 pathway is also activated in response to selective autophagy: autophagy promotes interaction between KEAP1 and SQSTM1/p62 and subsequent inactivation of the BCR(KEAP1) complex, leading to NFE2L2/NRF2 nuclear accumulation and expression of cytoprotective genes. May also be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region. Plays also an important role in the regulation of the innate immune response and antiviral cytosolic DNA sensing. It is a critical regulator of the innate immune response and survival during sepsis by maintaining redox homeostasis and restraint of the dysregulation of proinflammatory signaling pathways like MyD88-dependent and -independent and TNF-alpha signaling. Suppresses macrophage inflammatory response by blocking proinflammatory cytokine transcription and the induction of IL6. Binds to the proximity of proinflammatory genes in macrophages and inhibits RNA Pol II recruitment. The inhibition is independent of the NRF2-binding motif and reactive oxygen species level. Represses antiviral cytosolic DNA sensing by suppressing the expression of the adapter protein STING1 and decreasing responsiveness to STING1 agonists while increasing susceptibility to infection with DNA viruses. Once activated, limits the release of pro-inflammatory cytokines in response to human coronavirus SARS-CoV-2 infection and to virus-derived ligands through a mechanism that involves inhibition of IRF3 dimerization. Also inhibits both SARS-CoV-2 replication, as well as the replication of several other pathogenic viruses including Herpes Simplex Virus-1 and-2, Vaccinia virus, and Zika virus through a type I interferon (IFN)-independent mechanism."	.	HGNC:7782	NF2L2_HUMAN	Reviewed	ENSG00000116044	.	.	.	.	.
Mol00127	Protein	DNA-binding factor KBF1 (p105) (NFKB1)	DNA-binding factor KBF1; EBP-1; Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1	NFKB1	4790	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000226574.9, NFKB1-201, 4055; ENST00000505458.5, NFKB1-205, 3707; ENST00000394820.8, NFKB1-202, 3693; ENST00000600343.5, NFKB1-212, 4010; ENST00000507079.5, NFKB1-206, 965; ENST00000508584.1, NFKB1-207, 751; ENST00000511926.5, NFKB1-210, 609; ENST00000509165.1, NFKB1-208, 557; ENST00000652619.1, NFKB1-214, 4115; ENST00000652569.1, NFKB1-213, 3594; ENST00000510638.1, NFKB1-209, 628; ENST00000513803.5, NFKB1-211, 612; ENST00000504044.1, NFKB1-204, 580; ENST00000502367.1, NFKB1-203, 456"	MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI	chr4:102501331-102617302[+]	"NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105."	PDB: 1MDI; PDB: 1MDJ; PDB: 1MDK; PDB: 1NFI; PDB: 1SVC; PDB: 2DBF; PDB: 2O61; PDB: 3GUT; PDB: 7RG4; PDB: 7RG5	HGNC:7794	NFKB1_HUMAN	Reviewed	ENSG00000109320	.	.	.	.	.
Mol00128	Protein	Neurogenic locus notch homolog protein 1 (NOTCH1)	Notch 1; hN1; Translocation-associated notch protein TAN-1; NEXT; NICD; TAN1	NOTCH1	4851	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000651671.1, NOTCH1-204, 9568; ENST00000680668.1, NOTCH1-210, 9454; ENST00000680218.1, NOTCH1-209, 9448; ENST00000680133.1, NOTCH1-208, 9379; ENST00000680778.1, NOTCH1-211, 6995; ENST00000679595.1, NOTCH1-205, 9855; ENST00000681135.1, NOTCH1-214, 9649; ENST00000680924.1, NOTCH1-213, 9525; ENST00000681454.1, NOTCH1-216, 8966; ENST00000681298.1, NOTCH1-215, 6108; ENST00000679969.1, NOTCH1-206, 5891; ENST00000680003.1, NOTCH1-207, 5627; ENST00000645828.1, NOTCH1-202, 3719; ENST00000491649.2, NOTCH1-201, 799; ENST00000680882.1, NOTCH1-212, 567; ENST00000646957.2, NOTCH1-203, 506"	MPPLLAPLLCLALLPALAARGPRCSQPGETCLNGGKCEAANGTEACVCGGAFVGPRCQDPNPCLSTPCKNAGTCHVVDRRGVADYACSCALGFSGPLCLTPLDNACLTNPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFEASYICHCPPSFHGPTCRQDVNECGQKPGLCRHGGTCHNEVGSYRCVCRATHTGPNCERPYVPCSPSPCQNGGTCRPTGDVTHECACLPGFTGQNCEENIDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFHGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECSLGANPCEHAGKCINTLGSFECQCLQGYTGPRCEIDVNECVSNPCQNDATCLDQIGEFQCICMPGYEGVHCEVNTDECASSPCLHNGRCLDKINEFQCECPTGFTGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGSCKDGVATFTCLCRPGYTGHHCETNINECSSQPCRHGGTCQDRDNAYLCFCLKGTTGPNCEINLDDCASSPCDSGTCLDKIDGYECACEPGYTGSMCNINIDECAGNPCHNGGTCEDGINGFTCRCPEGYHDPTCLSEVNECNSNPCVHGACRDSLNGYKCDCDPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCLLPYTGATCEVVLAPCAPSPCRNGGECRQSEDYESFSCVCPTGWQGQTCEVDINECVLSPCRHGASCQNTHGGYRCHCQAGYSGRNCETDIDDCRPNPCHNGGSCTDGINTAFCDCLPGFRGTFCEEDINECASDPCRNGANCTDCVDSYTCTCPAGFSGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQHDVNECDSQPCLHGGTCQDGCGSYRCTCPQGYTGPNCQNLVHWCDSSPCKNGGKCWQTHTQYRCECPSGWTGLYCDVPSVSCEVAAQRQGVDVARLCQHGGLCVDAGNTHHCRCQAGYTGSYCEDLVDECSPSPCQNGATCTDYLGGYSCKCVAGYHGVNCSEEIDECLSHPCQNGGTCLDLPNTYKCSCPRGTQGVHCEINVDDCNPPVDPVSRSPKCFNNGTCVDQVGGYSCTCPPGFVGERCEGDVNECLSNPCDARGTQNCVQRVNDFHCECRAGHTGRRCESVINGCKGKPCKNGGTCAVASNTARGFICKCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGPFTGPECQFPASSPCLGGNPCYNQGTCEPTSESPFYRCLCPAKFNGLLCHILDYSFGGGAGRDIPPPLIEEACELPECQEDAGNKVCSLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSAGCLFDGFDCQRAEGQCNPLYDQYCKDHFSDGHCDQGCNSAECEWDGLDCAEHVPERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYGREEELRKHPIKRAAEGWAAPDALLGQVKASLLPGGSEGGRRRRELDPMDVRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVLPDLDDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGAPLGGTPTLSPPLCSPNGYLGSLKPGVQGKKVRKPSSKGLACGSKEAKDLKARRKKSQDGKGCLLDSSGMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSVPLNHLPGMPDTHLGIGHLNVAAKPEMAALGGGGRLAFETGPPRLSHLPVASGTSTVLGSSSGGALNFTVGGSTSLNGQCEWLSRLQSGMVPNQYNPLRGSVAPGPLSTQAPSLQHGMVGPLHSSLAASALSQMMSYQGLPSTRLATQPHLVQTQQVQPQNLQMQQQNLQPANIQQQQSLQPPPPPPQPHLGVSSAASGHLGRSFLSGEPSQADVQPLGPSSLAVHTILPQESPALPTSLPSSLVPPVTAAQFLTPPSQHSYSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNVSDWSEGVSSPPTSMQSQIARIPEAFK	chr9:136494433-136546048[-]	"Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO)."	PDB: 1PB5; PDB: 1TOZ; PDB: 1YYH; PDB: 2F8X; PDB: 2F8Y; PDB: 2HE0; PDB: 2VJ3; PDB: 3ETO; PDB: 3I08; PDB: 3L95; PDB: 3NBN; PDB: 3V79; PDB: 4CUD; PDB: 4CUE; PDB: 4CUF; PDB: 4D0E; PDB: 4D0F; PDB: 5FM9; PDB: 5FMA; PDB: 5KZO; PDB: 5L0R; PDB: 5UB5; PDB: 6IDF; PDB: 6PY8	HGNC:7881	NOTC1_HUMAN	Reviewed	ENSG00000148400	.	.	.	.	.
Mol00129	Protein	Nuclear receptor subfamily 1 group I3 (NR1I3)	Constitutive activator of retinoid response; Constitutive active response; Constitutive androstane receptor; CAR; Orphan nuclear receptor MB67; CAR	NR1I3	9970	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367983.9, NR1I3-205, 1371; ENST00000367980.6, NR1I3-202, 1403; ENST00000367982.8, NR1I3-204, 1322; ENST00000428574.6, NR1I3-209, 1117; ENST00000442691.6, NR1I3-211, 1114; ENST00000367981.7, NR1I3-203, 1076; ENST00000367985.7, NR1I3-207, 1074; ENST00000367979.6, NR1I3-201, 1074; ENST00000511676.5, NR1I3-228, 1061; ENST00000367984.8, NR1I3-206, 1059; ENST00000412844.6, NR1I3-208, 989; ENST00000505005.5, NR1I3-220, 985; ENST00000508740.5, NR1I3-226, 977; ENST00000437437.6, NR1I3-210, 973; ENST00000504010.5, NR1I3-219, 944; ENST00000512372.5, NR1I3-232, 861; ENST00000506209.5, NR1I3-223, 1441; ENST00000628566.2, NR1I3-235, 1201; ENST00000515621.5, NR1I3-234, 1130; ENST00000515452.1, NR1I3-233, 1093; ENST00000502985.5, NR1I3-217, 774; ENST00000508387.5, NR1I3-225, 634; ENST00000511944.5, NR1I3-230, 620; ENST00000511748.5, NR1I3-229, 480; ENST00000506018.5, NR1I3-222, 1380; ENST00000502848.5, NR1I3-216, 914; ENST00000512340.5, NR1I3-231, 891; ENST00000510951.5, NR1I3-227, 774; ENST00000507215.5, NR1I3-224, 620; ENST00000479324.1, NR1I3-213, 764; ENST00000488651.5, NR1I3-214, 580; ENST00000503547.1, NR1I3-218, 535; ENST00000464422.1, NR1I3-212, 480; ENST00000491193.1, NR1I3-215, 1435; ENST00000505944.5, NR1I3-221, 865"	MASREDELRNCVVCGDQATGYHFNALTCEGCKGFFRRTVSKSIGPTCPFAGSCEVSKTQRRHCPACRLQKCLDAGMRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVSPTVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRRPRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS	chr1:161229666-161238244[-]	Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element.	PDB: 1XV9; PDB: 1XVP	HGNC:7969	NR1I3_HUMAN	Reviewed	ENSG00000143257	.	.	.	.	.
Mol00130	Protein	Nuclear receptor subfamily 2 group C2 (NR2C2)	Orphan nuclear receptor TAK1; Orphan nuclear receptor TR4; Testicular receptor 4; TAK1; TR4	NR2C2	7182	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000425241.6, NR2C2-206, 8419; ENST00000617312.4, NR2C2-213, 8113; ENST00000323373.10, NR2C2-201, 2406; ENST00000393102.7, NR2C2-202, 1937; ENST00000406272.6, NR2C2-203, 1791; ENST00000437120.5, NR2C2-208, 739; ENST00000439011.5, NR2C2-209, 698; ENST00000413118.5, NR2C2-204, 564; ENST00000413194.1, NR2C2-205, 551; ENST00000435454.5, NR2C2-207, 495; ENST00000478572.1, NR2C2-211, 2767; ENST00000475707.5, NR2C2-210, 3308; ENST00000495282.1, NR2C2-212, 534"	MTSPSPRIQIISTDSAVASPQRIQIVTDQQTGQKIQIVTAVDASGSPKQQFILTSPDGAGTGKVILASPETSSAKQLIFTTSDNLVPGRIQIVTDSASVERLLGKTDVQRPQVVEYCVVCGDKASGRHYGAVSCEGCKGFFKRSVRKNLTYSCRSNQDCIINKHHRNRCQFCRLKKCLEMGMKMESVQSERKPFDVQREKPSNCAASTEKIYIRKDLRSPLIATPTFVADKDGARQTGLLDPGMLVNIQQPLIREDGTVLLATDSKAETSQGALGTLANVVTSLANLSESLNNGDTSEIQPEDQSASEITRAFDTLAKALNTTDSSSSPSLADGIDTSGGGSIHVISRDQSTPIIEVEGPLLSDTHVTFKLTMPSPMPEYLNVHYICESASRLLFLSMHWARSIPAFQALGQDCNTSLVRACWNELFTLGLAQCAQVMSLSTILAAIVNHLQNSIQEDKLSGDRIKQVMEHIWKLQEFCNSMAKLDIDGYEYAYLKAIVLFSPDHPGLTSTSQIEKFQEKAQMELQDYVQKTYSEDTYRLARILVRLPALRLMSSNITEELFFTGLIGNVSIDSIIPYILKMETAEYNGQITGASL	chr3:14947583-15053600[+]	"Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear receptor signaling pathways such as retinoic acid receptor, retinoid X, vitamin D3 receptor, thyroid hormone receptor and estrogen receptor pathways. May regulate gene expression during the late phase of spermatogenesis. Together with NR2C1, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription including that of GATA1. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Plays a fundamental role in early embryonic development and embryonic stem cells. Required for normal spermatogenesis and cerebellum development. Appears to be important for neurodevelopmentally regulated behavior (By similarity). Activates transcriptional activity of LHCG. Antagonist of PPARA-mediated transactivation."	PDB: 3P0U	HGNC:7972	NR2C2_HUMAN	Reviewed	ENSG00000177463	.	.	.	.	.
Mol00131	Protein	P2Y purinoceptor 1 (P2RY1)	P2Y1; ADP receptor; Purinergic receptor	P2RY1	5028	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305097.6, P2RY1-201, 6309"	MTEVLWPAVPNGTDAAFLAGPGSSWGNSTVASTAAVSSSFKCALTKTGFQFYYLPAVYILVFIIGFLGNSVAIWMFVFHMKPWSGISVYMFNLALADFLYVLTLPALIFYYFNKTDWIFGDAMCKLQRFIFHVNLYGSILFLTCISAHRYSGVVYPLKSLGRLKKKNAICISVLVWLIVVVAISPILFYSGTGVRKNKTITCYDTTSDEYLRSYFIYSMCTTVAMFCVPLVLILGCYGLIVRALIYKDLDNSPLRRKSIYLVIIVLTVFAVSYIPFHVMKTMNLRARLDFQTPAMCAFNDRVYATYQVTRGLASLNSCVDPILYFLAGDTFRRRLSRATRKASRRSEANLQSKSEDMTLNILPEFKQNGDTSL	chr3:152835131-152841439[+]	"Receptor for extracellular adenine nucleotides such as ADP. In platelets, binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and ultimately platelet aggregation."	PDB: 4XNV; PDB: 4XNW	HGNC:8539	P2RY1_HUMAN	Reviewed	ENSG00000169860	.	.	.	.	.
Mol00132	Protein	Serine/threonine-protein kinase PAK 1 (PAK1)	Alpha-PAK; p21-activated kinase 1; PAK-1; p65-PAK	PAK1	5058	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356341.8, PAK1-202, 3459; ENST00000278568.8, PAK1-201, 2543; ENST00000530617.5, PAK1-215, 3001; ENST00000528203.5, PAK1-210, 1878; ENST00000533285.1, PAK1-218, 878; ENST00000528592.5, PAK1-211, 581; ENST00000529248.5, PAK1-213, 576; ENST00000524847.5, PAK1-203, 559; ENST00000526968.1, PAK1-207, 502; ENST00000528633.1, PAK1-212, 450; ENST00000527457.5, PAK1-208, 1047; ENST00000527535.5, PAK1-209, 576; ENST00000525542.5, PAK1-204, 863; ENST00000532991.5, PAK1-217, 806; ENST00000533568.5, PAK1-220, 762; ENST00000526103.1, PAK1-205, 753; ENST00000530358.1, PAK1-214, 735; ENST00000533468.5, PAK1-219, 503; ENST00000526910.1, PAK1-206, 348; ENST00000532711.1, PAK1-216, 308"	MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH	chr11:77322017-77474635[-]	"Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion. In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling. In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization. In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC). Along with GIT1, positively regulates microtubule nucleation during interphase."	PDB: 1F3M; PDB: 1YHV; PDB: 1YHW; PDB: 1ZSG; PDB: 2HY8; PDB: 2QME; PDB: 3DVP; PDB: 3FXZ; PDB: 3FY0; PDB: 3Q4Z; PDB: 3Q52; PDB: 3Q53; PDB: 4DAW; PDB: 4EQC; PDB: 4O0R; PDB: 4O0T; PDB: 4P90; PDB: 4ZJI; PDB: 4ZJJ; PDB: 4ZLO; PDB: 4ZY4; PDB: 4ZY5; PDB: 4ZY6; PDB: 5DEW; PDB: 5DEY; PDB: 5DFP; PDB: 5IME; PDB: 5KBQ; PDB: 5KBR; PDB: 6B16	HGNC:8590	PAK1_HUMAN	Reviewed	ENSG00000149269	.	.	.	.	.
Mol00133	Protein	Poly[ADP-ribose] synthase 1 (PARP1)	PARP-1; ADP-ribosyltransferase diphtheria toxin-like 1; ARTD1; DNA ADP-ribosyltransferase PARP1; NAD(+) ADP-ribosyltransferase 1; ADPRT 1; Poly[ADP-ribose] synthase 1; Protein poly-ADP-ribosyltransferase PARP1; ADPRT; PPOL	PARP1	142	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000366794.10, PARP1-203, 3978; ENST00000677203.1, PARP1-216, 3850; ENST00000678560.1, PARP1-224, 4255; ENST00000677091.1, PARP1-214, 3768; ENST00000678144.1, PARP1-221, 3719; ENST00000678226.1, PARP1-222, 3274; ENST00000677189.1, PARP1-215, 2348; ENST00000677985.1, PARP1-220, 2285; ENST00000676481.1, PARP1-210, 1371; ENST00000366792.3, PARP1-202, 553; ENST00000469663.1, PARP1-206, 542; ENST00000676685.1, PARP1-212, 6210; ENST00000677374.1, PARP1-217, 5697; ENST00000498787.2, PARP1-209, 5629; ENST00000678781.1, PARP1-225, 5430; ENST00000679276.1, PARP1-226, 4918; ENST00000676709.1, PARP1-213, 4764; ENST00000677884.1, PARP1-219, 4620; ENST00000677815.1, PARP1-218, 3770; ENST00000676565.1, PARP1-211, 3577; ENST00000366790.4, PARP1-201, 3358; ENST00000490921.5, PARP1-207, 3165; ENST00000678288.1, PARP1-223, 2420; ENST00000463968.5, PARP1-204, 830; ENST00000468608.1, PARP1-205, 438; ENST00000491816.1, PARP1-208, 416"	MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW	chr1:226360210-226408154[-]	"Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and EEF1A1. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming."	PDB: 1UK0; PDB: 1UK1; PDB: 1WOK; PDB: 2COK; PDB: 2CR9; PDB: 2CS2; PDB: 2DMJ; PDB: 2JVN; PDB: 2L30; PDB: 2L31; PDB: 2N8A; PDB: 2RCW; PDB: 2RD6; PDB: 2RIQ; PDB: 3GJW; PDB: 3GN7; PDB: 3L3L; PDB: 3L3M; PDB: 3OD8; PDB: 3ODA; PDB: 3ODC; PDB: 3ODE; PDB: 4AV1; PDB: 4DQY; PDB: 4GV7; PDB: 4HHY; PDB: 4HHZ; PDB: 4L6S; PDB: 4OPX; PDB: 4OQA; PDB: 4OQB; PDB: 4PJT; PDB: 4R5W; PDB: 4R6E; PDB: 4RV6; PDB: 4UND; PDB: 4UXB; PDB: 4XHU; PDB: 4ZZZ; PDB: 5A00; PDB: 5DS3; PDB: 5HA9; PDB: 5KPN; PDB: 5KPO; PDB: 5KPP; PDB: 5KPQ; PDB: 5WRQ; PDB: 5WRY; PDB: 5WRZ; PDB: 5WS0; PDB: 5WS1; PDB: 5WTC; PDB: 5XSR; PDB: 5XST; PDB: 5XSU; PDB: 6BHV; PDB: 6GHK; PDB: 6M3I; PDB: 6NRF; PDB: 6NRG; PDB: 6NRH; PDB: 6NRI; PDB: 6NRJ; PDB: 6NTU; PDB: 6VKK; PDB: 6VKO; PDB: 6VKQ; PDB: 6XVW; PDB: 7AAA; PDB: 7AAB; PDB: 7AAC; PDB: 7AAD; PDB: 7CMW; PDB: 7KK2; PDB: 7KK3; PDB: 7KK4; PDB: 7KK5; PDB: 7KK6; PDB: 7ONR; PDB: 7ONS; PDB: 7ONT	HGNC:270	PARP1_HUMAN	Reviewed	ENSG00000143799	.	.	.	.	.
Mol00134	Protein	Programmed cell death 1 ligand 1 (PD-L1)	.	CD274	29126	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000381577.4, CD274-202, 3634; ENST00000381573.8, CD274-201, 3343; ENST00000498261.1, CD274-205, 704; ENST00000492923.1, CD274-204, 601; ENST00000474218.1, CD274-203, 442"	MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET	chr9:5450503-5470566[+]	"Plays a critical role in induction and maintenance of immune tolerance to self. As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response. Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10)."	PDB: 3BIK; PDB: 3BIS; PDB: 3FN3; PDB: 3SBW; PDB: 4Z18; PDB: 4ZQK; PDB: 5C3T; PDB: 5GGT; PDB: 5GRJ; PDB: 5IUS; PDB: 5J89; PDB: 5J8O; PDB: 5JDR; PDB: 5JDS; PDB: 5N2D; PDB: 5N2F; PDB: 5NIU; PDB: 5O45; PDB: 5O4Y; PDB: 5X8L; PDB: 5X8M; PDB: 5XJ4; PDB: 5XXY; PDB: 6L8R; PDB: 6NM7; PDB: 6NM8; PDB: 6NNV; PDB: 6NOJ; PDB: 6NOS; PDB: 6NP9; PDB: 6PV9; PDB: 6R3K; PDB: 6RPG; PDB: 6VQN; PDB: 6YCR; PDB: 7BEA; PDB: 7C88; PDB: 7CZD; PDB: 7NLD; PDB: 7OUN	HGNC:17635	PD1L1_HUMAN	Reviewed	ENSG00000120217	.	.	.	.	.
Mol00135	Protein	phosphoinositide-3-dependent protein kinase 1 (PDPK1)	hPDK1; PDK1	PDPK1	5170	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000342085.9, PDPK1-202, 7184; ENST00000268673.11, PDPK1-201, 4728; ENST00000441549.7, PDPK1-204, 1729; ENST00000389224.7, PDPK1-203, 2416; ENST00000461815.1, PDPK1-206, 611; ENST00000566659.1, PDPK1-215, 451; ENST00000474706.6, PDPK1-210, 699; ENST00000492021.6, PDPK1-213, 552; ENST00000478708.2, PDPK1-211, 445; ENST00000471311.1, PDPK1-209, 621; ENST00000561962.1, PDPK1-214, 570; ENST00000460496.1, PDPK1-205, 569; ENST00000462923.2, PDPK1-207, 550; ENST00000464702.6, PDPK1-208, 511; ENST00000569721.1, PDPK1-216, 330; ENST00000491073.5, PDPK1-212, 2387; ENST00000570136.5, PDPK1-217, 1125"	MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ	chr16:2537979-2603188[+]	"Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive."	PDB: 1H1W; PDB: 1OKY; PDB: 1OKZ; PDB: 1UU3; PDB: 1UU7; PDB: 1UU8; PDB: 1UU9; PDB: 1UVR; PDB: 1W1D; PDB: 1W1G; PDB: 1W1H; PDB: 1Z5M; PDB: 2BIY; PDB: 2PE0; PDB: 2PE1; PDB: 2PE2; PDB: 2R7B; PDB: 2VKI; PDB: 2XCH; PDB: 2XCK; PDB: 3H9O; PDB: 3HRC; PDB: 3HRF; PDB: 3ION; PDB: 3IOP; PDB: 3NAX; PDB: 3NAY; PDB: 3NUN; PDB: 3NUS; PDB: 3NUU; PDB: 3NUY; PDB: 3ORX; PDB: 3ORZ; PDB: 3OTU; PDB: 3PWY; PDB: 3QC4; PDB: 3QCQ; PDB: 3QCS; PDB: 3QCX; PDB: 3QCY; PDB: 3QD0; PDB: 3QD3; PDB: 3QD4; PDB: 3RCJ; PDB: 3RWP; PDB: 3RWQ; PDB: 3SC1; PDB: 4A06; PDB: 4A07; PDB: 4AW0; PDB: 4AW1; PDB: 4CT1; PDB: 4CT2; PDB: 4RQK; PDB: 4RQV; PDB: 4RRV; PDB: 4XX9; PDB: 5ACK; PDB: 5HKM; PDB: 5HNG; PDB: 5HO7; PDB: 5HO8; PDB: 5LVL; PDB: 5LVM; PDB: 5LVN; PDB: 5LVO; PDB: 5LVP; PDB: 5MRD; PDB: 6WJQ	HGNC:8816	PDPK1_HUMAN	Reviewed	ENSG00000140992	.	.	.	.	.
Mol00136	Protein	Astrocytic phosphoprotein PEA-15 (PEA15)	15 kDa phosphoprotein enriched in astrocytes; Phosphoprotein enriched in diabetes; PED	PEA15	8682	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000360472.9, PEA15-201, 2420; ENST00000368076.1, PEA15-202, 2694; ENST00000368077.5, PEA15-203, 1021; ENST00000488858.1, PEA15-204, 654"	MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEDELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA	chr1:160205380-160215376[+]	Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface.	PDB: 4IZ5; PDB: 4IZA; PDB: 6P6B; PDB: 6P6C	HGNC:8822	PEA15_HUMAN	Reviewed	ENSG00000162734	.	.	.	.	.
Mol00137	Protein	Platelet-derived growth factor receptor alpha (PDGFRA)	.	PDGFRA	5156	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000257290.10, PDGFRA-201, 6378; ENST00000508170.5, PDGFRA-206, 2202; ENST00000504461.5, PDGFRA-204, 771; ENST00000503856.5, PDGFRA-203, 586; ENST00000512143.1, PDGFRA-209, 580; ENST00000512522.1, PDGFRA-210, 573; ENST00000509490.5, PDGFRA-208, 2991; ENST00000509092.5, PDGFRA-207, 2417; ENST00000507536.1, PDGFRA-205, 1146; ENST00000461294.2, PDGFRA-202, 480"	MGTSHPAFLVLGCLLTGLSLILCQLSLPSILPNENEKVVQLNSSFSLRCFGESEVSWQYPMSEEESSDVEIRNEENNSGLFVTVLEVSSASAAHTGLYTCYYNHTQTEENELEGRHIYIYVPDPDVAFVPLGMTDYLVIVEDDDSAIIPCRTTDPETPVTLHNSEGVVPASYDSRQGFNGTFTVGPYICEATVKGKKFQTIPFNVYALKATSELDLEMEALKTVYKSGETIVVTCAVFNNEVVDLQWTYPGEVKGKGITMLEEIKVPSIKLVYTLTVPEATVKDSGDYECAARQATREVKEMKKVTISVHEKGFIEIKPTFSQLEAVNLHEVKHFVVEVRAYPPPRISWLKNNLTLIENLTEITTDVEKIQEIRYRSKLKLIRAKEEDSGHYTIVAQNEDAVKSYTFELLTQVPSSILDLVDDHHGSTGGQTVRCTAEGTPLPDIEWMICKDIKKCNNETSWTILANNVSNIITEIHSRDRSTVEGRVTFAKVEETIAVRCLAKNLLGAENRELKLVAPTLRSELTVAAAVLVLLVIVIISLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRVLGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFLSHHPEKPKKELDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDNSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVKCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL	chr4:54229280-54298245[+]	"Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor."	PDB: 1GQ5; PDB: 5GRN; PDB: 5K5X; PDB: 6A32; PDB: 6JOI; PDB: 6JOJ; PDB: 6JOK; PDB: 6JOL; PDB: 7LBF	HGNC:8803	PGFRA_HUMAN	Reviewed	ENSG00000134853	.	.	.	.	.
Mol00138	Protein	Platelet-derived growth factor receptor beta (PDGFRB)	.	PDGFRB	5159	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261799.9, PDGFRB-201, 5700; ENST00000517488.1, PDGFRB-202, 822; ENST00000517957.1, PDGFRB-204, 568; ENST00000520579.5, PDGFRB-207, 3860; ENST00000523456.1, PDGFRB-211, 1023; ENST00000519575.5, PDGFRB-205, 712; ENST00000517660.1, PDGFRB-203, 611; ENST00000520851.1, PDGFRB-208, 406; ENST00000521723.1, PDGFRB-209, 400; ENST00000520229.1, PDGFRB-206, 738; ENST00000522466.1, PDGFRB-210, 296"	MRLPGAMPALALKGELLLLSLLLLLEPQISQGLVVTPPGPELVLNVSSTFVLTCSGSAPVVWERMSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQVSSINVSVNAVQTVVRQGENITLMCIVIGNEVVNFEWTYPRKESGRLVEPVTDFLLDMPYHIRSILHIPSAELEDSGTYTCNVTESVNDHQDEKAINITVVESGYVRLLGEVGTLQFAELHRSRTLQVVFEAYPPPTVLWFKDNRTLGDSSAGEIALSTRNVSETRYVSELTLVRVKVAEAGHYTMRAFHEDAEVQLSFQLQINVPVRVLELSESHPDSGEQTVRCRGRGMPQPNIIWSACRDLKRCPRELPPTLLGNSSEEESQLETNVTYWEEEQEFEVVSTLRLQHVDRPLSVRCTLRNAVGQDTQEVIVVPHSLPFKVVVISAILALVVLTIISLIILIMLWQKKPRYEIRWKVIESVSSDGHEYIYVDPMQLPYDSTWELPRDQLVLGRTLGSGAFGQVVEATAHGLSHSQATMKVAVKMLKSTARSSEKQALMSELKIMSHLGPHLNVVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNKHTFLQHHSDKRRPPSAELYSNALPVGLPLPSHVSLTGESDGGYMDMSKDESVDYVPMLDMKGDVKYADIESSNYMAPYDNYVPSAPERTCRATLINESPVLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNSLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFYNAIKRGYRMAQPAHASDEIYEIMQKCWEEKFEIRPPFSQLVLLLERLLGEGYKKKYQQVDEEFLRSDHPAILRSQARLPGFHGLRSPLDTSSVLYTAVQPNEGDNDYIIPLPDPKPEVADEGPLEGSPSLASSTLNEVNTSSTISCDSPLEPQDEPEPEPQLELQVEPEPELEQLPDSGCPAPRAEAEDSFL	chr5:150113839-150155872[-]	"Tyrosine-protein kinase that acts as cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor."	PDB: 1GQ5; PDB: 1H9O; PDB: 1SHA; PDB: 2IUI; PDB: 2L6W; PDB: 2PLD; PDB: 2PLE; PDB: 3MJG	HGNC:8804	PGFRB_HUMAN	Reviewed	ENSG00000113721	.	.	.	.	.
Mol00139	Protein	PH domain leucine-rich repeat-containing protein phosphatase 1 (PHLPP1)	Pleckstrin homology domain-containing family E member 1; PH domain-containing family E member 1; Suprachiasmatic nucleus circadian oscillatory protein; hSCOP; KIAA0606; PHLPP; PLEKHE1; SCOP	PHLPP1	23239	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262719.10, PHLPP1-201, 6299; ENST00000591386.1, PHLPP1-207, 591; ENST00000588953.1, PHLPP1-205, 2198; ENST00000487409.1, PHLPP1-202, 665; ENST00000497351.5, PHLPP1-203, 572; ENST00000588452.5, PHLPP1-204, 559; ENST00000591106.1, PHLPP1-206, 549"	MEPAAAATVQRLPELGREDRASAPAAAAAAAAAAAAAAAALAAAAGGGRSPEPALTPAAPSGGNGSGSGAREEAPGEAPPGPLPGRAGGAGRRRRRGAPQPIAGGAAPVPGAGGGANSLLLRRGRLKRNLSAAAAAASSSSSSSAAAASHSPGAAGLPASCSASASLCTRSLDRKTLLLKHRQTLQLQPSDRDWVRHQLQRGCVHVFDRHMASTYLRPVLCTLDTTAGEVAARLLQLGHKGGGVVKVLGQGPGAAAAREPAEPPPEAGPRLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGSCEEKAAAAVAPGGLQSTPGRSGVTAEKAPPPPPPPTLYVQLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKPHSTGSSERIQLSGMYNVRKGKMQLPVNRWTRRQVILCGTCLIVSSVKDSLTGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTYYICFDTFTEYLRWLRQVSKVASQRISSVDLSCCSLEHLPANLFYSQDLTHLNLKQNFLRQNPSLPAARGLNELQRFTKLKSLNLSNNHLGDFPLAVCSIPTLAELNVSCNALRSVPAAVGVMHNLQTFLLDGNFLQSLPAELENMKQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMSGNCVETLRLQALRKMPHIKHVDLRLNVIRKLIADEVDFLQHVTQLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTLDICGYFLKALYASSNELVQLDVYPVPNYLSYMDVSRNRLENVPEWVCESRKLEVLDIGHNQICELPARLFCNSSLRKLLAGHNQLARLPERLERTSVEVLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNSILQELYLTNNSLTDKCVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVMQLPEIKCVDLSCNELSEVTLPENLPPKLQELDLTGNPRLVLDHKTLELLNNIRCFKIDQPSTGDASGAPAVWSHGYTEASGVKNKLCVAALSVNNFCDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNEEEYMVNTFIVMQRKLGTAGQKLGGAAVLCHIKHDPVDPGGSFTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQHKAIITEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNVPDALAAAKKLCTLAQSYGCHDSISAVVVQLSVTEDSFCCCELSAGGAVPPPSPGIFPPSVNMVIKDRPSDGLGVPSSSSGMASEISSELSTSEMSSEVGSTASDEPPPGALSENSPAYPSEQRCMLHPICLSNSFQRQLSSATFSSAFSDNGLDSDDEEPIEGVFTNGSRVEVEVDIHCSRAKEKEKQQHLLQVPAEASDEGIVISANEDEPGLPRKADFSAVGTIGRRRANGSVAPQERSHNVIEVATDAPLRKPGGYFAAPAQPDPDDQFIIPPELEEEVKEIMKHHQEQQQQQQPPPPPQLQPQLPRHYQLDQLPDYYDTPL	chr18:62715541-62980433[+]	"Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA. Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons. Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis. Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation. Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylates RAF1 inhibiting its kinase activity. May act as a negative regulator of K-Ras signaling in membrane rafts. Involved in the hippocampus-dependent long-term memory formation. Involved in circadian control by regulating the consolidation of circadian periodicity after resetting. Involved in development and function of regulatory T-cells."	.	HGNC:20610	PHLP1_HUMAN	Reviewed	ENSG00000081913	.	.	.	.	.
Mol00140	Protein	PI3-kinase gamma (PIK3CG)	PI3-kinase subunit gamma; PI3K-gamma; PI3Kgamma; PtdIns-3-kinase subunit gamma; Phosphatidylinositol 4;5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma; PtdIns-3-kinase subunit p110-gamma; p110gamma; Phosphoinositide-3-kinase catalytic gamma polypeptide; Serine/threonine protein kinase PIK3CG; p120-PI3K	PIK3CG	5294	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000496166.6, PIK3CG-205, 7059; ENST00000359195.3, PIK3CG-201, 5377; ENST00000440650.6, PIK3CG-202, 3828; ENST00000473541.5, PIK3CG-204, 821; ENST00000466738.1, PIK3CG-203, 448"	MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLHVAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEYVLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA	chr7:106865278-106908980[+]	"Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Together with PIK3CD participates in T-lymphocyte development. Required for B-lymphocyte development and signaling. Together with PIK3CD participates in neutrophil respiratory burst. Together with PIK3CD is involved in neutrophil chemotaxis and extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contributes to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis."	PDB: 1E8Y; PDB: 1E8Z; PDB: 1HE8; PDB: 2A4Z; PDB: 2A5U; PDB: 2CHW; PDB: 2CHX; PDB: 2CHZ; PDB: 2V4L; PDB: 3APC; PDB: 3APD; PDB: 3APF; PDB: 3CSF; PDB: 3CST; PDB: 3DBS; PDB: 3DPD; PDB: 3ENE; PDB: 3IBE; PDB: 3L08; PDB: 3L13; PDB: 3L16; PDB: 3L17; PDB: 3L54; PDB: 3LJ3; PDB: 3MJW; PDB: 3ML8; PDB: 3ML9; PDB: 3NZS; PDB: 3NZU; PDB: 3OAW; PDB: 3P2B; PDB: 3PRE; PDB: 3PRZ; PDB: 3PS6; PDB: 3QAQ; PDB: 3QAR; PDB: 3QJZ; PDB: 3QK0; PDB: 3R7Q; PDB: 3R7R; PDB: 3S2A; PDB: 3SD5; PDB: 3T8M; PDB: 3TJP; PDB: 3TL5; PDB: 3ZVV; PDB: 3ZW3; PDB: 4ANU; PDB: 4ANV; PDB: 4ANW; PDB: 4ANX; PDB: 4AOF; PDB: 4DK5; PDB: 4EZJ; PDB: 4EZK; PDB: 4EZL; PDB: 4F1S; PDB: 4FA6; PDB: 4FAD; PDB: 4FHJ; PDB: 4FHK; PDB: 4FJY; PDB: 4FJZ; PDB: 4FLH; PDB: 4FUL; PDB: 4G11; PDB: 4GB9; PDB: 4HLE; PDB: 4HVB; PDB: 4J6I; PDB: 4KZ0; PDB: 4KZC; PDB: 4PS3; PDB: 4PS7; PDB: 4PS8; PDB: 4URK; PDB: 4WWN; PDB: 4WWO; PDB: 4WWP; PDB: 4XX5; PDB: 4XZ4; PDB: 5EDS; PDB: 5G2N; PDB: 5G55; PDB: 5JHA; PDB: 5JHB; PDB: 5KAE; PDB: 5OQ4; PDB: 5T23; PDB: 6AUD; PDB: 6C1S; PDB: 6FH5; PDB: 6GQ7; PDB: 6T3B; PDB: 6T3C; PDB: 6XRL; PDB: 6XRM; PDB: 7JWE; PDB: 7JWZ; PDB: 7JX0; PDB: 7KKE; PDB: 7MEZ	HGNC:8978	PK3CG_HUMAN	Reviewed	ENSG00000105851	.	.	.	.	.
Mol00141	Protein	Zinc finger protein PLAGL2 (PLAGL2)	Pleiomorphic adenoma-like protein 2; KIAA0198	PLAGL2	5326	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000246229.5, PLAGL2-201, 5656"	MTTFFTSVPPWIQDAKQEEEVGWKLVPRPRGREAESQVKCQCEISGTPFSNGEKLRPHSLPQPEQRPYSCPQLHCGKAFASKYKLYRHMATHSAQKPHQCMYCDKMFHRKDHLRNHLQTHDPNKEALHCSECGKNYNTKLGYRRHLAMHAASSGDLSCKVCLQTFESTQALLEHLKAHSRRVAGGAKEKKHPCDHCDRRFYTRKDVRRHLVVHTGRKDFLCQYCAQRFGRKDHLTRHVKKSHSQELLKIKTEPVDMLGLLSCSSTVSVKEELSPVLCMASRDVMGTKAFPGMLPMGMYGAHIPTMPSTGVPHSLVHNTLPMGMSYPLESSPISSPAQLPPKYQLGSTSYLPDKLPKVEVDSFLAELPGSLSLSSAEPQPASPQPAAAAALLDEALLAKSPANLSEALCAANVDFSHLLGFLPLNLPPCNPPGATGGLVMGYSQAEAQPLLTTLQAQPQDSPGAGGPLNFGPLHSLPPVFTSGLSSTTLPRFHQAFQ	chr20:32192504-32207743[-]	Shows weak transcriptional activatory activity.	.	HGNC:9047	PLAL2_HUMAN	Reviewed	ENSG00000126003	.	.	.	.	.
Mol00142	Protein	Peroxisome proliferator-activated receptor gamma (PPARG)	PPAR-gamma; Nuclear receptor subfamily 1 group C member 3; NR1C3	PPARG	5468	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000651735.1, PPARG-217, 1774; ENST00000287820.10, PPARG-201, 1850; ENST00000682446.1, PPARG-224, 4064; ENST00000683586.1, PPARG-227, 2489; ENST00000397026.7, PPARG-208, 2029; ENST00000397010.7, PPARG-205, 2017; ENST00000644622.2, PPARG-216, 1962; ENST00000643197.2, PPARG-214, 1894; ENST00000309576.11, PPARG-202, 1870; ENST00000681982.1, PPARG-222, 1799; ENST00000397015.7, PPARG-206, 1772; ENST00000643888.2, PPARG-215, 1693; ENST00000652431.1, PPARG-219, 1366; ENST00000652522.1, PPARG-220, 1350; ENST00000683700.1, PPARG-230, 1334; ENST00000683699.1, PPARG-229, 1177; ENST00000397000.6, PPARG-204, 1122; ENST00000652098.1, PPARG-218, 1058; ENST00000397029.8, PPARG-209, 686; ENST00000438682.6, PPARG-210, 560; ENST00000455517.6, PPARG-211, 428; ENST00000683749.1, PPARG-231, 401; ENST00000397023.5, PPARG-207, 2002; ENST00000681966.1, PPARG-221, 1601; ENST00000396999.3, PPARG-203, 1335; ENST00000684065.1, PPARG-232, 1307; ENST00000683599.1, PPARG-228, 485; ENST00000684277.1, PPARG-234, 411; ENST00000682494.1, PPARG-225, 4527; ENST00000684094.1, PPARG-233, 2269; ENST00000682604.1, PPARG-226, 1853; ENST00000477039.5, PPARG-212, 1705; ENST00000682125.1, PPARG-223, 1672; ENST00000497594.5, PPARG-213, 1600"	MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY	chr3:12287368-12434356[+]	"Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels (By similarity)."	PDB: 1FM6; PDB: 1FM9; PDB: 1I7I; PDB: 1K74; PDB: 1KNU; PDB: 1NYX; PDB: 1PRG; PDB: 1RDT; PDB: 1WM0; PDB: 1ZEO; PDB: 1ZGY; PDB: 2ATH; PDB: 2F4B; PDB: 2FVJ; PDB: 2G0G; PDB: 2G0H; PDB: 2GTK; PDB: 2HFP; PDB: 2HWQ; PDB: 2HWR; PDB: 2I4J; PDB: 2I4P; PDB: 2I4Z; PDB: 2OM9; PDB: 2P4Y; PDB: 2POB; PDB: 2PRG; PDB: 2Q59; PDB: 2Q5P; PDB: 2Q5S; PDB: 2Q61; PDB: 2Q6R; PDB: 2Q6S; PDB: 2Q8S; PDB: 2QMV; PDB: 2VSR; PDB: 2VST; PDB: 2VV0; PDB: 2VV1; PDB: 2VV2; PDB: 2VV3; PDB: 2VV4; PDB: 2XKW; PDB: 2YFE; PDB: 2ZK0; PDB: 2ZK1; PDB: 2ZK2; PDB: 2ZK3; PDB: 2ZK4; PDB: 2ZK5; PDB: 2ZK6; PDB: 2ZNO; PDB: 2ZVT; PDB: 3ADS; PDB: 3ADT; PDB: 3ADU; PDB: 3ADV; PDB: 3ADW; PDB: 3ADX; PDB: 3AN3; PDB: 3AN4; PDB: 3B0Q; PDB: 3B0R; PDB: 3B1M; PDB: 3B3K; PDB: 3BC5; PDB: 3CDP; PDB: 3CDS; PDB: 3CS8; PDB: 3CWD; PDB: 3D6D; PDB: 3DZU; PDB: 3DZY; PDB: 3E00; PDB: 3ET0; PDB: 3ET3; PDB: 3FEJ; PDB: 3FUR; PDB: 3G9E; PDB: 3GBK; PDB: 3H0A; PDB: 3HO0; PDB: 3HOD; PDB: 3IA6; PDB: 3K8S; PDB: 3KMG; PDB: 3LMP; PDB: 3NOA; PDB: 3OSI; PDB: 3OSW; PDB: 3PBA; PDB: 3PO9; PDB: 3PRG; PDB: 3QT0; PDB: 3R5N; PDB: 3R8A; PDB: 3R8I; PDB: 3S9S; PDB: 3SZ1; PDB: 3T03; PDB: 3TY0; PDB: 3U9Q; PDB: 3V9T; PDB: 3V9V; PDB: 3V9Y; PDB: 3VJH; PDB: 3VJI; PDB: 3VN2; PDB: 3VSO; PDB: 3VSP; PDB: 3WJ4; PDB: 3WJ5; PDB: 3WMH; PDB: 3X1H; PDB: 3X1I; PDB: 4A4V; PDB: 4A4W; PDB: 4CI5; PDB: 4E4K; PDB: 4E4Q; PDB: 4EM9; PDB: 4EMA; PDB: 4F9M; PDB: 4FGY; PDB: 4HEE; PDB: 4JAZ; PDB: 4JL4; PDB: 4L96; PDB: 4L98; PDB: 4O8F; PDB: 4OJ4; PDB: 4PRG; PDB: 4PVU; PDB: 4PWL; PDB: 4R06; PDB: 4R2U; PDB: 4R6S; PDB: 4XLD; PDB: 4XTA; PDB: 4XUH; PDB: 4XUM; PDB: 4Y29; PDB: 4YT1; PDB: 5AZV; PDB: 5DSH; PDB: 5DV3; PDB: 5DV6; PDB: 5DV8; PDB: 5DVC; PDB: 5DWL; PDB: 5F9B; PDB: 5GTN; PDB: 5GTO; PDB: 5GTP; PDB: 5HZC; PDB: 5JI0; PDB: 5LSG; PDB: 5TTO; PDB: 5TWO; PDB: 5U5L; PDB: 5UGM; PDB: 5WQX; PDB: 5WR0; PDB: 5WR1; PDB: 5Y2O; PDB: 5Y2T; PDB: 5YCN; PDB: 5YCP; PDB: 5Z5S; PDB: 5Z6S; PDB: 6AD9; PDB: 6AN1; PDB: 6AUG; PDB: 6AVI; PDB: 6C1I; PDB: 6C5Q; PDB: 6C5T; PDB: 6D3E; PDB: 6D8X; PDB: 6D94; PDB: 6DBH; PDB: 6DCU; PDB: 6DGL; PDB: 6DGO; PDB: 6DGP; PDB: 6DGQ; PDB: 6DGR; PDB: 6DH9; PDB: 6DHA; PDB: 6E5A; PDB: 6ENQ; PDB: 6F2L; PDB: 6FZF; PDB: 6FZG; PDB: 6FZJ; PDB: 6FZP; PDB: 6FZY; PDB: 6ICJ; PDB: 6IJR; PDB: 6IJS; PDB: 6ILQ; PDB: 6IZM; PDB: 6IZN; PDB: 6JEY; PDB: 6JF0; PDB: 6JQ7; PDB: 6K0T; PDB: 6KTM; PDB: 6KTN; PDB: 6L89; PDB: 6L8B; PDB: 6MCZ; PDB: 6MD0; PDB: 6MD1; PDB: 6MD2; PDB: 6MD4; PDB: 6MS7; PDB: 6O67; PDB: 6O68; PDB: 6ONI; PDB: 6ONJ; PDB: 6PDZ; PDB: 6QJ5; PDB: 6T1S; PDB: 6T1V; PDB: 6T6B; PDB: 6T9C; PDB: 6TDC; PDB: 6TSG; PDB: 6VZL; PDB: 6VZM; PDB: 6VZN; PDB: 6VZO; PDB: 6Y3U; PDB: 6ZLY; PDB: 7A7H; PDB: 7AHJ; PDB: 7AWC; PDB: 7AWD; PDB: 7CXE; PDB: 7CXF; PDB: 7CXG; PDB: 7CXH; PDB: 7CXI; PDB: 7CXJ; PDB: 7CXK; PDB: 7CXL; PDB: 7E0A; PDB: 7EFQ; PDB: 7JQG; PDB: 7LOT	HGNC:9236	PPARG_HUMAN	Reviewed	ENSG00000132170	.	.	.	.	.
Mol00143	Protein	Prominin-1 (PROM1)	.	PROM1	8842	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000447510.7, PROM1-201, 4021; ENST00000505450.5, PROM1-206, 4349; ENST00000508167.5, PROM1-207, 4014; ENST00000510224.5, PROM1-210, 4006; ENST00000539194.6, PROM1-219, 3838; ENST00000675377.1, PROM1-221, 2529; ENST00000540805.6, PROM1-220, 2803; ENST00000675613.1, PROM1-222, 2478; ENST00000514967.5, PROM1-218, 568; ENST00000508940.1, PROM1-209, 567; ENST00000508322.1, PROM1-208, 551; ENST00000513946.2, PROM1-216, 3927; ENST00000511153.5, PROM1-211, 1595; ENST00000503884.5, PROM1-204, 622; ENST00000502943.1, PROM1-203, 760; ENST00000502501.1, PROM1-202, 568; ENST00000513108.1, PROM1-214, 565; ENST00000512304.2, PROM1-213, 540; ENST00000514693.5, PROM1-217, 530; ENST00000504842.5, PROM1-205, 507; ENST00000511270.1, PROM1-212, 291; ENST00000513448.5, PROM1-215, 2042"	MALVLGSLLLLGLCGNSFSGGQPSSTDAPKAWNYELPATNYETQDSHKAGPIGILFELVHIFLYVVQPRDFPEDTLRKFLQKAYESKIDYDKPETVILGLKIVYYEAGIILCCVLGLLFIILMPLVGYFFCMCRCCNKCGGEMHQRQKENGPFLRKCFAISLLVICIIISIGIFYGFVANHQVRTRIKRSRKLADSNFKDLRTLLNETPEQIKYILAQYNTTKDKAFTDLNSINSVLGGGILDRLRPNIIPVLDEIKSMATAIKETKEALENMNSTLKSLHQQSTQLSSSLTSVKTSLRSSLNDPLCLVHPSSETCNSIRLSLSQLNSNPELRQLPPVDAELDNVNNVLRTDLDGLVQQGYQSLNDIPDRVQRQTTTVVAGIKRVLNSIGSDIDNVTQRLPIQDILSAFSVYVNNTESYIHRNLPTLEEYDSYWWLGGLVICSLLTLIVIFYYLGLLCGVCGYDRHATPTTRGCVSNTGGVFLMVGVGLSFLFCWILMIIVVLTFVFGANVEKLICEPYTSKELFRVLDTPYLLNEDWEYYLSGKLFNKSKMKLTFEQVYSDCKKNRGTYGTLHLQNSFNISEHLNINEHTGSISSELESLKVNLNIFLLGAAGRKNLQDFAACGIDRMNYDSYLAQTGKSPAGVNLLSFAYDLEAKANSLPPGNLRNSLKRDAQTIKTIHQQRVLPIEQSLSTLYQSVKILQRTGNGLLERVTRILASLDFAQNFITNNTSSVIIEETKKYGRTIIGYFEHYLQWIEFSISEKVASCKPVATALDTAVDVFLCSYIIDPLNLFWFGIGKATVFLLPALIFAVKLAKYYRRMDSEDVYDDVETIPMKNMENGNNGYHKDHVYGIHNPVMTSPSQH	chr4:15963076-16084378[-]	"May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner."	.	HGNC:9454	PROM1_HUMAN	Reviewed	ENSG00000007062	.	.	.	.	.
Mol00144	Protein	Protein patched homolog 1 (PTCH1)	PTC; PTC1; PTCH	PTCH1	5727	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331920.11, PTCH1-201, 8662; ENST00000430669.6, PTCH1-205, 8232; ENST00000437951.6, PTCH1-206, 7905; ENST00000692981.1, PTCH1-227, 7000; ENST00000429896.6, PTCH1-204, 6563; ENST00000468211.6, PTCH1-207, 1254; ENST00000375271.4, PTCH1-202, 1058; ENST00000553011.5, PTCH1-223, 1037; ENST00000547672.5, PTCH1-212, 881; ENST00000546820.5, PTCH1-210, 864; ENST00000551845.5, PTCH1-222, 809; ENST00000548420.1, PTCH1-214, 553; ENST00000551630.1, PTCH1-221, 539; ENST00000375290.6, PTCH1-203, 10631; ENST00000690194.1, PTCH1-226, 7135; ENST00000550914.6, PTCH1-218, 630; ENST00000551623.1, PTCH1-220, 366; ENST00000693534.1, PTCH1-228, 4653; ENST00000548379.5, PTCH1-213, 548; ENST00000553256.5, PTCH1-224, 537; ENST00000547615.1, PTCH1-211, 525; ENST00000548945.6, PTCH1-215, 243; ENST00000551425.1, PTCH1-219, 241; ENST00000687744.1, PTCH1-225, 5236; ENST00000546744.5, PTCH1-209, 4389; ENST00000550136.1, PTCH1-217, 2388; ENST00000549678.1, PTCH1-216, 578; ENST00000488809.2, PTCH1-208, 301"	MASAGNAAEPQDRGGGGSGCIGAPGRPAGGGRRRRTGGLRRAAAPDRDYLHRPSYCDAAFALEQISKGKATGRKAPLWLRAKFQRLLFKLGCYIQKNCGKFLVVGLLIFGAFAVGLKAANLETNVEELWVEVGGRVSRELNYTRQKIGEEAMFNPQLMIQTPKEEGANVLTTEALLQHLDSALQASRVHVYMYNRQWKLEHLCYKSGELITETGYMDQIIEYLYPCLIITPLDCFWEGAKLQSGTAYLLGKPPLRWTNFDPLEFLEELKKINYQVDSWEEMLNKAEVGHGYMDRPCLNPADPDCPATAPNKNSTKPLDMALVLNGGCHGLSRKYMHWQEELIVGGTVKNSTGKLVSAHALQTMFQLMTPKQMYEHFKGYEYVSHINWNEDKAAAILEAWQRTYVEVVHQSVAQNSTQKVLSFTTTTLDDILKSFSDVSVIRVASGYLLMLAYACLTMLRWDCSKSQGAVGLAGVLLVALSVAAGLGLCSLIGISFNAATTQVLPFLALGVGVDDVFLLAHAFSETGQNKRIPFEDRTGECLKRTGASVALTSISNVTAFFMAALIPIPALRAFSLQAAVVVVFNFAMVLLIFPAILSMDLYRREDRRLDIFCCFTSPCVSRVIQVEPQAYTDTHDNTRYSPPPPYSSHSFAHETQITMQSTVQLRTEYDPHTHVYYTTAEPRSEISVQPVTVTQDTLSCQSPESTSSTRDLLSQFSDSSLHCLEPPCTKWTLSSFAEKHYAPFLLKPKAKVVVIFLFLGLLGVSLYGTTRVRDGLDLTDIVPRETREYDFIAAQFKYFSFYNMYIVTQKADYPNIQHLLYDLHRSFSNVKYVMLEENKQLPKMWLHYFRDWLQGLQDAFDSDWETGKIMPNNYKNGSDDGVLAYKLLVQTGSRDKPIDISQLTKQRLVDADGIINPSAFYIYLTAWVSNDPVAYAASQANIRPHRPEWVHDKADYMPETRLRIPAAEPIEYAQFPFYLNGLRDTSDFVEAIEKVRTICSNYTSLGLSSYPNGYPFLFWEQYIGLRHWLLLFISVVLACTFLVCAVFLLNPWTAGIIVMVLALMTVELFGMMGLIGIKLSAVPVVILIASVGIGVEFTVHVALAFLTAIGDKNRRAVLALEHMFAPVLDGAVSTLLGVLMLAGSEFDFIVRYFFAVLAILTILGVLNGLVLLPVLLSFFGPYPEVSPANGLNRLPTPSPEPPPSVVRFAMPPGHTHSGSDSSDSEYSSQTTVSGLSEELRHYEAQQGAGGPAHQVIVEATENPVFAHSTVVHPESRHHPPSNPRQQPHLDSGSLPPGRQGQQPRRDPPREGLWPPPYRPRRDAFEISTEGHSGPSNRARWGPRGARSHNPRNPASTAMGSSVPGYCQPITTVTASASVTVAVHPPPVPGPGRNPRGGLCPGYPETDHGLFEDPHVPFHVRCERRDSKVEVIELQDVECEERPRGSSSN	chr9:95442980-95517057[-]	"Acts as a receptor for sonic hedgehog (SHH), indian hedgehog (IHH) and desert hedgehog (DHH). Associates with the smoothened protein (SMO) to transduce the hedgehog's proteins signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis."	PDB: 6DMB; PDB: 6DMO; PDB: 6DMY; PDB: 6E1H; PDB: 6N7G; PDB: 6N7H; PDB: 6N7K; PDB: 6OEU; PDB: 6OEV; PDB: 6RMG; PDB: 6RTW; PDB: 6RTX; PDB: 6RTY; PDB: 6RVC; PDB: 6RVD	HGNC:9585	PTC1_HUMAN	Reviewed	ENSG00000185920	.	.	.	.	.
Mol00145	Protein	Phosphatase and tensin homolog (PTEN)	Mutated in multiple advanced cancers 1; Phosphatase and tensin homolog; MMAC1; TEP1	PTEN	5728	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371953.8, PTEN-201, 8515; ENST00000688308.1, PTEN-210, 3117; ENST00000693560.1, PTEN-212, 8701; ENST00000472832.2, PTEN-204, 644; ENST00000688158.1, PTEN-209, 8761; ENST00000686459.1, PTEN-208, 2712; ENST00000688922.1, PTEN-211, 2546; ENST00000618586.1, PTEN-207, 1581; ENST00000487939.1, PTEN-205, 477; ENST00000498703.1, PTEN-206, 554; ENST00000416679.1, PTEN-202, 499; ENST00000462694.1, PTEN-203, 383"	MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV	chr10:87862638-87971930[+]	"Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement."	PDB: 1D5R; PDB: 2KYL; PDB: 4O1V; PDB: 5BUG; PDB: 5BZX; PDB: 5BZZ; PDB: 7JUK; PDB: 7JUL; PDB: 7JVX	HGNC:9588	PTEN_HUMAN	Reviewed	ENSG00000171862	.	.	.	.	.
Mol00146	Protein	Protein-tyrosine kinase 6 (PTK6)	Breast tumor kinase; Tyrosine-protein kinase BRK; BRK	PTK6	5753	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000542869.3, PTK6-202, 2953; ENST00000217185.3, PTK6-201, 2401"	MVSRDQAHLGPKYVGLWDFKSRTDEELSFRAGDVFHVARKEEQWWWATLLDEAGGAVAQGYVPHNYLAERETVESEPWFFGCISRSEAVRRLQAEGNATGAFLIRVSEKPSADYVLSVRDTQAVRHYKIWRRAGGRLHLNEAVSFLSLPELVNYHRAQSLSHGLRLAAPCRKHEPEPLPHWDDWERPREEFTLCRKLGSGYFGEVFEGLWKDRVQVAIKVISRDNLLHQQMLQSEIQAMKKLRHKHILALYAVVSVGDPVYIITELMAKGSLLELLRDSDEKVLPVSELLDIAWQVAEGMCYLESQNYIHRDLAARNILVGENTLCKVGDFGLARLIKEDVYLSHDHNIPYKWTAPEALSRGHYSTKSDVWSFGILLHEMFSRGQVPYPGMSNHEAFLRVDAGYRMPCPLECPPSVHKLMLTCWCRDPEQRPCFKALRERLSSFTSYENPT	chr20:63528001-63537376[-]	"Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins: KHDRBS1/SAM68, KHDRBS2/SLM1, KHDRBS3/SLM2 and SFPQ/PSF; transcription factors: STAT3 and STAT5A/B and a variety of signaling molecules: ARHGAP35/p190RhoGAP, PXN/paxillin, BTK/ATK, STAP2/BKS. Associates also with a variety of proteins that are likely upstream of PTK6 in various signaling pathways, or for which PTK6 may play an adapter-like role. These proteins include ADAM15, EGFR, ERBB2, ERBB3 and IRS4. In normal or non-tumorigenic tissues, PTK6 promotes cellular differentiation and apoptosis. In tumors PTK6 contributes to cancer progression by sensitizing cells to mitogenic signals and enhancing proliferation, anchorage-independent survival and migration/invasion. Association with EGFR, ERBB2, ERBB3 may contribute to mammary tumor development and growth through enhancement of EGF-induced signaling via BTK/AKT and PI3 kinase. Contributes to migration and proliferation by contributing to EGF-mediated phosphorylation of ARHGAP35/p190RhoGAP, which promotes association with RASA1/p120RasGAP, inactivating RhoA while activating RAS. EGF stimulation resulted in phosphorylation of PNX/Paxillin by PTK6 and activation of RAC1 via CRK/CrKII, thereby promoting migration and invasion. PTK6 activates STAT3 and STAT5B to promote proliferation. Nuclear PTK6 may be important for regulating growth in normal epithelia, while cytoplasmic PTK6 might activate oncogenic signaling pathways.; FUNCTION: Isoform 2 inhibits PTK6 phosphorylation and PTK6 association with other tyrosine-phosphorylated proteins."	PDB: 1RJA; PDB: 2KGT; PDB: 5D7V; PDB: 5DA3; PDB: 5H2U; PDB: 6CZ2; PDB: 6CZ3; PDB: 6CZ4	HGNC:9617	PTK6_HUMAN	Reviewed	ENSG00000101213	.	.	.	.	.
Mol00147	Protein	Tyrosine-protein phosphatase non-receptor type 11 (PTPN11)	Protein-tyrosine phosphatase 1D; PTP-1D; Protein-tyrosine phosphatase 2C; PTP-2C; SH-PTP2; SHP-2; Shp2; SH-PTP3; PTP2C; SHPTP2	PTPN11	5781	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000351677.7, PTPN11-201, 6073; ENST00000392597.5, PTPN11-202, 1876; ENST00000635625.1, PTPN11-205, 1794; ENST00000690210.1, PTPN11-214, 6274; ENST00000687906.1, PTPN11-211, 5995; ENST00000688597.1, PTPN11-212, 5738; ENST00000639857.2, PTPN11-207, 4455; ENST00000635652.1, PTPN11-206, 588; ENST00000530818.1, PTPN11-203, 486; ENST00000685487.1, PTPN11-208, 6926; ENST00000692624.1, PTPN11-216, 6045; ENST00000690472.1, PTPN11-215, 5117; ENST00000531326.1, PTPN11-204, 573; ENST00000687120.1, PTPN11-209, 7648; ENST00000688701.1, PTPN11-213, 5152; ENST00000687624.1, PTPN11-210, 2354"	MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR	chr12:112418351-112509918[+]	"Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity. Dephosphorylates CDC73. Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification."	PDB: 2SHP; PDB: 3B7O; PDB: 3MOW; PDB: 3O5X; PDB: 3TKZ; PDB: 3TL0; PDB: 3ZM0; PDB: 3ZM1; PDB: 3ZM2; PDB: 3ZM3; PDB: 4DGP; PDB: 4DGX; PDB: 4GWF; PDB: 4H1O; PDB: 4H34; PDB: 4JE4; PDB: 4JEG; PDB: 4JMG; PDB: 4NWF; PDB: 4NWG; PDB: 4OHD; PDB: 4OHE; PDB: 4OHH; PDB: 4OHI; PDB: 4OHL; PDB: 4PVG; PDB: 4QSY; PDB: 4RDD; PDB: 5BK8; PDB: 5DF6; PDB: 5EHP; PDB: 5EHR; PDB: 5I6V; PDB: 5IBM; PDB: 5IBS; PDB: 5X7B; PDB: 5X94; PDB: 5XZR; PDB: 6ATD; PDB: 6BMR; PDB: 6BMU; PDB: 6BMV; PDB: 6BMW; PDB: 6BMX; PDB: 6BMY; PDB: 6BN5; PDB: 6CMP; PDB: 6CMQ; PDB: 6CMR; PDB: 6CMS; PDB: 6CRF; PDB: 6CRG; PDB: 6MD7; PDB: 6MD9; PDB: 6MDA; PDB: 6MDB; PDB: 6MDC; PDB: 6MDD; PDB: 6R5G; PDB: 6WU8; PDB: 7EMN; PDB: 7JVM; PDB: 7JVN; PDB: 7R75; PDB: 7R7D; PDB: 7R7I; PDB: 7R7L; PDB: 7RCT	HGNC:9644	PTN11_HUMAN	Reviewed	ENSG00000179295	.	.	.	.	.
Mol00148	Protein	Ras-related protein Rab-12 (RAB12)	.	RAB12	201475	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649141.2, RAB12-202, 2147; ENST00000580987.1, RAB12-201, 504"	MDPGAALQRRAGGGGGLGAGSPALSGGQGRRRKQPPRPADFKLQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVYDITKKETFDDLPKWMKMIDKYASEDAELLLVGNKLDCETDREITRQQGEKFAQQITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQPEPEIPPELPPPRPHVRCC	chr18:8609437-8639383[+]	"The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may play a role in protein transport from recycling endosomes to lysosomes regulating, for instance, the degradation of the transferrin receptor. Involved in autophagy (By similarity)."	PDB: 2IL1	HGNC:31332	RAB12_HUMAN	Reviewed	ENSG00000206418	.	.	.	.	.
Mol00149	Protein	Ras-related protein Rab-6A (RAP6A)	Rab-6; RAB6	RAB6A	5870	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000336083.8, RAB6A-202, 3326; ENST00000310653.10, RAB6A-201, 3389; ENST00000541973.5, RAB6A-209, 1104; ENST00000541588.5, RAB6A-207, 758; ENST00000536566.5, RAB6A-204, 1267; ENST00000540771.5, RAB6A-206, 699; ENST00000545625.5, RAB6A-210, 447; ENST00000537446.5, RAB6A-205, 447; ENST00000400470.3, RAB6A-203, 522; ENST00000541795.1, RAB6A-208, 1812"	MSTGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIIMLVGNKTDLADKRQVSIEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMESTQDRSREDMIDIKLEKPQEQPVSEGGCSC	chr11:73675638-73761137[-]	Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity. Involved in COPI-independent retrograde transport from the Golgi to the ER.	PDB: 1YZQ; PDB: 2GIL; PDB: 3BBP; PDB: 3CWZ; PDB: 4DKX; PDB: 5LEF	HGNC:9786	RAB6A_HUMAN	Reviewed	ENSG00000175582	.	.	.	.	.
Mol00150	Protein	GTPase KRas (KRAS)	K-Ras 2; Ki-Ras; c-K-ras; c-Ki-ras; KRAS2; RASK2	KRAS	3845	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000311936.8, KRAS-202, 5306; ENST00000256078.10, KRAS-201, 5430; ENST00000685328.1, KRAS-205, 5287; ENST00000688940.1, KRAS-210, 3630; ENST00000693229.1, KRAS-214, 5187; ENST00000692768.1, KRAS-213, 5075; ENST00000686969.1, KRAS-207, 2957; ENST00000556131.2, KRAS-203, 2937; ENST00000557334.6, KRAS-204, 1042; ENST00000686877.1, KRAS-206, 5420; ENST00000687356.1, KRAS-208, 5101; ENST00000690406.1, KRAS-211, 4919; ENST00000690804.1, KRAS-212, 2721; ENST00000688228.1, KRAS-209, 1163"	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM	chr12:25205246-25250936[-]	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation. Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner.	.	HGNC:6407	RASK_HUMAN	Reviewed	ENSG00000133703	.	.	.	.	.
Mol00151	Protein	RalA-binding protein 1 (RALBP1)	RalBP1; 76 kDa Ral-interacting protein; Dinitrophenyl S-glutathione ATPase; DNP-SG ATPase; Ral-interacting protein 1; RLIP; RLIP1; RLIP76	RALBP1	10928	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000383432.8, RALBP1-202, 4379; ENST00000019317.8, RALBP1-201, 4368; ENST00000609094.2, RALBP1-206, 3676; ENST00000585015.6, RALBP1-205, 945; ENST00000458039.3, RALBP1-203, 836; ENST00000577221.1, RALBP1-204, 503"	MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDVVSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQIDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKVDELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKVQEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVFFTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSSESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAKAEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI	chr18:9475009-9538114[+]	"Multifunctional protein that functions as a downstream effector of RALA and RALB. As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity. As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis. During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle. During mitosis, also controls mitochondrial fission as an effector of RALA. Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L."	PDB: 2KWH; PDB: 2KWI; PDB: 2MBG; PDB: 6ZQT; PDB: 6ZRN	HGNC:9841	RBP1_HUMAN	Reviewed	ENSG00000017797	.	.	.	.	.
Mol00152	Protein	Transforming protein RhoA (RHOA)	Rho cDNA clone 12; h12; ARH12; ARHA; RHO12	RHOA	387	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000418115.6, RHOA-202, 1805; ENST00000679208.1, RHOA-211, 1971; ENST00000422781.6, RHOA-203, 1944; ENST00000445425.6, RHOA-205, 1897; ENST00000678200.1, RHOA-209, 1789; ENST00000454011.7, RHOA-206, 1641; ENST00000678921.2, RHOA-210, 3941; ENST00000676712.2, RHOA-207, 1582; ENST00000677684.1, RHOA-208, 527; ENST00000431929.2, RHOA-204, 539; ENST00000265538.3, RHOA-201, 388"	MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLVL	chr3:49359139-49412998[-]	"Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis. Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center. May be an activator of PLCE1. In neurons, involved in the inhibition of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling. Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets."	PDB: 1A2B; PDB: 1CC0; PDB: 1CXZ; PDB: 1DPF; PDB: 1FTN; PDB: 1KMQ; PDB: 1LB1; PDB: 1OW3; PDB: 1S1C; PDB: 1TX4; PDB: 1X86; PDB: 1XCG; PDB: 2RGN; PDB: 3KZ1; PDB: 3LW8; PDB: 3LWN; PDB: 3LXR; PDB: 3MSX; PDB: 3T06; PDB: 4D0N; PDB: 4XH9; PDB: 4XOI; PDB: 4XSG; PDB: 4XSH; PDB: 5A0F; PDB: 5BWM; PDB: 5C2K; PDB: 5C4M; PDB: 5EZ6; PDB: 5FR1; PDB: 5FR2; PDB: 5HPY; PDB: 5IRC; PDB: 5JCP; PDB: 5JHG; PDB: 5JHH; PDB: 5M6X; PDB: 5M70; PDB: 5ZHX; PDB: 6BC0; PDB: 6BCA; PDB: 6BCB; PDB: 6KX2; PDB: 6KX3; PDB: 6R3V; PDB: 6V6M; PDB: 6V6U; PDB: 6V6V	HGNC:667	RHOA_HUMAN	Reviewed	ENSG00000067560	.	.	.	.	.
Mol00153	Protein	Rho-related GTP-binding protein RhoF (RHOF)	Rho family GTPase Rif; Rho in filopodia; ARHF; RIF	RHOF	54509	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000267205.7, RHOF-201, 2435; ENST00000541657.5, RHOF-205, 1626; ENST00000537171.5, RHOF-203, 1485; ENST00000546227.5, RHOF-207, 1219; ENST00000537265.5, RHOF-204, 699; ENST00000535560.1, RHOF-202, 670; ENST00000545544.1, RHOF-206, 826"	MDAPGALAQTAAPGPGRKELKIVIVGDGGCGKTSLLMVYSQGSFPEHYAPSVFEKYTASVTVGSKEVTLNLYDTAGQEDYDRLRPLSYQNTHLVLICYDVMNPTSYDNVLIKWFPEVTHFCRGIPMVLIGCKTDLRKDKEQLRKLRAAQLEPITYMQGLSACEQIRAALYLECSAKFRENVEDVFREAAKVALSALKKAQRQKKRRLCLLL	chr12:121777754-121803403[-]	"Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Causes the formation of thin, actin-rich surface projections called filopodia. Functions cooperatively with CDC42 and Rac to generate additional structures, increasing the diversity of actin-based morphology."	.	HGNC:15703	RHOF_HUMAN	Reviewed	ENSG00000139725	.	.	.	.	.
Mol00154	Protein	Ribosomal protein S6 (RPS6)	Phosphoprotein NP33; Small ribosomal subunit protein eS6; OK/SW-cl.2	RPS6	6194	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000380394.9, RPS6-204, 1369; ENST00000380384.5, RPS6-203, 1355; ENST00000380381.3, RPS6-202, 892; ENST00000315377.4, RPS6-201, 863; ENST00000498815.1, RPS6-205, 480"	MKLNISFPATGCQKLIEVDDERKLRTFYEKRMATEVAADALGEEWKGYVVRISGGNDKQGFPMKQGVLTHGRVRLLLSKGHSCYRPRRTGERKRKSVRGCIVDANLSVLNLVIVKKGEKDIPGLTDTTVPRRLGPKRASRIRKLFNLSKEDDVRQYVVRKPLNKEGKKPRTKAPKIQRLVTPRVLQHKRRRIALKKQRTKKNKEEAAEYAKLLAKRMKEAKEKRQEQIAKRRRLSSLRASTSKSESSQK	chr9:19375715-19380236[-]	Component of the 40S small ribosomal subunit. Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.	PDB: 4UG0; PDB: 4V6X; PDB: 5A2Q; PDB: 5AJ0; PDB: 5FLX; PDB: 5LKS; PDB: 5OA3; PDB: 5T2C; PDB: 5VYC; PDB: 6F4P; PDB: 6F4Q; PDB: 6FEC; PDB: 6G18; PDB: 6G4S; PDB: 6G4W; PDB: 6G51; PDB: 6G53; PDB: 6G5H; PDB: 6G5I; PDB: 6IP5; PDB: 6IP6; PDB: 6IP8; PDB: 6OLE; PDB: 6OLF; PDB: 6OLG; PDB: 6OLI; PDB: 6OLZ; PDB: 6OM0; PDB: 6OM7; PDB: 6QZP; PDB: 6XA1; PDB: 6Y0G; PDB: 6Y2L; PDB: 6Y57; PDB: 6YBW; PDB: 6Z6L; PDB: 6Z6M; PDB: 6Z6N; PDB: 6ZLW; PDB: 6ZM7; PDB: 6ZME; PDB: 6ZMI; PDB: 6ZMO; PDB: 6ZMT; PDB: 6ZMW; PDB: 6ZN5; PDB: 6ZOJ; PDB: 6ZOK; PDB: 6ZON; PDB: 6ZP4; PDB: 6ZUO; PDB: 6ZV6; PDB: 6ZVH; PDB: 6ZVJ; PDB: 6ZXD; PDB: 6ZXE; PDB: 6ZXF; PDB: 6ZXG; PDB: 6ZXH; PDB: 7A09; PDB: 7K5I; PDB: 7MQ8; PDB: 7MQ9; PDB: 7MQA	HGNC:10429	RS6_HUMAN	Reviewed	ENSG00000137154	.	.	.	.	.
Mol00155	Protein	Protein S100-A4 (S100A4)	Calvasculin; Metastasin; Placental calcium-binding protein; Protein Mts1; S100 calcium-binding protein A4; CAPL; MTS1	S100A4	6275	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368716.9, S100A4-204, 513; ENST00000368715.5, S100A4-203, 573; ENST00000354332.8, S100A4-201, 566; ENST00000368714.1, S100A4-202, 531; ENST00000481009.1, S100A4-206, 755; ENST00000468373.1, S100A4-205, 537"	MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK	chr1:153543613-153550136[-]	"Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9. Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis. Modulates also the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels. Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes. In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors."	PDB: 1M31; PDB: 2LNK; PDB: 2MRD; PDB: 2Q91; PDB: 3C1V; PDB: 3CGA; PDB: 3KO0; PDB: 3M0W; PDB: 3ZWH; PDB: 4CFQ; PDB: 4CFR; PDB: 4ETO; PDB: 4HSZ; PDB: 5LPU; PDB: 6T58	HGNC:10494	S10A4_HUMAN	Reviewed	ENSG00000196154	.	.	.	.	.
Mol00156	Protein	Solute carrier family 35 member F5 (SLC35F5)	Hepatitis C virus NS5A-transactivated protein 3; HCV NS5A-transactivated protein 3; NS5ATP3; UNQ2545/PRO6097	SLC35F5	80255	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000245680.7, SLC35F5-201, 10314; ENST00000409342.1, SLC35F5-203, 2284; ENST00000447673.1, SLC35F5-205, 725; ENST00000409106.5, SLC35F5-202, 3120; ENST00000420066.1, SLC35F5-204, 736; ENST00000470204.2, SLC35F5-210, 523; ENST00000498768.1, SLC35F5-212, 1711; ENST00000469702.5, SLC35F5-209, 784; ENST00000459683.5, SLC35F5-206, 744; ENST00000469314.1, SLC35F5-208, 628; ENST00000485214.1, SLC35F5-211, 577; ENST00000460863.1, SLC35F5-207, 466"	MVPPRRHRGAGRPGVLSSSPPFRLRSAKFSGIALEDLRRALKTRLQMVCVFVMNRMNSQNSGFTQRRRMALGIVILLLVDVIWVASSELTSYVFTQYNKPFFSTFAKTSMFVLYLLGFIIWKPWRQQCTRGLRGKHAAFFADAEGYFAACTTDTTMNSSLSEPLYVPVKFHDLPSEKPESTNIDTEKTPKKSRVRFSNIMEIRQLPSSHALEAKLSRMSYPVKEQESILKTVGKLTATQVAKISFFFCFVWFLANLSYQEALSDTQVAIVNILSSTSGLFTLILAAVFPSNSGDRFTLSKLLAVILSIGGVVLVNLAGSEKPAGRDTVGSIWSLAGAMLYAVYIVMIKRKVDREDKLDIPMFFGFVGLFNLLLLWPGFFLLHYTGFEDFEFPNKVVLMCIIINGLIGTVLSEFLWLWGCFLTSSLIGTLALSLTIPLSIIADMCMQKVQFSWLFFAGAIPVFFSFFIVTLLCHYNNWDPVMVGIRRIFAFICRKHRIQRVPEDSEQCESLISMHSVSQEDGAS	chr2:113705011-113756693[-]	Putative solute transporter.	.	HGNC:23617	S35F5_HUMAN	Reviewed	ENSG00000115084	.	.	.	.	.
Mol00157	Protein	Selenoprotein W (SEPW1)	SelW; SELW; SEPW1	SELENOW	6415	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000601048.6, SELENOW-211, 758; ENST00000593892.5, SELENOW-201, 550; ENST00000595615.1, SELENOW-203, 535; ENST00000599874.5, SELENOW-210, 636; ENST00000601419.5, SELENOW-212, 717; ENST00000595509.1, SELENOW-202, 675; ENST00000599302.1, SELENOW-207, 636; ENST00000599590.5, SELENOW-208, 572; ENST00000602163.1, SELENOW-214, 2503; ENST00000598273.5, SELENOW-205, 2437; ENST00000598956.5, SELENOW-206, 1032; ENST00000601937.5, SELENOW-213, 674; ENST00000598083.1, SELENOW-204, 546; ENST00000599627.1, SELENOW-209, 312"	MALAVRVVYCGAUGYKSKYLQLKKKLEDEFPGRLDICGEGTPQATGFFEVMVAGKLIHSKKKGDGYVDTESKFLKLVAAIKAALAQG	chr19:47778677-47784686[+]	Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency (By similarity).	.	HGNC:10752	SELW_HUMAN	Reviewed	ENSG00000178980	.	.	.	.	.
Mol00158	Protein	Secreted frizzled-related protein 1 (SFRP1)	FRP-1; sFRP-1; Secreted apoptosis-related protein 2; SARP-2; FRP; FRP1; SARP2	SFRP1	6422	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000220772.8, SFRP1-201, 4464; ENST00000379845.3, SFRP1-202, 3873"	MGIGRSEGGRRGAALGVLLALGAALLAVGSASEYDYVSFQSDIGPYQSGRFYTKPPQCVDIPADLRLCHNVGYKKMVLPNLLEHETMAEVKQQASSWVPLLNKNCHAGTQVFLCSLFAPVCLDRPIYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEGDVCIAMTPPNATEASKPQGTTVCPPCDNELKSEAIIEHLCASEFALRMKIKEVKKENGDKKIVPKKKKPLKLGPIKKKDLKKLVLYLKNGADCPCHQLDNLSHHFLIMGRKVKSQYLLTAIHKWDKKNKEFKNFMKKMKNHECPTFQSVFK	chr8:41261962-41309473[-]	"Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase (By similarity). In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription."	.	HGNC:10776	SFRP1_HUMAN	Reviewed	ENSG00000104332	.	.	.	.	.
Mol00159	Protein	SHC-transforming protein 1 (SHC1)	SHC-transforming protein 3; SHC-transforming protein A; Src homology 2 domain-containing-transforming protein C1; SH2 domain protein C1; SHC; SHCA	SHC1	6464	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000448116.7, SHC1-210, 3481; ENST00000368445.9, SHC1-202, 3472; ENST00000368453.8, SHC1-205, 3062; ENST00000368450.5, SHC1-204, 3059; ENST00000368449.8, SHC1-203, 2879; ENST00000444664.5, SHC1-209, 1305; ENST00000414115.5, SHC1-207, 780; ENST00000366442.2, SHC1-201, 780; ENST00000412170.5, SHC1-206, 692; ENST00000444179.5, SHC1-208, 550; ENST00000490667.1, SHC1-211, 727"	MDLLPPKPKYNPLRNESLSSLEEGASGSTPPEELPSPSASSLGPILPPLPGDDSPTTLCSFFPRMSNLRLANPAGGRPGSKGEPGRAADDGEGIVGAAMPDSGPLPLLQDMNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKL	chr1:154962298-154974395[-]	"Signaling adapter that couples activated growth factor receptors to signaling pathways. Participates in a signaling cascade initiated by activated KIT and KITLG/SCF. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span (By similarity). Participates in signaling downstream of the angiopoietin receptor TEK/TIE2, and plays a role in the regulation of endothelial cell migration and sprouting angiogenesis."	PDB: 1MIL; PDB: 1N3H; PDB: 1OY2; PDB: 1QG1; PDB: 1SHC; PDB: 1TCE; PDB: 2L1C; PDB: 4JMH; PDB: 4XWX; PDB: 5CZI; PDB: 6DM4	HGNC:10840	SHC1_HUMAN	Reviewed	ENSG00000160691	.	.	.	.	.
Mol00160	Protein	Sialyltransferase 4C (SIAT4C)	Alpha 2;3-ST 4; Beta-galactoside alpha-2;3-sialyltransferase 4; Alpha 2;3-sialyltransferase IV; Gal-NAc6S; Gal-beta-1;3-GalNAc-alpha-2;3-sialyltransferase; Gal-beta-1;4-GlcNAc-alpha-2;3-sialyltransferase; N-acetyllactosaminide alpha-2;3-sialyltransferase; SAT-3; ST-4; ST3Gal IV; ST3GalIV; ST3GalA.2; STZ; Sialyltransferase 4C; SIAT4-C; CGS23; NANTA3; SIAT4C; STZ	ST3GAL4	6484	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000444328.7, ST3GAL4-204, 1810; ENST00000526727.5, ST3GAL4-209, 1967; ENST00000534083.5, ST3GAL4-217, 1919; ENST00000532243.5, ST3GAL4-215, 1825; ENST00000227495.10, ST3GAL4-201, 1790; ENST00000392669.6, ST3GAL4-203, 1724; ENST00000530591.5, ST3GAL4-213, 1459; ENST00000676545.1, ST3GAL4-221, 2169; ENST00000356132.9, ST3GAL4-202, 1812; ENST00000678865.1, ST3GAL4-226, 1716; ENST00000677503.1, ST3GAL4-224, 1685; ENST00000449406.6, ST3GAL4-205, 1669; ENST00000524860.1, ST3GAL4-207, 1012; ENST00000534457.5, ST3GAL4-219, 987; ENST00000528858.5, ST3GAL4-212, 763; ENST00000526311.5, ST3GAL4-208, 574; ENST00000534452.5, ST3GAL4-218, 550; ENST00000676867.1, ST3GAL4-223, 1973; ENST00000531217.5, ST3GAL4-214, 1745; ENST00000677721.1, ST3GAL4-225, 1556; ENST00000534733.6, ST3GAL4-220, 545; ENST00000676831.1, ST3GAL4-222, 1759; ENST00000526756.5, ST3GAL4-210, 802; ENST00000524834.5, ST3GAL4-206, 788; ENST00000528605.5, ST3GAL4-211, 1100; ENST00000533826.1, ST3GAL4-216, 1037"	MVSKSRWKLLAMLALVLVVMVWYSISREDRYIELFYFPIPEKKEPCLQGEAESKASKLFGNYSRDQPIFLRLEDYFWVKTPSAYELPYGTKGSEDLLLRVLAITSSSIPKNIQSLRCRRCVVVGNGHRLRNSSLGDAINKYDVVIRLNNAPVAGYEGDVGSKTTMRLFYPESAHFDPKVENNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQIRILNPFFMEIAADKLLSLPMQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDAYNKKQTIHYYEQITLKSMAGSGHNVSQEALAIKRMLEMGAIKNLTSF	chr11:126355640-126440344[+]	"A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc- and Galbeta-(1->4)-GlcNAc-terminated glycoconjugates through an alpha2-3 linkage. Plays a major role in hemostasis. Responsible for sialylation of plasma VWF/von Willebrand factor, preventing its recognition by asialoglycoprotein receptors (ASGPR) and subsequent clearance. Regulates ASGPR-mediated clearance of platelets. Participates in the biosynthesis of the sialyl Lewis X epitopes, both on O- and N-glycans, which are recognized by SELE/E-selectin, SELP/P-selectin and SELL/L-selectin. Essential for selectin-mediated rolling and adhesion of leukocytes during extravasation. Contributes to adhesion and transendothelial migration of neutrophils likely through terminal sialylation of CXCR2. In glycosphingolipid biosynthesis, sialylates GM1 and GA1 gangliosides to form GD1a and GM1b, respectively. Metabolizes brain c-series ganglioside GT1c forming GQ1c. Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major structural component of peripheral nerve myelin."	.	HGNC:10864	SIA4C_HUMAN	Reviewed	ENSG00000110080	.	.	.	.	.
Mol00161	Protein	Sialyltransferase 7B (SIAT7B)	GalNAc alpha-2;6-sialyltransferase II; ST6GalNAc II; ST6GalNAcII; SThM; Sialyltransferase 7B; SIAT7-B; SIAT7B; SIATL1; STHM	ST6GALNAC2	10610	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000225276.10, ST6GALNAC2-201, 1904; ENST00000588920.1, ST6GALNAC2-207, 637; ENST00000588120.5, ST6GALNAC2-206, 746; ENST00000585736.1, ST6GALNAC2-203, 687; ENST00000585390.1, ST6GALNAC2-202, 536; ENST00000586520.5, ST6GALNAC2-204, 744; ENST00000588005.5, ST6GALNAC2-205, 582; ENST00000592979.1, ST6GALNAC2-209, 756; ENST00000592508.1, ST6GALNAC2-208, 287"	MGLPRGSFFWLLLLLTAACSGLLFALYFSAVQRYPGPAAGARDTTSFEAFFQSKASNSWTGKGQACRHLLHLAIQRHPHFRGLFNLSIPVLLWGDLFTPALWDRLSQHKAPYGWRGLSHQVIASTLSLLNGSESAKLFAPPRDTPPKCIRCAVVGNGGILNGSRQGPNIDAHDYVFRLNGAVIKGFERDVGTKTSFYGFTVNTMKNSLVSYWNLGFTSVPQGQDLQYIFIPSDIRDYVMLRSAILGVPVPEGLDKGDRPHAYFGPEASASKFKLLHPDFISYLTERFLKSKLINTHFGDLYMPSTGALMLLTALHTCDQVSAYGFITSNYWKFSDHYFERKMKPLIFYANHDLSLEAALWRDLHKAGILQLYQR	chr17:76565377-76586956[-]	Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins.	PDB: 6APJ; PDB: 6APL	HGNC:10867	SIA7B_HUMAN	Reviewed	ENSG00000070731	.	.	.	.	.
Mol00162	Protein	NAD-dependent protein deacetylase sirtuin-3 (SIRT3)	hSIRT3; Regulatory protein SIR2 homolog 3; SIR2-like protein 3; SIR2L3	SIRT3	23410	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000382743.9, SIRT3-201, 2882; ENST00000529382.5, SIRT3-210, 1225; ENST00000525319.5, SIRT3-204, 1475; ENST00000524564.5, SIRT3-202, 1395; ENST00000532956.5, SIRT3-215, 1235; ENST00000528469.1, SIRT3-207, 763; ENST00000525237.1, SIRT3-203, 430; ENST00000525776.1, SIRT3-205, 365; ENST00000529937.1, SIRT3-211, 2627; ENST00000532837.5, SIRT3-214, 1588; ENST00000526854.5, SIRT3-206, 785; ENST00000529055.5, SIRT3-209, 779; ENST00000530067.1, SIRT3-212, 681; ENST00000528702.5, SIRT3-208, 1251; ENST00000531753.5, SIRT3-213, 593; ENST00000534381.1, SIRT3-216, 561"	MAFWGWRAAAALRLWGRVVERVEAGGGVGPFQACGCRLVLGGRDDVSAGLRGSHGARGEPLDPARPLQRPPRPEVPRAFRRQPRAAAPSFFFSSIKGGRRSISFSVGASSVVGSGGSSDKGKLSLQDVAELIRARACQRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDLPYPEAIFELPFFFHNPKPFFTLAKELYPGNYKPNVTHYFLRLLHDKGLLLRLYTQNIDGLERVSGIPASKLVEAHGTFASATCTVCQRPFPGEDIRADVMADRVPRCPVCTGVVKPDIVFFGEPLPQRFLLHVVDFPMADLLLILGTSLEVEPFASLTEAVRSSVPRLLINRDLVGPLAWHPRSRDVAQLGDVVHGVESLVELLGWTEEMRDLVQRETGKLDGPDK	chr11:215030-236931[-]	"NAD-dependent protein deacetylase. Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues. Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5PO. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels. In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription. Acts as a regulator of ceramide metabolism by mediating deacetylation of ceramide synthases CERS1, CERS2 and CERS6, thereby increasing their activity and promoting mitochondrial ceramide accumulation."	PDB: 3GLR; PDB: 3GLS; PDB: 3GLT; PDB: 3GLU; PDB: 4BN4; PDB: 4BN5; PDB: 4BV3; PDB: 4BVB; PDB: 4BVE; PDB: 4BVF; PDB: 4BVG; PDB: 4BVH; PDB: 4C78; PDB: 4C7B; PDB: 4FVT; PDB: 4FZ3; PDB: 4HD8; PDB: 4JSR; PDB: 4JT8; PDB: 4JT9; PDB: 4O8Z; PDB: 5BWN; PDB: 5BWO; PDB: 5D7N; PDB: 5H4D; PDB: 5Y4H; PDB: 5YTK; PDB: 5Z93; PDB: 5Z94; PDB: 5ZGC; PDB: 6ISO	HGNC:14931	SIR3_HUMAN	Reviewed	ENSG00000142082	.	.	.	.	.
Mol00163	Protein	Mothers against decapentaplegic homolog 2 (SMAD2)	MAD homolog 2; Mothers against DPP homolog 2; JV18-1; Mad-related protein 2; hMAD-2; SMAD family member 2; SMAD 2; Smad2; hSMAD2; MADH2; MADR2	SMAD2	4087	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262160.11, SMAD2-201, 34626; ENST00000402690.6, SMAD2-203, 12075; ENST00000356825.8, SMAD2-202, 10445; ENST00000586040.5, SMAD2-205, 1971; ENST00000591214.5, SMAD2-212, 1714; ENST00000587269.5, SMAD2-208, 1042; ENST00000586514.5, SMAD2-207, 828; ENST00000585978.1, SMAD2-204, 663; ENST00000587421.5, SMAD2-210, 575; ENST00000589877.5, SMAD2-211, 527; ENST00000587353.5, SMAD2-209, 584; ENST00000586487.2, SMAD2-206, 564"	MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTPNTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS	chr18:47808957-47931146[-]	"Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator."	PDB: 1DEV; PDB: 1KHX; PDB: 1U7V; PDB: 2LB3; PDB: 5XOD; PDB: 5ZOJ; PDB: 6M64; PDB: 6YIA; PDB: 6ZVQ; PDB: 7CO1	HGNC:6768	SMAD2_HUMAN	Reviewed	ENSG00000175387	.	.	.	.	.
Mol00164	Protein	Mothers against decapentaplegic homolog 4 (SMAD4)	MAD homolog 4; Mothers against DPP homolog 4; Deletion target in pancreatic carcinoma 4; SMAD family member 4; SMAD 4; Smad4; hSMAD4; DPC4; MADH4	SMAD4	4089	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000342988.8, SMAD4-201, 8772; ENST00000398417.6, SMAD4-202, 8495; ENST00000588745.5, SMAD4-205, 1371; ENST00000588860.5, SMAD4-206, 779; ENST00000589941.1, SMAD4-209, 582; ENST00000589076.5, SMAD4-207, 576; ENST00000593223.1, SMAD4-215, 568; ENST00000590061.1, SMAD4-210, 544; ENST00000611848.2, SMAD4-216, 2906; ENST00000592186.5, SMAD4-213, 1306; ENST00000592911.5, SMAD4-214, 475; ENST00000688574.1, SMAD4-221, 8307; ENST00000691124.1, SMAD4-224, 5780; ENST00000684953.1, SMAD4-217, 5164; ENST00000591126.5, SMAD4-212, 4970; ENST00000685090.1, SMAD4-218, 4891; ENST00000685232.1, SMAD4-219, 2883; ENST00000688903.1, SMAD4-222, 1963; ENST00000690892.1, SMAD4-223, 1223; ENST00000688307.1, SMAD4-220, 1146; ENST00000586253.1, SMAD4-204, 784; ENST00000589706.1, SMAD4-208, 563; ENST00000590499.1, SMAD4-211, 545; ENST00000585448.1, SMAD4-203, 459"	MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTSQPASILGGSHSEGLLQIASGPQPGQQQNGFTGQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD	chr18:51028394-51085045[+]	"In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator."	PDB: 1DD1; PDB: 1G88; PDB: 1MR1; PDB: 1U7F; PDB: 1U7V; PDB: 1YGS; PDB: 5C4V; PDB: 5MEY; PDB: 5MEZ; PDB: 5MF0; PDB: 5UWU; PDB: 6YIC	HGNC:6770	SMAD4_HUMAN	Reviewed	ENSG00000141646	.	.	.	.	.
Mol00165	Protein	Zinc finger protein SNAI1 (SNAI1)	Protein snail homolog 1; Protein sna; SNAH	SNAI1	6615	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000244050.3, SNAI1-201, 1705"	MPRSFLVRKPSDPNRKPNYSELQDSNPEFTFQQPYDQAHLLAAIPPPEILNPTASLPMLIWDSVLAPQAQPIAWASLRLQESPRVAELTSLSDEDSGKGSQPPSPPSPAPSSFSSTSVSSLEAEAYAAFPGLGQVPKQLAQLSEAKDLQARKAFNCKYCNKEYLSLGALKMHIRSHTLPCVCGTCGKAFSRPWLLQGHVRTHTGEKPFSCPHCSRAFADRSNLRAHLQTHSDVKKYQCQACARTFSRMSLLHKHQESGCSGCPR	chr20:49982980-49988886[+]	"Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. The N-terminal SNAG domain competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (in vitro). During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3. In addition, may also activate the CDKN2B promoter by itself."	PDB: 2Y48; PDB: 3W5K; PDB: 3ZMT; PDB: 4QLI	HGNC:11128	SNAI1_HUMAN	Reviewed	ENSG00000124216	.	.	.	.	.
Mol00166	Protein	Suppressor of cytokine signaling 1 (SOCS1)	SOCS-1; JAK-binding protein; JAB; STAT-induced STAT inhibitor 1; SSI-1; Tec-interacting protein 3; TIP-3; SSI1; TIP3	SOCS1	8651	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000332029.4, SOCS1-201, 1238; ENST00000644787.1, SOCS1-202, 1784"	MVAHNQVAADNAVSTAAEPRRRPEPSSSSSSSPAAPARPRPCPAVPAPAPGDTHFRTFRSHADYRRITRASALLDACGFYWGPLSVHGAHERLRAEPVGTFLVRDSRQRNCFFALSVKMASGPTSIRVHFQAGRFHLDGSRESFDCLFELLEHYVAAPRRMLGAPLRQRRVRPLQELCRQRIVATVGRENLARIPLNPVLRDYLSSFPFQI	chr16:11254417-11256204[-]	"SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS1 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Through binding to JAKs and IFNGR1, inhibits their kinase activity. In vitro, also suppresses Tec protein-tyrosine activity. Appears to be a major regulator of signaling by interleukin 6 (IL6) and leukemia inhibitory factor (LIF). Regulates interferon-gamma mediated sensory neuron survival (By similarity). Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize JAK2. SOCS1 appears to be a negative regulator in IGF1R signaling pathway."	.	HGNC:19383	SOCS1_HUMAN	Reviewed	ENSG00000185338	.	.	.	.	.
Mol00167	Protein	Suppressor of cytokine signaling 2 (SOCS2)	SOCS-2; Cytokine-inducible SH2 protein 2; CIS-2; STAT-induced STAT inhibitor 2; SSI-2; CIS2; SSI2; STATI2	SOCS2	8835	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000551556.2, SOCS2-210, 2386; ENST00000622746.4, SOCS2-212, 2881; ENST00000340600.6, SOCS2-201, 2761; ENST00000549122.5, SOCS2-206, 2391; ENST00000549206.5, SOCS2-207, 2072; ENST00000536696.6, SOCS2-202, 1065; ENST00000548537.1, SOCS2-205, 3733; ENST00000549887.1, SOCS2-209, 984; ENST00000548091.5, SOCS2-204, 744; ENST00000551883.1, SOCS2-211, 719; ENST00000549510.1, SOCS2-208, 581; ENST00000547229.1, SOCS2-203, 462"	MTLRCLEPSGNGGEGTRSQWGTAGSAEEPSPQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV	chr12:93569814-93583487[+]	SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.	PDB: 2C9W; PDB: 4JGH; PDB: 5BO4; PDB: 6I4X; PDB: 6I5J; PDB: 6I5N; PDB: 7M6T	HGNC:19382	SOCS2_HUMAN	Reviewed	ENSG00000120833	.	.	.	.	.
Mol00168	Protein	Suppressor of cytokine signaling 5 (SOCS5)	SOCS-5; Cytokine-inducible SH2 protein 6; CIS-6; Cytokine-inducible SH2-containing protein 5; CIS6; CISH5; CISH6; KIAA0671	SOCS5	9655	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000394861.3, SOCS5-202, 4766; ENST00000306503.5, SOCS5-201, 4771; ENST00000650009.1, SOCS5-204, 839; ENST00000568862.1, SOCS5-203, 2463"	MDKVGKMWNNFKYRCQNLFGHEGGSRSENVDMNSNRCLSVKEKNISIGDSTPQQQSSPLRENIALQLGLSPSKNSSRRNQNCATEIPQIVEISIEKDNDSCVTPGTRLARRDSYSRHAPWGGKKKHSCSTKTQSSLDADKKFGRTRSGLQRRERRYGVSSVHDMDSVSSRTVGSRSLRQRLQDTVGLCFPMRTYSKQSKPLFSNKRKIHLSELMLEKCPFPAGSDLAQKWHLIKQHTAPVSPHSTFFDTFDPSLVSTEDEEDRLRERRRLSIEEGVDPPPNAQIHTFEATAQVNPLYKLGPKLAPGMTEISGDSSAIPQANCDSEEDTTTLCLQSRRQKQRQISGDSHTHVSRQGAWKVHTQIDYIHCLVPDLLQITGNPCYWGVMDRYEAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYNRSLHARIEQWNHNFSFDAHDPCVFHSSTVTGLLEHYKDPSSCMFFEPLLTISLNRTFPFSLQYICRAVICRCTTYDGIDGLPLPSMLQDFLKEYHYKQKVRVRWLEREPVKAK	chr2:46698952-46780245[+]	SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Inhibits for instance EGF signaling by mediating the degradation of the EGF receptor/EGFR. Involved in the regulation of T-helper cell differentiation by inhibiting of the IL4 signaling pathway which promotes differentiation into the Th2 phenotype. Can also partially inhibit IL6 and LIF signaling.	.	HGNC:16852	SOCS5_HUMAN	Reviewed	ENSG00000171150	.	.	.	.	.
Mol00169	Protein	Transcription factor SOX-2 (SOX2)	.	SOX2	6657	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000325404.3, SOX2-201, 2512"	MYNMMETELKPPGPQQTSGGGGGNSTAAAAGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGAGVNQRMDSYAHMNGWSNGSYSMMQDQLGYPQHPGLNAHGAAQMQPMHRYDVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMSQHYQSGPVPGTAINGTLPLSHM	chr3:181711925-181714436[+]	"Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Binds to the proximal enhancer region of NANOG. Critical for early embryogenesis and for embryonic stem cell pluripotency. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation. May function as a switch in neuronal development."	PDB: 1O4X; PDB: 2LE4; PDB: 6T7B; PDB: 6T90; PDB: 6WX7; PDB: 6WX8; PDB: 6WX9; PDB: 6YOV	HGNC:11195	SOX2_HUMAN	Reviewed	ENSG00000181449	.	.	.	.	.
Mol00170	Protein	Transcription factor SOX-4 (SOX4)	.	SOX4	6659	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000244745.4, SOX4-201, 4869"	MVQQTNNAENTEALLAGESSDSGAGLELGIASSPTPGSTASTGGKADDPSWCKTPSGHIKRPMNAFMVWSQIERRKIMEQSPDMHNAEISKRLGKRWKLLKDSDKIPFIREAERLRLKHMADYPDYKYRPRKKVKSGNANSSSSAAASSKPGEKGDKVGGSGGGGHGGGGGGGSSNAGGGGGGASGGGANSKPAQKKSCGSKVAGGAGGGVSKPHAKLILAGGGGGGKAAAAAAASFAAEQAGAAALLPLGAAADHHSLYKARTPSASASASSAASASAALAAPGKHLAEKKVKRVYLFGGLGTSSSPVGGVGAGADPSDPLGLYEEEGAGCSPDAPSLSGRSSAASSPAAGRSPADHRGYASLRAASPAPSSAPSHASSSASSHSSSSSSSGSSSSDDEFEDDLLDLNPSSNFESMSLGSFSSSSALDRDLDFNFEPGSGSHFEFPDYCTPEVSEMISGDWLESSISNLVFTY	chr6:21593751-21598619[+]	"Transcriptional activator that binds with high affinity to the T-cell enhancer motif 5'-AACAAAG-3' motif. Required for IL17A-producing Vgamma2-positive gamma-delta T-cell maturation and development, via binding to regulator loci of RORC to modulate expression. Involved in skeletal myoblast differentiation by promoting gene expression of CALD1."	.	HGNC:11200	SOX4_HUMAN	Reviewed	ENSG00000124766	.	.	.	.	.
Mol00171	Protein	Transcription factor SOX-9 (SOX9)	.	SOX9	6662	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000245479.3, SOX9-201, 3931"	MNLLDPFMKMTDEQEKGLSGAPSPTMSEDSAGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQPGKADLKREGRPLPEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTYTGSYGISSTAATPASAGHVWMSKQQAPPPPPQQPPQAPPAPQAPPQPQAAPPQQPAAPPQQPQAHTLTTLSSEPGQSQRTHIKTEQLSPSHYSEQQQHSPQQIAYSPFNLPHYSPSYPPITRSQYDYTDHQNSSSYYSHAAGQGTGLYSTFTYMNPAQRPMYTPIADTSGVPSIPQTHSPQHWEQPVYTQLTRP	chr17:72121020-72126416[+]	"Transcription factor that plays a key role in chondrocytes differentiation and skeletal development. Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6. Also binds to some promoter regions. Plays a central role in successive steps of chondrocyte differentiation. Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes. Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis. Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes by lowering beta-catenin (CTNNB1) signaling and RUNX2 expression. Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells and transactivating COL10A1 along with MEF2C. Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. Mechanistically, helps, but is not required, to remove epigenetic signatures of transcriptional repression and deposit active promoter and enhancer marks at chondrocyte-specific genes. Acts in cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3) transcription factors. In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells: involved in the lung epithelium during branching morphogenesis, by balancing proliferation and differentiation and regulating the extracellular matrix. Controls epithelial branching during kidney development."	PDB: 4EUW	HGNC:11204	SOX9_HUMAN	Reviewed	ENSG00000125398	.	.	.	.	.
Mol00172	Protein	Protein sprouty homolog 2 (SPRY2)	Spry-2	SPRY2	10253	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377104.4, SPRY2-202, 2286; ENST00000377102.5, SPRY2-201, 2708"	MEARAQSGNGSQPLLQTPRDGGRQRGEPDPRDALTQQVHVLSLDQIRAIRNTNEYTEGPTVVPRPGLKPAPRPSTQHKHERLHGLPEHRQPPRLQHSQVHSSARAPLSRSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPVADGIIRVQPKSELKPGELKPLSKEDLGLHAYRCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT	chr13:80335976-80341126[-]	"Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2. Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis. Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells. Inhibits CBL/C-CBL-mediated EGFR ubiquitination."	PDB: 3BUM; PDB: 3OB1; PDB: 5HKY; PDB: 5HKZ; PDB: 5HL0	HGNC:11270	SPY2_HUMAN	Reviewed	ENSG00000136158	.	.	.	.	.
Mol00173	Protein	Proto-oncogene tyrosine-protein kinase Src (SRC)	Proto-oncogene c-Src; pp60c-src; p60-Src; SRC1	SRC	6714	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373578.7, SRC-204, 4644; ENST00000692112.1, SRC-212, 4794; ENST00000692423.1, SRC-213, 4762; ENST00000373567.6, SRC-203, 4321; ENST00000358208.9, SRC-201, 4337; ENST00000373558.2, SRC-202, 4304; ENST00000693012.1, SRC-214, 1083; ENST00000477066.5, SRC-207, 3300; ENST00000477475.1, SRC-208, 584; ENST00000497734.5, SRC-211, 446; ENST00000493775.1, SRC-210, 559; ENST00000489153.1, SRC-209, 551; ENST00000467556.1, SRC-205, 502; ENST00000472968.1, SRC-206, 461"	MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL	chr20:37344685-37406050[+]	"Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Involved in anchorage-independent cell growth. Required for podosome formation. Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration."	PDB: 1A07; PDB: 1A08; PDB: 1A09; PDB: 1A1A; PDB: 1A1B; PDB: 1A1C; PDB: 1A1E; PDB: 1FMK; PDB: 1HCS; PDB: 1HCT; PDB: 1KSW; PDB: 1O41; PDB: 1O42; PDB: 1O43; PDB: 1O44; PDB: 1O45; PDB: 1O46; PDB: 1O47; PDB: 1O48; PDB: 1O49; PDB: 1O4A; PDB: 1O4B; PDB: 1O4C; PDB: 1O4D; PDB: 1O4E; PDB: 1O4F; PDB: 1O4G; PDB: 1O4H; PDB: 1O4I; PDB: 1O4J; PDB: 1O4K; PDB: 1O4L; PDB: 1O4M; PDB: 1O4N; PDB: 1O4O; PDB: 1O4P; PDB: 1O4Q; PDB: 1O4R; PDB: 1SHD; PDB: 1Y57; PDB: 1YI6; PDB: 1YOJ; PDB: 1YOL; PDB: 1YOM; PDB: 2BDF; PDB: 2BDJ; PDB: 2H8H; PDB: 2SRC; PDB: 3VRO; PDB: 3ZMP; PDB: 3ZMQ; PDB: 4F59; PDB: 4F5A; PDB: 4F5B; PDB: 4HXJ; PDB: 4K11; PDB: 4MXO; PDB: 4MXX; PDB: 4MXY; PDB: 4MXZ; PDB: 6ATE; PDB: 6C4S; PDB: 6E6E; PDB: 6EHJ; PDB: 7NG7	HGNC:11283	SRC_HUMAN	Reviewed	ENSG00000197122	.	.	.	.	.
Mol00174	Protein	Stathmin (STMN1)	Leukemia-associated phosphoprotein p18; Metablastin; Oncoprotein 18; Op18; Phosphoprotein p19; pp19; Prosolin; Protein Pr22; pp17; C1orf215; LAP18; OP18	STMN1	3925	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000455785.7, STMN1-206, 1443; ENST00000399728.5, STMN1-203, 1712; ENST00000357865.6, STMN1-201, 1137; ENST00000426559.6, STMN1-204, 948; ENST00000374291.5, STMN1-202, 867; ENST00000446334.1, STMN1-205, 665; ENST00000465604.1, STMN1-207, 2947; ENST00000513116.1, STMN1-209, 1783; ENST00000485226.1, STMN1-208, 449"	MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHIEEVRKNKESKDPADETEAD	chr1:25884181-25906991[-]	Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis. Involved in the control of the learned and innate fear (By similarity).	.	HGNC:6510	STMN1_HUMAN	Reviewed	ENSG00000117632	.	.	.	.	.
Mol00175	Protein	Tumor protein p53-inducible nuclear protein 1 (TP53INP1)	Stress-induced protein; p53-dependent damage-inducible nuclear protein 1; p53DINP1; P53DINP1; SIP	TP53INP1	94241	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000342697.5, TP53INP1-201, 5605; ENST00000448464.6, TP53INP1-202, 5631"	MFQRLNKMFVGEVSSSSNQEPEFNEKEDDEWILVDFIDTCTGFSAEEEEEEEDISEESPTEHPSVFSCLPASLECLADTSDSCFLQFESCPMEESWFITPPPCFTAGGLTTIKVETSPMENLLIEHPSMSVYAVHNSCPGLSEATRGTDELHSPSSPRVEAQNEMGQHIHCYVAALAAHTTFLEQPKSFRPSQWIKEHSERQPLNRNSLRRQNLTRDCHPRQVKHNGWVVHQPCPRQYNY	chr8:94925972-94949378[-]	"Antiproliferative and proapoptotic protein involved in cell stress response which acts as a dual regulator of transcription and autophagy. Acts as a positive regulator of autophagy. In response to cellular stress or activation of autophagy, relocates to autophagosomes where it interacts with autophagosome-associated proteins GABARAP, GABARAPL1/L2, MAP1LC3A/B/C and regulates autophagy. Acts as an antioxidant and plays a major role in p53/TP53-driven oxidative stress response. Possesses both a p53/TP53-independent intracellular reactive oxygen species (ROS) regulatory function and a p53/TP53-dependent transcription regulatory function. Positively regulates p53/TP53 and p73/TP73 and stimulates their capacity to induce apoptosis and regulate cell cycle. In response to double-strand DNA breaks, promotes p53/TP53 phosphorylation on 'Ser-46' and subsequent apoptosis. Acts as a tumor suppressor by inducing cell death by an autophagy and caspase-dependent mechanism. Can reduce cell migration by regulating the expression of SPARC."	.	HGNC:18022	T53I1_HUMAN	Reviewed	ENSG00000164938	.	.	.	.	.
Mol00176	Protein	Tafazzin (TAZ)	Taz; Protein G4.5; EFE2; G4.5; TAZ	TAFAZZIN	6901	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000601016.6, TAFAZZIN-213, 1906; ENST00000612460.5, TAFAZZIN-215, 1790; ENST00000613002.4, TAFAZZIN-216, 1485; ENST00000612012.5, TAFAZZIN-214, 1230; ENST00000475699.6, TAFAZZIN-205, 1632; ENST00000369776.8, TAFAZZIN-201, 1596; ENST00000652354.1, TAFAZZIN-226, 1469; ENST00000652390.1, TAFAZZIN-228, 1102; ENST00000651139.1, TAFAZZIN-225, 1037; ENST00000652644.1, TAFAZZIN-230, 980; ENST00000616020.5, TAFAZZIN-221, 891; ENST00000652358.1, TAFAZZIN-227, 832; ENST00000439735.2, TAFAZZIN-203, 567; ENST00000479875.1, TAFAZZIN-208, 399; ENST00000617701.5, TAFAZZIN-222, 2158; ENST00000615986.4, TAFAZZIN-220, 1900; ENST00000652682.1, TAFAZZIN-231, 1812; ENST00000426231.5, TAFAZZIN-202, 864; ENST00000620808.4, TAFAZZIN-223, 773; ENST00000494912.5, TAFAZZIN-211, 2286; ENST00000614595.2, TAFAZZIN-218, 2268; ENST00000652476.1, TAFAZZIN-229, 2247; ENST00000476800.2, TAFAZZIN-207, 2129; ENST00000470127.2, TAFAZZIN-204, 2053; ENST00000615658.5, TAFAZZIN-219, 1937; ENST00000652685.1, TAFAZZIN-232, 1928; ENST00000621647.2, TAFAZZIN-224, 1649; ENST00000483674.3, TAFAZZIN-209, 1483; ENST00000613634.4, TAFAZZIN-217, 1109; ENST00000476679.5, TAFAZZIN-206, 783; ENST00000498029.1, TAFAZZIN-212, 537; ENST00000483780.5, TAFAZZIN-210, 388"	MPLHVKWPFPAVPPLTWTLASSVVMGLVGTYSCFWTKYMNHLTVHNREVLYELIEKRGPATPLITVSNHQSCMDDPHLWGILKLRHIWNLKLMRWTPAAADICFTKELHSHFFSLGKCVPVCRGDGVYQKGMDFILEKLNHGDWVHIFPEGKVNMSSEFLRFKWGIGRLIAECHLNPIILPLWHVGMNDVLPNSPPYFPRFGQKITVLIGKPFSALPVLERLRAENKSAVEMRKALTDFIQEEFQHLKTQAEQLHNHLQPGR	chrX:154411524-154421726[+]	"Acyltransferase required to remodel newly synthesized phospholipid cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or CL), a key component of the mitochondrial inner membrane, with tissue specific acyl chains necessary for adequate mitochondrial function. Its role in cellular physiology is to improve mitochondrial performance. CL is critical for the coassembly of lipids and proteins in mitochondrial membranes, for instance, remodeling of the acyl groups of CL in the mitochondrial inner membrane affects the assembly and stability of respiratory chain complex IV and its supercomplex forms. Catalyzes the transacylacion between phospholipids and lysophospholipids, with the highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation, that means, it exchanges acyl groups between CL and PC by a combination of forward and reverse transacylations. Also catalyzes transacylations between other phospholipids such as phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not regiospecific, it transfers acyl groups into any of the sn-1 and sn-2 positions of the monolysocardiolipin (MLCL), which is an important prerequisite for uniformity and symmetry in CL acyl distribution. Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of an acyl acceptor. CoA-independent, it can reshuffle molecular species within a single phospholipid class. Redistributes fatty acids between MLCL, CL, and other lipids, which prolongs the half-life of CL. Its action is completely reversible, which allows for cyclic changes, such as fission and fusion or bending and flattening of the membrane. Hence, by contributing to the flexibility of the lipid composition, it plays an important role in the dynamics of mitochondria membranes. Essential for the final stage of spermatogenesis, spermatid individualization. Required for the initiation of mitophagy. Required to ensure progression of spermatocytes through meiosis. Exon 7 of human tafazzin is essential for catalysis."	.	HGNC:11577	TAZ_HUMAN	Reviewed	ENSG00000102125	.	.	.	.	.
Mol00177	Protein	Testis development-related protein 1 (TDRG1)	.	TDRG1	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MKRREAVCAHRHFLGTGKPPHPLGRSIPVEPCPGLPAFAEVDLLSLLVPIKISSTPPSGSRLDPQIASSAFPGLGSLGGQDSSGSLVQRASCELESPYEL	.	.	.	.	TDRG1_HUMAN	Reviewed	.	.	.	.	.	.
Mol00178	Protein	Methylcytosine dioxygenase TET2 (TET2)	KIAA1546; Nbla00191	TET2	54790	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000380013.9, TET2-203, 9589; ENST00000540549.5, TET2-209, 10166; ENST00000305737.6, TET2-202, 9233; ENST00000513237.5, TET2-207, 10166; ENST00000413648.2, TET2-204, 4973; ENST00000514870.1, TET2-208, 865; ENST00000265149.9, TET2-201, 9588; ENST00000504042.5, TET2-205, 455; ENST00000505801.1, TET2-206, 391"	MEQDRTNHVEGNRLSPFLIPSPPICQTEPLATKLQNGSPLPERAHPEVNGDTKWHSFKSYYGIPCMKGSQNSRVSPDFTQESRGYSKCLQNGGIKRTVSEPSLSGLLQIKKLKQDQKANGERRNFGVSQERNPGESSQPNVSDLSDKKESVSSVAQENAVKDFTSFSTHNCSGPENPELQILNEQEGKSANYHDKNIVLLKNKAVLMPNGATVSASSVEHTHGELLEKTLSQYYPDCVSIAVQKTTSHINAINSQATNELSCEITHPSHTSGQINSAQTSNSELPPKPAAVVSEACDADDADNASKLAAMLNTCSFQKPEQLQQQKSVFEICPSPAENNIQGTTKLASGEEFCSGSSSNLQAPGGSSERYLKQNEMNGAYFKQSSVFTKDSFSATTTPPPPSQLLLSPPPPLPQVPQLPSEGKSTLNGGVLEEHHHYPNQSNTTLLREVKIEGKPEAPPSQSPNPSTHVCSPSPMLSERPQNNCVNRNDIQTAGTMTVPLCSEKTRPMSEHLKHNPPIFGSSGELQDNCQQLMRNKEQEILKGRDKEQTRDLVPPTQHYLKPGWIELKAPRFHQAESHLKRNEASLPSILQYQPNLSNQMTSKQYTGNSNMPGGLPRQAYTQKTTQLEHKSQMYQVEMNQGQSQGTVDQHLQFQKPSHQVHFSKTDHLPKAHVQSLCGTRFHFQQRADSQTEKLMSPVLKQHLNQQASETEPFSNSHLLQHKPHKQAAQTQPSQSSHLPQNQQQQQKLQIKNKEEILQTFPHPQSNNDQQREGSFFGQTKVEECFHGENQYSKSSEFETHNVQMGLEEVQNINRRNSPYSQTMKSSACKIQVSCSNNTHLVSENKEQTTHPELFAGNKTQNLHHMQYFPNNVIPKQDLLHRCFQEQEQKSQQASVLQGYKNRNQDMSGQQAAQLAQQRYLIHNHANVFPVPDQGGSHTQTPPQKDTQKHAALRWHLLQKQEQQQTQQPQTESCHSQMHRPIKVEPGCKPHACMHTAPPENKTWKKVTKQENPPASCDNVQQKSIIETMEQHLKQFHAKSLFDHKALTLKSQKQVKVEMSGPVTVLTRQTTAAELDSHTPALEQQTTSSEKTPTKRTAASVLNNFIESPSKLLDTPIKNLLDTPVKTQYDFPSCRCVEQIIEKDEGPFYTHLGAGPNVAAIREIMEERFGQKGKAIRIERVIYTGKEGKSSQGCPIAKWVVRRSSSEEKLLCLVRERAGHTCEAAVIVILILVWEGIPLSLADKLYSELTETLRKYGTLTNRRCALNEERTCACQGLDPETCGASFSFGCSWSMYYNGCKFARSKIPRKFKLLGDDPKEEEKLESHLQNLSTLMAPTYKKLAPDAYNNQIEYEHRAPECRLGLKEGRPFSGVTACLDFCAHAHRDLHNMQNGSTLVCTLTREDNREFGGKPEDEQLHVLPLYKVSDVDEFGSVEAQEEKKRSGAIQVLSSFRRKVRMLAEPVKTCRQRKLEAKKAAAEKLSSLENSSNKNEKEKSAPSRTKQTENASQAKQLAELLRLSGPVMQQSQQPQPLQKQPPQPQQQQRPQQQQPHHPQTESVNSYSASGSTNPYMRRPNPVSPYPNSSHTSDIYGSTSPMNFYSTSSQAAGSYLNSSNPMNPYPGLLNQNTQYPSYQCNGNLSVDNCSPYLGSYSPQSQPMDLYRYPSQDPLSKLSLPPIHTLYQPRFGNSQSFTSKYLGYGNQNMQGDGFSSCTIRPNVHHVGKLPPYPTHEMDGHFMGATSRLPPNLSNPNMDYKNGEHHSPSHIIHNYSAAPGMFNSSLHALHLQNKENDMLSHTANGLSKMLPALNHDRTACVQGGLHKLSDANGQEKQPLALVQGVASGAEDNDEVWSDSEQSFLDPDIGGVAVAPTHGSILIECAKRELHATTPLKNPNRNHPTRISLVFYQHKSMNEPKHGLALWEAKMAEKAREKEEECEKYGPDYVPQKSHGKKVKREPAEPHETSEPTYLRFIKSLAERTMSVTTDSTVTTSPYAFTRVTGPYNRYI	chr4:105145875-105279816[+]	"Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT."	PDB: 4NM6; PDB: 5D9Y; PDB: 5DEU	HGNC:25941	TET2_HUMAN	Reviewed	ENSG00000168769	.	.	.	.	.
Mol00179	Protein	Transforming growth factor beta 1 (TGFB1)	LAP; TGF-beta-1; TGFB	TGFB1	7040	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000221930.6, TGFB1-201, 2780; ENST00000600196.2, TGFB1-204, 1250; ENST00000677934.1, TGFB1-205, 1084; ENST00000598758.5, TGFB1-203, 559; ENST00000597453.1, TGFB1-202, 392"	MPPSGLRLLLLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS	chr19:41301587-41353922[-]	"Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively."	.	HGNC:11766	TGFB1_HUMAN	Reviewed	ENSG00000105329	.	.	.	.	.
Mol00180	Protein	TGF-beta receptor type II (TGFBR2)	TGFR-2; TGF-beta type II receptor; Transforming growth factor-beta receptor type II; TGF-beta receptor type II; TbetaR-II	TGFBR2	7048	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000295754.10, TGFBR2-201, 4530; ENST00000359013.4, TGFBR2-202, 4605; ENST00000672866.1, TGFBR2-204, 5794; ENST00000672050.1, TGFBR2-203, 915; ENST00000673250.1, TGFBR2-206, 575; ENST00000673203.1, TGFBR2-205, 2803"	MGRGLLRGLWPLHIVLWTRIASTIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQVTGISLLPPLGVAISVIIIFYCYRVNRQQKLSSTWETGKTRKLMEFSEHCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSGRSCSEEKIPEDGSLNTTK	chr3:30606601-30694142[+]	"Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways."	PDB: 1KTZ; PDB: 1M9Z; PDB: 1PLO; PDB: 2PJY; PDB: 3KFD; PDB: 4P7U; PDB: 4XJJ; PDB: 5E8V; PDB: 5E8Y; PDB: 5E91; PDB: 5E92; PDB: 5QIN; PDB: 5TX4; PDB: 5TY4; PDB: 7DV6	HGNC:11773	TGFR2_HUMAN	Reviewed	ENSG00000163513	.	.	.	.	.
Mol00181	Protein	Metalloproteinase inhibitor 3 (TIMP3)	Protein MIG-5; Tissue inhibitor of metalloproteinases 3; TIMP-3	TIMP3	7078	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000266085.7, TIMP3-201, 4597"	MTPWLGLIVLLGSWSLGDWGAEACTCSPSHPQDAFCNSDIVIRAKVVGKKLVKEGPFGTLVYTIKQMKMYRGFTKMPHVQYIHTEASESLCGLKLEVNKYQYLLTGRVYDGKMYTGLCNFVERWDQLTLSQRKGLNYRYHLGCNCKIKSCYYLPCFVTSKNECLWTDMLSNFGYPGYQSKHYACIRQKGGYCSWYRGWAPPDKSIINATDP	chr22:32801705-32863041[+]	"Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15."	PDB: 3CKI	HGNC:11822	TIMP3_HUMAN	Reviewed	ENSG00000100234	.	.	.	.	.
Mol00182	Protein	Transmembrane protease serine 11E (TM11E)	Serine protease DESC1; Transmembrane protease serine 11E2; DESC1; TMPRSS11E2; UNQ742/PRO1461	TMPRSS11E	28983	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305363.9, TMPRSS11E-201, 2122; ENST00000510647.1, TMPRSS11E-202, 794"	MMYRPDVVRARKRVCWEPWVIGLVIFISLIVLAVCIGLTVHYVRYNQKKTYNYYSTLSFTTDKLYAEFGREASNNFTEMSQRLESMVKNAFYKSPLREEFVKSQVIKFSQQKHGVLAHMLLICRFHSTEDPETVDKIVQLVLHEKLQDAVGPPKVDPHSVKIKKINKTETDSYLNHCCGTRRSKTLGQSLRIVGGTEVEEGEWPWQASLQWDGSHRCGATLINATWLVSAAHCFTTYKNPARWTASFGVTIKPSKMKRGLRRIIVHEKYKHPSHDYDISLAELSSPVPYTNAVHRVCLPDASYEFQPGDVMFVTGFGALKNDGYSQNHLRQAQVTLIDATTCNEPQAYNDAITPRMLCAGSLEGKTDACQGDSGGPLVSSDARDIWYLAGIVSWGDECAKPNKPGVYTRVTALRDWITSKTGI	chr4:68447463-68497604[+]	Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position.	.	HGNC:24465	TM11E_HUMAN	Reviewed	ENSG00000087128	.	.	.	.	.
Mol00183	Protein	Tumor necrosis factor ligand superfamily member 6 (FASLG)	.	FASLG	356	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367721.3, FASLG-202, 1805; ENST00000340030.4, FASLG-201, 917"	MQQPFNYPYPQIYWVDSSASSPWAPPGTVLPCPTSVPRRPGQRRPPPPPPPPPLPPPPPPPPLPPLPLPPLKKRGNHSTGLCLLVMFFMVLVALVGLGLGMFQLFHLQKELAELRESTSQMHTASSLEKQIGHPSPPPEKKELRKVAHLTGKSNSRSMPLEWEDTYGIVLLSGVKYKKGGLVINETGLYFVYSKVYFRGQSCNNLPLSHKVYMRNSKYPQDLVMMEGKMMSYCTTGQMWARSSYLGAVFNLTSADHLYVNVSELSLVNFEESQTFFGLYKL	chr1:172659103-172666876[+]	"Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells. Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development. Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses. TNFRSF6/FAS-mediated apoptosis has also a role in the induction of peripheral tolerance. Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis."	PDB: 4MSV; PDB: 5L19; PDB: 5L36	HGNC:11936	TNFL6_HUMAN	Reviewed	ENSG00000117560	.	.	.	.	.
Mol00184	Protein	T-LAK cell-originated protein kinase(PBK)	Cancer/testis antigen 84; CT84; MAPKK-like protein kinase; Nori-3; PDZ-binding kinase; Spermatogenesis-related protein kinase; SPK; T-LAK cell-originated protein kinase; TOPK	PBK	55872	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000301905.9, PBK-201, 1836; ENST00000522944.5, PBK-203, 1499; ENST00000521226.2, PBK-202, 748; ENST00000524266.1, PBK-204, 819"	MEGISNFKTPSKLSEKKKSVLCSTPTINIPASPFMQKLGFGTGVNVYLMKRSPRGLSHSPWAVKKINPICNDHYRSVYQKRLMDEAKILKSLHHPNIVGYRAFTEANDGSLCLAMEYGGEKSLNDLIEERYKASQDPFPAAIILKVALNMARGLKYLHQEKKLLHGDIKSSNVVIKGDFETIKICDVGVSLPLDENMTVTDPEACYIGTEPWKPKEAVEENGVITDKADIFAFGLTLWEMMTLSIPHINLSNDDDDEDKTFDESDFDDEAYYAALGTRPPINMEELDESYQKVIELFSVCTNEDPKDRPSAAHIVEALETDV	chr8:27809624-27838082[-]	"Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage."	PDB: 5J0A	HGNC:18282	TOPK_HUMAN	Reviewed	ENSG00000168078	.	.	.	.	.
Mol00185	Protein	Tumor protein D52 (TPD52)	Protein N8	TPD52	7163	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000518937.6, TPD52-209, 4116; ENST00000448733.3, TPD52-203, 4339; ENST00000379096.9, TPD52-201, 4041; ENST00000520527.5, TPD52-213, 2638; ENST00000517427.5, TPD52-204, 2596; ENST00000379097.7, TPD52-202, 2563; ENST00000519303.6, TPD52-211, 1594; ENST00000520795.5, TPD52-215, 445; ENST00000517462.6, TPD52-206, 2702; ENST00000521354.5, TPD52-218, 785; ENST00000521241.6, TPD52-217, 723; ENST00000523753.5, TPD52-226, 587; ENST00000518517.5, TPD52-208, 584; ENST00000523395.5, TPD52-224, 773; ENST00000519250.5, TPD52-210, 585; ENST00000520877.5, TPD52-216, 576; ENST00000521561.1, TPD52-219, 570; ENST00000523783.1, TPD52-227, 548; ENST00000523564.2, TPD52-225, 480; ENST00000520035.5, TPD52-212, 462; ENST00000602950.1, TPD52-229, 340; ENST00000523193.5, TPD52-222, 877; ENST00000523319.6, TPD52-223, 863; ENST00000522364.5, TPD52-221, 716; ENST00000521618.1, TPD52-220, 580; ENST00000517445.5, TPD52-205, 461; ENST00000518500.1, TPD52-207, 460; ENST00000520741.1, TPD52-214, 430; ENST00000524194.5, TPD52-228, 334"	MDCREMDLYEDYQSPFDFDAGVNKSYLYLSPSGNSSPPGSPTLQKFGLLRTDPVPEEGEDVAATISATETLSEEEQEELRRELAKVEEEIQTLSQVLAAKEKHLAEIKRKLGINSLQELKQNIAKGWQDVTATSAYKKTSETLSQAGQKASAAFSSVGSVITKKLEDVKNSPTFKSFEEKVENLKSKVGGTKPAGGDFGEVLNSAANASATTTEPLPEKTQESL	chr8:80034745-80231232[-]	.	.	HGNC:12005	TPD52_HUMAN	Reviewed	ENSG00000076554	.	.	.	.	.
Mol00186	Protein	TNF receptor-associated factor 6 (TRAF6)	E3 ubiquitin-protein ligase TRAF6; Interleukin-1 signal transducer; RING finger protein 85; RING-type E3 ubiquitin transferase TRAF6; RNF85	TRAF6	7189	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000526995.6, TRAF6-202, 7885; ENST00000348124.5, TRAF6-201, 2558; ENST00000529150.1, TRAF6-203, 575"	MSLLNCENSCGSSQSESDCCVAMASSCSAVTKDDSVGGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALMDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAASMAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSVIPDSGYISEVRNFQETIHQLEGRLVRQDHQIRELTAKMETQSMYVSELKRTIRTLEDKVAEIEAQQCNGIYIWKIGNFGMHLKCQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPVRQNHEEIMDAKPELLAFQRPTIPRNPKGFGYVTFMHLEALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDAGV	chr11:36483769-36510272[-]	"E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and JUN. Seems to also play a role in dendritic cells (DCs) maturation and/or activation. Represses c-Myb-mediated transactivation, in B-lymphocytes. Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation. Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production."	PDB: 1LB4; PDB: 1LB5; PDB: 1LB6; PDB: 2ECI; PDB: 2JMD; PDB: 3HCS; PDB: 3HCT; PDB: 3HCU; PDB: 4Z8M; PDB: 5ZUJ; PDB: 6A33; PDB: 7L3L	HGNC:12036	TRAF6_HUMAN	Reviewed	ENSG00000175104	.	.	.	.	.
Mol00187	Protein	Tripartite motif-containing protein 14 (TRIM14)	KIAA0129	TRIM14	9830	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000341469.7, TRIM14-201, 4480; ENST00000375098.7, TRIM14-203, 1792; ENST00000342043.3, TRIM14-202, 1479; ENST00000475147.1, TRIM14-204, 639; ENST00000478530.1, TRIM14-206, 982; ENST00000478401.1, TRIM14-205, 814"	MAGAATGSRTPGRSELVEGCGWRCPEHGDRVAELFCRRCRRCVCALCPVLGAHRGHPVGLALEAAVHVQKLSQECLKQLAIKKQQHIDNITQIEDATEKLKANAESSKTWLKGKFTELRLLLDEEEALAKKFIDKNTQLTLQVYREQADSCREQLDIMNDLSNRVWSISQEPDPVQRLQAYTATEQEMQQQMSLGELCHPVPLSFEPVKSFFKGLVEAVESTLQTPLDIRLKESINCQLSDPSSTKPGTLLKTSPSPERSLLLKYARTPTLDPDTMHARLRLSADRLTVRCGLLGSLGPVPVLRFDALWQVLARDCFATGRHYWEVDVQEAGAGWWVGAAYASLRRRGASAAARLGCNRQSWCLKRYDLEYWAFHDGQRSRLRPRDDLDRLGVFLDYEAGVLAFYDVTGGMSHLHTFRATFQEPLYPALRLWEGAISIPRLP	chr9:98069275-98119222[-]	"Plays an essential role in the innate immune defense against viruses and bacteria. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways. Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation. Acts as a scaffold between TBK1 and STAT3 to promote phosphorylation of STAT3 and resolve interferon-stimulated gene (ISG) expression. Inhibits the transcriptional activity of SPI1 in a dose-dependent manner."	PDB: 6JBM	HGNC:16283	TRI14_HUMAN	Reviewed	ENSG00000106785	.	.	.	.	.
Mol00188	Protein	Tripartite motif-containing protein 16 (TRIM16)	E3 ubiquitin-protein ligase TRIM16; Estrogen-responsive B box protein; EBBP	TRIM16	10626	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649191.2, TRIM16-226, 3358; ENST00000578237.5, TRIM16-212, 3206; ENST00000416464.6, TRIM16-202, 3184; ENST00000336708.11, TRIM16-201, 2900; ENST00000577886.5, TRIM16-211, 1979; ENST00000579219.5, TRIM16-214, 999; ENST00000577446.5, TRIM16-210, 791; ENST00000580110.5, TRIM16-219, 580; ENST00000577372.5, TRIM16-209, 560; ENST00000578744.5, TRIM16-213, 552; ENST00000581200.1, TRIM16-221, 486; ENST00000494759.1, TRIM16-207, 426; ENST00000581224.5, TRIM16-222, 815; ENST00000460728.5, TRIM16-203, 793; ENST00000473540.5, TRIM16-205, 760; ENST00000582182.6, TRIM16-223, 581; ENST00000579272.5, TRIM16-215, 568; ENST00000579535.5, TRIM16-216, 567; ENST00000584142.5, TRIM16-225, 565; ENST00000473659.5, TRIM16-206, 559; ENST00000579630.1, TRIM16-217, 550; ENST00000582708.5, TRIM16-224, 521; ENST00000580388.5, TRIM16-220, 516; ENST00000579843.5, TRIM16-218, 459; ENST00000577326.1, TRIM16-208, 920; ENST00000473368.1, TRIM16-204, 471"	MAELDLMAPGPLPRATAQPPAPLSPDSGSPSPDSGSASPVEEEDVGSSEKLGRETEEQDSDSAEQGDPAGEGKEVLCDFCLDDTRRVKAVKSCLTCMVNYCEEHLQPHQVNIKLQSHLLTEPVKDHNWRYCPAHHSPLSAFCCPDQQCICQDCCQEHSGHTIVSLDAARRDKEAELQCTQLDLERKLKLNENAISRLQANQKSVLVSVSEVKAVAEMQFGELLAAVRKAQANVMLFLEEKEQAALSQANGIKAHLEYRSAEMEKSKQELERMAAISNTVQFLEEYCKFKNTEDITFPSVYVGLKDKLSGIRKVITESTVHLIQLLENYKKKLQEFSKEEEYDIRTQVSAVVQRKYWTSKPEPSTREQFLQYAYDITFDPDTAHKYLRLQEENRKVTNTTPWEHPYPDLPSRFLHWRQVLSQQSLYLHRYYFEVEIFGAGTYVGLTCKGIDRKGEERNSCISGNNFSWSLQWNGKEFTAWYSDMETPLKAGPFRRLGVYIDFPGGILSFYGVEYDTMTLVHKFACKFSEPVYAAFWLSKKENAIRIVDLGEEPEKPAPSLVGTAP	chr17:15627960-15684311[-]	"E3 ubiquitin ligase that plays an essential role in the organization of autophagic response and ubiquitination upon lysosomal and phagosomal damages. Plays a role in the stress-induced biogenesis and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2 signaling and particularly by modulating the ubiquitination levels and thus stability of NRF2. Acts as a scaffold protein and facilitates autophagic degradation of protein aggregates by interacting with p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell against oxidative stress-induced cell death as a consequence of endomembrane damage."	.	HGNC:17241	TRI16_HUMAN	Reviewed	ENSG00000221926	.	.	.	.	.
Mol00189	Protein	Thyroid receptor-interacting protein 6 (TRIP6)	TR-interacting protein 6; TRIP-6; Opa-interacting protein 1; OIP-1; Zyxin-related protein 1; ZRP-1; OIP1	TRIP6	7205	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000200457.9, TRIP6-201, 1693; ENST00000619988.4, TRIP6-209, 1303; ENST00000429658.1, TRIP6-203, 646; ENST00000417475.5, TRIP6-202, 992; ENST00000437505.5, TRIP6-204, 875; ENST00000476870.5, TRIP6-206, 1750; ENST00000463125.1, TRIP6-205, 835; ENST00000488670.1, TRIP6-207, 615; ENST00000496260.1, TRIP6-208, 451"	MSGPTWLPPKQPEPARAPQGRAIPRGTPGPPPAHGAALQPHPRVNFCPLPSEQCYQAPGGPEDRGPAWVGSHGVLQHTQGLPADRGGLRPGSLDAEIDLLSSTLAELNGGRGHASRRPDRQAYEPPPPPAYRTGSLKPNPASPLPASPYGGPTPASYTTASTPAGPAFPVQVKVAQPVRGCGPPRRGASQASGPLPGPHFPLPGRGEVWGPGYRSQREPGPGAKEEAAGVSGPAGRGRGGEHGPQVPLSQPPEDELDRLTKKLVHDMNHPPSGEYFGQCGGCGEDVVGDGAGVVALDRVFHVGCFVCSTCRAQLRGQHFYAVERRAYCEGCYVATLEKCATCSQPILDRILRAMGKAYHPGCFTCVVCHRGLDGIPFTVDATSQIHCIEDFHRKFAPRCSVCGGAIMPEPGQEETVRIVALDRSFHIGCYKCEECGLLLSSEGECQGCYPLDGHILCKACSAWRIQELSATVTTDC	chr7:100867387-100873454[+]	"Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor."	PDB: 1X61; PDB: 2DLO	HGNC:12311	TRIP6_HUMAN	Reviewed	ENSG00000087077	.	.	.	.	.
Mol00190	Protein	Thymidylate synthase (TYMS)	TS; TSase; TS; OK/SW-cl.29	TYMS	7298	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000323274.15, TYMS-203, 1613; ENST00000323224.7, TYMS-201, 1327; ENST00000323250.9, TYMS-202, 693; ENST00000581920.1, TYMS-205, 886; ENST00000584122.1, TYMS-206, 534; ENST00000579128.1, TYMS-204, 925"	MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV	chr18:657653-673578[+]	"Catalyzes the reductive methylation of 2'-deoxyuridine 5'-monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1-carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway."	PDB: 1HVY; PDB: 1HW3; PDB: 1HW4; PDB: 1HZW; PDB: 1I00; PDB: 1JU6; PDB: 1JUJ; PDB: 1YPV; PDB: 2ONB; PDB: 2RD8; PDB: 2RDA; PDB: 3EAW; PDB: 3EBU; PDB: 3ED7; PDB: 3EDW; PDB: 3EF9; PDB: 3EGY; PDB: 3EHI; PDB: 3EJL; PDB: 3GG5; PDB: 3GH0; PDB: 3GH2; PDB: 3H9K; PDB: 3HB8; PDB: 3N5E; PDB: 3N5G; PDB: 3OB7; PDB: 4E28; PDB: 4FGT; PDB: 4G2O; PDB: 4G6W; PDB: 4GD7; PDB: 4GYH; PDB: 4H1I; PDB: 4JEF; PDB: 4KPW; PDB: 4O1U; PDB: 4O1X; PDB: 4UP1; PDB: 5HS3; PDB: 5WRN; PDB: 5X4W; PDB: 5X4X; PDB: 5X4Y; PDB: 5X5A; PDB: 5X5D; PDB: 5X5Q; PDB: 5X66; PDB: 5X67; PDB: 5X69; PDB: 6OJU; PDB: 6OJV; PDB: 6PF3; PDB: 6PF4; PDB: 6PF5; PDB: 6PF6; PDB: 6QXG; PDB: 6QXH; PDB: 6QYQ; PDB: 6R2E; PDB: 6ZXO	HGNC:12441	TYSY_HUMAN	Reviewed	ENSG00000176890	.	.	.	.	.
Mol00191	Protein	UV radiation resistance-associated gene protein (UVRAG)	p63	UVRAG	7405	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356136.8, UVRAG-201, 5117; ENST00000531818.5, UVRAG-207, 3152; ENST00000528420.5, UVRAG-205, 2463; ENST00000532130.1, UVRAG-208, 1831; ENST00000533454.5, UVRAG-209, 1823; ENST00000528264.1, UVRAG-204, 511; ENST00000525183.1, UVRAG-202, 1325; ENST00000525872.1, UVRAG-203, 713; ENST00000530501.1, UVRAG-206, 525"	MSASASVGGPVPQPPPGPAAALPPGSAARALHVELPSQQRRLRHLRNIAARNIVNRNGHQLLDTYFTLHLCSTEKIYKEFYRSEVIKNSLNPTWRSLDFGIMPDRLDTSVSCFVVKIWGGKENIYQLLIEWKVCLDGLKYLGQQIHARNQNEIIFGLNDGYYGAPFEHKGYSNAQKTILLQVDQNCVRNSYDVFSLLRLHRAQCAIKQTQVTVQKIGKEIEEKLRLTSTSNELKKKSECLQLKILVLQNELERQKKALGREVALLHKQQIALQDKGSAFSAEHLKLQLQKESLNELRKECTAKRELFLKTNAQLTIRCRQLLSELSYIYPIDLNEHKDYFVCGVKLPNSEDFQAKDDGSIAVALGYTAHLVSMISFFLQVPLRYPIIHKGSRSTIKDNINDKLTEKEREFPLYPKGGEKLQFDYGVYLLNKNIAQLRYQHGLGTPDLRQTLPNLKNFMEHGLMVRCDRHHTSSAIPVPKRQSSIFGGADVGFSGGIPSPDKGHRKRASSENERLQYKTPPPSYNSALAQPVTTVPSMGETERKITSLSSSLDTSLDFSKENKKKGEDLVGSLNGGHANVHPSQEQGEALSGHRATVNGTLLPSEQAGSASVQLPGEFHPVSEAELCCTVEQAEEIIGLEATGFASGDQLEAFNCIPVDSAVAVECDEQVLGEFEEFSRRIYALNENVSSFRRPRRSSDK	chr11:75815210-76144232[+]	"Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P). During autophagy acts as regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3. Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2. Involved in maturation of autophagosomes and degradative endocytic trafficking independently of BECN1 but depending on its association with a class C Vps complex (possibly the HOPS complex); the association is also proposed to promote autophagosome recruitment and activation of Rab7 and endosome-endosome fusion events. Enhances class C Vps complex (possibly HOPS complex) association with a SNARE complex and promotes fusogenic SNARE complex formation during late endocytic membrane fusion. In case of negative-strand RNA virus infection is required for efficient virus entry, promotes endocytic transport of virions and is implicated in a VAMP8-specific fusogenic SNARE complex assembly."	PDB: 7BL1	HGNC:12640	UVRAG_HUMAN	Reviewed	ENSG00000198382	.	.	.	.	.
Mol00192	Protein	Vascular endothelial growth factor A (VEGFA)	VEGF-A; Vascular permeability factor; VPF; VEGF	VEGFA	7422	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000672860.3, VEGFA-226, 3609; ENST00000372067.8, VEGFA-205, 3535; ENST00000372064.9, VEGFA-204, 2909; ENST00000372077.8, VEGFA-206, 2834; ENST00000372055.9, VEGFA-203, 1286; ENST00000520948.5, VEGFA-222, 1199; ENST00000413642.8, VEGFA-207, 1197; ENST00000482630.7, VEGFA-213, 1146; ENST00000417285.7, VEGFA-208, 1081; ENST00000230480.10, VEGFA-201, 993; ENST00000324450.11, VEGFA-202, 954; ENST00000523950.5, VEGFA-225, 954; ENST00000523873.5, VEGFA-224, 784; ENST00000518689.5, VEGFA-218, 630; ENST00000518824.5, VEGFA-219, 606; ENST00000523125.5, VEGFA-223, 541; ENST00000457104.6, VEGFA-210, 414; ENST00000425836.8, VEGFA-209, 3535; ENST00000519767.5, VEGFA-220, 970; ENST00000520265.1, VEGFA-221, 336; ENST00000480614.1, VEGFA-212, 12167; ENST00000497139.5, VEGFA-215, 2746; ENST00000476772.5, VEGFA-211, 1683; ENST00000493786.2, VEGFA-214, 551; ENST00000518538.5, VEGFA-217, 535; ENST00000512683.1, VEGFA-216, 475"	MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR	chr6:43770184-43786487[+]	"Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development. Also binds the DEAR/FBXW7-AS1 receptor."	PDB: 1BJ1; PDB: 1CZ8; PDB: 1FLT; PDB: 1KAT; PDB: 1KMX; PDB: 1MJV; PDB: 1MKG; PDB: 1MKK; PDB: 1QTY; PDB: 1TZH; PDB: 1TZI; PDB: 1VGH; PDB: 1VPF; PDB: 1VPP; PDB: 2FJG; PDB: 2FJH; PDB: 2QR0; PDB: 2VGH; PDB: 2VPF; PDB: 3BDY; PDB: 3P9W; PDB: 3QTK; PDB: 3S1B; PDB: 3S1K; PDB: 3V2A; PDB: 4DEQ; PDB: 4GLN; PDB: 4GLS; PDB: 4KZN; PDB: 4QAF; PDB: 4WPB; PDB: 4ZFF; PDB: 5DN2; PDB: 5FV1; PDB: 5FV2; PDB: 5HHC; PDB: 5HHD; PDB: 5O4E; PDB: 5T89; PDB: 6BFT; PDB: 6D3O; PDB: 6T9D; PDB: 6V7K; PDB: 6Z13; PDB: 6Z3F; PDB: 6ZBR; PDB: 6ZCD; PDB: 6ZFL; PDB: 7LL8; PDB: 7LL9	HGNC:12680	VEGFA_HUMAN	Reviewed	ENSG00000112715	.	.	.	.	.
Mol00193	Protein	EGFR-coamplified and overexpressed protein (ECOP)	EGFR-coamplified and overexpressed protein; ECop; Glioblastoma-amplified secreted protein; Putative NF-kappa-B-activating protein 055N; ECOP; GASP	VOPP1	81552	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000285279.10, VOPP1-201, 2939; ENST00000433959.5, VOPP1-208, 2900; ENST00000625836.2, VOPP1-217, 1400; ENST00000418904.5, VOPP1-204, 1317; ENST00000427700.1, VOPP1-205, 632; ENST00000454227.5, VOPP1-212, 610; ENST00000428648.5, VOPP1-207, 2866; ENST00000428097.5, VOPP1-206, 1671; ENST00000453256.5, VOPP1-211, 649; ENST00000417399.5, VOPP1-203, 591; ENST00000455023.5, VOPP1-213, 574; ENST00000414113.5, VOPP1-202, 539; ENST00000452832.5, VOPP1-209, 485; ENST00000471168.1, VOPP1-215, 582; ENST00000453112.5, VOPP1-210, 552; ENST00000462326.5, VOPP1-214, 536; ENST00000481197.5, VOPP1-216, 583"	MRRQPAKVAALLLGLLLECTEAKKHCWYFEGLYPTYYICRSYEDCCGSRCCVRALSIQRLWYFWFLLMMGVLFCCGAGFFIRRRMYPPPLIEEPAFNVSYTRQPPNPGPGAQQPGPPYYTDPGGPGMNPVGNSMAMAFQVPPNSPQGSVACPPPPAYCNTPPPPYEQVVKAK	chr7:55436056-55572988[-]	"Increases the transcriptional activity of NFKB1 by facilitating its nuclear translocation, DNA-binding and associated apoptotic response, when overexpressed."	.	HGNC:34518	VOPP1_HUMAN	Reviewed	ENSG00000154978	.	.	.	.	.
Mol00194	Protein	E3 ubiquitin-protein ligase XIAP (XIAP)	Baculoviral IAP repeat-containing protein 4; IAP-like protein; ILP; hILP; Inhibitor of apoptosis protein 3; IAP-3; hIAP-3; hIAP3; RING-type E3 ubiquitin transferase XIAP; X-linked inhibitor of apoptosis protein; X-linked IAP; API3; BIRC4; IAP3	XIAP	331	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371199.8, XIAP-202, 8558; ENST00000355640.3, XIAP-201, 8584; ENST00000434753.7, XIAP-205, 8415; ENST00000430625.1, XIAP-204, 528; ENST00000422098.5, XIAP-203, 390; ENST00000468691.5, XIAP-207, 764; ENST00000496602.1, XIAP-209, 628; ENST00000481776.5, XIAP-208, 598; ENST00000497640.1, XIAP-210, 533; ENST00000497906.5, XIAP-211, 495; ENST00000468503.1, XIAP-206, 157"	MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS	chrX:123859724-123913976[+]	"Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Ubiquitinates and therefore mediates the proteosomal degradation of BCL2 in response to apoptosis. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program."	PDB: 1C9Q; PDB: 1F9X; PDB: 1G3F; PDB: 1G73; PDB: 1I3O; PDB: 1I4O; PDB: 1I51; PDB: 1KMC; PDB: 1NW9; PDB: 1TFQ; PDB: 1TFT; PDB: 2ECG; PDB: 2JK7; PDB: 2KNA; PDB: 2OPY; PDB: 2OPZ; PDB: 2POI; PDB: 2POP; PDB: 2QRA; PDB: 2VSL; PDB: 3CLX; PDB: 3CM2; PDB: 3CM7; PDB: 3EYL; PDB: 3G76; PDB: 3HL5; PDB: 3UW4; PDB: 3UW5; PDB: 4EC4; PDB: 4HY0; PDB: 4IC2; PDB: 4IC3; PDB: 4J3Y; PDB: 4J44; PDB: 4J45; PDB: 4J46; PDB: 4J47; PDB: 4J48; PDB: 4KJU; PDB: 4KJV; PDB: 4KMP; PDB: 4MTZ; PDB: 4OXC; PDB: 4WVS; PDB: 4WVT; PDB: 4WVU; PDB: 5C0K; PDB: 5C0L; PDB: 5C3H; PDB: 5C3K; PDB: 5C7A; PDB: 5C7B; PDB: 5C7C; PDB: 5C7D; PDB: 5C83; PDB: 5C84; PDB: 5M6E; PDB: 5M6F; PDB: 5M6H; PDB: 5M6L; PDB: 5M6M; PDB: 5O6T; PDB: 5OQW; PDB: 6EY2; PDB: 6GJW; PDB: 6QCI	HGNC:592	XIAP_HUMAN	Reviewed	ENSG00000101966	.	.	.	.	.
Mol00195	Protein	Transcriptional coactivator YAP1 (YAP1)	Yes-associated protein 1; Protein yorkie homolog; Yes-associated protein YAP65 homolog; YAP65	YAP1	10413	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000282441.10, YAP1-201, 5401; ENST00000615667.4, YAP1-210, 5398; ENST00000537274.5, YAP1-209, 5350; ENST00000345877.6, YAP1-202, 5284; ENST00000526343.5, YAP1-204, 2393; ENST00000524575.5, YAP1-203, 1638; ENST00000531439.5, YAP1-208, 1490; ENST00000629586.2, YAP1-211, 1365; ENST00000529029.1, YAP1-207, 1415; ENST00000528834.1, YAP1-206, 1025; ENST00000526594.1, YAP1-205, 785"	MDPGQQPPPQPAPQGQGQPPSQPPQGQGPPSGPGQPAPAATQAAPQAPPAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTPTGVVSGPAATPTAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPRKAMLSQMNVTAPTSPPVQQNMMNSASGPLPDGWEQAMTQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPQGGVMGGSNSNQQQQMRLQQLQMEKERLRLKQQELLRQAMRNINPSTANSPKCQELALRSQLPTLEQDGGTQNPVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSSDILNDMESVLAATKLDKESFLTWL	chr11:102110447-102233424[+]	"Transcriptional regulator which can act both as a coactivator and a corepressor and is the critical downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Plays a key role in tissue tension and 3D tissue shape by regulating cortical actomyosin network formation. Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization. Plays a key role in controlling cell proliferation in response to cell contact. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. The presence of TEAD transcription factors are required for it to stimulate gene expression, cell growth, anchorage-independent growth, and epithelial mesenchymal transition (EMT) induction. Suppresses ciliogenesis via acting as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1. In conjunction with WWTR1, involved in the regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation."	PDB: 1JMQ; PDB: 1K5R; PDB: 1K9Q; PDB: 1K9R; PDB: 2LAW; PDB: 2LAX; PDB: 2LAY; PDB: 2LTV; PDB: 2LTW; PDB: 3KYS; PDB: 3MHR; PDB: 4RE1; PDB: 4REX; PDB: 5OAQ; PDB: 5YDX; PDB: 5YDY; PDB: 6G6X; PDB: 6G8I; PDB: 6G8J; PDB: 6G8K; PDB: 6G8L; PDB: 6G8P; PDB: 6G8Q; PDB: 6GE3; PDB: 6GE4; PDB: 6GE5; PDB: 6GE6; PDB: 6GEC; PDB: 6GEE; PDB: 6GEG; PDB: 6GEI; PDB: 6GEK; PDB: 6HIK; PDB: 6HIL; PDB: 6Q2X	HGNC:16262	YAP1_HUMAN	Reviewed	ENSG00000137693	.	.	.	.	.
Mol00196	Protein	Zinc finger E-box-binding homeobox 2 (ZEB2)	Smad-interacting protein 1; SMADIP1; Zinc finger homeobox protein 1b; KIAA0569; SIP1; ZFHX1B; ZFX1B; HRIHFB2411	ZEB2	9839	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000627532.3, ZEB2-226, 9265; ENST00000409487.7, ZEB2-204, 5361; ENST00000539609.7, ZEB2-223, 4061; ENST00000558170.6, ZEB2-224, 4012; ENST00000636471.1, ZEB2-235, 9583; ENST00000638087.1, ZEB2-244, 9339; ENST00000637304.1, ZEB2-240, 9158; ENST00000638007.1, ZEB2-243, 9140; ENST00000637045.1, ZEB2-238, 9091; ENST00000636413.1, ZEB2-233, 8984; ENST00000638128.1, ZEB2-245, 8932; ENST00000636026.2, ZEB2-231, 5172; ENST00000440875.6, ZEB2-210, 4939; ENST00000303660.8, ZEB2-201, 3913; ENST00000465070.5, ZEB2-215, 2949; ENST00000637267.2, ZEB2-239, 2677; ENST00000470879.5, ZEB2-217, 2648; ENST00000629520.2, ZEB2-228, 2564; ENST00000427902.5, ZEB2-206, 2236; ENST00000675069.1, ZEB2-248, 2203; ENST00000419938.5, ZEB2-205, 1755; ENST00000647488.1, ZEB2-247, 1654; ENST00000392861.6, ZEB2-202, 1514; ENST00000639389.1, ZEB2-246, 1414; ENST00000465308.5, ZEB2-216, 1071; ENST00000431672.4, ZEB2-207, 709; ENST00000462355.2, ZEB2-214, 656; ENST00000409211.5, ZEB2-203, 587; ENST00000444559.5, ZEB2-211, 577; ENST00000435831.5, ZEB2-209, 554; ENST00000630572.2, ZEB2-230, 468; ENST00000637873.1, ZEB2-242, 100; ENST00000636732.2, ZEB2-236, 5073; ENST00000689298.1, ZEB2-250, 4090; ENST00000636445.1, ZEB2-234, 2947; ENST00000484313.3, ZEB2-221, 845; ENST00000434448.5, ZEB2-208, 583; ENST00000636820.1, ZEB2-237, 9115; ENST00000636179.1, ZEB2-232, 8984; ENST00000629955.1, ZEB2-229, 1435; ENST00000453352.5, ZEB2-212, 581; ENST00000479735.1, ZEB2-220, 543; ENST00000637591.2, ZEB2-241, 480; ENST00000472146.5, ZEB2-218, 3837; ENST00000625161.1, ZEB2-225, 3061; ENST00000675145.1, ZEB2-249, 3014; ENST00000628473.1, ZEB2-227, 2967; ENST00000461784.3, ZEB2-213, 751; ENST00000497268.1, ZEB2-222, 674; ENST00000476394.5, ZEB2-219, 601"	MKQPIMADGPRCKRRKQANPRRKNVVNYDNVVDTGSETDEEDKLHIAEDDGIANPLDQETSPASVPNHESSPHVSQALLPREEEEDEIREGGVEHPWHNNEILQASVDGPEEMKEDYDTMGPEATIQTAINNGTVKNANCTSDFEEYFAKRKLEERDGHAVSIEEYLQRSDTAIIYPEAPEELSRLGTPEANGQEENDLPPGTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNEENFSCPLCSYTFAYRTQLERHMVTHKPGTDQHQMLTQGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCIGLISVNGRMRNNIKTGSSPNSVSSSPTNSAITQLRNKLENGKPLSMSEQTGLLKIKTEPLDFNDYKVLMATHGFSGTSPFMNGGLGATSPLGVHPSAQSPMQHLGVGMEAPLLGFPTMNSNLSEVQKVLQIVDNTVSRQKMDCKAEEISKLKGYHMKDPCSQPEEQGVTSPNIPPVGLPVVSHNGATKSIIDYTLEKVNEAKACLQSLTTDSRRQISNIKKEKLRTLIDLVTDDKMIENHNISTPFSCQFCKESFPGPIPLHQHERYLCKMNEEIKAVLQPHENIVPNKAGVFVDNKALLLSSVLSEKGMTSPINPYKDHMSVLKAYYAMNMEPNSDELLKISIAVGLPQEFVKEWFEQRKVYQYSNSRSPSLERSSKPLAPNSNPPTKDSLLPRSPVKPMDSITSPSIAELHNSVTNCDPPLRLTKPSHFTNIKPVEKLDHSRSNTPSPLNLSSTSSKNSHSSSYTPNSFSSEELQAEPLDLSLPKQMKEPKSIIATKNKTKASSISLDHNSVSSSSENSDEPLNLTFIKKEFSNSNNLDNKSTNPVFSMNPFSAKPLYTALPPQSAFPPATFMPPVQTSIPGLRPYPGLDQMSFLPHMAYTYPTGAATFADMQQRRKYQRKQGFQGELLDGAQDYMSGLDDMTDSDSCLSRKKIKKTESGMYACDLCDKTFQKSSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAEREAREKGHLEPTELLMNRAYLQSITPQGYSDSEERESMPRDGESEKEHEKEGEDGYGKLGRQDGDEEFEEEEEESENKSMDTDPETIRDEEETGDHSMDDSSEDGKMETKSDHEEDNMEDGM	chr2:144364364-144521057[-]	Transcriptional inhibitor that binds to DNA sequence 5'-CACCT-3' in different promoters. Represses transcription of E-cadherin. Represses expression of MEOX2.	PDB: 2DA7	HGNC:14881	ZEB2_HUMAN	Reviewed	ENSG00000169554	.	.	.	.	.
Mol00197	Protein	E3 ubiquitin-protein ligase ZNRF2 (ZNRF2)	Protein Ells2; RING finger protein 202; RING-type E3 ubiquitin transferase ZNRF2; Zinc/RING finger protein 2; RNF202	ZNRF2	223082	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000323037.5, ZNRF2-201, 3167; ENST00000459998.1, ZNRF2-202, 489"	MGAKQSGPAAANGRTRAYSGSDLPSSSSGGANGTAGGGGGARAAAAGRFPAQVPSAHQPSASGGAAAAAAAPAAPAAPRSRSLGGAVGSVASGARAAQSPFSIPNSSSGPYGSQDSVHSSPEDGGGGRDRPVGGSPGGPRLVIGSLPAHLSPHMFGGFKCPVCSKFVSSDEMDLHLVMCLTKPRITYNEDVLSKDAGECAICLEELQQGDTIARLPCLCIYHKGCIDEWFEVNRSCPEHPSD	chr7:30284597-30367689[+]	May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.	.	HGNC:22316	ZNRF2_HUMAN	Reviewed	ENSG00000180233	.	.	.	.	.
Mol00198	Protein	Protein zeta/delta 14-3-3 (YWHAZ)	Protein kinase C inhibitor protein 1; KCIP-1	YWHAZ	7534	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000395958.6, YWHAZ-207, 5011; ENST00000395957.6, YWHAZ-206, 5248; ENST00000457309.2, YWHAZ-211, 3007; ENST00000395956.7, YWHAZ-205, 2974; ENST00000353245.7, YWHAZ-201, 2829; ENST00000395953.6, YWHAZ-204, 994; ENST00000395951.7, YWHAZ-203, 964; ENST00000419477.6, YWHAZ-209, 891; ENST00000521309.5, YWHAZ-216, 1399; ENST00000522542.5, YWHAZ-219, 1394; ENST00000418997.1, YWHAZ-208, 996; ENST00000522819.5, YWHAZ-220, 875; ENST00000395948.6, YWHAZ-202, 812; ENST00000521607.5, YWHAZ-218, 750; ENST00000437293.5, YWHAZ-210, 701; ENST00000523938.1, YWHAZ-223, 626; ENST00000523131.1, YWHAZ-221, 567; ENST00000521328.5, YWHAZ-217, 511; ENST00000523848.5, YWHAZ-222, 664; ENST00000492736.1, YWHAZ-213, 681; ENST00000480304.5, YWHAZ-212, 2247; ENST00000518736.5, YWHAZ-215, 883; ENST00000517727.5, YWHAZ-214, 876"	MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN	chr8:100916523-100953388[-]	"Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and membrane ruffle formation. In neurons, regulates spine maturation through the modulation of ARHGEF7 activity."	PDB: 1IB1; PDB: 1QJA; PDB: 1QJB; PDB: 2C1J; PDB: 2C1N; PDB: 2O02; PDB: 2WH0; PDB: 3CU8; PDB: 3NKX; PDB: 3RDH; PDB: 4BG6; PDB: 4FJ3; PDB: 4HKC; PDB: 4IHL; PDB: 4N7G; PDB: 4N7Y; PDB: 4N84; PDB: 4WRQ; PDB: 4ZDR; PDB: 5D2D; PDB: 5D3F; PDB: 5EWZ; PDB: 5EXA; PDB: 5J31; PDB: 5JM4; PDB: 5M35; PDB: 5M36; PDB: 5M37; PDB: 5NAS; PDB: 5ULO; PDB: 5WXN; PDB: 5XY9; PDB: 6EF5; PDB: 6EJL; PDB: 6EWW; PDB: 6F08; PDB: 6F09; PDB: 6FN9; PDB: 6FNA; PDB: 6FNB; PDB: 6FNC; PDB: 6Q0K; PDB: 6RLZ; PDB: 6U2H; PDB: 6XAG; PDB: 6YMO; PDB: 6YO8; PDB: 6YOS; PDB: 6ZFD; PDB: 6ZFG; PDB: 7D8H; PDB: 7D8P; PDB: 7D9V	HGNC:12855	1433Z_HUMAN	Reviewed	ENSG00000164924	.	.	.	.	.
Mol00199	Protein	PP2A subunit A isoform R1-beta (PPP2R1B)	PP2A subunit A isoform PR65-beta; PP2A subunit A isoform R1-beta	PPP2R1B	5519	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000527614.6, PPP2R1B-206, 5553; ENST00000311129.9, PPP2R1B-201, 2082; ENST00000341980.10, PPP2R1B-202, 1953; ENST00000426998.6, PPP2R1B-204, 1888; ENST00000393055.6, PPP2R1B-203, 1525; ENST00000531890.1, PPP2R1B-210, 670; ENST00000531373.1, PPP2R1B-209, 553; ENST00000534521.5, PPP2R1B-212, 2294; ENST00000534500.5, PPP2R1B-211, 582; ENST00000530787.1, PPP2R1B-208, 131; ENST00000526287.1, PPP2R1B-205, 101; ENST00000529672.1, PPP2R1B-207, 874"	MAGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKELGENLPIEDRETIIMNQILPYIKELVSDTNQHVKSALASVIMGLSTILGKENTIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA	chr11:111726908-111766389[-]	The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.	.	HGNC:9303	2AAB_HUMAN	Reviewed	ENSG00000137713	.	.	.	.	.
Mol00200	Protein	Cytosolic purine 5'-nucleotidase (NT5C2)	Cytosolic 5'-nucleotidase II; cN-II; Cytosolic IMP/GMP-specific 5'-nucleotidase; Cytosolic nucleoside phosphotransferase 5'N; High Km 5'-nucleotidase; NT5B; NT5CP; PNT5	NT5C2	22978	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000404739.8, NT5C2-203, 3525; ENST00000676449.1, NT5C2-227, 3670; ENST00000674696.1, NT5C2-215, 3497; ENST00000343289.9, NT5C2-201, 3435; ENST00000676428.1, NT5C2-226, 3425; ENST00000675326.1, NT5C2-221, 3118; ENST00000674860.1, NT5C2-217, 3614; ENST00000675985.1, NT5C2-225, 3413; ENST00000675645.1, NT5C2-223, 2648; ENST00000421281.1, NT5C2-204, 440; ENST00000674728.1, NT5C2-216, 4917; ENST00000675164.1, NT5C2-220, 4688; ENST00000675040.1, NT5C2-219, 3506; ENST00000675020.1, NT5C2-218, 3470; ENST00000369857.9, NT5C2-202, 3449; ENST00000675811.1, NT5C2-224, 3360; ENST00000675436.1, NT5C2-222, 3192; ENST00000470299.2, NT5C2-211, 1099; ENST00000461461.5, NT5C2-207, 902; ENST00000452156.5, NT5C2-205, 856; ENST00000552185.5, NT5C2-214, 642; ENST00000487810.5, NT5C2-213, 669; ENST00000467380.1, NT5C2-208, 427; ENST00000481549.1, NT5C2-212, 421; ENST00000470228.5, NT5C2-210, 891; ENST00000458345.5, NT5C2-206, 597; ENST00000469228.1, NT5C2-209, 495"	MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEEE	chr10:103087185-103277605[-]	"Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine. Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP. Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency. Through these activities regulates the purine nucleoside/nucleotide pools within the cell."	PDB: 2J2C; PDB: 2JC9; PDB: 2JCM; PDB: 2XCV; PDB: 2XCW; PDB: 2XCX; PDB: 2XJB; PDB: 2XJC; PDB: 2XJD; PDB: 2XJE; PDB: 2XJF; PDB: 4H4B; PDB: 5CQZ; PDB: 5CR7; PDB: 5K7Y; PDB: 5L4Z; PDB: 5L50; PDB: 5OPK; PDB: 5OPL; PDB: 5OPM; PDB: 5OPN; PDB: 5OPO; PDB: 5OPP; PDB: 6DD3; PDB: 6DDB; PDB: 6DDC; PDB: 6DDH; PDB: 6DDK; PDB: 6DDL; PDB: 6DDO; PDB: 6DDQ; PDB: 6DDX; PDB: 6DDY; PDB: 6DDZ; PDB: 6DE0; PDB: 6DE1; PDB: 6DE2; PDB: 6DE3; PDB: 6FIR; PDB: 6FIS; PDB: 6FIU; PDB: 6FIW; PDB: 6FXH	HGNC:8022	5NTC_HUMAN	Reviewed	ENSG00000076685	.	.	.	.	.
Mol00202	Protein	Autophagy-related protein 16-1 (ATG16L1)	APG16-like 1; APG16L; UNQ9393/PRO34307	ATG16L1	55054	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000392017.9, ATG16L1-203, 3298; ENST00000392018.1, ATG16L1-204, 3313; ENST00000392020.8, ATG16L1-205, 3213; ENST00000347464.9, ATG16L1-201, 2915; ENST00000373525.9, ATG16L1-202, 2767; ENST00000444735.5, ATG16L1-210, 691; ENST00000417017.5, ATG16L1-207, 684; ENST00000419681.5, ATG16L1-208, 644; ENST00000431917.5, ATG16L1-209, 589; ENST00000392021.7, ATG16L1-206, 3301; ENST00000498620.5, ATG16L1-218, 740; ENST00000464645.5, ATG16L1-211, 560; ENST00000474148.5, ATG16L1-214, 4208; ENST00000479942.5, ATG16L1-215, 3559; ENST00000472242.1, ATG16L1-212, 911; ENST00000473865.1, ATG16L1-213, 805; ENST00000492298.5, ATG16L1-217, 591; ENST00000485623.5, ATG16L1-216, 568"	MSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRVPATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKAVLWAQY	chr2:233210051-233295674[+]	"Plays an essential role in both canonical and non-canonical autophagy: interacts with ATG12-ATG5 to mediate the lipidation to ATG8 family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP). Acts as a molecular hub, coordinating autophagy pathways via distinct domains that support either canonical or non-canonical signaling. During canonical autophagy, interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to ATG8 proteins, to produce a membrane-bound activated form of ATG8. Thereby, controls the elongation of the nascent autophagosomal membrane. Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, probably by catalyzing conjugation of phosphatidylserine (PS) to ATG8. Non-canonical autophagy plays a key role in epithelial cells to limit lethal infection by influenza A (IAV) virus. Regulates mitochondrial antiviral signaling (MAVS)-dependent type I interferon (IFN-I) production. Negatively regulates NOD1- and NOD2-driven inflammatory cytokine response. Instead, promotes with NOD2 an autophagy-dependent antibacterial pathway. Plays a role in regulating morphology and function of Paneth cell."	PDB: 4GDK; PDB: 4GDL; PDB: 4NAW; PDB: 4TQ0; PDB: 5D7G; PDB: 5NPV; PDB: 5NPW; PDB: 5NUV; PDB: 5ZYX	HGNC:21498	A16L1_HUMAN	Reviewed	ENSG00000085978	.	.	.	.	.
Mol00203	Protein	Mth938 domain-containing protein (AAMDC)	Adipogenesis associated Mth938 domain-containing protein; C11orf67; PTD015	AAMDC	28971	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393427.7, AAMDC-202, 522; ENST00000527134.5, AAMDC-207, 693; ENST00000304716.12, AAMDC-201, 619; ENST00000526415.5, AAMDC-206, 579; ENST00000630098.2, AAMDC-212, 542; ENST00000525034.1, AAMDC-203, 511; ENST00000532481.5, AAMDC-210, 690; ENST00000533193.5, AAMDC-211, 606; ENST00000525409.5, AAMDC-204, 421; ENST00000526164.5, AAMDC-205, 726; ENST00000529666.1, AAMDC-208, 440; ENST00000531855.1, AAMDC-209, 458"	MTSPEIASLSWGQMKVKGSNTTYKDCKVWPGGSRTWDWRETGTEHSPGVQPADVKEVVEKGVQTLVIGRGMSEALKVPSSTVEYLKKHGIDVRVLQTEQAVKEYNALVAQGVRVGGVFHSTC	chr11:77821109-77918432[+]	May play a role in preadipocyte differentiation and adipogenesis.	PDB: 2AB1; PDB: 2Q4Q	HGNC:30205	AAMDC_HUMAN	Reviewed	ENSG00000087884	.	.	.	.	.
Mol00204	Protein	ATP-binding cassette sub-family A1 (ABCA1)	ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; Cholesterol efflux regulatory protein; ABC1; CERP	ABCA1	19	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374736.8, ABCA1-202, 10408; ENST00000678995.1, ABCA1-205, 10413; ENST00000423487.6, ABCA1-203, 1540; ENST00000374733.1, ABCA1-201, 923; ENST00000494467.1, ABCA1-204, 807"	MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV	chr9:104781006-104928155[-]	"Catalyzes the translocation of specific phospholipids from the cytoplasmic to the extracellular/lumenal leaflet of membrane coupled to the hydrolysis of ATP. Thereby, participates in phospholipid transfer to apoliproteins to form nascent high density lipoproteins/HDLs. Transports preferentially phosphatidylcholine over phosphatidylserine. May play a similar role in the efflux of intracellular cholesterol to apoliproteins and the formation of nascent high density lipoproteins/HDLs."	PDB: 5XJY	HGNC:29	ABCA1_HUMAN	Reviewed	ENSG00000165029	.	.	.	.	.
Mol00205	Protein	ATP-binding cassette sub-family A10 (ABCA10)	.	ABCA10	10349	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000690296.1, ABCA10-213, 6008; ENST00000269081.8, ABCA10-201, 6362; ENST00000521538.5, ABCA10-205, 531; ENST00000522787.5, ABCA10-207, 362; ENST00000522406.5, ABCA10-206, 6125; ENST00000518929.5, ABCA10-202, 5375; ENST00000523419.5, ABCA10-208, 4875; ENST00000523512.5, ABCA10-209, 1311; ENST00000524273.1, ABCA10-211, 584; ENST00000519732.5, ABCA10-203, 2183; ENST00000521526.2, ABCA10-204, 568; ENST00000524231.5, ABCA10-210, 1267; ENST00000588514.1, ABCA10-212, 472"	MNKMALASFMKGRTVIGTPDEETMDIELPKKYHEMVGVIFSDTFSYRLKFNWGYRIPVIKEHSEYTEHCWAMHGEIFCYLAKYWLKGFVAFQAAINAAIIEVTTNHSVMEELTSVIGINMKIPPFISKGEIMNEWFHFTCLVSFSSFIYFASLNVARERGKFKKLMTVMGLRESAFWLSWGLTYICFIFIMSIFMALVITSIPIVFHTGFMVIFTLYSLYGLSLIALAFLMSVLIRKPMLAGLAGFLFTVFWGCLGFTVLYRQLPLSLGWVLSLLSPFAFTAGMAQITHLDNYLSGVIFPDPSGDSYKMIATFFILAFDTLFYLIFTLYFERVLPDKDGHGDSPLFFLKSSFWSKHQNTHHEIFENEINPEHSSDDSFEPVSPEFHGKEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLKRKWGIGYHLSLHRNEMCDTEKITSLIKQHIPDAKLTTESEEKLVYSLPLEKTNKFPDLYSDLDKCSDQGIRNYAVSVTSLNEVFLNLEGKSAIDEPDFDIGKQEKIHVTRNTGDESEMEQVLCSLPETRKAVSSAALWRRQIYAVATLRFLKLRRERRALLCLLLVLGIAFIPIILEKIMYKVTRETHCWEFSPSMYFLSLEQIPKTPLTSLLIVNNTGSNIEDLVHSLKCQDIVLEIDDFRNRNGSDDPSYNGAIIVSGDQKDYRFSVACNTKKLNCFPVLMGIVSNALMGIFNFTELIQMESTSFSRDDIVLDLGFIDGSIFLLLITNCVSPFIGMSSISDYKKNVQSQLWISGLWPSAYWCGQALVDIPLYFLILFSIHLIYYFIFLGFQLSWELMFVLVVCIIGCAVSLIFLTYVLSFIFRKWRKNNGFWSFGFFIILICVSTIMVSTQYEKLNLILCMIFIPSFTLLGYVMLLIQLDFMRNLDSLDNRINEVNKTILLTTLIPYLQSVIFLFVIRCLEMKYGNEIMNKDPVFRISPRSRETHPNPEEPEEEDEDVQAERVQAANALTAPNLEEEPVITASCLHKEYYETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGRDYLLEIKMKEPTQVEALHTEILKLFPQAAWQERYSSLMAYKLPVEDVHPLSRAFFKLEAMKQTFNLEEYSLSQATLEQVFLELCKEQELGNVDDKIDTTVEWKLLPQEDP	chr17:69147214-69244846[-]	Probable transporter which may play a role in macrophage lipid transport and homeostasis.	.	HGNC:30	ABCAA_HUMAN	Reviewed	ENSG00000154263	.	.	.	.	.
Mol00206	Protein	ATP-binding cassette sub-family F2 (ABCF2)	Iron-inhibited ABC transporter 2; HUSSY-18	ABCF2	10061	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000287844.7, ABCF2-201, 4527; ENST00000468073.5, ABCF2-203, 1031; ENST00000441774.1, ABCF2-202, 941; ENST00000473874.1, ABCF2-204, 648; ENST00000477252.1, ABCF2-205, 249"	MPSDLAKKKAAKKKEAAKARQRPRKGHEENGDVVTEPQVAEKNEANGRETTEVDLLTKELEDFEMKKAAARAVTGVLASHPNSTDVHIINLSLTFHGQELLSDTKLELNSGRRYGLIGLNGIGKSMLLSAIGKREVPIPEHIDIYHLTREMPPSDKTPLHCVMEVDTERAMLEKEAERLAHEDAECEKLMELYERLEELDADKAEMRASRILHGLGFTPAMQRKKLKDFSGGWRMRVALARALFIRPFMLLLDEPTNHLDLDACVWLEEELKTFKRILVLVSHSQDFLNGVCTNIIHMHNKKLKYYTGNYDQYVKTRLELEENQMKRFHWEQDQIAHMKNYIARFGHGSAKLARQAQSKEKTLQKMMASGLTERVVSDKTLSFYFPPCGKIPPPVIMVQNVSFKYTKDGPCIYNNLEFGIDLDTRVALVGPNGAGKSTLLKLLTGELLPTDGMIRKHSHVKIGRYHQHLQEQLDLDLSPLEYMMKCYPEIKEKEEMRKIIGRYGLTGKQQVSPIRNLSDGQKCRVCLAWLAWQNPHMLFLDEPTNHLDIETIDALADAINEFEGGMMLVSHDFRLIQQVAQEIWVCEKQTITKWPGDILAYKEHLKSKLVDEEPQLTKRTHNV	chr7:151211484-151227205[-]	.	.	HGNC:71	ABCF2_HUMAN	Reviewed	ENSG00000033050	.	.	.	.	.
Mol00207	Protein	ATP-binding cassette sub-family E1 (ABCE1)	2'-5'-oligoadenylate-binding protein; HuHP68; RNase L inhibitor; Ribonuclease 4 inhibitor; RNS4I; RLI; RNASEL1; RNASELI; RNS4I; OK/SW-cl.40	ABCE1	6059	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000296577.9, ABCE1-201, 3887; ENST00000502586.5, ABCE1-202, 786; ENST00000507193.5, ABCE1-207, 2146; ENST00000504292.1, ABCE1-204, 625; ENST00000502803.5, ABCE1-203, 782; ENST00000506506.5, ABCE1-206, 421; ENST00000510321.1, ABCE1-209, 2529; ENST00000504683.1, ABCE1-205, 759; ENST00000515678.5, ABCE1-210, 750; ENST00000509593.1, ABCE1-208, 582"	MADKLTRIAIVNHDKCKPKKCRQECKKSCPVVRMGKLCIEVTPQSKIAWISETLCIGCGICIKKCPFGALSIVNLPSNLEKETTHRYCANAFKLHRLPIPRPGEVLGLVGTNGIGKSTALKILAGKQKPNLGKYDDPPDWQEILTYFRGSELQNYFTKILEDDLKAIIKPQYVDQIPKAAKGTVGSILDRKDETKTQAIVCQQLDLTHLKERNVEDLSGGELQRFACAVVCIQKADIFMFDEPSSYLDVKQRLKAAITIRSLINPDRYIIVVEHDLSVLDYLSDFICCLYGVPSAYGVVTMPFSVREGINIFLDGYVPTENLRFRDASLVFKVAETANEEEVKKMCMYKYPGMKKKMGEFELAIVAGEFTDSEIMVMLGENGTGKTTFIRMLAGRLKPDEGGEVPVLNVSYKPQKISPKSTGSVRQLLHEKIRDAYTHPQFVTDVMKPLQIENIIDQEVQTLSGGELQRVALALCLGKPADVYLIDEPSAYLDSEQRLMAARVVKRFILHAKKTAFVVEHDFIMATYLADRVIVFDGVPSKNTVANSPQTLLAGMNKFLSQLEITFRRDPNNYRPRINKLNSIKDVEQKKSGNYFFLDD	chr4:145098288-145129524[+]	"Cotranslational quality control factor involved in the No-Go Decay (NGD) pathway. Together with PELO and HBS1L, is required for 48S complex formation from 80S ribosomes and dissociation of vacant 80S ribosomes. Together with PELO and HBS1L, recognizes stalled ribosomes and promotes dissociation of elongation complexes assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and to degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway. Plays a role in the regulation of mRNA turnover. Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA. As part of the PINK1-regulated signaling, ubiquitinated by CNOT4 upon mitochondria damage; this modification generates polyubiquitin signals that recruit autophagy receptors to the mitochondrial outer membrane and initiate mitophagy. RNASEL-specific protein inhibitor which antagonizes the binding of 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) to RNASEL. Negative regulator of the anti-viral effect of the interferon-regulated 2-5A/RNASEL pathway."	PDB: 6ZME; PDB: 6ZVJ; PDB: 7A09	HGNC:69	ABCE1_HUMAN	Reviewed	ENSG00000164163	.	.	.	.	.
Mol00208	Protein	ATP-binding cassette sub-family G1 (ABCG1)	ATP-binding cassette transporter 8; White protein homolog; ABC8; WHT1	ABCG1	9619	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000398449.8, ABCG1-205, 2976; ENST00000398457.6, ABCG1-206, 3119; ENST00000343687.7, ABCG1-201, 3037; ENST00000361802.6, ABCG1-203, 3034; ENST00000347800.6, ABCG1-202, 2923; ENST00000398437.1, ABCG1-204, 3475; ENST00000450121.5, ABCG1-207, 918; ENST00000462050.5, ABCG1-208, 3037; ENST00000472587.5, ABCG1-210, 2903; ENST00000496783.1, ABCG1-211, 1725; ENST00000467818.1, ABCG1-209, 792"	MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGLPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQEKDEGRREMVKEILTALGLLSCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIICTIHQPSAKLFELFDQLYVLSQGQCVYRGKVCNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDHKRDLGGDAEVNPFLWHRPSEEVKQTKRLKGLRKDSSSMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMGVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIDETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER	chr21:42199689-42297244[+]	"Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta-hydroxycholesterol and this transport is coupled to hydrolysis of ATP. The lipid efflux is ALB-dependent. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol."	PDB: 7OZ1; PDB: 7R8C; PDB: 7R8D; PDB: 7R8E	HGNC:73	ABCG1_HUMAN	Reviewed	ENSG00000160179	.	.	.	.	.
Mol00209	Protein	Solute carrier family 21 member 6 (SLC21A6)	Liver-specific organic anion transporter 1; LST-1; OATP-C; Sodium-independent organic anion-transporting polypeptide 2; OATP-2; Solute carrier family 21 member 6; LST1; OATP1B1; OATP2; OATPC; SLC21A6	SLCO1B1	10599	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256958.3, SLCO1B1-201, 2787"	MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFEISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGYYRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNMLRGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYVDLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLETNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVFKYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLSFYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGITYISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAIQVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCIKWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASENGSVMDEANLESLNKNKHFVPSAGADSETHC	chr12:21131194-21239796[+]	"Mediates the Na(+)-independent uptake of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. Involved in the clearance of bile acids and organic anions from the liver."	.	HGNC:10959	SO1B1_HUMAN	Reviewed	ENSG00000134538	.	.	.	.	.
Mol00210	Protein	Solute carrier family 21 member 8 (SLC21A8)	Liver-specific organic anion transporter 2; LST-2; Organic anion transporter 8; Organic anion-transporting polypeptide 8; OATP-8; Solute carrier family 21 member 8; LST2; OATP1B3; OATP8; SLC21A8	SLCO1B3	28234	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000381545.8, SLCO1B3-202, 3013; ENST00000261196.6, SLCO1B3-201, 2840; ENST00000544370.1, SLCO1B3-204, 1771; ENST00000540853.5, SLCO1B3-203, 1002; ENST00000545880.1, SLCO1B3-205, 339"	MDQHQHLNKTAESASSEKKKTRRCNGFKMFLAALSFSYIAKALGGIIMKISITQIERRFDISSSLAGLIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCLLMGTGSILTSLPHFFMGYYRYSKETHINPSENSTSSLSTCLINQTLSFNGTSPEIVEKDCVKESGSHMWIYVFMGNMLRGIGETPIVPLGISYIDDFAKEGHSSLYLGSLNAIGMIGPVIGFALGSLFAKMYVDIGYVDLSTIRITPKDSRWVGAWWLGFLVSGLFSIISSIPFFFLPKNPNKPQKERKISLSLHVLKTNDDRNQTANLTNQGKNVTKNVTGFFQSLKSILTNPLYVIFLLLTLLQVSSFIGSFTYVFKYMEQQYGQSASHANFLLGIITIPTVATGMFLGGFIIKKFKLSLVGIAKFSFLTSMISFLFQLLYFPLICESKSVAGLTLTYDGNNSVASHVDVPLSYCNSECNCDESQWEPVCGNNGITYLSPCLAGCKSSSGIKKHTVFYNCSCVEVTGLQNRNYSAHLGECPRDNTCTRKFFIYVAIQVINSLFSATGGTTFILLTVKIVQPELKALAMGFQSMVIRTLGGILAPIYFGALIDKTCMKWSTNSCGAQGACRIYNSVFFGRVYLGLSIALRFPALVLYIVFIFAMKKKFQGKDTKASDNERKVMDEANLEFLNNGEHFVPSAGTDSKTCNLDMQDNAAAN	chr12:20810702-20916911[+]	"Mediates the Na(+)-independent uptake of organic anions such as 17-beta-glucuronosyl estradiol, taurocholate, triiodothyronine (T3), leukotriene C4, dehydroepiandrosterone sulfate (DHEAS), methotrexate and sulfobromophthalein (BSP). Involved in the clearance of bile acids and organic anions from the liver."	.	HGNC:10961	SO1B3_HUMAN	Reviewed	ENSG00000111700	.	.	.	.	.
Mol00211	Protein	Fatty acid CoA ligase Acsl3 (ACSL3)	Arachidonate--CoA ligase; Long-chain acyl-CoA synthetase 3; LACS 3; Long-chain-fatty-acid--CoA ligase 3; Medium-chain acyl-CoA ligase Acsl3; ACS3; FACL3; LACS3	ACSL3	2181	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357430.8, ACSL3-201, 5577; ENST00000679514.1, ACSL3-212, 5574; ENST00000680921.1, ACSL3-229, 5544; ENST00000680395.1, ACSL3-222, 5539; ENST00000681383.1, ACSL3-234, 5537; ENST00000681697.1, ACSL3-235, 5524; ENST00000680147.1, ACSL3-219, 5500; ENST00000679558.1, ACSL3-216, 5464; ENST00000680251.1, ACSL3-220, 5433; ENST00000680684.1, ACSL3-227, 5341; ENST00000392066.7, ACSL3-202, 3147; ENST00000679545.1, ACSL3-214, 5468; ENST00000679541.1, ACSL3-213, 5417; ENST00000681009.1, ACSL3-230, 5022; ENST00000413316.1, ACSL3-204, 650; ENST00000540115.1, ACSL3-210, 624; ENST00000681906.1, ACSL3-236, 6794; ENST00000680420.1, ACSL3-223, 5680; ENST00000680475.1, ACSL3-225, 5652; ENST00000680525.1, ACSL3-226, 5545; ENST00000680736.1, ACSL3-228, 5479; ENST00000681292.1, ACSL3-232, 5341; ENST00000407441.5, ACSL3-203, 5244; ENST00000680424.1, ACSL3-224, 5311; ENST00000679546.1, ACSL3-215, 2131; ENST00000421680.2, ACSL3-205, 639; ENST00000679932.1, ACSL3-217, 8441; ENST00000680100.1, ACSL3-218, 6769; ENST00000681326.1, ACSL3-233, 6741; ENST00000681017.1, ACSL3-231, 4538; ENST00000680382.1, ACSL3-221, 1900; ENST00000535678.2, ACSL3-209, 1762; ENST00000474422.1, ACSL3-207, 760; ENST00000495541.1, ACSL3-208, 749; ENST00000463813.1, ACSL3-206, 509; ENST00000542810.1, ACSL3-211, 428"	MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPVNSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPNGKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK	chr2:222860942-222944639[+]	"Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins). Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity."	.	HGNC:3570	ACSL3_HUMAN	Reviewed	ENSG00000123983	.	.	.	.	.
Mol00212	Protein	Activin receptor-like kinase 7 (ALK7)	Activin receptor type IC; ACTR-IC; Activin receptor-like kinase 7; ALK-7; ALK7	ACVR1C	130399	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000243349.13, ACVR1C-201, 8853; ENST00000409680.7, ACVR1C-204, 1786; ENST00000335450.7, ACVR1C-202, 1501; ENST00000348328.9, ACVR1C-203, 1270"	MTRALCSALRQALLLLAAAAELSPGLKCVCLLCDSSNFTCQTEGACWASVMLTNGKEQVIKSCVSLPELNAQVFCHSSNNVTKTECCFTDFCNNITLHLPTASPNAPKLGPMELAIIITVPVCLLSIAAMLTVWACQGRQCSYRKKKRPNVEEPLSECNLVNAGKTLKDLIYDVTASGSGSGLPLLVQRTIARTIVLQEIVGKGRFGEVWHGRWCGEDVAVKIFSSRDERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSEYHEQGSLYDYLNRNIVTVAGMIKLALSIASGLAHLHMEIVGTQGKPAIAHRDIKSKNILVKKCETCAIADLGLAVKHDSILNTIDIPQNPKVGTKRYMAPEMLDDTMNVNIFESFKRADIYSVGLVYWEIARRCSVGGIVEEYQLPYYDMVPSDPSIEEMRKVVCDQKFRPSIPNQWQSCEALRVMGRIMRECWYANGAARLTALRIKKTISQLCVKEDCKA	chr2:157526767-157628864[-]	"Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis."	.	HGNC:18123	ACV1C_HUMAN	Reviewed	ENSG00000123612	.	.	.	.	.
Mol00213	Protein	TNF alpha converting enzyme (ADAM17)	.	ADAM17	6868	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000310823.8, ADAM17-201, 4391; ENST00000648002.1, ADAM17-207, 656; ENST00000649227.1, ADAM17-211, 3488; ENST00000647979.1, ADAM17-206, 2839; ENST00000650116.1, ADAM17-215, 2813; ENST00000647610.1, ADAM17-204, 2513; ENST00000618923.2, ADAM17-203, 1883; ENST00000648548.1, ADAM17-208, 4242; ENST00000648857.1, ADAM17-209, 3327; ENST00000649686.1, ADAM17-212, 1761; ENST00000649972.1, ADAM17-214, 6573; ENST00000647622.1, ADAM17-205, 5715; ENST00000650241.1, ADAM17-216, 4055; ENST00000478059.1, ADAM17-202, 1073; ENST00000649068.1, ADAM17-210, 501; ENST00000649798.1, ADAM17-213, 467"	MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVVGEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQSPKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLKEGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGNAEDDTVCLDLGKCKDGKCIPFCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLSINTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHPSNVEMLSSMDSASVRIIKPFPAPQTPGRLQPAPVIPSAPAAPKLDHQRMDTIQEDPSTDSHMDEDGFEKDPFPNSSTAAKSFEDLTDHPVTRSEKAASFKLQRQNRVDSKETEC	chr2:9488486-9556732[-]	"Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R. Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells."	PDB: 1BKC; PDB: 1ZXC; PDB: 2A8H; PDB: 2DDF; PDB: 2FV5; PDB: 2FV9; PDB: 2I47; PDB: 2M2F; PDB: 2OI0; PDB: 3B92; PDB: 3CKI; PDB: 3E8R; PDB: 3EDZ; PDB: 3EWJ; PDB: 3G42; PDB: 3KMC; PDB: 3KME; PDB: 3L0T; PDB: 3L0V; PDB: 3LE9; PDB: 3LEA; PDB: 3LGP; PDB: 3O64	HGNC:195	ADA17_HUMAN	Reviewed	ENSG00000151694	.	.	.	.	.
Mol00214	Protein	Metalloproteinase-disintegrin ADAM22-3 (ADAM22)	ADAM 22; Metalloproteinase-disintegrin ADAM22-3; Metalloproteinase-like; disintegrin-like; and cysteine-rich protein 2; MDC2	ADAM22	53616	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000413139.2, ADAM22-207, 9508; ENST00000398204.8, ADAM22-204, 9334; ENST00000398209.7, ADAM22-205, 9144; ENST00000265727.11, ADAM22-201, 2891; ENST00000398201.8, ADAM22-202, 2784; ENST00000684002.1, ADAM22-214, 3998; ENST00000683525.1, ADAM22-213, 2857; ENST00000398203.8, ADAM22-203, 2694; ENST00000426930.5, ADAM22-208, 1259; ENST00000412441.5, ADAM22-206, 726; ENST00000682337.1, ADAM22-212, 2361; ENST00000476330.1, ADAM22-210, 613; ENST00000478920.1, ADAM22-211, 511; ENST00000439864.5, ADAM22-209, 2576"	MQAAVAVSVPFLLLCVLGTCPPARCGQAGDASLMELEKRKENRFVERQSIVPLRLIYRSGGEDESRHDALDTRVRGDLGGPQLTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVKGGEHCYYQGHIRGNPDSFVALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVYKSRLFEFSLDDLPSEFQQVNITPSKFILKPRPKRSKRQLRRYPRNVEEETKYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRDFIKEKSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECVLEGAECCKKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIHKMDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPVASFNFSTCLSSKEGTICSGNGVCSNELKCVCNRHWIGSDCNTYFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDSFYSDIPPGVSTNSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNLGGNKKKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEDKKVNRQSARLWETSI	chr7:87934143-88202889[+]	Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1.	PDB: 3G5C; PDB: 5Y2Z; PDB: 5Y31; PDB: 7CQF	HGNC:201	ADA22_HUMAN	Reviewed	ENSG00000008277	.	.	.	.	.
Mol00215	Protein	ADP/ATP translocase 2 (ANT2)	ADP;ATP carrier protein 2; ADP;ATP carrier protein; fibroblast isoform; Adenine nucleotide translocator 2; ANT 2; Solute carrier family 25 member 5; AAC2; ANT2	SLC25A5	292	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000317881.9, SLC25A5-201, 1307; ENST00000460013.1, SLC25A5-202, 775; ENST00000475354.1, SLC25A5-204, 483; ENST00000463551.1, SLC25A5-203, 433"	MTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQITADKQYKGIIDCVVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKRTQFWLYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKAGAEREFRGLGDCLVKIYKSDGIKGLYQGFNVSVQGIIIYRAAYFGIYDTAKGMLPDPKNTHIVISWMIAQTVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGGKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT	chrX:119468422-119471396[+]	"ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane. In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity. Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis. Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A5/ANT2 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it. Probably mediates mitochondrial uncoupling in tissues that do not express UCP1. Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death. It is however unclear if SLC25A5/ANT2 constitutes a pore-forming component of mPTP or regulates it. Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation."	.	HGNC:10991	ADT2_HUMAN	Reviewed	ENSG00000005022	.	.	.	.	.
Mol00216	Protein	Anterior gradient protein 2 homolog (AGR2)	AG-2; hAG-2; HPC8; Secreted cement gland protein XAG-2 homolog; AG2; UNQ515/PRO1030	AGR2	10551	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000419304.7, AGR2-203, 1697; ENST00000401412.5, AGR2-201, 782; ENST00000450569.5, AGR2-204, 671; ENST00000412973.1, AGR2-202, 670; ENST00000486219.1, AGR2-206, 117; ENST00000468419.1, AGR2-205, 585; ENST00000489523.5, AGR2-207, 572"	MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL	chr7:16791811-16833433[-]	"Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells. Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion."	PDB: 2LNS; PDB: 2LNT	HGNC:328	AGR2_HUMAN	Reviewed	ENSG00000106541	.	.	.	.	.
Mol00217	Protein	Adhesion G protein-coupled receptor A2 (ADGRA2)	G-protein coupled receptor 124; Tumor endothelial marker 5; GPR124; KIAA1531; TEM5	ADGRA2	25960	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000412232.3, ADGRA2-202, 6944; ENST00000315215.11, ADGRA2-201, 6270; ENST00000428068.5, ADGRA2-203, 571"	MGAGGRRMRGAPARLLLPLLPWLLLLLAPEARGAPGCPLSIRSCKCSGERPKGLSGGVPGPARRRVVCSGGDLPEPPEPGLLPNGTVTLLLSNNKITGLRNGSFLGLSLLEKLDLRNNIISTVQPGAFLGLGELKRLDLSNNRIGCLTSETFQGLPRLLRLNISGNIFSSLQPGVFDELPALKVVDLGTEFLTCDCHLRWLLPWAQNRSLQLSEHTLCAYPSALHAQALGSLQEAQLCCEGALELHTHHLIPSLRQVVFQGDRLPFQCSASYLGNDTRIRWYHNRAPVEGDEQAGILLAESLIHDCTFITSELTLSHIGVWASGEWECTVSMAQGNASKKVEIVVLETSASYCPAERVANNRGDFRWPRTLAGITAYQSCLQYPFTSVPLGGGAPGTRASRRCDRAGRWEPGDYSHCLYTNDITRVLYTFVLMPINASNALTLAHQLRVYTAEAASFSDMMDVVYVAQMIQKFLGYVDQIKELVEVMVDMASNLMLVDEHLLWLAQREDKACSRIVGALERIGGAALSPHAQHISVNARNVALEAYLIKPHSYVGLTCTAFQRREGGVPGTRPGSPGQNPPPEPEPPADQQLRFRCTTGRPNVSLSSFHIKNSVALASIQLPPSLFSSLPAALAPPVPPDCTLQLLVFRNGRLFHSHSNTSRPGAAGPGKRRGVATPVIFAGTSGCGVGNLTEPVAVSLRHWAEGAEPVAAWWSQEGPGEAGGWTSEGCQLRSSQPNVSALHCQHLGNVAVLMELSAFPREVGGAGAGLHPVVYPCTALLLLCLFATIITYILNHSSIRVSRKGWHMLLNLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLHYSSLSTLLWMGVKARVLHKELTWRAPPPQEGDPALPTPSPMLRFYLIAGGIPLIICGITAAVNIHNYRDHSPYCWLVWRPSLGAFYIPVALILLITWIYFLCAGLRLRGPLAQNPKAGNSRASLEAGEELRGSTRLRGSGPLLSDSGSLLATGSARVGTPGPPEDGDSLYSPGVQLGALVTTHFLYLAMWACGALAVSQRWLPRVVCSCLYGVAASALGLFVFTHHCARRRDVRASWRACCPPASPAAPHAPPRALPAAAEDGSPVFGEGPPSLKSSPSGSSGHPLALGPCKLTNLQLAQSQVCEAGAAAGGEGEPEPAGTRGNLAHRHPNNVHHGRRAHKSRAKGHRAGEACGKNRLKALRGGAAGALELLSSESGSLHNSPTDSYLGSSRNSPGAGLQLEGEPMLTPSEGSDTSAAPLSEAGRAGQRRSASRDSLKGGGALEKESHRRSYPLNAASLNGAPKGGKYDDVTLMGAEVASGGCMKTGLWKSETTV	chr8:37784191-37844896[+]	"Endothelial receptor which functions together with RECK to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B). Plays a key role in Wnt7-specific responses, such as endothelial cell sprouting and migration in the forebrain and neural tube, and establishment of the blood-brain barrier. Acts as a Wnt7-specific coactivator of canonical Wnt signaling: required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. ADGRA2-tethering function does not rely on its G-protein coupled receptor (GPCR) structure but instead on its combined capacity to interact with RECK extracellularly and recruit the Dishevelled scaffolding protein intracellularly. Binds to the glycosaminoglycans heparin, heparin sulfate, chondroitin sulfate and dermatan sulfate."	.	HGNC:17849	AGRA2_HUMAN	Reviewed	ENSG00000020181	.	.	.	.	.
Mol00218	Protein	Type-1 angiotensin II receptor (AGTR1)	AT1AR; AT1BR; Angiotensin II type-1 receptor; AT1; AGTR1A; AGTR1B; AT2R1; AT2R1B	AGTR1	185	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000349243.8, AGTR1-201, 2324; ENST00000497524.5, AGTR1-209, 2359; ENST00000418473.7, AGTR1-204, 2330; ENST00000404754.2, AGTR1-203, 2252; ENST00000402260.2, AGTR1-202, 2172; ENST00000474935.5, AGTR1-206, 1795; ENST00000475347.5, AGTR1-208, 1669; ENST00000461609.1, AGTR1-205, 1545; ENST00000475166.5, AGTR1-207, 753"	MILNSSTEDGIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPAIIHRNVFFIENTNITVCAFHYESQNSTLPIGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFKIIMAIVLFFFFSWIPHQIFTFLDVLIQLGIIRDCRIADIVDTAMPITICIAYFNNCLNPLFYGFLGKKFKRYFLQLLKYIPPKAKSHSNLSTKMSTLSYRPSDNVSSSTKKPAPCFEVE	chr3:148697784-148743008[+]	"Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.; FUNCTION: (Microbial infection) During SARS coronavirus-2/SARS-CoV-2 infection, it is able to recognize and internalize the complex formed by secreted ACE2 and SARS-CoV-2 spike protein through DNM2/dynamin 2-dependent endocytosis."	PDB: 4YAY; PDB: 4ZUD; PDB: 6DO1; PDB: 6OS0; PDB: 6OS1; PDB: 6OS2	HGNC:336	AGTR1_HUMAN	Reviewed	ENSG00000144891	.	.	.	.	.
Mol00219	Protein	Apoptosis-inducing factor 1 (AIFM1)	Programmed cell death protein 8; AIF; PDCD8	AIFM1	9131	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000287295.8, AIFM1-201, 2222; ENST00000676229.1, AIFM1-229, 4157; ENST00000535724.6, AIFM1-209, 2248; ENST00000460436.6, AIFM1-205, 1925; ENST00000674546.1, AIFM1-210, 2233; ENST00000319908.8, AIFM1-202, 2192; ENST00000675092.1, AIFM1-221, 2154; ENST00000675427.1, AIFM1-224, 2123; ENST00000675857.1, AIFM1-226, 2113; ENST00000675240.1, AIFM1-223, 2107; ENST00000676328.1, AIFM1-230, 2086; ENST00000676436.1, AIFM1-231, 2048; ENST00000346424.6, AIFM1-203, 1200; ENST00000674601.1, AIFM1-214, 711; ENST00000675050.1, AIFM1-220, 3083; ENST00000674957.1, AIFM1-216, 2434; ENST00000527892.5, AIFM1-206, 2105; ENST00000674555.1, AIFM1-211, 2077; ENST00000416073.7, AIFM1-204, 2061; ENST00000675037.1, AIFM1-219, 1962; ENST00000674722.1, AIFM1-215, 1905; ENST00000674997.1, AIFM1-217, 1883; ENST00000675774.1, AIFM1-225, 1454; ENST00000676144.1, AIFM1-228, 917; ENST00000529877.1, AIFM1-207, 723; ENST00000676048.1, AIFM1-227, 5137; ENST00000674582.1, AIFM1-212, 2200; ENST00000675111.1, AIFM1-222, 1920; ENST00000675015.1, AIFM1-218, 1689; ENST00000674591.1, AIFM1-213, 1485; ENST00000533719.2, AIFM1-208, 1465"	MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED	chrX:130124666-130165879[-]	"Functions both as NADH oxidoreductase and as regulator of apoptosis. In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Binds to DNA in a sequence-independent manner. Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis. Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells. In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import."	PDB: 1M6I; PDB: 4BUR; PDB: 4BV6; PDB: 4FDC; PDB: 4LII; PDB: 5FMH; PDB: 5FS6; PDB: 5FS7; PDB: 5FS8; PDB: 5FS9; PDB: 5KVH; PDB: 5KVI	HGNC:8768	AIFM1_HUMAN	Reviewed	ENSG00000156709	.	.	.	.	.
Mol00220	Protein	A-kinase anchor protein 12 (AKAP12)	AKAP-12; A-kinase anchor protein 250 kDa; AKAP 250; Gravin; Myasthenia gravis autoantigen; AKAP250	AKAP12	9590	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000402676.7, AKAP12-204, 8466; ENST00000253332.5, AKAP12-201, 6597; ENST00000354675.10, AKAP12-202, 6287; ENST00000359755.5, AKAP12-203, 6190; ENST00000490177.1, AKAP12-205, 561"	MGAGSSTEQRSPEQPPEGSSTPAEPEPSGGGPSAEAAPDTTADPAIAASDPATKLLQKNGQLSTINGVAEQDELSLQEGDLNGQKGALNGQGALNSQEEEEVIVTEVGQRDSEDVSKRDSDKEMATKSAVVHDITDDGQEETPEIIEQIPSSESNLEELTQPTESQANDIGFKKVFKFVGFKFTVKKDKTEKPDTVQLLTVKKDEGEGAAGAGDHKDPSLGAGEAASKESEPKQSTEKPEETLKREQSHAEISPPAESGQAVEECKEEGEEKQEKEPSKSAESPTSPVTSETGSTFKKFFTQGWAGWRKKTSFRKPKEDEVEASEKKKEQEPEKVDTEEDGKAEVASEKLTASEQAHPQEPAESAHEPRLSAEYEKVELPSEEQVSGSQGPSEEKPAPLATEVFDEKIEVHQEEVVAEVHVSTVEERTEEQKTEVEETAGSVPAEELVEMDAEPQEAEPAKELVKLKETCVSGEDPTQGADLSPDEKVLSKPPEGVVSEVEMLSSQERMKVQGSPLKKLFTSTGLKKLSGKKQKGKRGGGDEESGEHTQVPADSPDSQEEQKGESSASSPEEPEEITCLEKGLAEVQQDGEAEEGATSDGEKKREGVTPWASFKKMVTPKKRVRRPSESDKEDELDKVKSATLSSTESTASEMQEEMKGSVEEPKPEEPKRKVDTSVSWEALICVGSSKKRARRGSSSDEEGGPKAMGGDHQKADEAGKDKETGTDGILAGSQEHDPGQGSSSPEQAGSPTEGEGVSTWESFKRLVTPRKKSKSKLEEKSEDSIAGSGVEHSTPDTEPGKEESWVSIKKFIPGRRKKRPDGKQEQAPVEDAGPTGANEDDSDVPAVVPLSEYDAVEREKMEAQQAQKSAEQPEQKAATEVSKELSESQVHMMAAAVADGTRAATIIEERSPSWISASVTEPLEQVEAEAALLTEEVLEREVIAEEEPPTVTEPLPENREARGDTVVSEAELTPEAVTAAETAGPLGAEEGTEASAAEETTEMVSAVSQLTDSPDTTEEATPVQEVEGGVPDIEEQERRTQEVLQAVAEKVKEESQLPGTGGPEDVLQPVQRAEAERPEEQAEASGLKKETDVVLKVDAQEAKTEPFTQGKVVGQTTPESFEKAPQVTESIESSELVTTCQAETLAGVKSQEMVMEQAIPPDSVETPTDSETDGSTPVADFDAPGTTQKDEIVEIHEENEVASGTQSGGTEAEAVPAQKERPPAPSSFVFQEETKEQSKMEDTLEHTDKEVSVETVSILSKTEGTQEADQYADEKTKDVPFFEGLEGSIDTGITVSREKVTEVALKGEGTEEAECKKDDALELQSHAKSPPSPVEREMVVQVEREKTEAEPTHVNEEKLEHETAVTVSEEVSKQLLQTVNVPIIDGAKEVSSLEGSPPPCLGQEEAVCTKIQVQSSEASFTLTAAAEEEKVLGETANILETGETLEPAGAHLVLEEKSSEKNEDFAAHPGEDAVPTGPDCQAKSTPVIVSATTKKGLSSDLEGEKTTSLKWKSDEVDEQVACQEVKVSVAIEDLEPENGILELETKSSKLVQNIIQTAVDQFVRTEETATEMLTSELQTQAHVIKADSQDAGQETEKEGEEPQASAQDETPITSAKEESESTAVGQAHSDISKDMSEASEKTMTVEVEGSTVNDQQLEEVVLPSEEEGGGAGTKSVPEDDGHALLAERIEKSLVEPKEDEKGDDVDDPENQNSALADTDASGGLTKESPDTNGPKQKEKEDAQEVELQEGKVHSESDKAITPQAQEELQKQERESAKSELTES	chr6:151239967-151358559[+]	Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).	.	HGNC:370	AKA12_HUMAN	Reviewed	ENSG00000131016	.	.	.	.	.
Mol00221	Protein	RAC-alpha serine/threonine-protein kinase (AKT1)	Protein kinase B; PKB; Protein kinase B alpha; PKB alpha; Proto-oncogene c-Akt; RAC-PK-alpha; PKB; RAC	AKT1	207	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649815.2, AKT1-218, 2957; ENST00000554581.5, AKT1-208, 3916; ENST00000402615.6, AKT1-202, 3913; ENST00000555528.5, AKT1-214, 3066; ENST00000349310.7, AKT1-201, 2866; ENST00000407796.7, AKT1-203, 2779; ENST00000683722.1, AKT1-221, 2609; ENST00000554848.5, AKT1-211, 1595; ENST00000553797.2, AKT1-206, 3711; ENST00000554192.5, AKT1-207, 922; ENST00000555458.5, AKT1-213, 705; ENST00000554585.5, AKT1-209, 858; ENST00000544168.5, AKT1-204, 1564; ENST00000555380.1, AKT1-212, 534; ENST00000557552.1, AKT1-216, 8396; ENST00000610370.2, AKT1-217, 4373; ENST00000554826.2, AKT1-210, 2857; ENST00000553506.5, AKT1-205, 2830; ENST00000682269.1, AKT1-219, 2587; ENST00000683058.1, AKT1-220, 2277; ENST00000684058.1, AKT1-222, 1945; ENST00000556836.1, AKT1-215, 592"	MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA	chr14:104769349-104795751[-]	"AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development. Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility. Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation. Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation. Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor. Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity."	PDB: 1H10; PDB: 1UNP; PDB: 1UNQ; PDB: 1UNR; PDB: 2UVM; PDB: 2UZR; PDB: 2UZS; PDB: 3CQU; PDB: 3CQW; PDB: 3MV5; PDB: 3MVH; PDB: 3O96; PDB: 3OCB; PDB: 3OW4; PDB: 3QKK; PDB: 3QKL; PDB: 3QKM; PDB: 4EJN; PDB: 4EKK; PDB: 4EKL; PDB: 4GV1; PDB: 5KCV; PDB: 6BUU; PDB: 6CCY; PDB: 6HHF; PDB: 6HHG; PDB: 6HHH; PDB: 6HHI; PDB: 6HHJ; PDB: 6NPZ; PDB: 6S9W; PDB: 6S9X; PDB: 7APJ; PDB: 7NH4; PDB: 7NH5	HGNC:391	AKT1_HUMAN	Reviewed	ENSG00000142208	.	.	.	.	.
Mol00222	Protein	RAC-gamma serine/threonine-protein kinase (AKT3)	Protein kinase Akt-3; Protein kinase B gamma; PKB gamma; RAC-PK-gamma; STK-2; PKBG	AKT3	10000	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000673466.1, AKT3-217, 7281; ENST00000336199.9, AKT3-202, 1688; ENST00000263826.12, AKT3-201, 1583; ENST00000366540.5, AKT3-204, 1575; ENST00000366539.6, AKT3-203, 4967; ENST00000672578.1, AKT3-214, 4925; ENST00000672238.1, AKT3-211, 3417; ENST00000492957.2, AKT3-208, 3225; ENST00000680056.1, AKT3-219, 1314; ENST00000491219.6, AKT3-207, 602; ENST00000673400.1, AKT3-216, 427; ENST00000680118.1, AKT3-220, 2374; ENST00000672442.1, AKT3-212, 3415; ENST00000672460.1, AKT3-213, 2072; ENST00000681794.1, AKT3-222, 1543; ENST00000490018.1, AKT3-206, 664; ENST00000672679.1, AKT3-215, 589; ENST00000550388.1, AKT3-209, 572; ENST00000463991.5, AKT3-205, 422; ENST00000679831.1, AKT3-218, 7950; ENST00000681055.1, AKT3-221, 5343; ENST00000552631.2, AKT3-210, 557"	MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE	chr1:243488233-243851079[-]	"AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis."	PDB: 2X18	HGNC:393	AKT3_HUMAN	Reviewed	ENSG00000117020	.	.	.	.	.
Mol00223	Protein	Aldehyde dehydrogenase 6 (ALDH6)	Aldehyde dehydrogenase 6; Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; ALDH6	ALDH1A3	220	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000329841.10, ALDH1A3-201, 3469; ENST00000346623.6, ALDH1A3-202, 3104; ENST00000557963.1, ALDH1A3-203, 1670; ENST00000561338.5, ALDH1A3-207, 571; ENST00000558033.5, ALDH1A3-204, 713; ENST00000560555.1, ALDH1A3-206, 576; ENST00000558869.1, ALDH1A3-205, 586"	MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLGDKNP	chr15:100877714-100916626[+]	"NAD-dependent aldehyde dehydrogenase that catalyzes the formation of retinoic acid. Has high activity with all-trans retinal, and has much lower in vitro activity with acetaldehyde. Required for the biosynthesis of normal levels of retinoic acid in the embryonic ocular and nasal regions; retinoic acid is required for normal embryonic development of the eye and the nasal region."	PDB: 5FHZ; PDB: 6S6W; PDB: 6TE5; PDB: 6TGW; PDB: 6TRY; PDB: 7A6Q	HGNC:409	AL1A3_HUMAN	Reviewed	ENSG00000184254	.	.	.	.	.
Mol00224	Protein	ALK tyrosine kinase receptor (ALK)	.	ALK	238	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000389048.8, ALK-201, 6240; ENST00000642122.1, ALK-207, 2513; ENST00000618119.4, ALK-205, 4646; ENST00000453137.1, ALK-203, 577; ENST00000431873.6, ALK-202, 2520; ENST00000638605.1, ALK-206, 1757; ENST00000498037.1, ALK-204, 560"	MGAIGLLWLLPLLLSTAAVGSGMGTGQRAGSPAAGPPLQPREPLSYSRLQRKSLAVDFVVPSLFRVYARDLLLPPSSSELKAGRPEARGSLALDCAPLLRLLGPAPGVSWTAGSPAPAEARTLSRVLKGGSVRKLRRAKQLVLELGEEAILEGCVGPPGEAAVGLLQFNLSELFSWWIRQGEGRLRIRLMPEKKASEVGREGRLSAAIRASQPRLLFQIFGTGHSSLESPTNMPSPSPDYFTWNLTWIMKDSFPFLSHRSRYGLECSFDFPCELEYSPPLHDLRNQSWSWRRIPSEEASQMDLLDGPGAERSKEMPRGSFLLLNTSADSKHTILSPWMRSSSEHCTLAVSVHRHLQPSGRYIAQLLPHNEAAREILLMPTPGKHGWTVLQGRIGRPDNPFRVALEYISSGNRSLSAVDFFALKNCSEGTSPGSKMALQSSFTCWNGTVLQLGQACDFHQDCAQGEDESQMCRKLPVGFYCNFEDGFCGWTQGTLSPHTPQWQVRTLKDARFQDHQDHALLLSTTDVPASESATVTSATFPAPIKSSPCELRMSWLIRGVLRGNVSLVLVENKTGKEQGRMVWHVAAYEGLSLWQWMVLPLLDVSDRFWLQMVAWWGQGSRAIVAFDNISISLDCYLTISGEDKILQNTAPKSRNLFERNPNKELKPGENSPRQTPIFDPTVHWLFTTCGASGPHGPTQAQCNNAYQNSNLSVEVGSEGPLKGIQIWKVPATDTYSISGYGAAGGKGGKNTMMRSHGVSVLGIFNLEKDDMLYILVGQQGEDACPSTNQLIQKVCIGENNVIEEEIRVNRSVHEWAGGGGGGGGATYVFKMKDGVPVPLIIAAGGGGRAYGAKTDTFHPERLENNSSVLGLNGNSGAAGGGGGWNDNTSLLWAGKSLQEGATGGHSCPQAMKKWGWETRGGFGGGGGGCSSGGGGGGYIGGNAASNNDPEMDGEDGVSFISPLGILYTPALKVMEGHGEVNIKHYLNCSHCEVDECHMDPESHKVICFCDHGTVLAEDGVSCIVSPTPEPHLPLSLILSVVTSALVAALVLAFSGIMIVYRRKHQELQAMQMELQSPEYKLSKLRTSTIMTDYNPNYCFAGKTSSISDLKEVPRKNITLIRGLGHGAFGEVYEGQVSGMPNDPSPLQVAVKTLPEVCSEQDELDFLMEALIISKFNHQNIVRCIGVSLQSLPRFILLELMAGGDLKSFLRETRPRPSQPSSLAMLDLLHVARDIACGCQYLEENHFIHRDIAARNCLLTCPGPGRVAKIGDFGMARDIYRASYYRKGGCAMLPVKWMPPEAFMEGIFTSKTDTWSFGVLLWEIFSLGYMPYPSKSNQEVLEFVTSGGRMDPPKNCPGPVYRIMTQCWQHQPEDRPNFAIILERIEYCTQDPDVINTALPIEYGPLVEEEEKVPVRPKDPEGVPPLLVSQQAKREEERSPAAPPPLPTTSSGKAAKKPTAAEISVRVPRGPAVEGGHVNMAFSQSNPPSELHKVHGSRNKPTSLWNPTYGSWFTEKPTKKNNPIAKKEPHDRGNLGLEGSCTVPPNVATGRLPGASLLLEPSSLTANMKEVPLFRLRHFPCGNVNYGYQQQGLPLEAATAPGAGHYEDTILKSKNSMNQPGP	chr2:29192774-29921586[-]	"Neuronal receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system. Transduces signals from ligands at the cell surface, through specific activation of the mitogen-activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif. Following activation by ligand, ALK induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Acts as a receptor for ligands pleiotrophin (PTN), a secreted growth factor, and midkine (MDK), a PTN-related factor, thus participating in PTN and MDK signal transduction. PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation. MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction. Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase. Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK. Thinness gene involved in the resistance to weight gain: in hypothalamic neurons, controls energy expenditure acting as a negative regulator of white adipose tissue lipolysis and sympathetic tone to fine-tune energy homeostasis (By similarity)."	PDB: 2KUP; PDB: 2KUQ; PDB: 2XB7; PDB: 2XBA; PDB: 2XP2; PDB: 2YFX; PDB: 2YHV; PDB: 2YJR; PDB: 2YJS; PDB: 2YS5; PDB: 2YT2; PDB: 3AOX; PDB: 3L9P; PDB: 3LCS; PDB: 3LCT; PDB: 4ANL; PDB: 4ANQ; PDB: 4ANS; PDB: 4CCB; PDB: 4CCU; PDB: 4CD0; PDB: 4CLI; PDB: 4CLJ; PDB: 4CMO; PDB: 4CMT; PDB: 4CMU; PDB: 4CNH; PDB: 4CTB; PDB: 4CTC; PDB: 4DCE; PDB: 4FNW; PDB: 4FNX; PDB: 4FNY; PDB: 4FNZ; PDB: 4FOB; PDB: 4FOC; PDB: 4FOD; PDB: 4JOA; PDB: 4MKC; PDB: 4TT7; PDB: 4Z55; PDB: 5A9U; PDB: 5AA8; PDB: 5AA9; PDB: 5AAA; PDB: 5AAB; PDB: 5AAC; PDB: 5FTO; PDB: 5FTQ; PDB: 5IMX; PDB: 5IUG; PDB: 5IUH; PDB: 5IUI; PDB: 5KZ0; PDB: 5VZ5; PDB: 6AT9; PDB: 6CDT; PDB: 6E0R; PDB: 6EBW; PDB: 6EDL; PDB: 6MX8; PDB: 7BTT; PDB: 7JY4; PDB: 7JYR; PDB: 7JYS; PDB: 7JYT; PDB: 7NWZ; PDB: 7NX3; PDB: 7NX4	HGNC:427	ALK_HUMAN	Reviewed	ENSG00000171094	.	.	.	.	.
Mol00225	Protein	Androgen receptor (AR)	Dihydrotestosterone receptor; Nuclear receptor subfamily 3 group C member 4; DHTR; NR3C4	AR	367	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374690.9, AR-201, 10667; ENST00000504326.5, AR-204, 3615; ENST00000396044.8, AR-203, 2427; ENST00000612452.5, AR-207, 7630; ENST00000613054.2, AR-208, 3532; ENST00000514029.5, AR-206, 3899; ENST00000396043.3, AR-202, 1837; ENST00000513847.5, AR-205, 2420"	MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ	chrX:67544021-67730619[+]	"Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3."	PDB: 1E3G; PDB: 1GS4; PDB: 1T5Z; PDB: 1T63; PDB: 1T65; PDB: 1XJ7; PDB: 1XOW; PDB: 1XQ3; PDB: 1Z95; PDB: 2AM9; PDB: 2AMA; PDB: 2AMB; PDB: 2AO6; PDB: 2AX6; PDB: 2AX7; PDB: 2AX8; PDB: 2AX9; PDB: 2AXA; PDB: 2HVC; PDB: 2OZ7; PDB: 2PIO; PDB: 2PIP; PDB: 2PIQ; PDB: 2PIR; PDB: 2PIT; PDB: 2PIU; PDB: 2PIV; PDB: 2PIW; PDB: 2PIX; PDB: 2PKL; PDB: 2PNU; PDB: 2Q7I; PDB: 2Q7J; PDB: 2Q7K; PDB: 2Q7L; PDB: 2YHD; PDB: 2YLO; PDB: 2YLP; PDB: 2YLQ; PDB: 2Z4J; PDB: 3B5R; PDB: 3B65; PDB: 3B66; PDB: 3B67; PDB: 3B68; PDB: 3BTR; PDB: 3L3X; PDB: 3L3Z; PDB: 3RLJ; PDB: 3RLL; PDB: 3V49; PDB: 3V4A; PDB: 3ZQT; PDB: 4HLW; PDB: 4K7A; PDB: 4OEA; PDB: 4OED; PDB: 4OEY; PDB: 4OEZ; PDB: 4OFR; PDB: 4OFU; PDB: 4OGH; PDB: 4OH5; PDB: 4OH6; PDB: 4OHA; PDB: 4OIL; PDB: 4OIU; PDB: 4OJ9; PDB: 4OJB; PDB: 4OK1; PDB: 4OKB; PDB: 4OKT; PDB: 4OKW; PDB: 4OKX; PDB: 4OLM; PDB: 4QL8; PDB: 5CJ6; PDB: 5JJM; PDB: 5T8E; PDB: 5T8J; PDB: 5V8Q; PDB: 5VO4	HGNC:644	ANDR_HUMAN	Reviewed	ENSG00000169083	.	.	.	.	.
Mol00226	Protein	Ankyrin-2 (ANK2)	ANK-2; Ankyrin-B; Brain ankyrin; Non-erythroid ankyrin; ANKB	ANK2	287	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357077.9, ANK2-202, 14215; ENST00000506722.5, ANK2-212, 8051; ENST00000394537.7, ANK2-203, 6313; ENST00000509550.5, ANK2-214, 3638; ENST00000672240.1, ANK2-248, 15298; ENST00000671971.1, ANK2-240, 15262; ENST00000673363.1, ANK2-285, 15163; ENST00000672209.1, ANK2-246, 14932; ENST00000672830.1, ANK2-266, 14771; ENST00000672502.1, ANK2-259, 14732; ENST00000671809.1, ANK2-232, 14697; ENST00000672090.1, ANK2-244, 14661; ENST00000671906.1, ANK2-238, 14637; ENST00000672251.1, ANK2-250, 14606; ENST00000673573.1, ANK2-292, 14599; ENST00000672934.1, ANK2-271, 14563; ENST00000673109.1, ANK2-278, 14538; ENST00000672068.1, ANK2-242, 14485; ENST00000673298.1, ANK2-282, 14363; ENST00000673555.1, ANK2-291, 14092; ENST00000672930.1, ANK2-270, 13999; ENST00000673334.1, ANK2-283, 13915; ENST00000671882.1, ANK2-236, 13878; ENST00000503423.6, ANK2-206, 12641; ENST00000264366.10, ANK2-201, 11775; ENST00000673240.1, ANK2-280, 9007; ENST00000671762.1, ANK2-230, 8690; ENST00000672362.1, ANK2-255, 8619; ENST00000672402.1, ANK2-257, 8594; ENST00000673536.1, ANK2-288, 8525; ENST00000671825.1, ANK2-233, 8516; ENST00000672793.1, ANK2-265, 8484; ENST00000672366.1, ANK2-256, 8477; ENST00000672779.1, ANK2-264, 8467; ENST00000672965.1, ANK2-273, 8442; ENST00000672955.1, ANK2-272, 8434; ENST00000672177.1, ANK2-245, 8418; ENST00000672312.1, ANK2-251, 8417; ENST00000672854.1, ANK2-267, 8351; ENST00000673546.1, ANK2-290, 8344; ENST00000671704.1, ANK2-227, 8338; ENST00000671951.1, ANK2-239, 8316; ENST00000672221.1, ANK2-247, 8314; ENST00000672684.1, ANK2-260, 8308; ENST00000671793.1, ANK2-231, 8303; ENST00000672759.1, ANK2-263, 8283; ENST00000671727.1, ANK2-228, 8257; ENST00000671756.1, ANK2-229, 8241; ENST00000673430.1, ANK2-286, 8186; ENST00000672990.1, ANK2-275, 8129; ENST00000673255.1, ANK2-281, 8123; ENST00000672880.1, ANK2-268, 8093; ENST00000672088.1, ANK2-243, 8080; ENST00000672045.1, ANK2-241, 8074; ENST00000672356.1, ANK2-254, 8043; ENST00000672350.1, ANK2-253, 8031; ENST00000671854.1, ANK2-234, 7995; ENST00000672696.1, ANK2-261, 7947; ENST00000673044.1, ANK2-276, 7770; ENST00000672315.1, ANK2-252, 7770; ENST00000673453.1, ANK2-287, 7765; ENST00000672246.1, ANK2-249, 7729; ENST00000672731.1, ANK2-262, 7721; ENST00000672986.1, ANK2-274, 7620; ENST00000671893.1, ANK2-237, 7522; ENST00000673231.1, ANK2-279, 6370; ENST00000673048.1, ANK2-277, 6062; ENST00000672915.1, ANK2-269, 6045; ENST00000673353.1, ANK2-284, 5956; ENST00000505342.6, ANK2-210, 5732; ENST00000672411.1, ANK2-258, 5730; ENST00000504454.5, ANK2-208, 5270; ENST00000514960.5, ANK2-222, 5160; ENST00000612754.2, ANK2-225, 4810; ENST00000510275.8, ANK2-215, 4305; ENST00000634436.1, ANK2-226, 3584; ENST00000503271.5, ANK2-205, 3537; ENST00000673943.1, ANK2-294, 3317; ENST00000506344.5, ANK2-211, 895; ENST00000511380.1, ANK2-216, 573; ENST00000504415.5, ANK2-207, 561; ENST00000514167.1, ANK2-220, 243; ENST00000673778.1, ANK2-293, 159; ENST00000671863.1, ANK2-235, 8384; ENST00000673538.1, ANK2-289, 6171; ENST00000683089.1, ANK2-305, 2315; ENST00000682900.1, ANK2-302, 1998; ENST00000683464.1, ANK2-311, 593; ENST00000504887.1, ANK2-209, 556; ENST00000515034.1, ANK2-223, 545; ENST00000512999.1, ANK2-218, 414; ENST00000514246.1, ANK2-221, 398; ENST00000683972.1, ANK2-320, 11469; ENST00000682959.1, ANK2-303, 8973; ENST00000683310.1, ANK2-307, 7778; ENST00000684730.1, ANK2-329, 7743; ENST00000682189.1, ANK2-297, 7511; ENST00000684378.1, ANK2-323, 7094; ENST00000684470.1, ANK2-324, 6591; ENST00000684225.1, ANK2-321, 6095; ENST00000681990.1, ANK2-295, 6006; ENST00000683826.1, ANK2-317, 6003; ENST00000683354.1, ANK2-308, 5461; ENST00000682198.1, ANK2-298, 5445; ENST00000682049.1, ANK2-296, 5214; ENST00000683908.1, ANK2-319, 5123; ENST00000683777.1, ANK2-316, 4880; ENST00000683893.1, ANK2-318, 4417; ENST00000502701.2, ANK2-204, 4339; ENST00000514160.2, ANK2-219, 4003; ENST00000684591.1, ANK2-325, 3671; ENST00000683595.1, ANK2-313, 3612; ENST00000682211.1, ANK2-299, 3607; ENST00000684230.1, ANK2-322, 3577; ENST00000683723.1, ANK2-315, 3539; ENST00000683662.1, ANK2-314, 3245; ENST00000683568.1, ANK2-312, 3085; ENST00000682346.1, ANK2-300, 2961; ENST00000682678.1, ANK2-301, 2885; ENST00000683360.1, ANK2-309, 2486; ENST00000683389.1, ANK2-310, 2432; ENST00000683180.1, ANK2-306, 2197; ENST00000515644.2, ANK2-224, 2088; ENST00000512298.2, ANK2-217, 1917; ENST00000684653.1, ANK2-326, 1830; ENST00000684727.1, ANK2-328, 1534; ENST00000684681.1, ANK2-327, 1467; ENST00000683070.1, ANK2-304, 1002; ENST00000508007.5, ANK2-213, 840"	MMNEDAAQKSDSGEKFNGSSQRRKRPKKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNDETESTETSVLKSHLVNEVPVLASPDLLSEVSEMKQDLIKMTAILTTDVSDKAGSIKVKELVKAAEEEPGEPFEIVERVKEDLEKVNEILRSGTCTRDESSVQSSRSERGLVEEEWVIVSDEEIEEARQKAPLEITEYPCVEVRIDKEIKGKVEKDSTGLVNYLTDDLNTCVPLPKEQLQTVQDKAGKKCEALAVGRSSEKEGKDIPPDETQSTQKQHKPSLGIKKPVRRKLKEKQKQKEEGLQASAEKAELKKGSSEESLGEDPGLAPEPLPTVKATSPLIEETPIGSIKDKVKALQKRVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTKTERHSPVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQPPVSPTSKTERIEETMSVRELMKAFQSGQDPSKHKTGLFEHKSAKQKQPQEKGKVRVEKEKGPILTQREAQKTENQTIKRGQRLPVTGTAESKRGVRVSSIGVKKEDAAGGKEKVLSHKIPEPVQSVPEEESHRESEVPKEKMADEQGDMDLQISPDRKTSTDFSEVIKQELEDNDKYQQFRLSEETEKAQLHLDQVLTSPFNTTFPLDYMKDEFLPALSLQSGALDGSSESLKNEGVAGSPCGSLMEGTPQISSEESYKHEGLAETPETSPESLSFSPKKSEEQTGETKESTKTETTTEIRSEKEHPTTKDITGGSEERGATVTEDSETSTESFQKEATLGSPKDTSPKRQDDCTGSCSVALAKETPTGLTEEAACDEGQRTFGSSAHKTQTDSEVQESTATSDETKALPLPEASVKTDTGTESKPQGVIRSPQGLELALPSRDSEVLSAVADDSLAVSHKDSLEASPVLEDNSSHKTPDSLEPSPLKESPCRDSLESSPVEPKMKAGIFPSHFPLPAAVAKTELLTEVASVRSRLLRDPDGSAEDDSLEQTSLMESSGKSPLSPDTPSSEEVSYEVTPKTTDVSTPKPAVIHECAEEDDSENGEKKRFTPEEEMFKMVTKIKMFDELEQEAKQKRDYKKEPKQEESSSSSDPDADCSVDVDEPKHTGSGEDESGVPVLVTSESRKVSSSSESEPELAQLKKGADSGLLPEPVIRVQPPSPLPSSMDSNSSPEEVQFQPVVSKQYTFKMNEDTQEEPGKSEEEKDSESHLAEDRHAVSTEAEDRSYDKLNRDTDQPKICDGHGCEAMSPSSSAAPVSSGLQSPTGDDVDEQPVIYKESLALQGTHEKDTEGEELDVSRAESPQADCPSESFSSSSSLPHCLVSEGKELDEDISATSSIQKTEVTKTDETFENLPKDCPSQDSSITTQTDRFSMDVPVSDLAENDEIYDPQITSPYENVPSQSFFSSEESKTQTDANHTTSFHSSEVYSVTITSPVEDVVVASSSSGTVLSKESNFEGQDIKMESQQESTLWEMQSDSVSSSFEPTMSATTTVVGEQISKVIITKTDVDSDSWSEIREDDEAFEARVKEEEQKIFGLMVDRQSQGTTPDTTPARTPTEEGTPTSEQNPFLFQEGKLFEMTRSGAIDMTKRSYADESFHFFQIGQESREETLSEDVKEGATGADPLPLETSAESLALSESKETVDDEADLLPDDVSEEVEEIPASDAQLNSQMGISASTETPTKEAVSVGTKDLPTVQTGDIPPLSGVKQISCPDSSEPAVQVQLDFSTLTRSVYSDRGDDSPDSSPEEQKSVIEIPTAPMENVPFTESKSKIPVRTMPTSTPAPPSAEYESSVSEDFLSSVDEENKADEAKPKSKLPVKVPLQRVEQQLSDLDTSVQKTVAPQGQDMASIAPDNRSKSESDASSLDSKTKCPVKTRSYTETETESRERAEELELESEEGATRPKILTSRLPVKSRSTTSSCRGGTSPTKESKEHFFDLYRNSIEFFEEISDEASKLVDRLTQSEREQEIVSDDESSSALEVSVIENLPPVETEHSVPEDIFDTRPIWDESIETLIERIPDENGHDHAEDPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE	chr4:112818032-113384221[+]	"Plays an essential role in the localization and membrane stabilization of ion transporters and ion channels in several cell types, including cardiomyocytes, as well as in striated muscle cells. In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions. In cardiomyocytes, required for coordinate assembly of Na/Ca exchanger, SLC8A1/NCX1, Na/K ATPases ATP1A1 and ATP1A2 and inositol 1,4,5-trisphosphate (InsP3) receptors at sarcoplasmic reticulum/sarcolemma sites. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate. In the inner segment of rod photoreceptors, required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1). Plays a role in endocytosis and intracellular protein transport. Associates with phosphatidylinositol 3-phosphate (PI3P)-positive organelles and binds dynactin to promote long-range motility of cells. Recruits RABGAP1L to (PI3P)-positive early endosomes, where RABGAP1L inactivates RAB22A, and promotes polarized trafficking to the leading edge of the migrating cells. Part of the ANK2/RABGAP1L complex which is required for the polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma membrane that enables continuous directional cell migration."	PDB: 4D8O; PDB: 4RLV; PDB: 4RLY; PDB: 5Y4D; PDB: 5Y4E; PDB: 5Y4F; PDB: 5YIR; PDB: 5YIS; PDB: 6KZJ; PDB: 6M3Q	HGNC:493	ANK2_HUMAN	Reviewed	ENSG00000145362	.	.	.	.	.
Mol00227	Protein	Annexin A1 (ANXA1)	Annexin I; Annexin-1; Calpactin II; Calpactin-2; Chromobindin-9; Lipocortin I; Phospholipase A2 inhibitory protein; p35; ANX1; LPC1	ANXA1	301	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000257497.11, ANXA1-201, 1401; ENST00000376911.1, ANXA1-202, 2209; ENST00000456643.5, ANXA1-204, 799; ENST00000415424.5, ANXA1-203, 526; ENST00000491192.1, ANXA1-207, 1400; ENST00000495713.5, ANXA1-208, 905; ENST00000468639.5, ANXA1-205, 800; ENST00000489109.1, ANXA1-206, 749"	MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN	chr9:73151865-73170393[+]	"Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells. Has no effect on unstimulated T cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton. Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions. Displays Ca(2+)-dependent binding to phospholipid membranes. Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton."	PDB: 1AIN; PDB: 1BO9; PDB: 1QLS; PDB: 5VFW	HGNC:533	ANXA1_HUMAN	Reviewed	ENSG00000135046	.	.	.	.	.
Mol00228	Protein	Transcription factor AP2 alpha (TFAP2A)	AP2-alpha; AP-2 transcription factor; Activating enhancer-binding protein 2-alpha; Activator protein 2; AP-2; AP2TF; TFAP2	TFAP2A	7020	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000379613.10, TFAP2A-203, 3143; ENST00000379608.9, TFAP2A-202, 3831; ENST00000319516.8, TFAP2A-201, 2035; ENST00000482890.6, TFAP2A-213, 2071; ENST00000466073.5, TFAP2A-208, 987; ENST00000475264.5, TFAP2A-211, 675; ENST00000465858.1, TFAP2A-207, 617; ENST00000461628.5, TFAP2A-204, 582; ENST00000498450.3, TFAP2A-219, 417; ENST00000489805.5, TFAP2A-216, 2739; ENST00000488193.7, TFAP2A-215, 1894; ENST00000497266.5, TFAP2A-218, 1014; ENST00000490875.5, TFAP2A-217, 893; ENST00000486038.1, TFAP2A-214, 702; ENST00000473652.1, TFAP2A-209, 658; ENST00000462727.1, TFAP2A-205, 569; ENST00000474952.5, TFAP2A-210, 1621; ENST00000464323.1, TFAP2A-206, 1387; ENST00000478375.5, TFAP2A-212, 1349"	MLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALSSGLGDLSIHSLPHAIEEVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK	chr6:10393186-10419659[-]	"Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region."	.	HGNC:11742	AP2A_HUMAN	Reviewed	ENSG00000137203	.	.	.	.	.
Mol00229	Protein	Transcription factor AP2 gamma (TFAP2C)	AP2-gamma; Activating enhancer-binding protein 2 gamma; Transcription factor ERF-1	TFAP2C	7022	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000201031.3, TFAP2C-201, 2862; ENST00000416606.1, TFAP2C-202, 482"	MLWKITDNVKYEEDCEDRHDGSSNGNPRVPHLSSAGQHLYSPAPPLSHTGVAEYQPPPYFPPPYQQLAYSQSADPYSHLGEAYAAAINPLHQPAPTGSQQQAWPGRQSQEGAGLPSHHGRPAGLLPHLSGLEAGAVSARRDAYRRSDLLLPHAHALDAAGLAENLGLHDMPHQMDEVQNVDDQHLLLHDQTVIRKGPISMTKNPLNLPCQKELVGAVMNPTEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAAHVTLLTSLVEGEAVHLARDFAYVCEAEFPSKPVAEYLTRPHLGGRNEMAARKNMLLAAQQLCKEFTELLSQDRTPHGTSRLAPVLETNIQNCLSHFSLITHGFGSQAICAAVSALQNYIKEALIVIDKSYMNPGDQSPADSNKTLEKMEKHRK	chr20:56629306-56639283[+]	"Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer."	.	HGNC:11744	AP2C_HUMAN	Reviewed	ENSG00000087510	.	.	.	.	.
Mol00230	Protein	Phorbol-12-myristate-13-acetate-induced protein 1 (PMAIP1)	PMA-induced protein 1; Immediate-early-response protein APR; Protein Noxa; NOXA	PMAIP1	5366	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000316660.7, PMAIP1-202, 1899; ENST00000269518.9, PMAIP1-201, 1262; ENST00000590596.1, PMAIP1-203, 804"	MPGKKARKNAQPSPARAPAELEVECATQLRRFGDKLNFRQKLLNLISKLFCSGT	chr18:59899996-59904305[+]	Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BAK1 for binding to MCL1 and can displace BAK1 from its binding site on MCL1 (By similarity). Competes with BIM/BCL2L11 for binding to MCL1 and can displace BIM/BCL2L11 from its binding site on MCL1.	PDB: 3MQP	HGNC:9108	APR_HUMAN	Reviewed	ENSG00000141682	.	.	.	.	.
Mol00231	Protein	Beta adrenoceptor kinase 1 (GRK2)	Beta-ARK-1; G-protein coupled receptor kinase 2; ADRBK1; BARK; BARK1	GRK2	156	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308595.10, GRK2-201, 3403; ENST00000526285.1, GRK2-204, 1458; ENST00000527176.5, GRK2-206, 970; ENST00000532099.5, GRK2-211, 886; ENST00000524899.1, GRK2-203, 751; ENST00000529738.1, GRK2-207, 500; ENST00000530291.5, GRK2-209, 324; ENST00000416281.6, GRK2-202, 4493; ENST00000533077.5, GRK2-213, 3453; ENST00000526572.5, GRK2-205, 789; ENST00000529815.1, GRK2-208, 589; ENST00000531390.1, GRK2-210, 524; ENST00000534651.5, GRK2-214, 424; ENST00000532611.1, GRK2-212, 410"	MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFRDFCLNHLEEARPLVEFYEEIKKYEKLETEEERVARSREIFDSYIMKELLACSHPFSKSATEHVQGHLGKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARKKAKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSLLTMEEIQSVEETQIKERKCLLLKIRGGKQFILQCDSDPELVQWKKELRDAYREAQQLVQRVPKMKNKPRSPVVELSKVPLVQRGSANGL	chr11:67266473-67286556[+]	"Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner. Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity. Inhibits relaxation of airway smooth muscle in response to blue light."	PDB: 1BAK; PDB: 3CIK; PDB: 3KRW; PDB: 3KRX; PDB: 3V5W; PDB: 4MK0; PDB: 4PNK; PDB: 5HE1; PDB: 5UKK; PDB: 5UKL; PDB: 5UUU; PDB: 5UVC; PDB: 5WG3; PDB: 5WG4; PDB: 5WG5; PDB: 6C2Y; PDB: 6U7C; PDB: 7K7L; PDB: 7K7Z; PDB: 7PWD	HGNC:289	ARBK1_HUMAN	Reviewed	ENSG00000173020	.	.	.	.	.
Mol00232	Protein	Activity-regulated cytoskeleton-associated protein (ARC)	hArc; Activity-regulated gene 3.1 protein homolog; ARC/ARG3.1; Arg3.1; KIAA0278	ARC	23237	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356613.4, ARC-201, 2950; ENST00000581404.1, ARC-202, 407"	MELDHRTSGGLHAYPGPRGGQVAKPNVILQIGKCRAEMLEHVRRTHRHLLAEVSKQVERELKGLHRSVGKLESNLDGYVPTSDSQRWKKSIKACLCRCQETIANLERWVKREMHVWREVFYRLERWADRLESTGGKYPVGSESARHTVSVGVGGPESYCHEADGYDYTVSPYAITPPPAAGELPGQEPAEAQQYQPWVPGEDGQPSPGVDTQIFEDPREFLSHLEEYLRQVGGSEEYWLSQIQNHMNGPAKKWWEFKQGSVKNWVEFKKEFLQYSEGTLSREAIQRELDLPQKQGEPLDQFLWRKRDLYQTLYVDADEEEIIQYVVGTLQPKLKRFLRHPLPKTLEQLIQRGMEVQDDLEQAAEPAGPHLPVEDEAETLTPAPNSESVASDRTQPE	chr8:142611049-142614479[-]	"Master regulator of synaptic plasticity that self-assembles into virion-like capsids that encapsulate RNAs and mediate intercellular RNA transfer in the nervous system. ARC protein is released from neurons in extracellular vesicles that mediate the transfer of ARC mRNA into new target cells, where ARC mRNA can undergo activity-dependent translation. ARC capsids are endocytosed and are able to transfer ARC mRNA into the cytoplasm of neurons. Acts as a key regulator of synaptic plasticity: required for protein synthesis-dependent forms of long-term potentiation (LTP) and depression (LTD) and for the formation of long-term memory. Regulates synaptic plasticity by promoting endocytosis of AMPA receptors (AMPARs) in response to synaptic activity: this endocytic pathway maintains levels of surface AMPARs in response to chronic changes in neuronal activity through synaptic scaling, thereby contributing to neuronal homeostasis. Acts as a postsynaptic mediator of activity-dependent synapse elimination in the developing cerebellum by mediating elimination of surplus climbing fiber synapses. Accumulates at weaker synapses, probably to prevent their undesired enhancement. This suggests that ARC-containing virion-like capsids may be required to eliminate synaptic material. Required to transduce experience into long-lasting changes in visual cortex plasticity and for long-term memory (By similarity). Involved in postsynaptic trafficking and processing of amyloid-beta A4 (APP) via interaction with PSEN1 (By similarity). In addition to its role in synapses, also involved in the regulation of the immune system: specifically expressed in skin-migratory dendritic cells and regulates fast dendritic cell migration, thereby regulating T-cell activation (By similarity)."	PDB: 6TN7; PDB: 6TNQ; PDB: 6TQ0; PDB: 6YTU	HGNC:648	ARC_HUMAN	Reviewed	ENSG00000198576	.	.	.	.	.
Mol00233	Protein	Neuroepithelial cell-transforming gene 1 protein (NET1)	Proto-oncogene p65 Net1; Rho guanine nucleotide exchange factor 8; ARHGEF8	NET1	10276	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000355029.9, NET1-201, 3989; ENST00000380359.3, NET1-202, 3253; ENST00000449083.5, NET1-203, 637; ENST00000484741.1, NET1-205, 757; ENST00000486354.1, NET1-206, 599; ENST00000465087.1, NET1-204, 403"	MEPELAAQKQPRPRRRSRRASGLSTEGATGPSADTSGSELDGRCSLRRGSSFTFLTPGPNWDFTLKRKRREKDDDVVSLSSLDLKEPSNKRVRPLARVTSLANLISPVRNGAVRRFGQTIQSFTLRGDHRSPASAQKFSSRSTVPTPAKRRSSALWSEMLDITMKESLTTREIRRQEAIYEMSRGEQDLIEDLKLARKAYHDPMLKLSIMSEEELTHIFGDLDSYIPLHEDLLTRIGEATKPDGTVEQIGHILVSWLPRLNAYRGYCSNQLAAKALLDQKKQDPRVQDFLQRCLESPFSRKLDLWSFLDIPRSRLVKYPLLLKEILKHTPKEHPDVQLLEDAILIIQGVLSDINLKKGESECQYYIDKLEYLDEKQRDPRIEASKVLLCHGELRSKSGHKLYIFLFQDILVLTRPVTRNERHSYQVYRQPIPVQELVLEDLQDGDVRMGGSFRGAFSNSEKAKNIFRIRFHDPSPAQSHTLQANDVFHKQQWFNCIRAAIAPFQSAGSPPELQGLPELHEECEGNHPSARKLTAQRRASTVSSVTQVEVDENAYRCGSGMQMAEDSKSLKTHQTQPGIRRARDKALSGGKRKETLV	chr10:5412557-5459056[+]	Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway Stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.	PDB: 3EO2; PDB: 4XH9	HGNC:14592	ARHG8_HUMAN	Reviewed	ENSG00000173848	.	.	.	.	.
Mol00234	Protein	AT-rich interactive domain-containing protein 1A (ARID1A)	ARID domain-containing protein 1A; B120; BRG1-associated factor 250; BAF250; BRG1-associated factor 250a; BAF250A; Osa homolog 1; hOSA1; SWI-like protein; SWI/SNF complex protein p270; SWI/SNF-related; matrix-associated; actin-dependent regulator of chromatin subfamily F member 1; hELD; BAF250; BAF250A; C1orf4; OSA1; SMARCF1	ARID1A	8289	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000324856.13, ARID1A-201, 8595; ENST00000457599.6, ARID1A-205, 6268; ENST00000636219.1, ARID1A-211, 7058; ENST00000430799.7, ARID1A-204, 6521; ENST00000374152.7, ARID1A-202, 6460; ENST00000637465.1, ARID1A-215, 699; ENST00000524572.1, ARID1A-207, 546; ENST00000466382.2, ARID1A-206, 2699; ENST00000532781.1, ARID1A-208, 2583; ENST00000636958.1, ARID1A-214, 1388; ENST00000636794.1, ARID1A-213, 1068; ENST00000636110.1, ARID1A-210, 3450; ENST00000637788.1, ARID1A-216, 3046; ENST00000636422.1, ARID1A-212, 1324; ENST00000636072.1, ARID1A-209, 1128; ENST00000430291.2, ARID1A-203, 580"	MAAQVAPAAASSLGNPPPPPPSELKKAEQQQREEAGGEAAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLTEPPGGGGGGSSDGVGAPPHSAAAALPPPAYGFGQPYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPAPAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYSGGPQDGGAGKGPADMASQCWGAAAAAAAAAAASGGAQQRSHHAPMSPGSSGGGGQPLARTPQPSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGGLSYTQQIPPYGQQGPSGYGQQGQTPYYNQQSPHPQQQQPPYSQQPPSQTPHAQPSYQQQPQSQPPQLQSSQPPYSQQPSQPPHQQSPAPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPAPSTLSQQAAYPQPQSQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYSSPQPGSALSPRQPSGGQIHTGMGSYQQNSMGSYGPQGGQYGPQGGYPRQPNYNALPNANYPSAGMAGGINPMGAGGQMHGQPGIPPYGTLPPGRMSHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQETAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYSMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFNDGSDSTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGNVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMSTGAPQPNLMPSNPDSGMYSPSRYPPQQQQQQQQRHDSYGNQFSTQGTPSGSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSTGQGQPQQQQLPPAQPQPASQQQAAQPSPQQDVYNQYGNAYPATATAATERRPAGGPQNQFPFQFGRDRVSAPPGTNAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQSTGSAPQGPAYHGVNRTDEMLHTDQRANHEGSWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMQNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPAPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFSKVSSPAPMEGGEEEEELLGPKLEEEEEEEVVENDEEIAFSGKDKPASENSEEKLISKFDKLPVKIVQKNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKTELLPSRPHAPCPPAPRKHVTTAEGTPGTTDQEGPPPDGPPEKRITATMDDMLSTRSSTLTEDGAKSSEAIKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCNKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS	chr1:26693236-26782104[+]	"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity)."	PDB: 1RYU; PDB: 6LTH; PDB: 6LTJ	HGNC:11110	ARI1A_HUMAN	Reviewed	ENSG00000117713	.	.	.	.	.
Mol00235	Protein	AT-rich interactive domain-containing protein 4B (ARID4B)	ARID domain-containing protein 4B; 180 kDa Sin3-associated polypeptide; Sin3-associated polypeptide p180; Breast cancer-associated antigen BRCAA1; Histone deacetylase complex subunit SAP180; Retinoblastoma-binding protein 1-like 1; BRCAA1; RBBP1L1; RBP1L1; SAP180	ARID4B	51742	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264183.9, ARID4B-201, 6022; ENST00000366603.6, ARID4B-203, 5946; ENST00000349213.7, ARID4B-202, 5811; ENST00000418304.1, ARID4B-204, 1759; ENST00000444620.2, ARID4B-206, 1660; ENST00000421364.5, ARID4B-205, 5151; ENST00000474953.5, ARID4B-211, 3463; ENST00000494543.1, ARID4B-213, 453; ENST00000471257.5, ARID4B-209, 4195; ENST00000491632.5, ARID4B-212, 3823; ENST00000466653.1, ARID4B-208, 2315; ENST00000474401.1, ARID4B-210, 578; ENST00000462969.1, ARID4B-207, 273"	MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDEDEDDRKQIDELLGKVVCVDYISLDKKKALWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTAPKPDAVLKQAFEQALEFHKSRTIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYKKYLYGFEEYCRSANIEFQMALPEKVVNKQCKECENVKEIKVKEENETEIKEIKMEEERNIIPREEKPIEDEIERKENIKPSLGSKKNLLESIPTHSDQEKEVNIKKPEDNENLDDKDDDTTRVDESLNIKVEAEEEKAKSGDETNKEEDEDDEEAEEEEEEEEEEEDEDDDDNNEEEEFECYPPGMKVQVRYGRGKNQKMYEASIKDSDVEGGEVLYLVHYCGWNVRYDEWIKADKIVRPADKNVPKIKHRKKIKNKLDKEKDKDEKYSPKNCKLRRLSKPPFQTNPSPEMVSKLDLTDAKNSDTAHIKSIEITSILNGLQASESSAEDSEQEDERGAQDMDNNGKEESKIDHLTNNRNDLISKEEQNSSSLLEENKVHADLVISKPVSKSPERLRKDIEVLSEDTDYEEDEVTKKRKDVKKDTTDKSSKPQIKRGKRRYCNTEECLKTGSPGKKEEKAKNKESLCMENSSNSSSDEDEEETKAKMTPTKKYNGLEEKRKSLRTTGFYSGFSEVAEKRIKLLNNSDERLQNSRAKDRKDVWSSIQGQWPKKTLKELFSDSDTEAAASPPHPAPEEGVAEESLQTVAEEESCSPSVELEKPPPVNVDSKPIEEKTVEVNDRKAEFPSSGSNSVLNTPPTTPESPSSVTVTEGSRQQSSVTVSEPLAPNQEEVRSIKSETDSTIEVDSVAGELQDLQSEGNSSPAGFDASVSSSSSNQPEPEHPEKACTGQKRVKDAQGGGSSSKKQKRSHKATVVNNKKKGKGTNSSDSEELSAGESITKSQPVKSVSTGMKSHSTKSPARTQSPGKCGKNGDKDPDLKEPSNRLPKVYKWSFQMSDLENMTSAERITILQEKLQEIRKHYLSLKSEVASIDRRRKRLKKKERESAATSSSSSSPSSSSITAAVMLTLAEPSMSSASQNGMSVECR	chr1:235131634-235328219[-]	"Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes. Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4A. Involved in spermatogenesis, together with ARID4A, where it functions as a transcriptional coactivator for AR (androgen receptor) and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier. Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor."	PDB: 7DM4	HGNC:15550	ARI4B_HUMAN	Reviewed	ENSG00000054267	.	.	.	.	.
Mol00236	Protein	Arylamine N-acetyltransferase 1 (NAT1)	Arylamide acetylase 1; Monomorphic arylamine N-acetyltransferase; MNAT; N-acetyltransferase type 1; NAT-1; AAC1	NAT1	9	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000307719.9, NAT1-201, 1799; ENST00000517492.5, NAT1-203, 2280; ENST00000518029.5, NAT1-205, 2162; ENST00000545197.3, NAT1-208, 1902; ENST00000520546.1, NAT1-207, 1446; ENST00000517441.5, NAT1-202, 1059; ENST00000519006.5, NAT1-206, 804; ENST00000517574.5, NAT1-204, 333"	MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVVRRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYIVDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDLLEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLTHRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI	chr8:18170477-18223689[+]	Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens.	PDB: 2IJA; PDB: 2PQT	HGNC:7645	ARY1_HUMAN	Reviewed	ENSG00000171428	.	.	.	.	.
Mol00237	Protein	Autophagy-related protein 2 homolog B (ATG2B)	C14orf103	ATG2B	55102	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359933.6, ATG2B-202, 13162; ENST00000261834.9, ATG2B-201, 1920; ENST00000473234.1, ATG2B-203, 550; ENST00000488421.1, ATG2B-204, 522; ENST00000554151.1, ATG2B-206, 333; ENST00000555263.1, ATG2B-207, 492; ENST00000553643.1, ATG2B-205, 482"	MPWPFSESIKKRACRYLLQRYLGHFLQEKLSLEQLSLDLYQGTGSLAQVPLDKWCLNEILESADAPLEVTEGFIQSISLSVPWGSLLQDNCALEVRGLEMVFRPRPRPATGSEPMYWSSFMTSSMQLAKECLSQKLTDEQGEGSQPFEGLEKFAETIETVLRRVKVTFIDTVLRIEHVPENSKTGTALEIRIERTVYCDETADESSGINVHQPTAFAHKLLQLSGVSLFWDEFSASAKSSPVCSTAPVETEPKLSPSWNPKIIYEPHPQLTRNLPEIAPSDPVQIGRLIGRLELSLTLKQNEVLPGAKLDVDGQIDSIHLLLSPRQVHLLLDMLAAIAGPENSSKIGLANKDRKNRPMQQEDEYRIQMELNRYYLRKDSLSVGVSSEQSFYETETARTPSSREEEVFFSMADMDMSHSLSSLPPLGDPPNMDLELSLTSTYTNTPAGSPLSATVLQPTWGEFLDHHKEQPVRGSTFPSNLVHPTPLQKTSLPSRSVSVDESRPELIFRLAVGTFSISVLHIDPLSPPETSQNLNPLTPMAVAFFTCIEKIDPARFSTEDFKSFRAVFAEACSHDHLRFIGTGIKVSYEQRQRSASRYFSTDMSIGQMEFLECLFPTDFHSVPPHYTELLTFHSKEETGSHSPVCLQLHYKHSENRGPQGNQARLSSVPHKAELQIKLNPVCCELDISIVDRLNSLLQPQKLATVEMMASHMYTSYNKHISLHKAFTEVFLDDSHSPANCRISVQVATPALNLSVRFPIPDLRSDQERGPWFKKSLQKEILYLAFTDLEFKTEFIGGSTPEQIKLELTFRELIGSFQEEKGDPSIKFFHVSSGVDGDTTSSDDFDWPRIVLKINPPAMHSILERIAAEEEEENDGHYQEEEEGGAHSLKDVCDLRRPAPSPFSSRRVMFENEQMVMPGDPVEMTEFQDKAISNSHYVLELTLPNIYVTLPNKSFYEKLYNRIFNDLLLWEPTAPSPVETFENISYGIGLSVASQLINTFNKDSFSAFKSAVHYDEESGSEEETLQYFSTVDPNYRSRRKKKLDSQNKNSQSFLSVLLNINHGLIAVFTDVKQDNGDLLENKHGEFWLEFNSGSLFCVTKYEGFDDKHYICLHSSSFSLYHKGIVNGVILPTETRLPSSTRPHWLEPTIYSSEEDGLSKTSSDGVGGDSLNMLSVAVKILSDKSESNTKEFLIAVGLKGATLQHRMLPSGLSWHEQILYFLNIADEPVLGYNPPTSFTTFHVHLWSCALDYRPLYLPIRSLLTVETFSVSSSVALDKSSSTLRIILDEAALHLSDKCNTVTINLSRDYVRVMDMGLLELTITAVKSDSDGEQTEPRFELHCSSDVVHIRTCSDSCAALMNLIQYIASYGDLQTPNKADMKPGAFQRRSKVDSSGRSSSRGPVLPEADQQMLRDLMSDAMEEIDMQQGTSSVKPQANGVLDEKSQIQEPCCSDLFLFPDESGNVSQESGPTYASFSHHFISDAMTGVPTENDDFCILFAPKAAMQEKEEEPVIKIMVDDAIVIRDNYFSLPVNKTDTSKAPLHFPIPVIRYVVKEVSLVWHLYGGKDFGIVPPTSPAKSYISPHSSPSHTPTRHGRNTVCGGKGRNHDFLMEIQLSKVKFQHEVYPPCKPDCDSSLSEHPVSRQVFIVQDLEIRDRLATSQMNKFLYLYCSKEMPRKAHSNMLTVKALHVCPESGRSPQECCLRVSLMPLRLNIDQDALFFLKDFFTSLSAEVELQMTPDPEVKKSPGADVTCSLPRHLSTSKEPNLVISFSGPKQPSQNDSANSVEVVNGMEEKNFSAEEASFRDQPVFFREFRFTSEVPIRLDYHGKHVSMDQGTLAGILIGLAQLNCSELKLKRLSYRHGLLGVDKLFSYAITEWLNDIKKNQLPGILGGVGPMHSLVQLVQGLKDLVWLPIEQYRKDGRIVRGFQRGAASFGTSTAMAALELTNRMVQTIQAAAETAYDMVSPGTLSIEPKKTKRFPHHRLAHQPVDLREGVAKAYSVVKEGITDTAQTIYETAAREHESRGVTGAVGEVLRQIPPAVVKPLIVATEATSNVLGGMRNQIRPDVRQDESQKWRHGDD	chr14:96279195-96363341[-]	"Lipid transfer protein required for both autophagosome formation and regulation of lipid droplet morphology and dispersion. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to the IM for membrane expansion. Lipid transfer activity is enhanced by WDR45/WIPI4, which promotes ATG2B-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes."	.	HGNC:20187	ATG2B_HUMAN	Reviewed	ENSG00000066739	.	.	.	.	.
Mol00238	Protein	Ubiquitin-like-conjugating enzyme ATG3 (ATG3)	Autophagy-related protein 3; APG3-like; hApg3; Protein PC3-96; APG3; APG3L	ATG3	64422	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000283290.10, ATG3-201, 1568; ENST00000402314.6, ATG3-202, 3010; ENST00000492886.5, ATG3-206, 639; ENST00000496423.1, ATG3-209, 737; ENST00000495756.5, ATG3-208, 1455; ENST00000494571.1, ATG3-207, 2758; ENST00000488910.1, ATG3-205, 681; ENST00000465980.1, ATG3-203, 560; ENST00000467275.1, ATG3-204, 559"	MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTGKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLENKDNIRLQDCSALCEEEEDEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM	chr3:112532510-112562046[-]	"E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway."	PDB: 4NAW	HGNC:20962	ATG3_HUMAN	Reviewed	ENSG00000144848	.	.	.	.	.
Mol00239	Protein	Cysteine protease ATG4B (ATG4B)	AUT-like 1 cysteine endopeptidase; Autophagy-related cysteine endopeptidase 1; Autophagin-1; Autophagy-related protein 4 homolog B; HsAPG4B; hAPG4B; APG4B; AUTL1; KIAA0943	ATG4B	23192	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000404914.8, ATG4B-205, 2797; ENST00000405546.7, ATG4B-206, 3294; ENST00000402096.5, ATG4B-204, 1685; ENST00000400771.7, ATG4B-202, 663; ENST00000419606.5, ATG4B-208, 553; ENST00000625810.2, ATG4B-226, 370; ENST00000344376.9, ATG4B-201, 1566; ENST00000400772.6, ATG4B-203, 625; ENST00000415107.5, ATG4B-207, 356; ENST00000430617.6, ATG4B-212, 623; ENST00000491867.5, ATG4B-222, 435; ENST00000482507.5, ATG4B-220, 2414; ENST00000494465.5, ATG4B-225, 2365; ENST00000475693.1, ATG4B-217, 2237; ENST00000483778.5, ATG4B-221, 1103; ENST00000493618.5, ATG4B-223, 899; ENST00000460211.5, ATG4B-213, 871; ENST00000494132.1, ATG4B-224, 828; ENST00000425239.5, ATG4B-209, 807; ENST00000475195.5, ATG4B-216, 762; ENST00000468018.5, ATG4B-215, 721; ENST00000465399.5, ATG4B-214, 581; ENST00000428861.1, ATG4B-210, 580; ENST00000479554.5, ATG4B-218, 556; ENST00000429899.1, ATG4B-211, 524; ENST00000479941.1, ATG4B-219, 374"	MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRKNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFIDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRTSVPCAGATAFPADSDRHCNGFPAGAEVTNRPSPWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPTDGCFIPDESFHCQHPPCRMSIAELDPSIAVGFFCKTEDDFNDWCQQVKKLSLLGGALPMFELVELQPSHLACPDVLNLSLDSSDVERLERFFDSEDEDFEILSL	chr2:241637213-241673857[+]	"Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3. In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS). Compared to other members of the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for proteolytic activation of ATG8 proteins, while it displays weaker delipidation activity than other ATG4 paralogs. Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy."	PDB: 2CY7; PDB: 2D1I; PDB: 2Z0D; PDB: 2Z0E; PDB: 2ZZP; PDB: 5LXH; PDB: 5LXI	HGNC:20790	ATG4B_HUMAN	Reviewed	ENSG00000168397	.	.	.	.	.
Mol00240	Protein	Autophagy-related protein 9A (ATG9A)	APG9-like 1; mATG9; APG9L1	ATG9A	79065	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361242.9, ATG9A-201, 3770; ENST00000409618.5, ATG9A-205, 4025; ENST00000396761.6, ATG9A-202, 3799; ENST00000409422.5, ATG9A-204, 2512; ENST00000436856.5, ATG9A-212, 893; ENST00000432520.5, ATG9A-210, 796; ENST00000429920.1, ATG9A-208, 733; ENST00000428226.5, ATG9A-207, 700; ENST00000457841.5, ATG9A-217, 699; ENST00000443140.5, ATG9A-214, 685; ENST00000439812.5, ATG9A-213, 589; ENST00000431715.5, ATG9A-209, 581; ENST00000434939.1, ATG9A-211, 568; ENST00000409033.7, ATG9A-203, 3701; ENST00000456708.5, ATG9A-216, 576; ENST00000412355.5, ATG9A-206, 574; ENST00000455079.5, ATG9A-215, 558; ENST00000488833.1, ATG9A-221, 487; ENST00000475339.1, ATG9A-219, 812; ENST00000466217.5, ATG9A-218, 594; ENST00000486766.2, ATG9A-220, 579"	MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSAGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAASLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAHSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPDEGGEGARAPQSIPRSASYPCAAPRPGAPETTALHGGFQRRYGGITDPGTVPRVPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV	chr2:219219380-219229717[-]	"Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1. In addition to autophagy, also plays a role in necrotic cell death."	PDB: 6WQZ; PDB: 6WR4; PDB: 7JLO; PDB: 7JLP; PDB: 7JLQ	HGNC:22408	ATG9A_HUMAN	Reviewed	ENSG00000198925	.	.	.	.	.
Mol00241	Protein	Serine-protein kinase ATM (ATM)	Ataxia telangiectasia mutated; A-T mutated	ATM	472	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000675843.1, ATM-229, 12915; ENST00000452508.6, ATM-203, 12954; ENST00000683468.1, ATM-242, 4908; ENST00000682465.1, ATM-235, 2862; ENST00000683150.1, ATM-240, 593; ENST00000639953.1, ATM-226, 587; ENST00000640388.1, ATM-227, 578; ENST00000526567.5, ATM-209, 560; ENST00000639240.1, ATM-225, 498; ENST00000683914.1, ATM-246, 442; ENST00000530958.5, ATM-214, 5718; ENST00000531525.2, ATM-215, 1513; ENST00000684029.1, ATM-247, 1374; ENST00000601453.2, ATM-222, 582; ENST00000532931.5, ATM-217, 481; ENST00000278616.9, ATM-201, 12717; ENST00000638443.1, ATM-223, 2146; ENST00000675595.1, ATM-228, 9309; ENST00000527805.6, ATM-212, 9287; ENST00000684037.1, ATM-248, 3020; ENST00000529588.5, ATM-213, 502; ENST00000683524.1, ATM-244, 6870; ENST00000682286.1, ATM-231, 6403; ENST00000638786.2, ATM-224, 4344; ENST00000682516.1, ATM-236, 3011; ENST00000682147.1, ATM-230, 1344; ENST00000682430.1, ATM-234, 993; ENST00000525178.5, ATM-207, 880; ENST00000533979.5, ATM-221, 705; ENST00000532765.1, ATM-216, 610; ENST00000419286.2, ATM-202, 302; ENST00000525012.5, ATM-205, 258; ENST00000533526.1, ATM-218, 234; ENST00000683174.1, ATM-241, 13130; ENST00000684447.1, ATM-253, 8139; ENST00000684152.1, ATM-250, 7062; ENST00000682302.1, ATM-233, 6064; ENST00000524792.5, ATM-204, 5912; ENST00000683100.1, ATM-239, 5156; ENST00000683488.1, ATM-243, 5020; ENST00000684180.1, ATM-252, 4120; ENST00000525056.2, ATM-206, 3608; ENST00000533690.5, ATM-219, 3354; ENST00000682569.1, ATM-237, 3013; ENST00000683605.1, ATM-245, 2884; ENST00000533733.6, ATM-220, 2565; ENST00000684061.1, ATM-249, 2529; ENST00000682956.1, ATM-238, 2353; ENST00000684179.1, ATM-251, 2243; ENST00000525537.3, ATM-208, 1799; ENST00000682289.1, ATM-232, 1337; ENST00000527181.1, ATM-210, 740; ENST00000527389.2, ATM-211, 401"	MSLVLNDLLICCRQLEHDRATERKKEVEKFKRLIRDPETIKHLDRHSDSKQGKYLNWDAVFRFLQKYIQKETECLRIAKPNVSASTQASRQKKMQEISSLVKYFIKCANRRAPRLKCQELLNYIMDTVKDSSNGAIYGADCSNILLKDILSVRKYWCEISQQQWLELFSVYFRLYLKPSQDVHRVLVARIIHAVTKGCCSQTDGLNSKFLDFFSKAIQCARQEKSSSGLNHILAALTIFLKTLAVNFRIRVCELGDEILPTLLYIWTQHRLNDSLKEVIIELFQLQIYIHHPKGAKTQEKGAYESTKWRSILYNLYDLLVNEISHIGSRGKYSSGFRNIAVKENLIELMADICHQVFNEDTRSLEISQSYTTTQRESSDYSVPCKRKKIELGWEVIKDHLQKSQNDFDLVPWLQIATQLISKYPASLPNCELSPLLMILSQLLPQQRHGERTPYVLRCLTEVALCQDKRSNLESSQKSDLLKLWNKIWCITFRGISSEQIQAENFGLLGAIIQGSLVEVDREFWKLFTGSACRPSCPAVCCLTLALTTSIVPGTVKMGIEQNMCEVNRSFSLKESIMKWLLFYQLEGDLENSTEVPPILHSNFPHLVLEKILVSLTMKNCKAAMNFFQSVPECEHHQKDKEELSFSEVEELFLQTTFDKMDFLTIVRECGIEKHQSSIGFSVHQNLKESLDRCLLGLSEQLLNNYSSEITNSETLVRCSRLLVGVLGCYCYMGVIAEEEAYKSELFQKAKSLMQCAGESITLFKNKTNEEFRIGSLRNMMQLCTRCLSNCTKKSPNKIASGFFLRLLTSKLMNDIADICKSLASFIKKPFDRGEVESMEDDTNGNLMEVEDQSSMNLFNDYPDSSVSDANEPGESQSTIGAINPLAEEYLSKQDLLFLDMLKFLCLCVTTAQTNTVSFRAADIRRKLLMLIDSSTLEPTKSLHLHMYLMLLKELPGEEYPLPMEDVLELLKPLSNVCSLYRRDQDVCKTILNHVLHVVKNLGQSNMDSENTRDAQGQFLTVIGAFWHLTKERKYIFSVRMALVNCLKTLLEADPYSKWAILNVMGKDFPVNEVFTQFLADNHHQVRMLAAESINRLFQDTKGDSSRLLKALPLKLQQTAFENAYLKAQEGMREMSHSAENPETLDEIYNRKSVLLTLIAVVLSCSPICEKQALFALCKSVKENGLEPHLVKKVLEKVSETFGYRRLEDFMASHLDYLVLEWLNLQDTEYNLSSFPFILLNYTNIEDFYRSCYKVLIPHLVIRSHFDEVKSIANQIQEDWKSLLTDCFPKILVNILPYFAYEGTRDSGMAQQRETATKVYDMLKSENLLGKQIDHLFISNLPEIVVELLMTLHEPANSSASQSTDLCDFSGDLDPAPNPPHFPSHVIKATFAYISNCHKTKLKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSLLLKDIKSGLGGAWAFVLRDVIYTLIHYINQRPSCIMDVSLRSFSLCCDLLSQVCQTAVTYCKDALENHLHVIVGTLIPLVYEQVEVQKQVLDLLKYLVIDNKDNENLYITIKLLDPFPDHVVFKDLRITQQKIKYSRGPFSLLEEINHFLSVSVYDALPLTRLEGLKDLRRQLELHKDQMVDIMRASQDNPQDGIMVKLVVNLLQLSKMAINHTGEKEVLEAVGSCLGEVGPIDFSTIAIQHSKDASYTKALKLFEDKELQWTFIMLTYLNNTLVEDCVKVRSAAVTCLKNILATKTGHSFWEIYKMTTDPMLAYLQPFRTSRKKFLEVPRFDKENPFEGLDDINLWIPLSENHDIWIKTLTCAFLDSGGTKCEILQLLKPMCEVKTDFCQTVLPYLIHDILLQDTNESWRNLLSTHVQGFFTSCLRHFSQTSRSTTPANLDSESEHFFRCCLDKKSQRTMLAVVDYMRRQKRPSSGTIFNDAFWLDLNYLEVAKVAQSCAAHFTALLYAEIYADKKSMDDQEKRSLAFEEGSQSTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSLYGCGGGKMLQPITRLRTYEHEAMWGKALVTYDLETAIPSSTRQAGIIQALQNLGLCHILSVYLKGLDYENKDWCPELEELHYQAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEVEEMCKRSLESVYSLYPTLSRLQAIGELESIGELFSRSVTHRQLSEVYIKWQKHSQLLKDSDFSFQEPIMALRTVILEILMEKEMDNSQRECIKDILTKHLVELSILARTFKNTQLPERAIFQIKQYNSVSCGVSEWQLEEAQVFWAKKEQSLALSILKQMIKKLDASCAANNPSLKLTYTECLRVCGNWLAETCLENPAVIMQTYLEKAVEVAGNYDGESSDELRNGKMKAFLSLARFSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTNRYTVKVQRELELDELALRALKEDRKRFLCKAVENYINCLLSGEEHDMWVFRLCSLWLENSGVSEVNGMMKRDGMKIPTYKFLPLMYQLAARMGTKMMGGLGFHEVLNNLISRISMDHPHHTLFIILALANANRDEFLTKPEVARRSRITKNVPKQSSQLDEDRTEAANRIICTIRSRRPQMVRSVEALCDAYIILANLDATQWKTQRKGINIPADQPITKLKNLEDVVVPTMEIKVDHTGEYGNLVTIQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVKGRDDLRQDAVMQQVFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDGAHKRYRPNDFSAFQCQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFLDPAIWFEKRLAYTRSVATSSIVGYILGLGDRHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFRRCCEKTMEVMRNSQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDETELHPTLNADDQECKRNLSDIDQSFNKVAERVLMRLQEKLKGVEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGWKAWV	chr11:108223044-108369102[+]	"Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response. Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks. Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization."	PDB: 5NP0; PDB: 5NP1; PDB: 6HKA; PDB: 6K9K; PDB: 6K9L; PDB: 7NI4; PDB: 7NI5; PDB: 7NI6	HGNC:795	ATM_HUMAN	Reviewed	ENSG00000149311	.	.	.	.	.
Mol00242	Protein	ATM interactor (ATMIN)	ATM/ATR-substrate CHK2-interacting zinc finger protein; ASCIZ; Zinc finger protein 822; KIAA0431; ZNF822	ATMIN	23300	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000299575.5, ATMIN-201, 4881; ENST00000566488.1, ATMIN-206, 5343; ENST00000564241.5, ATMIN-204, 4803; ENST00000565237.1, ATMIN-205, 587; ENST00000539819.5, ATMIN-202, 2434; ENST00000562969.1, ATMIN-203, 505"	MAASEAAAAAGSAALAAGARAVPAATTGAAAAASGPWVPPGPRLRGSRPRPAGATQQPAVPAPPAGELIQPSVSELSRAVRTNILCTVRGCGKILPNSPALNMHLVKSHRLQDGIVNPTIRKDLKTGPKFYCCPIEGCPRGPERPFSQFSLVKQHFMKMHAEKKHKCSKCSNSYGTEWDLKRHAEDCGKTFRCTCGCPYASRTALQSHIYRTGHEIPAEHRDPPSKKRKMENCAQNQKLSNKTIESLNNQPIPRPDTQELEASEIKLEPSFEDSCGSNTDKQTLTTPPRYPQKLLLPKPKVALVKLPVMQFSVMPVFVPTADSSAQPVVLGVDQGSATGAVHLMPLSVGTLILGLDSEACSLKESLPLFKIANPIAGEPISTGVQVNFGKSPSNPLQELGNTCQKNSISSINVQTDLSYASQNFIPSAQWATADSSVSSCSQTDLSFDSQVSLPISVHTQTFLPSSKVTSSIAAQTDAFMDTCFQSGGVSRETQTSGIESPTDDHVQMDQAGMCGDIFESVHSSYNVATGNIISNSLVAETVTHSLLPQNEPKTLNQDIEKSAPIINFSAQNSMLPSQNMTDNQTQTIDLLSDLENILSSNLPAQTLDHRSLLSDTNPGPDTQLPSGPAQNPGIDFDIEEFFSASNIQTQTEESELSTMTTEPVLESLDIETQTDFLLADTSAQSYGCRGNSNFLGLEMFDTQTQTDLNFFLDSSPHLPLGSILKHSSFSVSTDSSDTETQTEGVSTAKNIPALESKVQLNSTETQTMSSGFETLGSLFFTSNETQTAMDDFLLADLAWNTMESQFSSVETQTSAEPHTVSNF	chr16:81035842-81047350[+]	Transcription factor. Plays a crucial role in cell survival and RAD51 foci formation in response to methylating DNA damage. Involved in regulating the activity of ATM in the absence of DNA damage. May play a role in stabilizing ATM. Binds to the DYNLL1 promoter and activates its transcription.	.	HGNC:29034	ATMIN_HUMAN	Reviewed	ENSG00000166454	.	.	.	.	.
Mol00243	Protein	Bcl-2-like protein 1 (BCL2L1)	Bcl2-L-1; Apoptosis regulator Bcl-X; BCL2L; BCLX	BCL2L1	598	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000307677.5, BCL2L1-201, 2574; ENST00000676582.1, BCL2L1-210, 3212; ENST00000376062.6, BCL2L1-203, 2578; ENST00000456404.6, BCL2L1-209, 2562; ENST00000678563.1, BCL2L1-214, 2544; ENST00000376055.9, BCL2L1-202, 2496; ENST00000420488.6, BCL2L1-204, 2444; ENST00000434194.2, BCL2L1-206, 2441; ENST00000439267.2, BCL2L1-207, 2426; ENST00000676942.1, BCL2L1-211, 2413; ENST00000677194.1, BCL2L1-212, 2373; ENST00000422920.2, BCL2L1-205, 2227; ENST00000450273.2, BCL2L1-208, 1292; ENST00000678671.1, BCL2L1-215, 3257; ENST00000677494.1, BCL2L1-213, 1515"	MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK	chr20:31664452-31723989[-]	"Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.; FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release."	PDB: 1BXL; PDB: 1G5J; PDB: 1LXL; PDB: 1MAZ; PDB: 1R2D; PDB: 1R2E; PDB: 1R2G; PDB: 1R2H; PDB: 1R2I; PDB: 1YSG; PDB: 1YSI; PDB: 1YSN; PDB: 2B48; PDB: 2LP8; PDB: 2LPC; PDB: 2M03; PDB: 2M04; PDB: 2ME8; PDB: 2ME9; PDB: 2MEJ; PDB: 2O1Y; PDB: 2O2M; PDB: 2O2N; PDB: 2P1L; PDB: 2PON; PDB: 2YJ1; PDB: 2YQ6; PDB: 2YQ7; PDB: 2YXJ; PDB: 3CVA; PDB: 3FDL; PDB: 3FDM; PDB: 3INQ; PDB: 3IO8; PDB: 3PL7; PDB: 3QKD; PDB: 3R85; PDB: 3SP7; PDB: 3SPF; PDB: 3WIZ; PDB: 3ZK6; PDB: 3ZLN; PDB: 3ZLO; PDB: 3ZLR; PDB: 4A1U; PDB: 4A1W; PDB: 4AQ3; PDB: 4BPK; PDB: 4C52; PDB: 4C5D; PDB: 4CIN; PDB: 4EHR; PDB: 4HNJ; PDB: 4IEH; PDB: 4PPI; PDB: 4QVE; PDB: 4QVF; PDB: 4QVX; PDB: 4TUH; PDB: 4Z9V; PDB: 5AGW; PDB: 5AGX; PDB: 5B1Z; PDB: 5C3G; PDB: 5FMJ; PDB: 5FMK; PDB: 5VAY; PDB: 5VX3; PDB: 6BF2; PDB: 6DCN; PDB: 6DCO; PDB: 6F46; PDB: 6HJL; PDB: 6IJQ; PDB: 6LHD; PDB: 6O0K; PDB: 6O0L; PDB: 6O0M; PDB: 6O0O; PDB: 6O0P; PDB: 6RNU; PDB: 6ST2; PDB: 6UVC; PDB: 6UVD; PDB: 6UVE; PDB: 6UVF; PDB: 6UVG; PDB: 6UVH; PDB: 6VWC; PDB: 6X7I; PDB: 6YLI; PDB: 6ZHC; PDB: 7CA4; PDB: 7JGV; PDB: 7JGW; PDB: 7LH7	HGNC:992	B2CL1_HUMAN	Reviewed	ENSG00000171552	.	.	.	.	.
Mol00244	Protein	Transcription regulator protein BACH2 (BACH2)	BTB and CNC homolog 2	BACH2	60468	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000257749.9, BACH2-201, 9215; ENST00000406998.7, BACH2-203, 4047; ENST00000343122.7, BACH2-202, 3981; ENST00000453877.6, BACH2-204, 3151; ENST00000695952.1, BACH2-210, 2888; ENST00000695954.1, BACH2-212, 689; ENST00000494747.2, BACH2-209, 540; ENST00000472023.5, BACH2-206, 498; ENST00000695955.1, BACH2-213, 480; ENST00000493201.5, BACH2-208, 436; ENST00000481150.1, BACH2-207, 395; ENST00000695953.1, BACH2-211, 2800; ENST00000470301.6, BACH2-205, 621"	MSVDEKPDSPMYVYESTVHCTNILLGLNDQRKKDILCDVTLIVERKEFRAHRAVLAACSEYFWQALVGQTKNDLVVSLPEEVTARGFGPLLQFAYTAKLLLSRENIREVIRCAEFLRMHNLEDSCFSFLQTQLLNSEDGLFVCRKDAACQRPHEDCENSAGEEEDEEEETMDSETAKMACPRDQMLPEPISFEAAAIPVAEKEEALLPEPDVPTDTKESSEKDALTQYPRYKKYQLACTKNVYNASSHSTSGFASTFREDNSSNSLKPGLARGQIKSEPPSEENEEESITLCLSGDEPDAKDRAGDVEMDRKQPSPAPTPTAPAGAACLERSRSVASPSCLRSLFSITKSVELSGLPSTSQQHFARSPACPFDKGITQGDLKTDYTPFTGNYGQPHVGQKEVSNFTMGSPLRGPGLEALCKQEGELDRRSVIFSSSACDQVSTSVHSYSGVSSLDKDLSEPVPKGLWVGAGQSLPSSQAYSHGGLMADHLPGRMRPNTSCPVPIKVCPRSPPLETRTRTSSSCSSYSYAEDGSGGSPCSLPLCEFSSSPCSQGARFLATEHQEPGLMGDGMYNQVRPQIKCEQSYGTNSSDESGSFSEADSESCPVQDRGQEVKLPFPVDQITDLPRNDFQMMIKMHKLTSEQLEFIHDVRRRSKNRIAAQRCRKRKLDCIQNLECEIRKLVCEKEKLLSERNQLKACMGELLDNFSCLSQEVCRDIQSPEQIQALHRYCPVLRPMDLPTASSINPAPLGAEQNIAASQCAVGENVPCCLEPGAAPPGPPWAPSNTSENCTSGRRLEGTDPGTFSERGPPLEPRSQTVTVDFCQEMTDKCTTDEQPRKDYT	chr6:89926528-90296843[-]	"Transcriptional regulator that acts as repressor or activator. Binds to Maf recognition elements (MARE). Plays an important role in coordinating transcription activation and repression by MAFK. Induces apoptosis in response to oxidative stress through repression of the antiapoptotic factor HMOX1. Positively regulates the nuclear import of actin. Is a key regulator of adaptive immunity, crucial for the maintenance of regulatory T-cell function and B-cell maturation."	PDB: 3OHU; PDB: 3OHV	HGNC:14078	BACH2_HUMAN	Reviewed	ENSG00000112182	.	.	.	.	.
Mol00245	Protein	Bcl-2-associated agonist of cell death (BAD)	BAD; Bcl-2-binding component 6; Bcl-2-like protein 8; Bcl2-L-8; Bcl-xL/Bcl-2-associated death promoter; Bcl2 antagonist of cell death; BBC6; BCL2L8	BAD	572	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000309032.8, BAD-201, 929; ENST00000394532.7, BAD-203, 1157; ENST00000394531.3, BAD-202, 631; ENST00000544785.1, BAD-207, 525; ENST00000492141.1, BAD-204, 359; ENST00000493798.1, BAD-205, 325; ENST00000544271.1, BAD-206, 552"	MFQIPEFEPSEQEDSSSAERGLGPSPAGDGPSGSGKHHRQAPGLLWDASHQQEQPTSSSHHGGAGAVEIRSRHSSYPAGTEDDEGMGEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFVDSFKKGLPRPKSAGTATQMRQSSSWTRVFQSWWDRNLGRGSSAPSQ	chr11:64269830-64284704[-]	"Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways."	PDB: 1G5J	HGNC:936	BAD_HUMAN	Reviewed	ENSG00000002330	.	.	.	.	.
Mol00246	Protein	BAG family molecular chaperone regulator 1 (BAG1)	BAG-1; Bcl-2-associated athanogene 1; HAP	BAG1	573	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000634734.3, BAG1-210, 3820; ENST00000379704.7, BAG1-202, 1128; ENST00000473781.1, BAG1-207, 681; ENST00000635077.1, BAG1-211, 658; ENST00000473464.2, BAG1-206, 551; ENST00000488499.1, BAG1-208, 485; ENST00000379707.7, BAG1-203, 1396; ENST00000467389.6, BAG1-204, 1173; ENST00000493917.5, BAG1-209, 526; ENST00000379701.5, BAG1-201, 1977; ENST00000468274.1, BAG1-205, 935"	MAQRGGARRPRGDRERLGSRLRALRPGREPRQSEPPAQRGPPPSGRPPARSTASGHDRPTRGAAAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEMAAAGLTVTVTHSNEKHDLHVTSQQGSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKKNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE	chr9:33247820-33264720[-]	"Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli."	PDB: 1HX1; PDB: 1WXV; PDB: 3FZF; PDB: 3FZH; PDB: 3FZK; PDB: 3FZL; PDB: 3FZM; PDB: 3LDQ; PDB: 3M3Z; PDB: 5AQF; PDB: 5AQG; PDB: 5AQH; PDB: 5AQI; PDB: 5AQJ; PDB: 5AQK; PDB: 5AQL; PDB: 5AQM; PDB: 5AQN; PDB: 5AQO; PDB: 5AQP; PDB: 5AQQ; PDB: 5AQR; PDB: 5AQS; PDB: 5AQT; PDB: 5AQU; PDB: 5AQV	HGNC:937	BAG1_HUMAN	Reviewed	ENSG00000107262	.	.	.	.	.
Mol00247	Protein	BAG family molecular chaperone regulator 3 (BAG3)	BAG-3; Bcl-2-associated athanogene 3; Bcl-2-binding protein Bis; Docking protein CAIR-1; BIS	BAG3	9531	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369085.8, BAG3-201, 2561; ENST00000450186.1, BAG3-202, 1146"	MSAATHSPMMQVASGNGDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPSEGPKETPSSANGPSREGSRLPPAREGHPVYPQLRPGYIPIPVLHEGAENRQVHPFHVYPQPGMQRFRTEAAAAAPQRSQSPLRGMPETTQPDKQCGQVAAAAAAQPPASHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYISIPVIHEQNVTRPAAQPSFHQAQKTHYPAQQGEYQTHQPVYHKIQGDDWEPRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVDRPQQPMTHRETAPVSQPENKPESKPGPVGPELPPGHIPIQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAPSTAPAEATPPKPGEAEAPPKHPGVLKVEAILEKVQGLEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKAIDVPGQVQVYELQPSNLEADQPLQAIMEMGAVAADKGKKNAGNAEDPHTETQQPEATAAATSNPSSMTDTPGNPAAP	chr10:119651380-119677819[+]	Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport.	.	HGNC:939	BAG3_HUMAN	Reviewed	ENSG00000151929	.	.	.	.	.
Mol00248	Protein	Bcl-2 homologous antagonist/killer (BAK1)	Apoptosis regulator BAK; Bcl-2-like protein 7; Bcl2-L-7; BAK; BCL2L7; CDN1	BAK1	578	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374467.4, BAK1-201, 2170; ENST00000442998.6, BAK1-202, 2212"	MASGQGPGPPRQECGEPALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILNVLVVLGVVLLGQFVVRRFFKS	chr6:33572547-33580293[-]	"Plays a role in the mitochondrial apoptosic process. Upon arrival of cell death signals, promotes mitochondrial outer membrane (MOM) permeabilization by oligomerizing to form pores within the MOM. This releases apoptogenic factors into the cytosol, including cytochrome c, promoting the activation of caspase 9 which in turn processes and activates the effector caspases."	PDB: 1BXL; PDB: 2IMS; PDB: 2IMT; PDB: 2JBY; PDB: 2JCN; PDB: 2LP8; PDB: 2M5B; PDB: 2XPX; PDB: 2YV6; PDB: 3I1H; PDB: 3QBR; PDB: 4D2L; PDB: 4U2U; PDB: 4U2V; PDB: 4UF1; PDB: 5AJK; PDB: 5FMI; PDB: 5FMK; PDB: 5VWV; PDB: 5VWW; PDB: 5VWX; PDB: 5VWY; PDB: 5VWZ; PDB: 5VX0; PDB: 5VX1; PDB: 6ODH; PDB: 6UXM; PDB: 6UXN; PDB: 6UXO; PDB: 6UXP; PDB: 6UXQ; PDB: 6UXR; PDB: 7K02; PDB: 7OFM; PDB: 7OFO	HGNC:949	BAK_HUMAN	Reviewed	ENSG00000030110	.	.	.	.	.
Mol00249	Protein	Beclin 1-associated autophagy-related key regulator (ATG14)	Barkor; Autophagy-related protein 14-like protein; Atg14L; ATG14L; KIAA0831	ATG14	22863	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000247178.6, ATG14-201, 4715; ENST00000558189.1, ATG14-202, 4689"	MASPSGKGARALEAPGCGPRPLARDLVDSVDDAEGLYVAVERCPLCNTTRRRLTCAKCVQSGDFVYFDGRDRERFIDKKERLSRLKSKQEEFQKEVLKAMEGKWITDQLRWKIMSCKMRIEQLKQTICKGNEEMEKNSEGLLKTKEKNQKLYSRAQRHQEKKEKIQRHNRKLGDLVEKKTIDLRSHYERLANLRRSHILELTSVIFPIEEVKTGVRDPADVSSESDSAMTSSTVSKLAEARRTTYLSGRWVCDDHNGDTSISITGPWISLPNNGDYSAYYSWVEEKKTTQGPDMEQSNPAYTISAALCYATQLVNILSHILDVNLPKKLCNSEFCGENLSKQKFTRAVKKLNANILYLCFSQHVNLDQLQPLHTLRNLMYLVSPSSEHLGRSGPFEVRADLEESMEFVDPGVAGESDESGDERVSDEETDLGTDWENLPSPRFCDIPSQSVEVSQSQSTQASPPIASSSAGGMISSAAASVTSWFKAYTGHR	chr14:55366391-55411830[-]	"Required for both basal and inducible autophagy. Determines the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1. Plays a role in autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine. Promotes BECN1 translocation from the trans-Golgi network to autophagosomes. Enhances PIK3C3 activity in a BECN1-dependent manner. Essential for the autophagy-dependent phosphorylation of BECN1. Stimulates the phosphorylation of BECN1, but suppresses the phosphorylation PIK3C3 by AMPK. Binds to STX17-SNAP29 binary t-SNARE complex on autophagosomes and primes it for VAMP8 interaction to promote autophagosome-endolysosome fusion. Modulates the hepatic lipid metabolism."	PDB: 6HOL	HGNC:19962	BAKOR_HUMAN	Reviewed	ENSG00000126775	.	.	.	.	.
Mol00250	Protein	B-cell lymphoma/leukemia 10 (BCL10)	B-cell CLL/lymphoma 10; Bcl-10; CARD-containing molecule enhancing NF-kappa-B; CARD-like apoptotic protein; hCLAP; CED-3/ICH-1 prodomain homologous E10-like regulator; CIPER; Cellular homolog of vCARMEN; cCARMEN; Cellular-E10; c-E10; Mammalian CARD-containing adapter molecule E10; mE10; CIPER; CLAP	BCL10	8915	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000648566.1, BCL10-202, 2833; ENST00000620248.2, BCL10-201, 776; ENST00000649060.1, BCL10-203, 1561; ENST00000650582.1, BCL10-205, 1131; ENST00000649434.1, BCL10-204, 573"	MEPTAPSLTEEDLTEVKKDALENLRVYLCEKIIAERHFDHLRAKKILSREDTEEISCRTSSRKRAGKLLDYLQENPKGLDTLVESIRREKTQNFLIQKITDEVLKLRNIKLEHLKGLKCSSCEPFPDGATNNLSRSNSDESNFSEKLRASTVMYHPEGESSTTPFFSTNSSLNLPVLEVGRTENTIFSSTTLPRPGDPGAPPLPPDLQLEEEGTCANSSEMFLPLRSRTVSRQ	chr1:85265776-85276632[-]	"Plays a key role in both adaptive and innate immune signaling by bridging CARD domain-containing proteins to immune activation. Acts by channeling adaptive and innate immune signaling downstream of CARD domain-containing proteins CARD9, CARD11 and CARD14 to activate NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Recruited by activated CARD domain-containing proteins: homooligomerized CARD domain-containing proteins form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10, subsequent recruitment of MALT1 and formation of a CBM complex. This leads to activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Activated by CARD9 downstream of C-type lectin receptors; CARD9-mediated signals are essential for antifungal immunity. Activated by CARD11 downstream of T-cell receptor (TCR) and B-cell receptor (BCR). Promotes apoptosis, pro-caspase-9 maturation and activation of NF-kappa-B via NIK and IKK."	PDB: 2MB9; PDB: 6BZE; PDB: 6GK2	HGNC:989	BCL10_HUMAN	Reviewed	ENSG00000142867	.	.	.	.	.
Mol00252	Protein	BH3-interacting domain death agonist (BID)	p22 BID; BID; p15 BID; p13 BID; p11 BID	BID	637	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000622694.5, BID-211, 2177; ENST00000317361.11, BID-201, 2495; ENST00000614949.4, BID-210, 1988; ENST00000399765.5, BID-203, 1879; ENST00000399767.6, BID-204, 907; ENST00000551952.5, BID-208, 700; ENST00000342111.9, BID-202, 854; ENST00000473439.5, BID-205, 638; ENST00000552886.1, BID-209, 330; ENST00000494097.5, BID-206, 2429; ENST00000550946.5, BID-207, 1394"	MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD	chr22:17734138-17774770[-]	Induces caspases and apoptosis. Counters the protective effect of BCL2.	PDB: 1ZY3; PDB: 2BID; PDB: 2KBW; PDB: 2M5B; PDB: 2M5I; PDB: 4BD2; PDB: 4QVE; PDB: 4ZEQ; PDB: 4ZIG; PDB: 4ZII; PDB: 5AJJ; PDB: 5C3F	HGNC:1050	BID_HUMAN	Reviewed	ENSG00000015475	.	.	.	.	.
Mol00253	Protein	Endoplasmic reticulum chaperone BiP (HSPA5)	78 kDa glucose-regulated protein; GRP-78; Binding-immunoglobulin protein; BiP; Heat shock protein 70 family protein 5; HSP70 family protein 5; Heat shock protein family A member 5; Immunoglobulin heavy chain-binding protein; GRP78	HSPA5	3309	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000324460.7, HSPA5-201, 3921; ENST00000680272.1, HSPA5-207, 3825; ENST00000680032.1, HSPA5-204, 2231; ENST00000680494.1, HSPA5-208, 5402; ENST00000680640.1, HSPA5-209, 4929; ENST00000681774.1, HSPA5-215, 4919; ENST00000681045.1, HSPA5-210, 4858; ENST00000681675.1, HSPA5-214, 4577; ENST00000681424.1, HSPA5-211, 4333; ENST00000679475.1, HSPA5-203, 4281; ENST00000680257.1, HSPA5-206, 4234; ENST00000679355.1, HSPA5-202, 4052; ENST00000681544.1, HSPA5-213, 4028; ENST00000681540.1, HSPA5-212, 3518; ENST00000680234.1, HSPA5-205, 3221"	MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL	chr9:125234853-125241382[-]	"Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation."	PDB: 3IUC; PDB: 3LDL; PDB: 3LDN; PDB: 3LDO; PDB: 3LDP; PDB: 5E84; PDB: 5E85; PDB: 5E86; PDB: 5EVZ; PDB: 5EX5; PDB: 5EXW; PDB: 5EY4; PDB: 5F0X; PDB: 5F1X; PDB: 5F2R; PDB: 6ASY; PDB: 6CZ1; PDB: 6DFM; PDB: 6DFO; PDB: 6DO2; PDB: 6DWS; PDB: 6ZMD	HGNC:5238	BIP_HUMAN	Reviewed	ENSG00000044574	.	.	.	.	.
Mol00254	Protein	Baculoviral IAP repeat-containing protein 1 (BIRC1)	Neuronal apoptosis inhibitory protein; BIRC1	NAIP	4671	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000517649.6, NAIP-208, 7093; ENST00000194097.8, NAIP-201, 6088; ENST00000503719.6, NAIP-204, 5347; ENST00000523981.5, NAIP-210, 4543; ENST00000508426.6, NAIP-205, 4153; ENST00000514857.2, NAIP-207, 579; ENST00000519014.1, NAIP-209, 1078; ENST00000447012.7, NAIP-203, 894; ENST00000315147.8, NAIP-202, 5935; ENST00000508794.6, NAIP-206, 1073"	MATQQKASDERISQFDHNLLPELSALLGLDAVQLAKELEEEEQKERAKMQKGYNSQMRSEAKRLKTFVTYEPYSSWIPQEMAAAGFYFTGVKSGIQCFCCSLILFGAGLTRLPIEDHKRFHPDCGFLLNKDVGNIAKYDIRVKNLKSRLRGGKMRYQEEEARLASFRNWPFYVQGISPCVLSEAGFVFTGKQDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLRSKKSSEEITQYIQSYKGFVDITGEHFVNSWVQRELPMASAYCNDSIFAYEELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQNMKSSAEVTPDLQSRGELCELLETTSESNLEDSIAVGPIVPEMAQGEAQWFQEAKNLNEQLRAAYTSASFRHMSLLDISSDLATDHLLGCDLSIASKHISKPVQEPLVLPEVFGNLNSVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLNRFQLVFYLSLSSTRPDEGLASIICDQLLEKEGSVTEMCVRNIIQQLKNQVLFLLDDYKEICSIPQVIGKLIQKNHLSRTCLLIAVRTNRARDIRRYLETILEIKAFPFYNTVCILRKLFSHNMTRLRKFMVYFGKNQSLQKIQKTPLFVAAICAHWFQYPFDPSFDDVAVFKSYMERLSLRNKATAEILKATVSSCGELALKGFFSCCFEFNDDDLAEAGVDEDEDLTMCLMSKFTAQRLRPFYRFLSPAFQEFLAGMRLIELLDSDRQEHQDLGLYHLKQINSPMMTVSAYNNFLNYVSSLPSTKAGPKIVSHLLHLVDNKESLENISENDDYLKHQPEISLQMQLLRGLWQICPQAYFSMVSEHLLVLALKTAYQSNTVAACSPFVLQFLQGRTLTLGALNLQYFFDHPESLSLLRSIHFPIRGNKTSPRAHFSVLETCFDKSQVPTIDQDYASAFEPMNEWERNLAEKEDNVKSYMDMQRRASPDLSTGYWKLSPKQYKIPCLEVDVNDIDVVGQDMLEILMTVFSASQRIELHLNHSRGFIESIRPALELSKASVTKCSISKLELSAAEQELLLTLPSLESLEVSGTIQSQDQIFPNLDKFLCLKELSVDLEGNINVFSVIPEEFPNFHHMEKLLIQISAEYDPSKLVKLIQNSPNLHVFHLKCNFFSDFGSLMTMLVSCKKLTEIKFSDSFFQAVPFVASLPNFISLKILNLEGQQFPDEETSEKFAYILGSLSNLEELILPTGDGIYRVAKLIIQQCQQLHCLRVLSFFKTLNDDSVVEIAKVAISGGFQKLENLKLSINHKITEEGYRNFFQALDNMPNLQELDISRHFTECIKAQATTVKSLSQCVLRLPRLIRLNMLSWLLDADDIALLNVMKERHPQSKYLTILQKWILPFSPIIQK	chr5:70968166-71025339[-]	"Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.; FUNCTION: Acts as a sensor component of the NLRC4 inflammasome that specifically recognizes and binds needle protein CprI from pathogenic bacteria C.violaceum. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria such as C.violaceum and L.pneumophila."	PDB: 2VM5	HGNC:7634	BIRC1_HUMAN	Reviewed	ENSG00000249437	.	.	.	.	.
Mol00255	Protein	Baculoviral IAP repeat-containing protein 6 (BIRC6)	BIR repeat-containing ubiquitin-conjugating enzyme; BRUCE; RING-type E3 ubiquitin transferase BIRC6; Ubiquitin-conjugating BIR domain enzyme apollon; APOLLON; KIAA1289	BIRC6	57448	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000421745.7, BIRC6-201, 15687; ENST00000648282.1, BIRC6-213, 11526; ENST00000444173.5, BIRC6-203, 575; ENST00000431454.2, BIRC6-202, 508; ENST00000471232.5, BIRC6-209, 4226; ENST00000465130.1, BIRC6-206, 910; ENST00000483194.1, BIRC6-210, 702; ENST00000466527.1, BIRC6-207, 585; ENST00000496555.1, BIRC6-211, 582; ENST00000497023.1, BIRC6-212, 578; ENST00000461788.1, BIRC6-204, 577; ENST00000470250.1, BIRC6-208, 472; ENST00000462504.1, BIRC6-205, 317"	MVTGGGAAPPGTVTEPLPSVIVLSAGRKMAAAAAAASGPGCSSAAGAGAAGVSEWLVLRDGCMHCDADGLHSLSYHPALNAILAVTSRGTIKVIDGTSGATLQASALSAKPGGQVKCQYISAVDKVIFVDDYAVGCRKDLNGILLLDTALQTPVSKQDDVVQLELPVTEAQQLLSACLEKVDISSTEGYDLFITQLKDGLKNTSHETAANHKVAKWATVTFHLPHHVLKSIASAIVNELKKINQNVAALPVASSVMDRLSYLLPSARPELGVGPGRSVDRSLMYSEANRRETFTSWPHVGYRWAQPDPMAQAGFYHQPASSGDDRAMCFTCSVCLVCWEPTDEPWSEHERHSPNCPFVKGEHTQNVPLSVTLATSPAQFPCTDGTDRISCFGSGSCPHFLAAATKRGKICIWDVSKLMKVHLKFEINAYDPAIVQQLILSGDPSSGVDSRRPTLAWLEDSSSCSDIPKLEGDSDDLLEDSDSEEHSRSDSVTGHTSQKEAMEVSLDITALSILQQPEKLQWEIVANVLEDTVKDLEELGANPCLTNSKSEKTKEKHQEQHNIPFPCLLAGGLLTYKSPATSPISSNSHRSLDGLSRTQGESISEQGSTDNESCTNSELNSPLVRRTLPVLLLYSIKESDEKAGKIFSQMNNIMSKSLHDDGFTVPQIIEMELDSQEQLLLQDPPVTYIQQFADAAANLTSPDSEKWNSVFPKPGTLVQCLRLPKFAEEENLCIDSITPCADGIHLLVGLRTCPVESLSAINQVEALNNLNKLNSALCNRRKGELESNLAVVNGANISVIQHESPADVQTPLIIQPEQRNVSGGYLVLYKMNYATRIVTLEEEPIKIQHIKDPQDTITSLILLPPDILDNREDDCEEPIEDMQLTSKNGFEREKTSDISTLGHLVITTQGGYVKILDLSNFEILAKVEPPKKEGTEEQDTFVSVIYCSGTDRLCACTKGGELHFLQIGGTCDDIDEADILVDGSLSKGIEPSSEGSKPLSNPSSPGISGVDLLVDQPFTLEILTSLVELTRFETLTPRFSATVPPCWVEVQQEQQQRRHPQHLHQQHHGDAAQHTRTWKLQTDSNSWDEHVFELVLPKACMVGHVDFKFVLNSNITNIPQIQVTLLKNKAPGLGKVNALNIEVEQNGKPSLVDLNEEMQHMDVEESQCLRLCPFLEDHKEDILCGPVWLASGLDLSGHAGMLTLTSPKLVKGMAGGKYRSFLIHVKAVNERGTEEICNGGMRPVVRLPSLKHQSNKGYSLASLLAKVAAGKEKSSNVKNENTSGTRKSENLRGCDLLQEVSVTIRRFKKTSISKERVQRCAMLQFSEFHEKLLNTLCRKTDDGQITEHAQSLVLDTLCWLAGVHSNGPGSSKEGNENLLSKTRKFLSDIVRVCFFEAGRSIAHKCARFLALCISNGKCDPCQPAFGPVLLKALLDNMSFLPAATTGGSVYWYFVLLNYVKDEDLAGCSTACASLLTAVSRQLQDRLTPMEALLQTRYGLYSSPFDPVLFDLEMSGSSCKNVYNSSIGVQSDEIDLSDVLSGNGKVSSCTAAEGSFTSLTGLLEVEPLHFTCVSTSDGTRIERDDAMSSFGVTPAVGGLSSGTVGEASTALSSAAQVALQSLSHAMASAEQQLQVLQEKQQQLLKLQQQKAKLEAKLHQTTAAAAAAASAVGPVHNSVPSNPVAAPGFFIHPSDVIPPTPKTTPLFMTPPLTPPNEAVSVVINAELAQLFPGSVIDPPAVNLAAHNKNSNKSRMNPLGSGLALAISHASHFLQPPPHQSIIIERMHSGARRFVTLDFGRPILLTDVLIPTCGDLASLSIDIWTLGEEVDGRRLVVATDISTHSLILHDLIPPPVCRFMKITVIGRYGSTNARAKIPLGFYYGHTYILPWESELKLMHDPLKGEGESANQPEIDQHLAMMVALQEDIQCRYNLACHRLETLLQSIDLPPLNSANNAQYFLRKPDKAVEEDSRVFSAYQDCIQLQLQLNLAHNAVQRLKVALGASRKMLSETSNPEDLIQTSSTEQLRTIIRYLLDTLLSLLHASNGHSVPAVLQSTFHAQACEELFKHLCISGTPKIRLHTGLLLVQLCGGERWWGQFLSNVLQELYNSEQLLIFPQDRVFMLLSCIGQRSLSNSGVLESLLNLLDNLLSPLQPQLPMHRRTEGVLDIPMISWVVMLVSRLLDYVATVEDEAAAAKKPLNGNQWSFINNNLHTQSLNRSSKGSSSLDRLYSRKIRKQLVHHKQQLNLLKAKQKALVEQMEKEKIQSNKGSSYKLLVEQAKLKQATSKHFKDLIRLRRTAEWSRSNLDTEVTTAKESPEIEPLPFTLAHERCISVVQKLVLFLLSMDFTCHADLLLFVCKVLARIANATRPTIHLCEIVNEPQLERLLLLLVGTDFNRGDISWGGAWAQYSLTCMLQDILAGELLAPVAAEAMEEGTVGDDVGATAGDSDDSLQQSSVQLLETIDEPLTHDITGAPPLSSLEKDKEIDLELLQDLMEVDIDPLDIDLEKDPLAAKVFKPISSTWYDYWGADYGTYNYNPYIGGLGIPVAKPPANTEKNGSQTVSVSVSQALDARLEVGLEQQAELMLKMMSTLEADSILQALTNTSPTLSQSPTGTDDSLLGGLQAANQTSQLIIQLSSVPMLNVCFNKLFSMLQVHHVQLESLLQLWLTLSLNSSSTGNKENGADIFLYNANRIPVISLNQASITSFLTVLAWYPNTLLRTWCLVLHSLTLMTNMQLNSGSSSAIGTQESTAHLLVSDPNLIHVLVKFLSGTSPHGTNQHSPQVGPTATQAMQEFLTRLQVHLSSTCPQIFSEFLLKLIHILSTERGAFQTGQGPLDAQVKLLEFTLEQNFEVVSVSTISAVIESVTFLVHHYITCSDKVMSRSGSDSSVGARACFGGLFANLIRPGDAKAVCGEMTRDQLMFDLLKLVNILVQLPLSGNREYSARVSVTTNTTDSVSDEEKVSGGKDGNGSSTSVQGSPAYVADLVLANQQIMSQILSALGLCNSSAMAMIIGASGLHLTKHENFHGGLDAISVGDGLFTILTTLSKKASTVHMMLQPILTYMACGYMGRQGSLATCQLSEPLLWFILRVLDTSDALKAFHDMGGVQLICNNMVTSTRAIVNTARSMVSTIMKFLDSGPNKAVDSTLKTRILASEPDNAEGIHNFAPLGTITSSSPTAQPAEVLLQATPPHRRARSAAWSYIFLPEEAWCDLTIHLPAAVLLKEIHIQPHLASLATCPSSVSVEVSADGVNMLPLSTPVVTSGLTYIKIQLVKAEVASAVCLRLHRPRDASTLGLSQIKLLGLTAFGTTSSATVNNPFLPSEDQVSKTSIGWLRLLHHCLTHISDLEGMMASAAAPTANLLQTCAALLMSPYCGMHSPNIEVVLVKIGLQSTRIGLKLIDILLRNCAASGSDPTDLNSPLLFGRLNGLSSDSTIDILYQLGTTQDPGTKDRIQALLKWVSDSARVAAMKRSGRMNYMCPNSSTVEYGLLMPSPSHLHCVAAILWHSYELLVEYDLPALLDQELFELLFNWSMSLPCNMVLKKAVDSLLCSMCHVHPNYFSLLMGWMGITPPPVQCHHRLSMTDDSKKQDLSSSLTDDSKNAQAPLALTESHLATLASSSQSPEAIKQLLDSGLPSLLVRSLASFCFSHISSSESIAQSIDISQDKLRRHHVPQQCNKMPITADLVAPILRFLTEVGNSHIMKDWLGGSEVNPLWTALLFLLCHSGSTSGSHNLGAQQTSARSASLSSAATTGLTTQQRTAIENATVAFFLQCISCHPNNQKLMAQVLCELFQTSPQRGNLPTSGNISGFIRRLFLQLMLEDEKVTMFLQSPCPLYKGRINATSHVIQHPMYGAGHKFRTLHLPVSTTLSDVLDRVSDTPSITAKLISEQKDDKEKKNHEEKEKVKAENGFQDNYSVVVASGLKSQSKRAVSATPPRPPSRRGRTIPDKIGSTSGAEAANKIITVPVFHLFHKLLAGQPLPAEMTLAQLLTLLYDRKLPQGYRSIDLTVKLGSRVITDPSLSKTDSYKRLHPEKDHGDLLASCPEDEALTPGDECMDGILDESLLETCPIQSPLQVFAGMGGLALIAERLPMLYPEVIQQVSAPVVTSTTQEKPKDSDQFEWVTIEQSGELVYEAPETVAAEPPPIKSAVQTMSPIPAHSLAAFGLFLRLPGYAEVLLKERKHAQCLLRLVLGVTDDGEGSHILQSPSANVLPTLPFHVLRSLFSTTPLTTDDGVLLRRMALEIGALHLILVCLSALSHHSPRVPNSSVNQTEPQVSSSHNPTSTEEQQLYWAKGTGFGTGSTASGWDVEQALTKQRLEEEHVTCLLQVLASYINPVSSAVNGEAQSSHETRGQNSNALPSVLLELLSQSCLIPAMSSYLRNDSVLDMARHVPLYRALLELLRAIASCAAMVPLLLPLSTENGEEEEEQSECQTSVGTLLAKMKTCVDTYTNRLRSKRENVKTGVKPDASDQEPEGLTLLVPDIQKTAEIVYAATTSLRQANQEKKLGEYSKKAAMKPKPLSVLKSLEEKYVAVMKKLQFDTFEMVSEDEDGKLGFKVNYHYMSQVKNANDANSAARARRLAQEAVTLSTSLPLSSSSSVFVRCDEERLDIMKVLITGPADTPYANGCFEFDVYFPQDYPSSPPLVNLETTGGHSVRFNPNLYNDGKVCLSILNTWHGRPEEKWNPQTSSFLQVLVSVQSLILVAEPYFNEPGYERSRGTPSGTQSSREYDGNIRQATVKWAMLEQIRNPSPCFKEVIHKHFYLKRVEIMAQCEEWIADIQQYSSDKRVGRTMSHHAAALKRHTAQLREELLKLPCPEGLDPDTDDAPEVCRATTGAEETLMHDQVKPSSSKELPSDFQL	chr2:32357023-32618878[+]	"Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 ubiquitin ligase. Its tragets include CASP9 and DIABLO/SMAC. Acts as an inhibitor of CASP3, CASP7 and CASP9. Important regulator for the final stages of cytokinesis. Crucial for normal vesicle targeting to the site of abscission, but also for the integrity of the midbody and the midbody ring, and its striking ubiquitin modification."	PDB: 3CEG	HGNC:13516	BIRC6_HUMAN	Reviewed	ENSG00000115760	.	.	.	.	.
Mol00256	Protein	Bcl-2-modifying factor (BMF)	.	BMF	90427	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354670.9, BMF-201, 4692; ENST00000397573.5, BMF-202, 4545; ENST00000561282.5, BMF-209, 747; ENST00000561360.5, BMF-210, 735; ENST00000558774.5, BMF-206, 671; ENST00000559701.5, BMF-207, 630; ENST00000431415.3, BMF-203, 492; ENST00000557870.1, BMF-204, 505; ENST00000560430.1, BMF-208, 490; ENST00000558057.1, BMF-205, 450"	MEPSQCVEELEDDVFQPEDGEPVTQPGSLLSADLFAQSLLDCPLSRLQLFPLTHCCGPGLRPTSQEDKATQTLSPASPSQGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAVLPIGEQPPEGQWQHQAEVQIARKLQCIADQFHRLHVQQHQQNQNRVWWQILLFLHNLALNGEENRNGAGPR	chr15:40087890-40108892[-]	May play a role in apoptosis. Isoform 1 seems to be the main initiator.	PDB: 7CNU	HGNC:24132	BMF_HUMAN	Reviewed	ENSG00000104081	.	.	.	.	.
Mol00257	Protein	Polycomb complex protein BMI-1 (BMI1)	Polycomb group RING finger protein 4; RING finger protein 51; PCGF4; RNF51	BMI1	100532731	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000602390.5, COMMD3-BMI1-205, 1419; ENST00000475460.6, COMMD3-BMI1-203, 508; ENST00000489125.2, COMMD3-BMI1-204, 329; ENST00000417470.1, COMMD3-BMI1-201, 745; ENST00000463409.6, COMMD3-BMI1-202, 605; ENST00000602395.1, COMMD3-BMI1-206, 621"	MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDKRIITDDEIISLSIEFFDQNRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFANRPRKSSVNGSSATSSG	chr10:22316388-22329542[+]	"Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2."	PDB: 2H0D; PDB: 2NA1; PDB: 3RPG; PDB: 4R8P; PDB: 5FR6; PDB: 6WI7; PDB: 6WI8; PDB: 7ND1	HGNC:48326	BMI1_HUMAN	Reviewed	ENSG00000269897	.	.	.	.	.
Mol00258	Protein	Bcl-2/adenovirus E1B 19 kDa protein-interacting protein 2 (BNIP2)	NIP2	BNIP2	663	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000607373.6, BNIP2-212, 6111; ENST00000612191.4, BNIP2-213, 2515; ENST00000267859.8, BNIP2-201, 6325; ENST00000415213.7, BNIP2-202, 1509; ENST00000439052.5, BNIP2-204, 1305; ENST00000448414.5, BNIP2-205, 806; ENST00000478981.1, BNIP2-208, 1415; ENST00000417312.5, BNIP2-203, 636; ENST00000464390.1, BNIP2-206, 967; ENST00000477543.1, BNIP2-207, 863; ENST00000560458.5, BNIP2-210, 832; ENST00000557987.5, BNIP2-209, 603; ENST00000560776.1, BNIP2-211, 323"	MEGVELKEEWQDEDFPIPLPEDDSIEADILAITGPEDQPGSLEVNGNKVRKKLMAPDISLTLDPSDGSVLSDDLDESGEIDLDGLDTPSENSNEFEWEDDLPKPKTTEVIRKGSITEYTAAEEKEDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESSQPNYRYLMDNLFKYVIGTLELLVAENYMIVYLNGATTRRKMPSLGWLRKCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQVDQELNGKQDEPKNEQ	chr15:59659146-59689534[-]	Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins.	.	HGNC:1083	BNIP2_HUMAN	Reviewed	ENSG00000140299	.	.	.	.	.
Mol00259	Protein	Bromodomain-containing protein 4 (BRD4)	Protein HUNK1; HUNK1	BRD4	23476	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000679869.1, BRD4-213, 7231; ENST00000263377.6, BRD4-201, 7169; ENST00000371835.8, BRD4-203, 4624; ENST00000360016.9, BRD4-202, 3240; ENST00000594841.5, BRD4-205, 1821; ENST00000601941.1, BRD4-210, 604; ENST00000597315.5, BRD4-208, 892; ENST00000678800.1, BRD4-212, 1251; ENST00000602230.1, BRD4-211, 751; ENST00000601071.1, BRD4-209, 430; ENST00000594842.2, BRD4-206, 1294; ENST00000594066.1, BRD4-204, 587; ENST00000595926.1, BRD4-207, 582"	MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF	chr19:15235519-15332545[-]	"Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters. Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6. BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II. Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II. According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo. In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B. Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters."	PDB: 2I8N; PDB: 2LSP; PDB: 2MJV; PDB: 2N3K; PDB: 2NCZ; PDB: 2ND0; PDB: 2ND1; PDB: 2NNU; PDB: 2OSS; PDB: 2OUO; PDB: 2YEL; PDB: 2YEM; PDB: 3MXF; PDB: 3P5O; PDB: 3SVF; PDB: 3SVG; PDB: 3U5J; PDB: 3U5K; PDB: 3U5L; PDB: 3UVW; PDB: 3UVX; PDB: 3UVY; PDB: 3UW9; PDB: 3ZYU; PDB: 4A9L; PDB: 4BJX; PDB: 4BW1; PDB: 4BW2; PDB: 4BW3; PDB: 4BW4; PDB: 4C66; PDB: 4C67; PDB: 4CFK; PDB: 4CFL; PDB: 4CL9; PDB: 4CLB; PDB: 4DON; PDB: 4E96; PDB: 4F3I; PDB: 4GPJ; PDB: 4HBV; PDB: 4HBW; PDB: 4HBX; PDB: 4HBY; PDB: 4HXK; PDB: 4HXL; PDB: 4HXM; PDB: 4HXN; PDB: 4HXO; PDB: 4HXP; PDB: 4HXR; PDB: 4HXS; PDB: 4IOO; PDB: 4IOQ; PDB: 4IOR; PDB: 4J0R; PDB: 4J0S; PDB: 4J3I; PDB: 4KV1; PDB: 4KV4; PDB: 4LR6; PDB: 4LRG; PDB: 4LYI; PDB: 4LYS; PDB: 4LYW; PDB: 4LZR; PDB: 4LZS; PDB: 4MEN; PDB: 4MEO; PDB: 4MEP; PDB: 4MEQ; PDB: 4MR3; PDB: 4MR4; PDB: 4NQM; PDB: 4NR8; PDB: 4NUC; PDB: 4NUD; PDB: 4NUE; PDB: 4O70; PDB: 4O71; PDB: 4O72; PDB: 4O74; PDB: 4O75; PDB: 4O76; PDB: 4O77; PDB: 4O78; PDB: 4O7A; PDB: 4O7B; PDB: 4O7C; PDB: 4O7E; PDB: 4O7F; PDB: 4OGI; PDB: 4OGJ; PDB: 4PCE; PDB: 4PCI; PDB: 4PS5; PDB: 4QB3; PDB: 4QR3; PDB: 4QR4; PDB: 4QR5; PDB: 4QZS; PDB: 4UIX; PDB: 4UIY; PDB: 4UIZ; PDB: 4UYD; PDB: 4WHW; PDB: 4WIV; PDB: 4X2I; PDB: 4XY9; PDB: 4XYA; PDB: 4YH3; PDB: 4YH4; PDB: 4Z1Q; PDB: 4Z1S; PDB: 4Z93; PDB: 4ZC9; PDB: 4ZW1; PDB: 5A5S; PDB: 5A85; PDB: 5ACY; PDB: 5AD2; PDB: 5AD3; PDB: 5BT4; PDB: 5CFW; PDB: 5COI; PDB: 5CP5; PDB: 5CPE; PDB: 5CQT; PDB: 5CRM; PDB: 5CRZ; PDB: 5CS8; PDB: 5CTL; PDB: 5CY9; PDB: 5D0C; PDB: 5D24; PDB: 5D25; PDB: 5D26; PDB: 5D3H; PDB: 5D3J; PDB: 5D3L; PDB: 5D3N; PDB: 5D3P; PDB: 5D3R; PDB: 5D3S; PDB: 5D3T; PDB: 5DLX; PDB: 5DLZ; PDB: 5DW2; PDB: 5DX4; PDB: 5E0R; PDB: 5EGU; PDB: 5EI4; PDB: 5EIS; PDB: 5F5Z; PDB: 5F60; PDB: 5F61; PDB: 5F62; PDB: 5F63; PDB: 5FBX; PDB: 5H21; PDB: 5HCL; PDB: 5HLS; PDB: 5HM0; PDB: 5HQ5; PDB: 5HQ6; PDB: 5HQ7; PDB: 5I80; PDB: 5I88; PDB: 5IGK; PDB: 5JWM; PDB: 5KDH; PDB: 5KHM; PDB: 5KJ0; PDB: 5KU3; PDB: 5LJ1; PDB: 5LJ2; PDB: 5LRQ; PDB: 5LUU; PDB: 5M39; PDB: 5M3A; PDB: 5MKZ; PDB: 5MLI; PDB: 5N2M; PDB: 5NNC; PDB: 5NND; PDB: 5NNE; PDB: 5NNF; PDB: 5NNG; PDB: 5O97; PDB: 5OVB; PDB: 5OWM; PDB: 5OWW; PDB: 5S9P; PDB: 5S9Q; PDB: 5S9R; PDB: 5T35; PDB: 5TI2; PDB: 5TI3; PDB: 5TI4; PDB: 5TI5; PDB: 5TI6; PDB: 5TI7; PDB: 5U28; PDB: 5U2C; PDB: 5U2E; PDB: 5U2F; PDB: 5UEO; PDB: 5UEP; PDB: 5UEQ; PDB: 5UER; PDB: 5UES; PDB: 5UET; PDB: 5UEU; PDB: 5UEV; PDB: 5UEX; PDB: 5UEY; PDB: 5UEZ; PDB: 5UF0; PDB: 5ULA; PDB: 5UOO; PDB: 5UVS; PDB: 5UVT; PDB: 5UVU; PDB: 5UVV; PDB: 5UVW; PDB: 5UVX; PDB: 5UVY; PDB: 5UVZ; PDB: 5V67; PDB: 5VBO; PDB: 5VBP; PDB: 5VOM; PDB: 5VZS; PDB: 5W55; PDB: 5WA5; PDB: 5WMA; PDB: 5WMD; PDB: 5WMG; PDB: 5WUU; PDB: 5XHY; PDB: 5XI2; PDB: 5XI3; PDB: 5XI4; PDB: 5Y1Y; PDB: 5Y8C; PDB: 5Y8W; PDB: 5Y8Y; PDB: 5Y8Z; PDB: 5Y93; PDB: 5Y94; PDB: 5YOU; PDB: 5YOV; PDB: 5YQX; PDB: 5Z1R; PDB: 5Z1S; PDB: 5Z1T; PDB: 5Z5T; PDB: 5Z5U; PDB: 5Z5V; PDB: 5Z8G; PDB: 5Z8R; PDB: 5Z8Z; PDB: 5Z90; PDB: 5Z9C; PDB: 5Z9K; PDB: 6AFR; PDB: 6AJV; PDB: 6AJW; PDB: 6AJX; PDB: 6AJY; PDB: 6AJZ; PDB: 6BN7; PDB: 6BN8; PDB: 6BN9; PDB: 6BNB; PDB: 6BNH; PDB: 6BOY; PDB: 6C7Q; PDB: 6C7R; PDB: 6CD4; PDB: 6CD5; PDB: 6CIS; PDB: 6CIY; PDB: 6CJ1; PDB: 6CJ2; PDB: 6CKR; PDB: 6CKS; PDB: 6CZU; PDB: 6CZV; PDB: 6DJC; PDB: 6DL2; PDB: 6DMJ; PDB: 6DML; PDB: 6DNE; PDB: 6DUV; PDB: 6E4A; PDB: 6FFD; PDB: 6FNX; PDB: 6FO5; PDB: 6FSY; PDB: 6FT3; PDB: 6FT4; PDB: 6G0D; PDB: 6G0E; PDB: 6G0F; PDB: 6G0G; PDB: 6G0H; PDB: 6G0O; PDB: 6G0P; PDB: 6G0Q; PDB: 6G0R; PDB: 6G0S; PDB: 6HDQ; PDB: 6HOV; PDB: 6I7X; PDB: 6I7Y; PDB: 6IN1; PDB: 6JI3; PDB: 6JI4; PDB: 6JI5; PDB: 6JJ3; PDB: 6JJ5; PDB: 6JJ6; PDB: 6JJB; PDB: 6KEC; PDB: 6KED; PDB: 6KEE; PDB: 6KEF; PDB: 6KEG; PDB: 6KEH; PDB: 6KEI; PDB: 6KEJ; PDB: 6KEK; PDB: 6KO2; PDB: 6LG4; PDB: 6LG5; PDB: 6LG6; PDB: 6LG7; PDB: 6LG8; PDB: 6LG9; PDB: 6LIH; PDB: 6LIM; PDB: 6MAU; PDB: 6MH1; PDB: 6MH7; PDB: 6MNL; PDB: 6P05; PDB: 6PRT; PDB: 6PS9; PDB: 6PSB; PDB: 6Q3Y; PDB: 6Q3Z; PDB: 6RWJ; PDB: 6S25; PDB: 6S4B; PDB: 6S6K; PDB: 6SA2; PDB: 6SA3; PDB: 6SAH; PDB: 6SAJ; PDB: 6SB8; PDB: 6SE4; PDB: 6SIS; PDB: 6SWN; PDB: 6SWQ; PDB: 6TPX; PDB: 6TPY; PDB: 6TPZ; PDB: 6U0D; PDB: 6U6K; PDB: 6U6L; PDB: 6U72; PDB: 6U74; PDB: 6U8G; PDB: 6U8I; PDB: 6U8M; PDB: 6ULS; PDB: 6ULV; PDB: 6UVJ; PDB: 6UVM; PDB: 6UWU; PDB: 6UWX; PDB: 6V0U; PDB: 6V1K; PDB: 6V1L; PDB: 6V1U; PDB: 6VIW; PDB: 6VIX; PDB: 6VIZ; PDB: 6VUB; PDB: 6VUC; PDB: 6VUF; PDB: 6VUJ; PDB: 6WGX; PDB: 6WVX; PDB: 6WW8; PDB: 6X7B; PDB: 6X7C; PDB: 6X7D; PDB: 6XUZ; PDB: 6XV3; PDB: 6XV7; PDB: 6XVC; PDB: 6YIN; PDB: 6YQN; PDB: 6YQO; PDB: 6YQP; PDB: 6YQZ; PDB: 6Z7G; PDB: 6Z7L; PDB: 6Z7M; PDB: 6ZB3; PDB: 6ZCI; PDB: 6ZED; PDB: 6ZEL; PDB: 6ZF9; PDB: 7A9U; PDB: 7AJN; PDB: 7AXR; PDB: 7C2Z; PDB: 7C6P; PDB: 7DHS; PDB: 7JKW; PDB: 7JKX; PDB: 7JKY; PDB: 7JKZ; PDB: 7K6G; PDB: 7K6H; PDB: 7KHH; PDB: 7KHL; PDB: 7KO0; PDB: 7M16; PDB: 7MCE; PDB: 7MCF; PDB: 7MLQ; PDB: 7MLR; PDB: 7MLS; PDB: 7O18; PDB: 7OEO; PDB: 7P6V; PDB: 7P6W; PDB: 7P6Y; PDB: 7REK; PDB: 7REL; PDB: 7REM	HGNC:13575	BRD4_HUMAN	Reviewed	ENSG00000141867	.	.	.	.	.
Mol00260	Protein	Bromodomain-containing protein 7 (BRD7)	75 kDa bromodomain protein; Protein CELTIX-1; BP75; CELTIX1	BRD7	29117	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000394688.8, BRD7-201, 5424; ENST00000394689.2, BRD7-202, 2145; ENST00000562383.6, BRD7-205, 2580; ENST00000569774.6, BRD7-207, 416; ENST00000401491.7, BRD7-203, 1338; ENST00000475877.5, BRD7-204, 671; ENST00000567826.1, BRD7-206, 740"	MGKKHKKHKSDKHLYEEYVEKPLKLVLKVGGNEVTELSTGSSGHDSSLFEDKNDHDKHKDRKRKKRKKGEKQIPGEEKGRKRRRVKEDKKKRDRDRVENEAEKDLQCHAPVRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMADLQKTRKQKDGTDTSQSGEDGGCWQREREDSGDAEAHAFKSPSKENKKKDKDMLEDKFKSNNLEREQEQLDRIVKESGGKLTRRLVNSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNKVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPSDFSIHEFLATCQDYPYVMADSLLDVLTKGGHSRTLQEMEMSLPEDEGHTRTLDTAKEMEITEVEPPGRLDSSTQDRLIALKAVTNFGVPVEVFDSEEAEIFQKKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMHLAEQVTNNLKELAQQVTPGDIVSTYGVRKAMGISIPSPVMENNFVDLTEDTEEPKKTDVAECGPGGS	chr16:50313487-50368988[-]	"Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR (By similarity). Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase."	PDB: 2I7K; PDB: 5MQ1; PDB: 6PPA; PDB: 6V0Q; PDB: 6V16; PDB: 6V17; PDB: 6V1E; PDB: 6V1F; PDB: 6V1H	HGNC:14310	BRD7_HUMAN	Reviewed	ENSG00000166164	.	.	.	.	.
Mol00261	Protein	B-cell translocation gene 1 (BTG1)	B-cell translocation gene 1 protein	BTG1	694	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256015.5, BTG1-201, 4629; ENST00000673901.1, BTG1-203, 1375; ENST00000552315.1, BTG1-202, 504"	MHPFYTRAATMIGEIAAAVSFISKFLRTKGLTSERQLQTFSQSLQELLAEHYKHHWFPEKPCKGSGYRCIRINHKMDPLIGQAAQRIGLSSQELFRLLPSELTLWVDPYEVSYRIGEDGSICVLYEASPAGGSTQNSTNVQMVDSRISCKEELLLGRTSPSKNYNMMTVSG	chr12:92140278-92145846[-]	Anti-proliferative protein.	.	HGNC:1130	BTG1_HUMAN	Reviewed	ENSG00000133639	.	.	.	.	.
Mol00262	Protein	Tyrosine-protein kinase BTK (BTK)	Agammaglobulinemia tyrosine kinase; ATK; B-cell progenitor kinase; BPK; Bruton tyrosine kinase; AGMX1; ATK; BPK	BTK	695	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308731.8, BTK-201, 2575; ENST00000621635.4, BTK-208, 2767; ENST00000695615.1, BTK-210, 2743; ENST00000695614.1, BTK-209, 2658; ENST00000697417.1, BTK-231, 2203; ENST00000695617.1, BTK-212, 2679; ENST00000695623.1, BTK-218, 2558; ENST00000695622.1, BTK-217, 2501; ENST00000695625.1, BTK-220, 2431; ENST00000695630.1, BTK-225, 707; ENST00000470329.1, BTK-205, 572; ENST00000695643.1, BTK-230, 515; ENST00000695629.1, BTK-224, 501; ENST00000695631.1, BTK-226, 238; ENST00000695616.1, BTK-211, 2677; ENST00000695618.1, BTK-213, 2673; ENST00000695620.1, BTK-215, 2666; ENST00000695621.1, BTK-216, 2624; ENST00000695619.1, BTK-214, 2431; ENST00000695627.1, BTK-222, 1010; ENST00000695626.1, BTK-221, 817; ENST00000695628.1, BTK-223, 621; ENST00000695634.1, BTK-229, 680; ENST00000695632.1, BTK-227, 527; ENST00000488970.2, BTK-207, 4568; ENST00000478995.2, BTK-206, 3929; ENST00000695633.1, BTK-228, 1851; ENST00000695624.1, BTK-219, 1638; ENST00000464006.2, BTK-202, 801; ENST00000464567.1, BTK-203, 587; ENST00000470069.1, BTK-204, 424"	MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPAAAPVSTSELKKVVALYDYMPMNANDLQLRKGDEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGDPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSQQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES	chrX:101349338-101390796[-]	"Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members. PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK. BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways. Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway. The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense. Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells. Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation. BTK plays also a critical role in transcription regulation. Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes. BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B. Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR. GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression. ARID3A and NFAT are other transcriptional target of BTK. BTK is required for the formation of functional ARID3A DNA-binding complexes. There is however no evidence that BTK itself binds directly to DNA. BTK has a dual role in the regulation of apoptosis."	PDB: 1AWW; PDB: 1AWX; PDB: 1B55; PDB: 1BTK; PDB: 1BWN; PDB: 1K2P; PDB: 1QLY; PDB: 2GE9; PDB: 2Z0P; PDB: 3GEN; PDB: 3K54; PDB: 3OCS; PDB: 3OCT; PDB: 3P08; PDB: 3PIX; PDB: 3PIY; PDB: 3PIZ; PDB: 3PJ1; PDB: 3PJ2; PDB: 3PJ3; PDB: 4NWM; PDB: 4OT5; PDB: 4OT6; PDB: 4OTF; PDB: 4OTQ; PDB: 4OTR; PDB: 4RFY; PDB: 4RFZ; PDB: 4RG0; PDB: 4RX5; PDB: 4YHF; PDB: 4Z3V; PDB: 4ZLY; PDB: 4ZLZ; PDB: 5BPY; PDB: 5BQ0; PDB: 5FBN; PDB: 5FBO; PDB: 5J87; PDB: 5JRS; PDB: 5KUP; PDB: 5P9F; PDB: 5P9G; PDB: 5P9H; PDB: 5P9I; PDB: 5P9J; PDB: 5P9K; PDB: 5P9L; PDB: 5P9M; PDB: 5T18; PDB: 5U9D; PDB: 5VFI; PDB: 5VGO; PDB: 5XYZ; PDB: 5ZZ4; PDB: 6AUA; PDB: 6AUB; PDB: 6BIK; PDB: 6BKE; PDB: 6BKH; PDB: 6BKW; PDB: 6BLN; PDB: 6DI0; PDB: 6DI1; PDB: 6DI3; PDB: 6DI5; PDB: 6DI9; PDB: 6E4F; PDB: 6EP9; PDB: 6HRP; PDB: 6HRT; PDB: 6HTF; PDB: 6J6M; PDB: 6N9P; PDB: 6NFH; PDB: 6NFI; PDB: 6NZM; PDB: 6O8I; PDB: 6OMU; PDB: 6S90; PDB: 6TFP; PDB: 6TSE; PDB: 6TT2; PDB: 6TUH; PDB: 6TVN; PDB: 6VXQ; PDB: 6W06; PDB: 6W07; PDB: 6W7O; PDB: 6W8I; PDB: 6X3N; PDB: 6X3O; PDB: 6X3P; PDB: 6XE4; PDB: 6YYF; PDB: 6YYG; PDB: 6YYK; PDB: 7KXL; PDB: 7KXM; PDB: 7KXN; PDB: 7KXO; PDB: 7KXP; PDB: 7KXQ; PDB: 7N5O; PDB: 7N5R; PDB: 7N5X; PDB: 7N5Y; PDB: 7R60; PDB: 7R61	HGNC:1133	BTK_HUMAN	Reviewed	ENSG00000010671	.	.	.	.	.
Mol00263	Protein	Mitotic checkpoint serine/threonine-protein kinase BUB1 (BUB1)	hBUB1; BUB1A; BUB1L	BUB1	699	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000302759.11, BUB1-201, 3762; ENST00000535254.6, BUB1-212, 3532; ENST00000409311.5, BUB1-202, 3287; ENST00000666956.1, BUB1-213, 1417; ENST00000420328.5, BUB1-203, 566; ENST00000447014.5, BUB1-205, 551; ENST00000436916.1, BUB1-204, 540; ENST00000671097.1, BUB1-214, 1891; ENST00000478175.2, BUB1-210, 1380; ENST00000477481.1, BUB1-209, 831; ENST00000466333.5, BUB1-207, 2501; ENST00000465029.5, BUB1-206, 1999; ENST00000490632.1, BUB1-211, 755; ENST00000468927.1, BUB1-208, 714"	MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEVNPARMGPSVGSQQELRAPCLPVTYQQTPVNMEKNPREAPPVVPPLANAISAALVSPATSQSIAPPVPLKAQTVTDSMFAVASKDAGCVNKSTHEFKPQSGAEIKEGCETHKVANTSSFHTTPNTSLGMVQATPSKVQPSPTVHTKEALGFIMNMFQAPTLPDISDDKDEWQSLDQNEDAFEAQFQKNVRSSGAWGVNKIISSLSSAFHVFEDGNKENYGLPQPKNKPTGARTFGERSVSRLPSKPKEEVPHAEEFLDDSTVWGIRCNKTLAPSPKSPGDFTSAAQLASTPFHKLPVESVHILEDKENVVAKQCTQATLDSCEENMVVPSRDGKFSPIQEKSPKQALSSHMYSASLLRLSQPAAGGVLTCEAELGVEACRLTDTDAAIAEDPPDAIAGLQAEWMQMSSLGTVDAPNFIVGNPWDDKLIFKLLSGLSKPVSSYPNTFEWQCKLPAIKPKTEFQLGSKLVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLVGELYSYGTLLNAINLYKNTPEKVMPQGLVISFAMRMLYMIEQVHDCEIIHGDIKPDNFILGNGFLEQDDEDDLSAGLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRLIVLLLECKRSRK	chr2:110637528-110678063[-]	"Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis."	PDB: 2LAH; PDB: 4A1G; PDB: 4QPM; PDB: 4R8Q; PDB: 5DMZ; PDB: 6F7B; PDB: 7B1F; PDB: 7B1H; PDB: 7B1J	HGNC:1148	BUB1_HUMAN	Reviewed	ENSG00000169679	.	.	.	.	.
Mol00264	Protein	Cadherin-2 (CDH2)	.	CDH2	1000	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000269141.8, CDH2-201, 4016; ENST00000399380.7, CDH2-202, 3737; ENST00000676445.1, CDH2-211, 3243; ENST00000430882.6, CDH2-205, 3143; ENST00000413878.2, CDH2-203, 2574; ENST00000675173.1, CDH2-207, 1397; ENST00000418492.5, CDH2-204, 740; ENST00000675708.1, CDH2-209, 3860; ENST00000675688.1, CDH2-208, 899; ENST00000674998.1, CDH2-206, 3627; ENST00000676041.1, CDH2-210, 2947"	MCRIAGALRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLTEESVKESAEVEEIVFPRQFSKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRIVSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDIIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRMDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD	chr18:27932879-28177946[-]	"Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density."	.	HGNC:1759	CADH2_HUMAN	Reviewed	ENSG00000170558	.	.	.	.	.
Mol00265	Protein	Caspase recruitment domain-containing protein 11 (CARD11)	CARD-containing MAGUK protein 1; Carma 1; CARMA1	CARD11	84433	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000396946.9, CARD11-203, 4287; ENST00000355508.3, CARD11-201, 815; ENST00000356408.3, CARD11-202, 584; ENST00000480332.1, CARD11-204, 841"	MPGGGPEMDDYMETLKDEEDALWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPELYKLVTGKEPTRRFSTIVVEEGHEGLTHFLMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQELQSIIQAGKRSLPDSDKAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSLPRNLPVTIISQDFGDASPRTNGQEADDSSTSEESPEDSKYFLPYHPPQRRMNLKGIQLQRAKSPISLKRTSDFQAKGHEEEGTDASPSSCGSLPITNSFTKMQPPRSRSSIMSITAEPPGNDSIVRRYKEDAPHRSTVEEDNDSGGFDALDLDDDSHERYSFGPSSIHSSSSSHQSEGLDAYDLEQVNLMFRKFSLERPFRPSVTSVGHVRGPGPSVQHTTLNGDSLTSQLTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGCIRGERQSVPLDTCTKEEAHWTIQRCSGPVTLHYKVNHEGYRKLVKDMEDGLITSGDSFYIRLNLNISSQLDACTMSLKCDDVVHVRDTMYQDRHEWLCARVDPFTDHDLDMGTIPSYSRAQQLLLVKLQRLMHRGSREEVDGTHHTLRALRNTLQPEEALSTSDPRVSPRLSRASFLFGQLLQFVSRSENKYKRMNSNERVRIISGSPLGSLARSSLDATKLLTEKQEELDPESELGKNLSLIPYSLVRAFYCERRRPVLFTPTVLAKTLVQRLLNSGGAMEFTICKSDIVTRDEFLRRQKTETIIYSREKNPNAFECIAPANIEAVAAKNKHCLLEAGIGCTRDLIKSNIYPIVLFIRVCEKNIKRFRKLLPRPETEEEFLRVCRLKEKELEALPCLYATVEPDMWGSVEELLRVVKDKIGEEQRKTIWVDEDQL	chr7:2906142-3043867[-]	"Adapter protein that plays a key role in adaptive immune response by transducing the activation of NF-kappa-B downstream of T-cell receptor (TCR) and B-cell receptor (BCR) engagement. Transduces signals downstream TCR or BCR activation via the formation of a multiprotein complex together with BCL10 and MALT1 that induces NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways. Upon activation in response to TCR or BCR triggering, CARD11 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to I-kappa-B kinase (IKK) phosphorylation and degradation, and release of NF-kappa-B proteins for nuclear translocation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Promotes linear ubiquitination of BCL10 by promoting the targeting of BCL10 to RNF31/HOIP. Stimulates the phosphorylation of BCL10. Also activates the TORC1 signaling pathway."	PDB: 4JUP; PDB: 4LWD	HGNC:16393	CAR11_HUMAN	Reviewed	ENSG00000198286	.	.	.	.	.
Mol00266	Protein	Caspase-1 (CASP1)	CASP-1; Interleukin-1 beta convertase; IL-1BC; Interleukin-1 beta-converting enzyme; ICE; IL-1 beta-converting enzyme; p45; IL1BC; IL1BCE	CASP1	834	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000533400.6, CASP1-212, 1996; ENST00000525825.6, CASP1-202, 1844; ENST00000436863.7, CASP1-201, 1477; ENST00000695719.1, CASP1-219, 1307; ENST00000526568.5, CASP1-204, 1061; ENST00000534497.5, CASP1-213, 825; ENST00000531166.5, CASP1-210, 300; ENST00000695717.1, CASP1-217, 2505; ENST00000695720.1, CASP1-220, 2386; ENST00000695715.1, CASP1-215, 2216; ENST00000695718.1, CASP1-218, 1860; ENST00000527979.5, CASP1-206, 1521; ENST00000528974.1, CASP1-208, 1402; ENST00000695721.1, CASP1-221, 1284; ENST00000695722.1, CASP1-222, 1280; ENST00000532439.6, CASP1-211, 832; ENST00000695716.1, CASP1-216, 2050; ENST00000695714.1, CASP1-214, 1693; ENST00000529871.1, CASP1-209, 1392; ENST00000526511.6, CASP1-203, 1206; ENST00000528424.1, CASP1-207, 578; ENST00000527625.5, CASP1-205, 424"	MADKVLKEKRKLFIRSMGEGTINGLLDELLQTRVLNKEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAGTLGLSADQTSGNYLNMQDSQGVLSSFPAPQAVQDNPAMPTSSGSEGNVKLCSLEEAQRIWKQKSAEIYPIMDKSSRTRLALIICNEEFDSIPRRTGAEVDITGMTMLLQNLGYSVDVKKNLTASDMTTELEAFAHRPEHKTSDSTFLVFMSHGIREGICGKKHSEQVPDILQLNAIFNMLNTKNCPSLKDKPKVIIIQACRGDSPGVVWFKDSVGVSGNLSLPTTEEFEDDAIKKAHIEKDFIAFCSSTPDNVSWRHPTMGSVFIGRLIEHMQEYACSCDVEEIFRKVRFSFEQPDGRAQMPTTERVTLTRCFYLFPGH	chr11:105025397-105035250[-]	"Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a proinflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukins IL1B and IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly."	PDB: 1BMQ; PDB: 1IBC; PDB: 1ICE; PDB: 1RWK; PDB: 1RWM; PDB: 1RWN; PDB: 1RWO; PDB: 1RWP; PDB: 1RWV; PDB: 1RWW; PDB: 1RWX; PDB: 1SC1; PDB: 1SC3; PDB: 1SC4; PDB: 2FQQ; PDB: 2H48; PDB: 2H4W; PDB: 2H4Y; PDB: 2H51; PDB: 2H54; PDB: 2HBQ; PDB: 2HBR; PDB: 2HBY; PDB: 2HBZ; PDB: 3D6F; PDB: 3D6H; PDB: 3D6M; PDB: 3E4C; PDB: 3NS7; PDB: 5FNA; PDB: 5MMV; PDB: 5MTK; PDB: 6BZ9; PDB: 6F6R; PDB: 6KN0; PDB: 6PZP; PDB: 6VIE; PDB: 7KEU	HGNC:1499	CASP1_HUMAN	Reviewed	ENSG00000137752	.	.	.	.	.
Mol00267	Protein	Caspase-3 (CASP3)	CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1; CPP32	CASP3	836	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308394.9, CASP3-201, 2645; ENST00000393585.6, CASP3-202, 2624; ENST00000523916.5, CASP3-206, 2540; ENST00000517513.5, CASP3-205, 964; ENST00000393588.8, CASP3-203, 677; ENST00000447121.2, CASP3-204, 549"	MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH	chr4:184627696-184649509[-]	"Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface."	PDB: 1CP3; PDB: 1GFW; PDB: 1I3O; PDB: 1NME; PDB: 1NMQ; PDB: 1NMS; PDB: 1PAU; PDB: 1QX3; PDB: 1RE1; PDB: 1RHJ; PDB: 1RHK; PDB: 1RHM; PDB: 1RHQ; PDB: 1RHR; PDB: 1RHU; PDB: 2C1E; PDB: 2C2K; PDB: 2C2M; PDB: 2C2O; PDB: 2CDR; PDB: 2CJX; PDB: 2CJY; PDB: 2CNK; PDB: 2CNL; PDB: 2CNN; PDB: 2CNO; PDB: 2DKO; PDB: 2H5I; PDB: 2H5J; PDB: 2H65; PDB: 2J30; PDB: 2J31; PDB: 2J32; PDB: 2J33; PDB: 2XYG; PDB: 2XYH; PDB: 2XYP; PDB: 2XZD; PDB: 2XZT; PDB: 2Y0B; PDB: 3DEH; PDB: 3DEI; PDB: 3DEJ; PDB: 3DEK; PDB: 3EDQ; PDB: 3GJQ; PDB: 3GJR; PDB: 3GJS; PDB: 3GJT; PDB: 3H0E; PDB: 3ITN; PDB: 3KJF; PDB: 3PCX; PDB: 3PD0; PDB: 3PD1; PDB: 4DCJ; PDB: 4DCO; PDB: 4DCP; PDB: 4EHA; PDB: 4EHD; PDB: 4EHF; PDB: 4EHH; PDB: 4EHK; PDB: 4EHL; PDB: 4EHN; PDB: 4JJE; PDB: 4JQY; PDB: 4JQZ; PDB: 4JR0; PDB: 4PRY; PDB: 4PS0; PDB: 4QTX; PDB: 4QTY; PDB: 4QU0; PDB: 4QU5; PDB: 4QU8; PDB: 4QU9; PDB: 4QUA; PDB: 4QUB; PDB: 4QUD; PDB: 4QUE; PDB: 4QUG; PDB: 4QUH; PDB: 4QUI; PDB: 4QUJ; PDB: 4QUL; PDB: 5I9B; PDB: 5I9T; PDB: 5IAB; PDB: 5IAE; PDB: 5IAG; PDB: 5IAJ; PDB: 5IAK; PDB: 5IAN; PDB: 5IAR; PDB: 5IAS; PDB: 5IBC; PDB: 5IBP; PDB: 5IBR; PDB: 5IC4	HGNC:1504	CASP3_HUMAN	Reviewed	ENSG00000164305	.	.	.	.	.
Mol00268	Protein	Caspase-7 (CASP7)	CASP-7; Apoptotic protease Mch-3; CMH-1; ICE-like apoptotic protease 3; ICE-LAP3; MCH3	CASP7	840	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369318.8, CASP7-203, 2344; ENST00000345633.8, CASP7-201, 2659; ENST00000369321.6, CASP7-204, 2620; ENST00000614447.4, CASP7-210, 2555; ENST00000621345.4, CASP7-211, 2467; ENST00000369315.5, CASP7-202, 2421; ENST00000369331.8, CASP7-205, 2380; ENST00000621607.4, CASP7-212, 2378; ENST00000452490.3, CASP7-207, 2271; ENST00000672138.1, CASP7-213, 2351; ENST00000429617.5, CASP7-206, 834; ENST00000468790.1, CASP7-208, 607; ENST00000487232.1, CASP7-209, 799"	MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ	chr10:113679162-113730907[+]	"Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9."	PDB: 1F1J; PDB: 1GQF; PDB: 1I4O; PDB: 1I51; PDB: 1K86; PDB: 1K88; PDB: 1KMC; PDB: 1SHJ; PDB: 1SHL; PDB: 2QL5; PDB: 2QL7; PDB: 2QL9; PDB: 2QLB; PDB: 2QLF; PDB: 2QLJ; PDB: 3EDR; PDB: 3H1P; PDB: 3IBC; PDB: 3IBF; PDB: 3R5K; PDB: 4FDL; PDB: 4FEA; PDB: 4HQ0; PDB: 4HQR; PDB: 4JB8; PDB: 4JJ8; PDB: 4JR1; PDB: 4JR2; PDB: 4LSZ; PDB: 4ZVO; PDB: 4ZVP; PDB: 4ZVQ; PDB: 4ZVR; PDB: 4ZVS; PDB: 4ZVT; PDB: 4ZVU; PDB: 5IC6; PDB: 5K20; PDB: 5V6U; PDB: 5V6Z	HGNC:1508	CASP7_HUMAN	Reviewed	ENSG00000165806	.	.	.	.	.
Mol00269	Protein	Caspase-8 (CASP8)	CASP-8; Apoptotic cysteine protease; Apoptotic protease Mch-5; CAP4; FADD-homologous ICE/ced-3-like protease; FADD-like ICE; FLICE; ICE-like apoptotic protease 5; MORT1-associated ced-3 homolog; MACH; MCH5	CASP8	841	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000673742.1, CASP8-218, 2659; ENST00000358485.8, CASP8-204, 2930; ENST00000696067.1, CASP8-220, 2728; ENST00000413726.6, CASP8-207, 2677; ENST00000323492.11, CASP8-202, 2650; ENST00000696087.1, CASP8-225, 2562; ENST00000264275.9, CASP8-201, 1906; ENST00000440732.6, CASP8-211, 1658; ENST00000392263.6, CASP8-206, 1630; ENST00000432109.6, CASP8-209, 1629; ENST00000392258.7, CASP8-205, 1060; ENST00000696085.1, CASP8-223, 2749; ENST00000444430.3, CASP8-212, 2305; ENST00000696069.1, CASP8-222, 1607; ENST00000450491.6, CASP8-214, 1324; ENST00000429881.2, CASP8-208, 922; ENST00000447616.6, CASP8-213, 798; ENST00000696068.1, CASP8-221, 2490; ENST00000339403.6, CASP8-203, 1723; ENST00000437283.5, CASP8-210, 777; ENST00000696086.1, CASP8-224, 1751; ENST00000490412.5, CASP8-216, 230; ENST00000490682.6, CASP8-217, 2913; ENST00000696066.1, CASP8-219, 1145; ENST00000471383.5, CASP8-215, 969"	MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD	chr2:201233443-201361836[+]	"Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood. Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. Binding to the adapter molecule FADD recruits it to either receptor TNFRSF6/FAS mediated or TNFRSF1A. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response. Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-D (GSDMD): GSDMD cleavage promoting release of the N-terminal moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis. Initiates pyroptosis following inactivation of MAP3K7/TAK1. Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production. May participate in the Granzyme B (GZMB) cell death pathways. Cleaves PARP1."	PDB: 1F9E; PDB: 1I4E; PDB: 1QDU; PDB: 1QTN; PDB: 2C2Z; PDB: 2FUN; PDB: 2K7Z; PDB: 2Y1L; PDB: 3H11; PDB: 3KJN; PDB: 3KJQ; PDB: 4JJ7; PDB: 4PRZ; PDB: 4PS1; PDB: 4ZBW; PDB: 5H31; PDB: 5H33; PDB: 5JQE; PDB: 5L08; PDB: 6AGW; PDB: 6PX9	HGNC:1509	CASP8_HUMAN	Reviewed	ENSG00000064012	.	.	.	.	.
Mol00270	Protein	Caveolin-2 (CAV2)	.	CAV2	858	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000222693.5, CAV2-201, 2953; ENST00000343213.2, CAV2-202, 776; ENST00000393480.3, CAV2-203, 1179; ENST00000462876.5, CAV2-205, 1861; ENST00000498493.5, CAV2-215, 1561; ENST00000467035.5, CAV2-207, 1200; ENST00000477018.5, CAV2-209, 1119; ENST00000478226.5, CAV2-210, 995; ENST00000484871.5, CAV2-211, 971; ENST00000472470.5, CAV2-208, 857; ENST00000495841.1, CAV2-214, 787; ENST00000490906.5, CAV2-213, 714; ENST00000485561.5, CAV2-212, 577; ENST00000460222.5, CAV2-204, 531; ENST00000465451.1, CAV2-206, 466"	MGLETEKADVQLFMDDDSYSHHSGLEYADPEKFADSDQDRDPHRLNSHLKLGFEDVIAEPVTTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVIIAPLCTSVGRCFSSVSLQLSQD	chr7:116287380-116508541[+]	"May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity)."	.	HGNC:1528	CAV2_HUMAN	Reviewed	ENSG00000105971	.	.	.	.	.
Mol00271	Protein	E3 ubiquitin-protein ligase CBL (CBL)	Casitas B-lineage lymphoma proto-oncogene; Proto-oncogene c-Cbl; RING finger protein 55; RING-type E3 ubiquitin transferase CBL; Signal transduction protein CBL; CBL2; RNF55	CBL	867	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264033.6, CBL-201, 11168; ENST00000634840.1, CBL-204, 4813; ENST00000634586.1, CBL-203, 3457; ENST00000637974.1, CBL-205, 3030; ENST00000634301.1, CBL-202, 340"	MAGNVKKSSGAGGGSGSGGSGSGGLIGLMKDAFQPHHHHHHHLSPHPPGTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTILSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDTLFMMKELAGAKVERPPSPFSMAPQASLPPVPPRLDLLPQRVCVPSSASALGTASKAASGSLHKDKPLPVPPTLRDLPPPPPPDRPYSVGAESRPQRRPLPCTPGDCPSRDKLPPVPSSRLGDSWLPRPIPKVPVSAPSSSDPWTGRELTNRHSLPFSLPSQMEPRPDVPRLGSTFSLDTSMSMNSSPLVGPECDHPKIKPSSSANAIYSLAARPLPVPKLPPGEQCEGEEDTEYMTPSSRPLRPLDTSQSSRACDCDQQIDSCTYEAMYNIQSQAPSITESSTFGEGNLAAAHANTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTTNVTEGSQVPERPPKPFPRRINSERKAGSCQQGSGPAASAATASPQLSSEIENLMSQGYSYQDIQKALVIAQNNIEMAKNILREFVSISSPAHVAT	chr11:119206298-119313926[+]	"Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Ubiquitinates SPRY2. Ubiquitinates EGFR. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA."	PDB: 1B47; PDB: 1FBV; PDB: 1YVH; PDB: 2CBL; PDB: 2JUJ; PDB: 2K4D; PDB: 2OO9; PDB: 2Y1M; PDB: 2Y1N; PDB: 3BUM; PDB: 3BUN; PDB: 3BUO; PDB: 3BUW; PDB: 3BUX; PDB: 3OB1; PDB: 3OB2; PDB: 3PLF; PDB: 4A49; PDB: 4A4B; PDB: 4A4C; PDB: 4GPL; PDB: 5HKW; PDB: 5HKX; PDB: 5HKY; PDB: 5HKZ; PDB: 5HL0; PDB: 5J3X; PDB: 5O76; PDB: 6O02; PDB: 6O03; PDB: 6XAR	HGNC:1541	CBL_HUMAN	Reviewed	ENSG00000110395	.	.	.	.	.
Mol00272	Protein	E3 ubiquitin-protein ligase CBL-B (CBLB)	Casitas B-lineage lymphoma proto-oncogene b; RING finger protein 56; RING-type E3 ubiquitin transferase CBL-B; SH3-binding protein CBL-B; Signal transduction protein CBL-B; RNF56; Nbla00127	CBLB	868	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000394030.8, CBLB-201, 6749; ENST00000403724.5, CBLB-202, 3350; ENST00000405772.5, CBLB-203, 3237; ENST00000447441.6, CBLB-207, 803; ENST00000643403.1, CBLB-213, 659; ENST00000438603.6, CBLB-205, 597; ENST00000443752.2, CBLB-206, 582; ENST00000643192.1, CBLB-211, 481; ENST00000645759.1, CBLB-215, 6755; ENST00000646499.1, CBLB-216, 3964; ENST00000645425.1, CBLB-214, 3861; ENST00000643322.1, CBLB-212, 3706; ENST00000646825.1, CBLB-217, 3669; ENST00000642241.1, CBLB-209, 1924; ENST00000642907.1, CBLB-210, 553; ENST00000476370.1, CBLB-208, 4722; ENST00000407712.1, CBLB-204, 1493"	MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFGMPMLDLDDDDDREESLMMNRLANVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPPERPPPIPPDNRLSRHIHHVESVPSRDPPMPLEAWCPRDVFGTNQLVGCRLLGEGSPKPGITASSNVNGRHSRVGSDPVLMRKHRRHDLPLEGAKVFSNGHLGSEEYDVPPRLSPPPPVTTLLPSIKCTGPLANSLSEKTRDPVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCMLNGTHGPSSEKKSNIPDLSIYLKGDVFDSASDPVPLPPARPPTRDNPKHGSSLNRTPSDYDLLIPPLGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFVDLASGQVPLPPARRLPGENVKTNRTSQDYDQLPSCSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNVEVARSILREFAFPPPVSPRLNL	chr3:105655461-105869552[-]	"E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity)."	PDB: 2AK5; PDB: 2BZ8; PDB: 2DO6; PDB: 2J6F; PDB: 2JNH; PDB: 2LDR; PDB: 2OOA; PDB: 2OOB; PDB: 3PFV; PDB: 3VGO; PDB: 3ZNI	HGNC:1542	CBLB_HUMAN	Reviewed	ENSG00000114423	.	.	.	.	.
Mol00273	Protein	CREB-binding protein (CREBBP)	Histone lysine acetyltransferase CREBBP; Protein-lysine acetyltransferase CREBBP; CBP	CREBBP	1387	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262367.10, CREBBP-201, 10790; ENST00000382070.7, CREBBP-202, 7598; ENST00000570939.2, CREBBP-203, 3316; ENST00000572134.1, CREBBP-206, 846; ENST00000573517.6, CREBBP-208, 718; ENST00000571826.5, CREBBP-205, 627; ENST00000637492.1, CREBBP-219, 100; ENST00000635919.1, CREBBP-216, 100; ENST00000635753.1, CREBBP-214, 100; ENST00000635899.1, CREBBP-215, 100; ENST00000636895.1, CREBBP-218, 100; ENST00000638158.1, CREBBP-220, 97; ENST00000636002.1, CREBBP-217, 84; ENST00000576720.1, CREBBP-212, 3578; ENST00000573672.1, CREBBP-209, 922; ENST00000572569.1, CREBBP-207, 553; ENST00000571763.5, CREBBP-204, 548; ENST00000574740.1, CREBBP-210, 523; ENST00000575237.2, CREBBP-211, 403; ENST00000634839.1, CREBBP-213, 339"	MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL	chr16:3725054-3880713[-]	"Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-ARNTL/BMAL1 and CLOCK-ARNTL/BMAL1 heterodimers. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region. Acetylates DDX21, thereby inhibiting DDX21 helicase activity. Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway."	PDB: 1JSP; PDB: 1LIQ; PDB: 1RDT; PDB: 1WO3; PDB: 1WO4; PDB: 1WO5; PDB: 1WO6; PDB: 1WO7; PDB: 1ZOQ; PDB: 2D82; PDB: 2KJE; PDB: 2KWF; PDB: 2L84; PDB: 2L85; PDB: 2LXS; PDB: 2LXT; PDB: 2N1A; PDB: 2RNY; PDB: 3DWY; PDB: 3P1C; PDB: 3P1D; PDB: 3P1E; PDB: 3P1F; PDB: 3SVH; PDB: 4A9K; PDB: 4N3W; PDB: 4N4F; PDB: 4NR4; PDB: 4NR5; PDB: 4NR6; PDB: 4NR7; PDB: 4NYV; PDB: 4NYW; PDB: 4NYX; PDB: 4OUF; PDB: 4TQN; PDB: 4TS8; PDB: 4WHU; PDB: 4YK0; PDB: 5CGP; PDB: 5DBM; PDB: 5EIC; PDB: 5ENG; PDB: 5EP7; PDB: 5GH9; PDB: 5H85; PDB: 5I83; PDB: 5I86; PDB: 5I89; PDB: 5I8B; PDB: 5I8G; PDB: 5J0D; PDB: 5JEM; PDB: 5KTU; PDB: 5KTW; PDB: 5KTX; PDB: 5LPJ; PDB: 5LPL; PDB: 5MME; PDB: 5MMG; PDB: 5MPK; PDB: 5MPN; PDB: 5MPZ; PDB: 5MQE; PDB: 5MQG; PDB: 5MQK; PDB: 5NLK; PDB: 5NRW; PDB: 5NU3; PDB: 5OWK; PDB: 5SVH; PDB: 5TB6; PDB: 5W0E; PDB: 5W0F; PDB: 5W0L; PDB: 5W0Q; PDB: 5XXH; PDB: 6ALB; PDB: 6ALC; PDB: 6AXQ; PDB: 6AY3; PDB: 6AY5; PDB: 6DMK; PDB: 6ES5; PDB: 6ES6; PDB: 6ES7; PDB: 6FQO; PDB: 6FQT; PDB: 6FQU; PDB: 6FR0; PDB: 6FRF; PDB: 6M64; PDB: 6QST; PDB: 6SQE; PDB: 6SQF; PDB: 6SQM; PDB: 6SXX; PDB: 6YIJ; PDB: 6YIK; PDB: 6YIL; PDB: 6YIM; PDB: 7CO1; PDB: 7JFL; PDB: 7JFM; PDB: 7JUO	HGNC:2348	CBP_HUMAN	Reviewed	ENSG00000005339	.	.	.	.	.
Mol00274	Protein	Monocyte chemotactic and activating factor (CCL2)	HC11; Monocyte chemoattractant protein 1; Monocyte chemotactic and activating factor; MCAF; Monocyte chemotactic protein 1; MCP-1; Monocyte secretory protein JE; Small-inducible cytokine A2; MCP1; SCYA2	CCL2	6347	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000225831.4, CCL2-201, 741; ENST00000580907.6, CCL2-202, 1139; ENST00000624362.2, CCL2-203, 1919"	MKVSAALLCLLLIAATFIPQGLAQPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT	chr17:34255274-34257208[+]	Acts as a ligand for C-C chemokine receptor CCR2. Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions. Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis.	PDB: 1DOK; PDB: 1DOL; PDB: 1DOM; PDB: 1DON; PDB: 1ML0; PDB: 2BDN; PDB: 2NZ1; PDB: 3IFD; PDB: 4DN4; PDB: 4R8I; PDB: 4ZK9	HGNC:10618	CCL2_HUMAN	Reviewed	ENSG00000108691	.	.	.	.	.
Mol00275	Protein	CCN family member 1 (CYR61)	Cellular communication network factor 1; Cysteine-rich angiogenic inducer 61; Insulin-like growth factor-binding protein 10; IBP-10; IGF-binding protein 10; IGFBP-10; Protein CYR61; Protein GIG1; CYR61; GIG1; IGFBP10	CCN1	3491	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000451137.7, CCN1-201, 2278; ENST00000675083.1, CCN1-205, 1868; ENST00000480413.1, CCN1-202, 551; ENST00000674818.1, CCN1-204, 3080; ENST00000674743.1, CCN1-203, 2446; ENST00000676007.1, CCN1-206, 1957"	MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVTGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDGRCCTPQLTRTVKMRFRCEDGETFSKNVMMIQSCKCNYNCPHANEAAFPFYRLFNDIHKFRD	chr1:85580761-85584589[+]	"Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CCN1-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3."	PDB: 4D0Z; PDB: 4D11	HGNC:2654	CCN1_HUMAN	Reviewed	ENSG00000142871	.	.	.	.	.
Mol00276	Protein	Cyclin-A2 (CCNA2)	Cyclin-A; Cyclin A; CCN1; CCNA	CCNA2	890	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000274026.10, CCNA2-201, 2748"	MLGNSAPGPATREAGSALLALQQTALQEDQENINPEKAAPVQQPRTRAALAVLKSGNPRGLAQQQRPKTRRVAPLKDLPVNDEHVTVPPWKANSKQPAFTIHVDEAEKEAQKKPAESQKIEREDALAFNSAISLPGPRKPLVPLDYPMDGSFESPHTMDMSIILEDEKPVSVNEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSKYHGVSLLNPPETLNL	chr4:121816444-121823883[-]	Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle.	PDB: 1E9H; PDB: 1FIN; PDB: 1FVV; PDB: 1GY3; PDB: 1H1P; PDB: 1H1Q; PDB: 1H1R; PDB: 1H1S; PDB: 1H24; PDB: 1H25; PDB: 1H26; PDB: 1H27; PDB: 1H28; PDB: 1JST; PDB: 1JSU; PDB: 1OGU; PDB: 1OI9; PDB: 1OIU; PDB: 1OIY; PDB: 1OKV; PDB: 1OKW; PDB: 1OL1; PDB: 1OL2; PDB: 1P5E; PDB: 1PKD; PDB: 1QMZ; PDB: 1URC; PDB: 1VYW; PDB: 2BKZ; PDB: 2BPM; PDB: 2C4G; PDB: 2C5N; PDB: 2C5O; PDB: 2C5V; PDB: 2C5X; PDB: 2C6T; PDB: 2CCH; PDB: 2CCI; PDB: 2CJM; PDB: 2I40; PDB: 2IW6; PDB: 2IW8; PDB: 2IW9; PDB: 2UUE; PDB: 2UZB; PDB: 2UZD; PDB: 2UZE; PDB: 2UZL; PDB: 2V22; PDB: 2WEV; PDB: 2WFY; PDB: 2WHB; PDB: 2WIH; PDB: 2WIP; PDB: 2WMA; PDB: 2WMB; PDB: 2WPA; PDB: 2WXV; PDB: 2X1N; PDB: 3EID; PDB: 3EJ1; PDB: 3EOC; PDB: 3F5X; PDB: 4BCK; PDB: 4BCM; PDB: 4BCN; PDB: 4BCP; PDB: 4CFM; PDB: 4CFN; PDB: 4CFU; PDB: 4CFV; PDB: 4CFW; PDB: 4CFX; PDB: 4EOI; PDB: 4EOJ; PDB: 4EOK; PDB: 4EOL; PDB: 4EOM; PDB: 4EON; PDB: 4EOO; PDB: 4EOP; PDB: 4EOQ; PDB: 4EOR; PDB: 4EOS; PDB: 4FX3; PDB: 5CYI; PDB: 5IF1; PDB: 5LMK; PDB: 5NEV; PDB: 6ATH; PDB: 6GVA; PDB: 6P3W; PDB: 6Q6G; PDB: 6Q6H; PDB: 6RIJ; PDB: 6SG4; PDB: 7ACK; PDB: 7B5L; PDB: 7B5R; PDB: 7B7S; PDB: 7LUO	HGNC:1578	CCNA2_HUMAN	Reviewed	ENSG00000145386	.	.	.	.	.
Mol00277	Protein	G2/mitotic-specific cyclin-B1 (CCNB1)	CCNB	CCNB1	891	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256442.10, CCNB1-201, 2029; ENST00000506572.5, CCNB1-204, 1331; ENST00000505500.5, CCNB1-203, 1190; ENST00000508407.5, CCNB1-206, 780; ENST00000507798.1, CCNB1-205, 767; ENST00000503507.1, CCNB1-202, 750; ENST00000513102.1, CCNB1-207, 463"	MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV	chr5:69167135-69178245[+]	Essential for the control of the cell cycle at the G2/M (mitosis) transition.	PDB: 2B9R; PDB: 2JGZ; PDB: 4Y72; PDB: 4YC3; PDB: 5HQ0; PDB: 5LQF; PDB: 6GU2; PDB: 6GU3; PDB: 6GU4; PDB: 7NJ0	HGNC:1579	CCNB1_HUMAN	Reviewed	ENSG00000134057	.	.	.	.	.
Mol00278	Protein	Cyclin-dependent kinase 1 (CDK1)	CDK1; Cell division control protein 2 homolog; Cell division protein kinase 1; p34 protein kinase; CDC2; CDC28A; CDKN1; P34CDC2	CDK1	983	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000395284.8, CDK1-203, 1889; ENST00000316629.8, CDK1-201, 1733; ENST00000373809.2, CDK1-202, 1613; ENST00000448257.6, CDK1-204, 1948; ENST00000519078.6, CDK1-207, 723; ENST00000519760.1, CDK1-208, 276; ENST00000475504.6, CDK1-205, 1720; ENST00000487784.1, CDK1-206, 598"	MEDYTKIEKIGEGTYGVVYKGRHKTTGQVVAMKKIRLESEEEGVPSTAIREISLLKELRHPNIVSLQDVLMQDSRLYLIFEFLSMDLKKYLDSIPPGQYMDSSLVKSYLYQILQGIVFCHSRRVLHRDLKPQNLLIDDKGTIKLADFGLARAFGIPIRVYTHEVVTLWYRSPEVLLGSARYSTPVDIWSIGTIFAELATKKPLFHGDSEIDQLFRIFRALGTPNNEVWPEVESLQDYKNTFPKWKPGSLASHVKNLDENGLDLLSKMLIYDPAKRISGKMALNHPYFNDLDNQIKKM	chr10:60778331-60794852[+]	"Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, KAT5, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, TPPP, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2, CGAS and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis. Regulates the amplitude of the cyclic expression of the core clock gene ARNTL/BMAL1 by phosphorylating its transcriptional repressor NR1D1, and this phosphorylation is necessary for SCF(FBXW7)-mediated ubiquitination and proteasomal degradation of NR1D1. Phosphorylates EML3 at 'Thr-881' which is essential for its interaction with HAUS augmin-like complex and TUBG1. Phosphorylates CGAS during mitosis, leading to its inhibition, thereby preventing CGAS activation by self DNA during mitosis."	PDB: 4Y72; PDB: 4YC3; PDB: 4YC6; PDB: 5HQ0; PDB: 5LQF; PDB: 6GU2; PDB: 6GU3; PDB: 6GU4; PDB: 6GU6; PDB: 6GU7; PDB: 6TWN; PDB: 7NJ0	HGNC:1722	CDK1_HUMAN	Reviewed	ENSG00000170312	.	.	.	.	.
Mol00279	Protein	G1/S-specific cyclin-D1 (CCND1)	B-cell lymphoma 1 protein; BCL-1; BCL-1 oncogene; PRAD1 oncogene; BCL1; PRAD1	CCND1	595	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000227507.3, CCND1-201, 4238; ENST00000536559.1, CCND1-203, 553; ENST00000539241.1, CCND1-204, 920; ENST00000535993.1, CCND1-202, 568; ENST00000542367.1, CCND1-205, 476; ENST00000545484.1, CCND1-206, 430"	MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI	chr11:69641156-69654474[+]	"Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity. Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner."	PDB: 2W96; PDB: 2W99; PDB: 2W9F; PDB: 2W9Z; PDB: 5VZU; PDB: 6P8E; PDB: 6P8F; PDB: 6P8G; PDB: 6P8H	HGNC:1582	CCND1_HUMAN	Reviewed	ENSG00000110092	.	.	.	.	.
Mol00280	Protein	G1/S-specific cyclin-E1 (CCNE1)	CCNE	CCNE1	898	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262643.8, CCNE1-201, 1954; ENST00000444983.6, CCNE1-203, 1680; ENST00000357943.9, CCNE1-202, 1641; ENST00000576532.1, CCNE1-206, 1085; ENST00000575243.5, CCNE1-205, 820; ENST00000574121.1, CCNE1-204, 1295; ENST00000586912.1, CCNE1-207, 415"	MPRERRERDAKERDTMKEDGGAEFSARSRKRKANVTVFLQDPDEEMAKIDRTARDQCGSQPWDNNAVCADPCSLIPTPDKEDDDRVYPNSTCKPRIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVYMQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKAMLSEQNRASPLPSGLLTPPQSGKKQSSGPEMA	chr19:29811991-29824312[+]	Essential for the control of the cell cycle at the G1/S (start) transition.	PDB: 1W98; PDB: 5L2W; PDB: 7KJS	HGNC:1589	CCNE1_HUMAN	Reviewed	ENSG00000105173	.	.	.	.	.
Mol00281	Protein	Cyclin-G1 (CCNG1)	Cyclin-G; CCNG; CYCG1	CCNG1	900	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000340828.7, CCNG1-201, 2444; ENST00000393929.5, CCNG1-202, 2366; ENST00000510664.5, CCNG1-208, 994; ENST00000512163.5, CCNG1-211, 919; ENST00000504553.2, CCNG1-203, 732; ENST00000510097.5, CCNG1-207, 564; ENST00000511490.4, CCNG1-209, 418; ENST00000511683.6, CCNG1-210, 1071; ENST00000509425.1, CCNG1-206, 759; ENST00000509143.1, CCNG1-205, 562; ENST00000506186.1, CCNG1-204, 580; ENST00000514367.1, CCNG1-213, 573; ENST00000512532.1, CCNG1-212, 540"	MIEVLTTTDSQKLLHQLNALLEQESRCQPKVCGLRLIESAHDNGLRMTARLRDFEVKDLLSLTQFFGFDTETFSLAVNLLDRFLSKMKVQPKHLGCVGLSCFYLAVKSIEEERNVPLATDLIRISQYRFTVSDLMRMEKIVLEKVCWKVKATTAFQFLQLYYSLLQENLPLERRNSINFERLEAQLKACHCRIIFSKAKPSVLALSIIALEIQAQKCVELTEGIECLQKHSKINGRDLTFWQELVSKCLTEYSSNKCSKPNVQKLKWIVSGRTARQLKHSYYRITHLPTIPEMVP	chr5:163437569-163446151[+]	May play a role in growth regulation. Is associated with G2/M phase arrest in response to DNA damage. May be an intermediate by which p53 mediates its role as an inhibitor of cellular proliferation (By similarity).	.	HGNC:1592	CCNG1_HUMAN	Reviewed	ENSG00000113328	.	.	.	.	.
Mol00282	Protein	Cyclin-G2 (CCNG2)	.	CCNG2	901	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000316355.10, CCNG2-201, 5471; ENST00000502280.5, CCNG2-204, 1459; ENST00000395640.5, CCNG2-202, 1410; ENST00000509972.1, CCNG2-205, 1549; ENST00000512918.5, CCNG2-206, 578; ENST00000497512.5, CCNG2-203, 2051; ENST00000514756.1, CCNG2-207, 518"	MKDLGAEHLAGHEGVQLLGLLNVYLEQEERFQPREKGLSLIEATPENDNTLCPGLRNAKVEDLRSLANFFGSCTETFVLAVNILDRFLALMKVKPKHLSCIGVCSFLLAARIVEEDCNIPSTHDVIRISQCKCTASDIKRMEKIISEKLHYELEATTALNFLHLYHTIILCHTSERKEILSLDKLEAQLKACNCRLIFSKAKPSVLALCLLNLEVETLKSVELLEILLLVKKHSKINDTEFFYWRELVSKCLAEYSSPECCKPDLKKLVWIVSRRTAQNLHNSYYSVPELPTIPEGGCFDESESEDSCEDMSCGEESLSSSPPSDQECTFFFNFKVAQTLCFPS	chr4:77157207-77433388[+]	May play a role in growth regulation and in negative regulation of cell cycle progression.	.	HGNC:1593	CCNG2_HUMAN	Reviewed	ENSG00000138764	.	.	.	.	.
Mol00283	Protein	CD166 antigen (ALCAM)	.	ALCAM	214	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000306107.9, ALCAM-201, 4701; ENST00000472644.6, ALCAM-205, 4189; ENST00000465413.6, ALCAM-203, 2496; ENST00000486979.6, ALCAM-207, 1818; ENST00000481337.5, ALCAM-206, 1242; ENST00000460954.1, ALCAM-202, 564; ENST00000491388.6, ALCAM-209, 2845; ENST00000470756.5, ALCAM-204, 1770; ENST00000489178.1, ALCAM-208, 783"	MESKGASSCRLLFCLLISATVFRPGLGWYTVNSAYGDTIIIPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLNLSENYTLSISNARISDEKRFVCMLVTEDNVFEAPTIVKVFKQPSKPEIVSKALFLETEQLKKLGDCISEDSYPDGNITWYRNGKVLHPLEGAVVIIFKKEMDPVTQLYTMTSTLEYKTTKADIQMPFTCSVTYYGPSGQKTIHSEQAVFDIYYPTEQVTIQVLPPKNAIKEGDNITLKCLGNGNPPPEEFLFYLPGQPEGIRSSNTYTLTDVRRNATGDYKCSLIDKKSMIASTAITVHYLDLSLNPSGEVTRQIGDALPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADEISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA	chr3:105366909-105576900[+]	"Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6. Contributes to the formation and maturation of the immunological synapse via its interactions with CD6. Mediates homotypic interactions with cells that express ALCAM. Acts as a ligand for the LILRB4 receptor, enhancing LILRB4-mediated inhibition of T cell proliferation. Required for normal hematopoietic stem cell engraftment in the bone marrow. Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation. Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM. Mediates outgrowth and pathfinding for retinal ganglion cell axons."	PDB: 5A2F	HGNC:400	CD166_HUMAN	Reviewed	ENSG00000170017	.	.	.	.	.
Mol00284	Protein	Extracellular matrix receptor III (CD44)	.	CD44	960	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000428726.8, CD44-208, 5431; ENST00000263398.11, CD44-201, 4288; ENST00000415148.6, CD44-206, 2369; ENST00000433892.6, CD44-209, 2292; ENST00000434472.6, CD44-210, 1634; ENST00000352818.8, CD44-205, 1023; ENST00000278386.10, CD44-203, 484; ENST00000442151.6, CD44-211, 1825; ENST00000526025.2, CD44-222, 1025; ENST00000525211.6, CD44-214, 874; ENST00000526669.6, CD44-224, 870; ENST00000279452.10, CD44-204, 862; ENST00000531110.6, CD44-231, 806; ENST00000525685.6, CD44-219, 729; ENST00000526000.6, CD44-221, 721; ENST00000525469.1, CD44-218, 705; ENST00000278385.10, CD44-202, 697; ENST00000528455.5, CD44-228, 687; ENST00000528672.1, CD44-229, 586; ENST00000531873.5, CD44-234, 584; ENST00000533222.5, CD44-236, 581; ENST00000526553.6, CD44-223, 571; ENST00000525688.5, CD44-220, 560; ENST00000527889.6, CD44-226, 548; ENST00000524922.1, CD44-212, 352; ENST00000425428.6, CD44-207, 1768; ENST00000528922.1, CD44-230, 1319; ENST00000528086.5, CD44-227, 580; ENST00000525209.5, CD44-213, 574; ENST00000531118.5, CD44-232, 877; ENST00000534296.5, CD44-238, 863; ENST00000527326.1, CD44-225, 718; ENST00000532339.1, CD44-235, 589; ENST00000525293.5, CD44-216, 569; ENST00000525348.1, CD44-217, 568; ENST00000534082.1, CD44-237, 564; ENST00000531141.1, CD44-233, 537; ENST00000525241.1, CD44-215, 440"	MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTADETRNLQNVDMKIGV	chr11:35138882-35232402[+]	"Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion."	PDB: 1POZ; PDB: 1UUH; PDB: 2I83; PDB: 4PZ3; PDB: 4PZ4; PDB: 6TXS	HGNC:1681	CD44_HUMAN	Reviewed	ENSG00000026508	.	.	.	.	.
Mol00285	Protein	T-lymphocyte activation antigen CD80 (CD80)	.	CD80	941	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264246.8, CD80-201, 2737; ENST00000478182.5, CD80-204, 1491; ENST00000383669.3, CD80-202, 771; ENST00000463729.1, CD80-203, 737"	MGHTRRQGTSPSKCPYLNFFQLLVLAGLSHFCSGVIHVTKEVKEVATLSCGHNVSVEELAQTRIYWQKEKKMVLTMMSGDMNIWPEYKNRTIFDITNNLSIVILALRPSDEGTYECVVLKYEKDAFKREHLAEVTLSVKADFPTPSISDFEIPTSNIRRIICSTSGGFPEPHLSWLENGEELNAINTTVSQDPETELYAVSSKLDFNMTTNHSFMCLIKYGHLRVNQTFNWNTTKQEHFPDNLLPSWAITLISVNGIFVICCLTYCFAPRCRERRRNERLRRESVRPV	chr3:119524293-119559614[-]	"Involved in the costimulatory signal essential for T-lymphocyte activation. T-cell proliferation and cytokine production is induced by the binding of CD28, binding to CTLA-4 has opposite effects and inhibits T-cell activation."	PDB: 1DR9; PDB: 1I8L	HGNC:1700	CD80_HUMAN	Reviewed	ENSG00000121594	.	.	.	.	.
Mol00286	Protein	Cell division cycle protein 27 homolog (CDC27)	Anaphase-promoting complex subunit 3; APC3; CDC27 homolog; CDC27Hs; H-NUC; ANAPC3; D0S1430E; D17S978E	CDC27	996	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000066544.8, CDC27-201, 5830; ENST00000531206.5, CDC27-207, 3177; ENST00000527547.5, CDC27-204, 2579; ENST00000575483.5, CDC27-217, 781; ENST00000571643.5, CDC27-213, 716; ENST00000533415.5, CDC27-210, 2570; ENST00000526866.5, CDC27-203, 1420; ENST00000573502.1, CDC27-214, 888; ENST00000570818.5, CDC27-212, 656; ENST00000570740.1, CDC27-211, 594; ENST00000573550.5, CDC27-215, 583; ENST00000576484.1, CDC27-219, 548; ENST00000532893.5, CDC27-209, 515; ENST00000574304.5, CDC27-216, 514; ENST00000528748.5, CDC27-206, 859; ENST00000532575.1, CDC27-208, 765; ENST00000575830.2, CDC27-218, 397; ENST00000525495.6, CDC27-202, 1459; ENST00000528147.1, CDC27-205, 463"	MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSNCLPNSCTTQVPNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSAVISPDTVPLGTGTSILSKQVQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSPGDGSYLQNYTNTPPVIDVPSTGAPSKKSVARIGQTGTKSVFSQSGNSREVTPILAQTQSSGPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGITQPNINDSLEITKLDSSIISEGKISTITPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQIGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF	chr17:47117703-47189422[-]	"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains."	PDB: 3T1N; PDB: 4RG6; PDB: 4RG7; PDB: 4RG9; PDB: 4UI9; PDB: 5A31; PDB: 5G04; PDB: 5G05; PDB: 5KHR; PDB: 5KHU; PDB: 5L9T; PDB: 5L9U; PDB: 5LCW; PDB: 6Q6G; PDB: 6Q6H; PDB: 6TLJ; PDB: 6TM5; PDB: 6TNT	HGNC:1728	CDC27_HUMAN	Reviewed	ENSG00000004897	.	.	.	.	.
Mol00287	Protein	Cyclin-dependent kinase 2 (CDK2)	Cell division protein kinase 2; p33 protein kinase; CDKN2	CDK2	1017	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000266970.9, CDK2-201, 2240; ENST00000354056.4, CDK2-202, 1260; ENST00000440311.6, CDK2-203, 1031; ENST00000553376.5, CDK2-204, 1725; ENST00000555408.5, CDK2-208, 2598; ENST00000555357.1, CDK2-207, 1367; ENST00000556656.5, CDK2-212, 1136; ENST00000556146.1, CDK2-209, 911; ENST00000556276.5, CDK2-210, 665; ENST00000556464.5, CDK2-211, 609; ENST00000554545.1, CDK2-205, 445; ENST00000554619.5, CDK2-206, 1802"	MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL	chr12:55966781-55972789[+]	"Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1. Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability. Phosphorylates CDK2AP2. Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks."	PDB: 1AQ1; PDB: 1B38; PDB: 1B39; PDB: 1BUH; PDB: 1CKP; PDB: 1DI8; PDB: 1DM2; PDB: 1E1V; PDB: 1E1X; PDB: 1E9H; PDB: 1F5Q; PDB: 1FIN; PDB: 1FQ1; PDB: 1FVT; PDB: 1FVV; PDB: 1G5S; PDB: 1GIH; PDB: 1GII; PDB: 1GIJ; PDB: 1GY3; PDB: 1GZ8; PDB: 1H00; PDB: 1H01; PDB: 1H07; PDB: 1H08; PDB: 1H0V; PDB: 1H0W; PDB: 1H1P; PDB: 1H1Q; PDB: 1H1R; PDB: 1H1S; PDB: 1H24; PDB: 1H25; PDB: 1H26; PDB: 1H27; PDB: 1H28; PDB: 1HCK; PDB: 1HCL; PDB: 1JST; PDB: 1JSU; PDB: 1JSV; PDB: 1JVP; PDB: 1KE5; PDB: 1KE6; PDB: 1KE7; PDB: 1KE8; PDB: 1KE9; PDB: 1OGU; PDB: 1OI9; PDB: 1OIQ; PDB: 1OIR; PDB: 1OIT; PDB: 1OIU; PDB: 1OIY; PDB: 1OKV; PDB: 1OKW; PDB: 1OL1; PDB: 1OL2; PDB: 1P2A; PDB: 1P5E; PDB: 1PF8; PDB: 1PKD; PDB: 1PW2; PDB: 1PXI; PDB: 1PXJ; PDB: 1PXK; PDB: 1PXL; PDB: 1PXM; PDB: 1PXN; PDB: 1PXO; PDB: 1PXP; PDB: 1PYE; PDB: 1QMZ; PDB: 1R78; PDB: 1URC; PDB: 1URW; PDB: 1V1K; PDB: 1VYW; PDB: 1VYZ; PDB: 1W0X; PDB: 1W8C; PDB: 1W98; PDB: 1WCC; PDB: 1Y8Y; PDB: 1Y91; PDB: 1YKR; PDB: 2A0C; PDB: 2A4L; PDB: 2B52; PDB: 2B53; PDB: 2B54; PDB: 2B55; PDB: 2BHE; PDB: 2BHH; PDB: 2BKZ; PDB: 2BPM; PDB: 2BTR; PDB: 2BTS; PDB: 2C4G; PDB: 2C5N; PDB: 2C5O; PDB: 2C5V; PDB: 2C5X; PDB: 2C5Y; PDB: 2C68; PDB: 2C69; PDB: 2C6I; PDB: 2C6K; PDB: 2C6L; PDB: 2C6M; PDB: 2C6O; PDB: 2C6T; PDB: 2CCH; PDB: 2CCI; PDB: 2CJM; PDB: 2CLX; PDB: 2DS1; PDB: 2DUV; PDB: 2EXM; PDB: 2FVD; PDB: 2G9X; PDB: 2I40; PDB: 2IW6; PDB: 2IW8; PDB: 2IW9; PDB: 2J9M; PDB: 2JGZ; PDB: 2R3F; PDB: 2R3G; PDB: 2R3H; PDB: 2R3I; PDB: 2R3J; PDB: 2R3K; PDB: 2R3L; PDB: 2R3M; PDB: 2R3N; PDB: 2R3O; PDB: 2R3P; PDB: 2R3Q; PDB: 2R3R; PDB: 2R64; PDB: 2UUE; PDB: 2UZB; PDB: 2UZD; PDB: 2UZE; PDB: 2UZL; PDB: 2UZN; PDB: 2UZO; PDB: 2V0D; PDB: 2V22; PDB: 2VTA; PDB: 2VTH; PDB: 2VTI; PDB: 2VTJ; PDB: 2VTL; PDB: 2VTM; PDB: 2VTN; PDB: 2VTO; PDB: 2VTP; PDB: 2VTQ; PDB: 2VTR; PDB: 2VTS; PDB: 2VTT; PDB: 2VU3; PDB: 2VV9; PDB: 2W05; PDB: 2W06; PDB: 2W17; PDB: 2W1H; PDB: 2WEV; PDB: 2WFY; PDB: 2WHB; PDB: 2WIH; PDB: 2WIP; PDB: 2WMA; PDB: 2WMB; PDB: 2WPA; PDB: 2WXV; PDB: 2X1N; PDB: 2XMY; PDB: 2XNB; PDB: 3BHT; PDB: 3BHU; PDB: 3BHV; PDB: 3DDP; PDB: 3DDQ; PDB: 3DOG; PDB: 3EID; PDB: 3EJ1; PDB: 3EOC; PDB: 3EZR; PDB: 3EZV; PDB: 3F5X; PDB: 3FZ1; PDB: 3IG7; PDB: 3IGG; PDB: 3LE6; PDB: 3LFN; PDB: 3LFQ; PDB: 3LFS; PDB: 3MY5; PDB: 3NS9; PDB: 3PJ8; PDB: 3PXF; PDB: 3PXQ; PDB: 3PXR; PDB: 3PXY; PDB: 3PXZ; PDB: 3PY0; PDB: 3PY1; PDB: 3QHR; PDB: 3QHW; PDB: 3QL8; PDB: 3QQF; PDB: 3QQG; PDB: 3QQH; PDB: 3QQJ; PDB: 3QQK; PDB: 3QQL; PDB: 3QRT; PDB: 3QRU; PDB: 3QTQ; PDB: 3QTR; PDB: 3QTS; PDB: 3QTU; PDB: 3QTW; PDB: 3QTX; PDB: 3QTZ; PDB: 3QU0; PDB: 3QWJ; PDB: 3QWK; PDB: 3QX2; PDB: 3QX4; PDB: 3QXO; PDB: 3QXP; PDB: 3QZF; PDB: 3QZG; PDB: 3QZH; PDB: 3QZI; PDB: 3R1Q; PDB: 3R1S; PDB: 3R1Y; PDB: 3R28; PDB: 3R6X; PDB: 3R71; PDB: 3R73; PDB: 3R7E; PDB: 3R7I; PDB: 3R7U; PDB: 3R7V; PDB: 3R7Y; PDB: 3R83; PDB: 3R8L; PDB: 3R8M; PDB: 3R8P; PDB: 3R8U; PDB: 3R8V; PDB: 3R8Z; PDB: 3R9D; PDB: 3R9H; PDB: 3R9N; PDB: 3R9O; PDB: 3RAH; PDB: 3RAI; PDB: 3RAK; PDB: 3RAL; PDB: 3RJC; PDB: 3RK5; PDB: 3RK7; PDB: 3RK9; PDB: 3RKB; PDB: 3RM6; PDB: 3RM7; PDB: 3RMF; PDB: 3RNI; PDB: 3ROY; PDB: 3RPO; PDB: 3RPR; PDB: 3RPV; PDB: 3RPY; PDB: 3RZB; PDB: 3S00; PDB: 3S0O; PDB: 3S1H; PDB: 3S2P; PDB: 3SQQ; PDB: 3SW4; PDB: 3SW7; PDB: 3TI1; PDB: 3TIY; PDB: 3TIZ; PDB: 3TNW; PDB: 3ULI; PDB: 3UNJ; PDB: 3UNK; PDB: 3WBL; PDB: 4ACM; PDB: 4BCK; PDB: 4BCM; PDB: 4BCN; PDB: 4BCO; PDB: 4BCP; PDB: 4BCQ; PDB: 4BGH; PDB: 4BZD; PDB: 4CFM; PDB: 4CFN; PDB: 4CFU; PDB: 4CFV; PDB: 4CFW; PDB: 4CFX; PDB: 4D1X; PDB: 4D1Z; PDB: 4EK3; PDB: 4EK4; PDB: 4EK5; PDB: 4EK6; PDB: 4EK8; PDB: 4EOI; PDB: 4EOJ; PDB: 4EOK; PDB: 4EOL; PDB: 4EOM; PDB: 4EON; PDB: 4EOO; PDB: 4EOP; PDB: 4EOQ; PDB: 4EOR; PDB: 4EOS; PDB: 4ERW; PDB: 4EZ3; PDB: 4EZ7; PDB: 4FKG; PDB: 4FKI; PDB: 4FKJ; PDB: 4FKL; PDB: 4FKO; PDB: 4FKP; PDB: 4FKQ; PDB: 4FKR; PDB: 4FKS; PDB: 4FKT; PDB: 4FKU; PDB: 4FKV; PDB: 4FKW; PDB: 4FX3; PDB: 4GCJ; PDB: 4I3Z; PDB: 4II5; PDB: 4KD1; PDB: 4LYN; PDB: 4NJ3; PDB: 4RJ3; PDB: 5A14; PDB: 5AND; PDB: 5ANE; PDB: 5ANG; PDB: 5ANI; PDB: 5ANJ; PDB: 5ANK; PDB: 5ANO; PDB: 5CYI; PDB: 5D1J; PDB: 5FP5; PDB: 5FP6; PDB: 5IEV; PDB: 5IEX; PDB: 5IEY; PDB: 5IF1; PDB: 5JQ5; PDB: 5JQ8; PDB: 5K4J; PDB: 5L2W; PDB: 5LMK; PDB: 5MHQ; PDB: 5NEV; PDB: 5OO0; PDB: 5OO1; PDB: 5OO3; PDB: 5OSJ; PDB: 5OSM; PDB: 5UQ1; PDB: 5UQ2; PDB: 5UQ3; PDB: 6ATH; PDB: 6GUB; PDB: 6GUC; PDB: 6GUE; PDB: 6GUF; PDB: 6GUH; PDB: 6GUK; PDB: 6GVA; PDB: 6INL; PDB: 6JGM; PDB: 6OQI; PDB: 6P3W; PDB: 6Q3B; PDB: 6Q3C; PDB: 6Q3F; PDB: 6Q48; PDB: 6Q49; PDB: 6Q4A; PDB: 6Q4B; PDB: 6Q4C; PDB: 6Q4D; PDB: 6Q4E; PDB: 6Q4F; PDB: 6Q4G; PDB: 6Q4H; PDB: 6Q4I; PDB: 6Q4J; PDB: 6Q4K; PDB: 6RIJ; PDB: 6SG4; PDB: 6YL1; PDB: 6YL6; PDB: 6YLK; PDB: 7ACK; PDB: 7B5L; PDB: 7B5R; PDB: 7B7S; PDB: 7E34; PDB: 7KJS; PDB: 7M2F; PDB: 7NVQ	HGNC:1771	CDK2_HUMAN	Reviewed	ENSG00000123374	.	.	.	.	.
Mol00288	Protein	Cyclin-dependent kinase 8 (CDK8)	Cell division protein kinase 8; Mediator complex subunit CDK8; Mediator of RNA polymerase II transcription subunit CDK8; Protein kinase K35	CDK8	1024	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000381527.8, CDK8-201, 3065; ENST00000625988.1, CDK8-206, 795; ENST00000465820.6, CDK8-202, 586; ENST00000536792.5, CDK8-205, 3032; ENST00000480323.1, CDK8-204, 1996; ENST00000477277.5, CDK8-203, 1770"	MDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPGNQDSSHTQGPPLKKVRVVPPTTTSGGLIMTSDYQRSNPHAAYPNPGPSTSQPQSSMGYSATSQQPPQYSHQTHRY	chr13:26254104-26405238[+]	"Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Phosphorylates CCNH leading to down-regulation of the TFIIH complex and transcriptional repression. Recruited through interaction with MAML1 to hyperphosphorylate the intracellular domain of NOTCH, leading to its degradation."	PDB: 3RGF; PDB: 4CRL; PDB: 4F6S; PDB: 4F6U; PDB: 4F6W; PDB: 4F70; PDB: 4F7J; PDB: 4F7L; PDB: 4F7N; PDB: 4F7S; PDB: 4G6L; PDB: 5BNJ; PDB: 5CEI; PDB: 5FGK; PDB: 5HBE; PDB: 5HBH; PDB: 5HBJ; PDB: 5HNB; PDB: 5HVY; PDB: 5I5Z; PDB: 5ICP; PDB: 5IDN; PDB: 5IDP; PDB: 5XQX; PDB: 5XS2; PDB: 6QTG; PDB: 6QTJ; PDB: 6R3S; PDB: 6T41; PDB: 6TPA; PDB: 6Y0A	HGNC:1779	CDK8_HUMAN	Reviewed	ENSG00000132964	.	.	.	.	.
Mol00289	Protein	Cyclin-dependent kinase inhibitor 2A (CDKN2A)	Cyclin-dependent kinase 4 inhibitor A; CDK4I; Multiple tumor suppressor 1; MTS-1; p16-INK4a; p16-INK4; p16INK4A; CDKN2; MTS1	CDKN2A	1029	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000304494.10, CDKN2A-201, 978; ENST00000579755.2, CDKN2A-214, 1052; ENST00000494262.5, CDKN2A-206, 989; ENST00000498628.6, CDKN2A-209, 926; ENST00000498124.1, CDKN2A-208, 880; ENST00000530628.2, CDKN2A-210, 748; ENST00000578845.2, CDKN2A-212, 678; ENST00000579122.1, CDKN2A-213, 666; ENST00000497750.1, CDKN2A-207, 565; ENST00000479692.2, CDKN2A-205, 544; ENST00000380151.3, CDKN2A-203, 794; ENST00000470819.2, CDKN2A-204, 856; ENST00000380150.2, CDKN2A-202, 493; ENST00000577854.1, CDKN2A-211, 442"	MEPAAGSSMEPSADWLATAAARGRVEEVRALLEAGALPNAPNSYGRRPIQVMMMGSARVAELLLLHGAEPNCADPATLTRPVHDAAREGFLDTLVVLHRAGARLDVRDAWGRLPVDLAEELGHRDVARYLRAAAGGTRGSNHARIDAAEGPSDIPD	chr9:21967752-21995301[-]	Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein.	PDB: 1A5E; PDB: 1BI7; PDB: 1DC2; PDB: 2A5E	HGNC:1787	CDN2A_HUMAN	Reviewed	ENSG00000147889	.	.	.	.	.
Mol00290	Protein	Phosphatidate cytidylyltransferase 2 (CDS2)	CDP-DAG synthase 2; CDP-DG synthase 2; CDP-diacylglycerol synthase 2; CDS 2; CDP-diglyceride pyrophosphorylase 2; CDP-diglyceride synthase 2; CTP:phosphatidate cytidylyltransferase 2	CDS2	8760	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000460006.6, CDS2-203, 9076; ENST00000450570.1, CDS2-202, 945; ENST00000379070.3, CDS2-201, 2713; ENST00000468817.5, CDS2-205, 2706; ENST00000467923.5, CDS2-204, 783; ENST00000486875.1, CDS2-206, 709"	MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQLHIFNTLRSHLIDKGMLTSTTEDE	chr20:5126879-5197887[+]	"Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol. Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid. Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis."	.	HGNC:1801	CDS2_HUMAN	Reviewed	ENSG00000101290	.	.	.	.	.
Mol00291	Protein	Centromere protein R (CENPR)	CENP-R; Beta-3-endonexin; Integrin beta-3-binding protein; Nuclear receptor-interacting factor 3; CENPR; NRIF3	ITGB3BP	23421	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000271002.15, ITGB3BP-201, 961; ENST00000371092.7, ITGB3BP-202, 1044; ENST00000489099.5, ITGB3BP-212, 1285; ENST00000461681.5, ITGB3BP-205, 1096; ENST00000465781.5, ITGB3BP-208, 1025; ENST00000460251.5, ITGB3BP-203, 1012; ENST00000463803.5, ITGB3BP-207, 948; ENST00000476508.5, ITGB3BP-209, 945; ENST00000460394.5, ITGB3BP-204, 873; ENST00000462285.5, ITGB3BP-206, 657; ENST00000489863.5, ITGB3BP-213, 619; ENST00000492655.1, ITGB3BP-214, 589; ENST00000478538.1, ITGB3BP-211, 524; ENST00000478138.1, ITGB3BP-210, 504"	MPVKRSLKLDGLLEENSFDPSKITRKKSVITYSPTTGTCQMSLFASPTSSEEQKHRNGLSNEKRKKLNHPSLTESKESTTKDNDEFMMLLSKVEKLSEEIMEIMQNLSSIQALEGSRELENLIGISCASHFLKREMQKTKELMTKVNKQKLFEKSTGLPHKASRHLDSYEFLKAILN	chr1:63440770-63593721[-]	"Transcription coregulator that can have both coactivator and corepressor functions. Isoform 1, but not other isoforms, is involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. In contrast, it does not coactivate nuclear receptors for retinoic acid, vitamin D, progesterone receptor, nor glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit, possibly by interfering with the transactivation domain of NFKB1. Induces apoptosis in breast cancer cells, but not in other cancer cells, via a caspase-2 mediated pathway that involves mitochondrial membrane permeabilization but does not require other caspases. May also act as an inhibitor of cyclin A-associated kinase. Also acts a component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex."	.	HGNC:6157	CENPR_HUMAN	Reviewed	ENSG00000142856	.	.	.	.	.
Mol00292	Protein	Matrix protein P1 (HSPD1)	60 kDa chaperonin; Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; Hsp60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; HSP60	HSPD1	3329	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000388968.8, HSPD1-202, 2245; ENST00000418022.2, HSPD1-203, 2540; ENST00000439605.2, HSPD1-207, 2510; ENST00000428204.6, HSPD1-205, 2449; ENST00000452200.6, HSPD1-209, 2407; ENST00000426480.2, HSPD1-204, 2312; ENST00000345042.6, HSPD1-201, 2299; ENST00000677913.1, HSPD1-218, 2257; ENST00000678761.1, HSPD1-222, 2252; ENST00000678621.1, HSPD1-221, 2413; ENST00000676933.1, HSPD1-214, 2200; ENST00000678170.1, HSPD1-219, 2022; ENST00000430176.6, HSPD1-206, 745; ENST00000678545.1, HSPD1-220, 2564; ENST00000677403.1, HSPD1-215, 2468; ENST00000677454.1, HSPD1-216, 2320; ENST00000679291.1, HSPD1-224, 2210; ENST00000677792.1, HSPD1-217, 2195; ENST00000440114.2, HSPD1-208, 2178; ENST00000461097.2, HSPD1-210, 4930; ENST00000678969.1, HSPD1-223, 3772; ENST00000476746.6, HSPD1-211, 3230; ENST00000491249.1, HSPD1-213, 860; ENST00000486181.5, HSPD1-212, 648"	MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF	chr2:197486584-197516737[-]	"Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable)."	PDB: 4PJ1; PDB: 6HT7; PDB: 6MRC; PDB: 6MRD; PDB: 7AZP; PDB: 7L7S	HGNC:5261	CH60_HUMAN	Reviewed	ENSG00000144381	.	.	.	.	.
Mol00293	Protein	Chromodomain-helicase-DNA-binding protein 5 (CHD5)	CHD-5; ATP-dependent helicase CHD5; KIAA0444	CHD5	26038	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262450.8, CHD5-201, 9850; ENST00000475121.1, CHD5-204, 558; ENST00000496404.1, CHD5-206, 4966; ENST00000462991.5, CHD5-203, 4396; ENST00000377999.5, CHD5-202, 3044; ENST00000491020.1, CHD5-205, 646"	MRGPVGTEEELPRLFAEEMENEDEMSEEEDGGLEAFDDFFPVEPVSLPKKKKPKKLKENKCKGKRKKKEGSNDELSENEEDLEEKSESEGSDYSPNKKKKKKLKDKKEKKAKRKKKDEDEDDNDDGCLKEPKSSGQLMAEWGLDDVDYLFSEEDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTISPPLAVSPPQVPQPVPIRKAKTKEGKGPGVRKKIKGSKDGKKKGKGKKTAGLKFRFGGISNKRKKGSSSEEDEREESDFDSASIHSASVRSECSAALGKKSKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDDEEEEGGCEEEEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPDVEPSLPPPKPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMIHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDDIDIPYYDNLKQAYWGHRELMLGEDTRLPKRLLKKGKKLRDDKQEKPPDTPIVDPTVKFDKQPWYIDSTGGTLHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVTYTGDKESRSVIRENEFSFEDNAIRSGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKKYYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLPNGSYDGSSLVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGLRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTEELFKDDVEGMMSQGQRPVTPIPDVQSSKGGNLAASAKKKHGSTPPGDNKDVEDSSVIHYDDAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREIIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSEDEDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRWGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLIPEGPEGKKSGEVISSDPNTPVPASPAHLLPAPLGLPDKMEAQLGYMDEKDPGAQKPRQPLEVQALPAALDRVESEDKHESPASKERAREERPEETEKAPPSPEQLPREEVLPEKEKILDKLELSLIHSRGDSSELRPDDTKAEEKEPIETQQNGDKEEDDEGKKEDKKGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYDIWHRRHDYWLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEVHKGNYLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQGAFGSSQMYSNNFGPNFRGPGPGGIVNYNQMPLGPYVTDI	chr1:6101787-6180321[-]	"Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa."	PDB: 6GUU	HGNC:16816	CHD5_HUMAN	Reviewed	ENSG00000116254	.	.	.	.	.
Mol00294	Protein	Serine/threonine-protein kinase Chk1 (CHK1)	CHK1 checkpoint homolog; Cell cycle checkpoint kinase; Checkpoint kinase-1; CHK1	CHEK1	1111	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000438015.7, CHEK1-204, 4128; ENST00000534070.5, CHEK1-213, 3513; ENST00000532449.6, CHEK1-211, 3390; ENST00000428830.6, CHEK1-203, 1845; ENST00000427383.6, CHEK1-202, 1670; ENST00000544373.5, CHEK1-215, 1653; ENST00000278916.8, CHEK1-201, 1571; ENST00000527013.6, CHEK1-208, 668; ENST00000532669.5, CHEK1-212, 617; ENST00000534685.5, CHEK1-214, 583; ENST00000526937.5, CHEK1-207, 562; ENST00000531607.5, CHEK1-210, 462; ENST00000524737.6, CHEK1-205, 1913; ENST00000525396.5, CHEK1-206, 769; ENST00000531062.2, CHEK1-209, 1773"	MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDFSPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRRNNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKIWLPAT	chr11:125625163-125676255[+]	"Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Binds to and phosphorylates CDC25A, CDC25B and CDC25C. Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C. Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A. Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A. Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression. Also phosphorylates NEK6. Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination. Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation. Also promotes repair of DNA cross-links through phosphorylation of FANCE. Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A. This may enhance chromatin assembly both in the presence or absence of DNA damage. May also play a role in replication fork maintenance through regulation of PCNA. May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones. Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes. May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest. Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin. Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity."	PDB: 1IA8; PDB: 1NVQ; PDB: 1NVR; PDB: 1NVS; PDB: 1ZLT; PDB: 1ZYS; PDB: 2AYP; PDB: 2BR1; PDB: 2BRB; PDB: 2BRG; PDB: 2BRH; PDB: 2BRM; PDB: 2BRN; PDB: 2BRO; PDB: 2C3J; PDB: 2C3K; PDB: 2C3L; PDB: 2CGU; PDB: 2CGV; PDB: 2CGW; PDB: 2CGX; PDB: 2E9N; PDB: 2E9O; PDB: 2E9P; PDB: 2E9U; PDB: 2E9V; PDB: 2GDO; PDB: 2GHG; PDB: 2HOG; PDB: 2HXL; PDB: 2HXQ; PDB: 2HY0; PDB: 2QHM; PDB: 2QHN; PDB: 2R0U; PDB: 2WMQ; PDB: 2WMR; PDB: 2WMS; PDB: 2WMT; PDB: 2WMU; PDB: 2WMV; PDB: 2WMW; PDB: 2WMX; PDB: 2X8D; PDB: 2X8E; PDB: 2X8I; PDB: 2XEY; PDB: 2XEZ; PDB: 2XF0; PDB: 2YDI; PDB: 2YDJ; PDB: 2YDK; PDB: 2YER; PDB: 2YEX; PDB: 2YM3; PDB: 2YM4; PDB: 2YM5; PDB: 2YM6; PDB: 2YM7; PDB: 2YM8; PDB: 2YWP; PDB: 3F9N; PDB: 3JVR; PDB: 3JVS; PDB: 3NLB; PDB: 3OT3; PDB: 3OT8; PDB: 3PA3; PDB: 3PA4; PDB: 3PA5; PDB: 3TKH; PDB: 3TKI; PDB: 3U9N; PDB: 4FSM; PDB: 4FSN; PDB: 4FSQ; PDB: 4FSR; PDB: 4FST; PDB: 4FSU; PDB: 4FSW; PDB: 4FSY; PDB: 4FSZ; PDB: 4FT0; PDB: 4FT3; PDB: 4FT5; PDB: 4FT7; PDB: 4FT9; PDB: 4FTA; PDB: 4FTC; PDB: 4FTI; PDB: 4FTJ; PDB: 4FTK; PDB: 4FTL; PDB: 4FTM; PDB: 4FTN; PDB: 4FTO; PDB: 4FTQ; PDB: 4FTR; PDB: 4FTT; PDB: 4FTU; PDB: 4GH2; PDB: 4HYH; PDB: 4HYI; PDB: 4JIK; PDB: 4QYE; PDB: 4QYF; PDB: 4QYG; PDB: 4QYH; PDB: 4RVK; PDB: 4RVL; PDB: 4RVM; PDB: 5DLS; PDB: 5F4N; PDB: 5OOP; PDB: 5OOR; PDB: 5OOT; PDB: 5OP2; PDB: 5OP4; PDB: 5OP5; PDB: 5OP7; PDB: 5OPB; PDB: 5OPR; PDB: 5OPS; PDB: 5OPU; PDB: 5OPV; PDB: 5OQ5; PDB: 5OQ6; PDB: 5OQ7; PDB: 5OQ8; PDB: 5WI2; PDB: 6FC8; PDB: 6FCF; PDB: 6FCK; PDB: 7AKM; PDB: 7AKO; PDB: 7BJD; PDB: 7BJE; PDB: 7BJH; PDB: 7BJJ; PDB: 7BJM; PDB: 7BJO; PDB: 7BJR; PDB: 7BJX; PDB: 7BK1; PDB: 7BK2; PDB: 7BK3; PDB: 7BKN; PDB: 7BKO; PDB: 7MCK	HGNC:1925	CHK1_HUMAN	Reviewed	ENSG00000149554	.	.	.	.	.
Mol00295	Protein	Claudin-2 (CLDN2)	SP82; PSEC0059; SP82; UNQ705/PRO1356	CLDN2	9075	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000336803.2, CLDN2-201, 2961; ENST00000540876.1, CLDN2-202, 2919; ENST00000541806.6, CLDN2-203, 1871"	MASLGLQLVGYILGLLGLLGTLVAMLLPSWKTSSYVGASIVTAVGFSKGLWMECATHSTGITQCDIYSTLLGLPADIQAAQAMMVTSSAISSLACIISVVGMRCTVFCQESRAKDRVAVAGGVFFILGGLLGFIPVAWNLHGILRDFYSPLVPDSMKFEIGEALYLGIISSLFSLIAGIILCFSCSSQRNRSNYYDAYQAQPLATRSSPRPGQPPKVKSEFNSYSLTGYV	chrX:106900164-106930861[+]	"Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity."	PDB: 4YYX	HGNC:2041	CLD2_HUMAN	Reviewed	ENSG00000165376	.	.	.	.	.
Mol00296	Protein	Clathrin heavy chain 1 (CLTC)	Clathrin heavy chain on chromosome 17; CLH-17; CLH17; CLTCL2; KIAA0034	CLTC	1213	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000269122.8, CLTC-201, 8369; ENST00000621829.4, CLTC-215, 8587; ENST00000393043.5, CLTC-202, 5292; ENST00000579456.5, CLTC-210, 2301; ENST00000472651.5, CLTC-205, 665; ENST00000580081.1, CLTC-212, 575; ENST00000475458.1, CLTC-206, 479; ENST00000483176.2, CLTC-207, 760; ENST00000584313.5, CLTC-213, 715; ENST00000579815.1, CLTC-211, 609; ENST00000498711.1, CLTC-209, 2941; ENST00000466513.1, CLTC-203, 793; ENST00000496076.1, CLTC-208, 678; ENST00000472129.3, CLTC-204, 654; ENST00000585198.1, CLTC-214, 477"	MAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGAEELFARKFNALFAQGNYSEAAKVAANAPKGILRTPDTIRRFQSVPAQPGQTSPLLQYFGILLDQGQLNKYESLELCRPVLQQGRKQLLEKWLKEDKLECSEELGDLVKSVDPTLALSVYLRANVPNKVIQCFAETGQVQKIVLYAKKVGYTPDWIFLLRNVMRISPDQGQQFAQMLVQDEEPLADITQIVDVFMEYNLIQQCTAFLLDALKNNRPSEGPLQTRLLEMNLMHAPQVADAILGNQMFTHYDRAHIAQLCEKAGLLQRALEHFTDLYDIKRAVVHTHLLNPEWLVNYFGSLSVEDSLECLRAMLSANIRQNLQICVQVASKYHEQLSTQSLIELFESFKSFEGLFYFLGSIVNFSQDPDVHFKYIQAACKTGQIKEVERICRESNCYDPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVIGGLLDVDCSEDVIKNLILVVRGQFSTDELVAEVEKRNRLKLLLPWLEARIHEGCEEPATHNALAKIYIDSNNNPERFLRENPYYDSRVVGKYCEKRDPHLACVAYERGQCDLELINVCNENSLFKSLSRYLVRRKDPELWGSVLLESNPYRRPLIDQVVQTALSETQDPEEVSVTVKAFMTADLPNELIELLEKIVLDNSVFSEHRNLQNLLILTAIKADRTRVMEYINRLDNYDAPDIANIAISNELFEEAFAIFRKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQLAKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVETELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFYLEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKDSLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNIMDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPPQAPFGYGYTAPPYGQPQPGFGYSM	chr17:59619689-59696956[+]	Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Plays a role in early autophagosome formation.	PDB: 2XZG; PDB: 4G55; PDB: 6E4L; PDB: 6QNN; PDB: 6QNP	HGNC:2092	CLH1_HUMAN	Reviewed	ENSG00000141367	.	.	.	.	.
Mol00297	Protein	Clusterin (CLU)	Aging-associated gene 4 protein; Apolipoprotein J; Apo-J; Complement cytolysis inhibitor; CLI; Complement-associated protein SP-40;40; Ku70-binding protein 1; NA1/NA2; Sulfated glycoprotein 2; SGP-2; Testosterone-repressed prostate message 2; TRPM-2; ApoJalpha; Complement cytolysis inhibitor a chain; ApoJbeta; Complement cytolysis inhibitor b chain; APOJ; CLI; KUB1; AAG4	CLU	1191	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000316403.15, CLU-201, 2749; ENST00000523500.5, CLU-215, 2381; ENST00000405140.7, CLU-202, 2098; ENST00000560566.5, CLU-217, 1039; ENST00000523589.5, CLU-216, 878; ENST00000522098.1, CLU-209, 850; ENST00000522238.1, CLU-210, 791; ENST00000520796.5, CLU-207, 737; ENST00000522413.5, CLU-212, 654; ENST00000519742.5, CLU-205, 583; ENST00000520491.5, CLU-206, 580; ENST00000521770.1, CLU-208, 520; ENST00000523396.1, CLU-214, 426; ENST00000519472.5, CLU-204, 303; ENST00000522299.5, CLU-211, 2807; ENST00000518050.1, CLU-203, 718; ENST00000522502.1, CLU-213, 594"	MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE	chr8:27596917-27614700[-]	"[Isoform 1]: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Protects cells against apoptosis and against cytolysis by complement. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3. Plays a role in the clearance of immune complexes that arise during cell injury."	.	HGNC:2095	CLUS_HUMAN	Reviewed	ENSG00000120885	.	.	.	.	.
Mol00298	Protein	Collagen alpha-1(I) chain (COL1A1)	Alpha-1 type I collagen	COL1A1	1277	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000225964.10, COL1A1-201, 5914; ENST00000507689.1, COL1A1-211, 549; ENST00000471344.1, COL1A1-203, 1192; ENST00000510710.3, COL1A1-212, 1147; ENST00000486572.1, COL1A1-207, 836; ENST00000511732.1, COL1A1-213, 789; ENST00000474644.1, COL1A1-204, 640; ENST00000463440.1, COL1A1-202, 614; ENST00000476387.1, COL1A1-205, 600; ENST00000495677.1, COL1A1-209, 594; ENST00000504289.1, COL1A1-210, 481; ENST00000485870.1, COL1A1-206, 403; ENST00000494334.1, COL1A1-208, 396"	MFSFVDLRLLLLLAATALLTHGQEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDNGKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPGGPPGPKGNSGEPGAPGSKGDTGAKGEPGPVGVQGPPGPAGEEGKRGARGEPGPTGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGESGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGAKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPAGPVGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGAPGKDGLNGLPGPIGPPGPRGRTGDAGPVGPPGPPGPPGPPGPPSAGFDFSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKDKRHVWFGESMTDGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTVDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPVCFL	chr17:50184101-50201632[-]	Type I collagen is a member of group I collagen (fibrillar forming collagen).	PDB: 1Q7D; PDB: 2LLP; PDB: 3EJH; PDB: 3GXE; PDB: 5CTD; PDB: 5CTI; PDB: 5CVA; PDB: 5CVB; PDB: 5K31; PDB: 5OU8; PDB: 5OU9; PDB: 7E7B; PDB: 7E7D	HGNC:2197	CO1A1_HUMAN	Reviewed	ENSG00000108821	.	.	.	.	.
Mol00299	Protein	Solute carrier family 31 member 1 (SLC31A1)	Copper transporter 1; hCTR1; Solute carrier family 31 member 1; COPT1; CTR1	SLC31A1	1317	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374212.5, SLC31A1-201, 4762; ENST00000496650.1, SLC31A1-202, 475"	MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFGFKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH	chr9:113221544-113264492[+]	"High-affinity, saturable copper transporter involved in dietary copper uptake."	PDB: 2LS2; PDB: 2LS3; PDB: 2LS4	HGNC:11016	COPT1_HUMAN	Reviewed	ENSG00000136868	.	.	.	.	.
Mol00300	Protein	Cytochrome P450 family 1 subfamily B member1 (CYP1B1)	CYPIB1; Hydroperoxy icosatetraenoate dehydratase	CYP1B1	1545	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000610745.5, CYP1B1-205, 5218; ENST00000614273.1, CYP1B1-207, 2174; ENST00000494864.1, CYP1B1-204, 1479; ENST00000490576.1, CYP1B1-201, 567; ENST00000492443.1, CYP1B1-203, 745; ENST00000613082.1, CYP1B1-206, 573; ENST00000491456.1, CYP1B1-202, 289"	MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLIGNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAFASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVALLVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSLVDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSAEKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAELDQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVVFVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQLFLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKETCQ	chr2:38066973-38109902[-]	"A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Exhibits catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2- and 4-hydroxy E1 and E2. Displays a predominant hydroxylase activity toward E2 at the C-4 position. Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites. May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system. Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2. Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products. Plays an important role in retinal vascular development. Under hyperoxic O2 conditions, promotes retinal angiogenesis and capillary morphogenesis, likely by metabolizing the oxygenated products generated during the oxidative stress. Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression."	PDB: 3PM0; PDB: 6IQ5	HGNC:2597	CP1B1_HUMAN	Reviewed	ENSG00000138061	.	.	.	.	.
Mol00301	Protein	Cytochrome P450 family 3 subfamily A  member1 (CYP3A4)	1;4-cineole 2-exo-monooxygenase; 1;8-cineole 2-exo-monooxygenase; Albendazole monooxygenase (sulfoxide-forming); Albendazole sulfoxidase; CYPIIIA3; CYPIIIA4; Cholesterol 25-hydroxylase; Cytochrome P450 3A3; Cytochrome P450 HLp; Cytochrome P450 NF-25; Cytochrome P450-PCN1; Nifedipine oxidase; Quinine 3-monooxygenase; CYP3A3	CYP3A4	1576	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000651514.1, CYP3A4-206, 2781; ENST00000354593.6, CYP3A4-202, 2342; ENST00000336411.7, CYP3A4-201, 2165; ENST00000652018.1, CYP3A4-207, 1982; ENST00000415003.1, CYP3A4-203, 564; ENST00000651162.1, CYP3A4-205, 1401; ENST00000480043.1, CYP3A4-204, 651"	MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA	chr7:99756960-99784248[-]	"A cytochrome P450 monooxygenase involved in the metabolism of sterols, steroid hormones, retinoids and fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C-16 position. Plays a role in the metabolism of androgens, particularly in oxidative deactivation of testosterone. Metabolizes testosterone to less biologically active 2beta- and 6beta-hydroxytestosterones. Contributes to the formation of hydroxycholesterols (oxysterols), particularly A-ring hydroxylated cholesterol at the C-4beta position, and side chain hydroxylated cholesterol at the C-25 position, likely contributing to cholesterol degradation and bile acid biosynthesis. Catalyzes bisallylic hydroxylation of polyunsaturated fatty acids (PUFA). Catalyzes the epoxidation of double bonds of PUFA with a preference for the last double bond. Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling. Plays a role in the metabolism of retinoids. Displays high catalytic activity for oxidation of all-trans-retinol to all-trans-retinal, a rate-limiting step for the biosynthesis of all-trans-retinoic acid (atRA). Further metabolizes atRA toward 4-hydroxyretinoate and may play a role in hepatic atRA clearance. Responsible for oxidative metabolism of xenobiotics. Acts as a 2-exo-monooxygenase for plant lipid 1,8-cineole (eucalyptol). Metabolizes the majority of the administered drugs. Catalyzes sulfoxidation of the anthelmintics albendazole and fenbendazole. Hydroxylates antimalarial drug quinine. Acts as a 1,4-cineole 2-exo-monooxygenase. Also involved in vitamin D catabolism and calcium homeostasis. Catalyzes the inactivation of the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3))."	PDB: 1TQN; PDB: 1W0E; PDB: 1W0F; PDB: 1W0G; PDB: 2J0D; PDB: 2V0M; PDB: 3NXU; PDB: 3TJS; PDB: 3UA1; PDB: 4D6Z; PDB: 4D75; PDB: 4D78; PDB: 4D7D; PDB: 4I3Q; PDB: 4I4G; PDB: 4I4H; PDB: 4K9T; PDB: 4K9U; PDB: 4K9V; PDB: 4K9W; PDB: 4K9X; PDB: 4NY4; PDB: 5A1P; PDB: 5A1R; PDB: 5G5J; PDB: 5TE8; PDB: 5VC0; PDB: 5VCC; PDB: 5VCD; PDB: 5VCE; PDB: 5VCG; PDB: 6BCZ; PDB: 6BD5; PDB: 6BD6; PDB: 6BD7; PDB: 6BD8; PDB: 6BDH; PDB: 6BDI; PDB: 6BDK; PDB: 6BDM; PDB: 6OO9; PDB: 6OOA; PDB: 6OOB; PDB: 7KS8; PDB: 7KSA; PDB: 7KVH; PDB: 7KVI; PDB: 7KVJ; PDB: 7KVK; PDB: 7KVM; PDB: 7KVN; PDB: 7KVO; PDB: 7KVP; PDB: 7KVQ; PDB: 7KVS; PDB: 7LXL	HGNC:2637	CP3A4_HUMAN	Reviewed	ENSG00000160868	.	.	.	.	.
Mol00302	Protein	Cytoplasmic polyadenylation element-binding protein 2 (CPEB2)	CPE-BP2; CPE-binding protein 2; hCPEB-2	CPEB2	132864	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000538197.7, CPEB2-208, 7069; ENST00000442003.6, CPEB2-204, 6797; ENST00000382395.8, CPEB2-202, 6786; ENST00000382401.8, CPEB2-203, 6771; ENST00000507071.6, CPEB2-206, 3327; ENST00000345451.8, CPEB2-201, 3237; ENST00000509684.1, CPEB2-207, 635; ENST00000503926.1, CPEB2-205, 467"	MPPPSPDSENGFYPGLPSSMNPAFFPSFSPVSPHGCTGLSVPTSGGGGGGFGGPFSATAVPPPPPPAMNIPQQQPPPPAAPQQPQSRRSPVSPQLQQQHQAAAAAFLQQRNSYNHHQPLLKQSPWSNHQSSGWGTGSMSWGAMHGRDHRRTGNMGIPGTMNQISPLKKPFSGNVIAPPKFTRSTPSLTPKSWIEDNVFRTDNNSNTLLPLQVRSSLQLPAWGSDSLQDSWCTAAGTSRIDQDRSRMYDSLNMHSLENSLIDIMRAEHDPLKGRLSYPHPGTDNLLMLNGRSSLFPIDDGLLDDGHSDQVGVLNSPTCYSAHQNGERIERFSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGDIDKRVEVKPYVLDDQMCDECQGARCGGKFAPFFCANVTCLQYYCEFCWANIHSRAGREFHKPLVKEGADRPRQIHFRWN	chr4:15002481-15070153[+]	"May play a role in translational regulation of stored mRNAs in transcriptionally inactive haploid spermatids. Binds to poly(U) RNA oligomers. Required for cell cycle progression, specifically for the transition from metaphase to anaphase."	.	HGNC:21745	CPEB2_HUMAN	Reviewed	ENSG00000137449	.	.	.	.	.
Mol00303	Protein	Calpain small subunit 1 (CAPNS1)	CSS1; Calcium-activated neutral proteinase small subunit; CANP small subunit; Calcium-dependent protease small subunit; CDPS; Calcium-dependent protease small subunit 1; Calpain regulatory subunit; CAPN4; CAPNS	CAPNS1	826	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000246533.8, CAPNS1-201, 1428; ENST00000588815.5, CAPNS1-206, 1471; ENST00000587718.5, CAPNS1-204, 1558; ENST00000628018.2, CAPNS1-215, 1509; ENST00000628306.2, CAPNS1-216, 1389; ENST00000588780.5, CAPNS1-205, 1035; ENST00000590874.5, CAPNS1-211, 926; ENST00000591041.5, CAPNS1-212, 812; ENST00000629983.2, CAPNS1-217, 799; ENST00000592354.5, CAPNS1-213, 690; ENST00000586851.5, CAPNS1-202, 616; ENST00000589146.5, CAPNS1-207, 578; ENST00000586963.1, CAPNS1-203, 570; ENST00000592483.5, CAPNS1-214, 431; ENST00000590211.5, CAPNS1-210, 403; ENST00000590049.5, CAPNS1-209, 592; ENST00000589162.1, CAPNS1-208, 701"	MFLVNSFLKGGGGGGGGGGGLGGGLGNVLGGLISGAGGGGGGGGGGGGGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRTHYSNIEANESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKRWQAIYKQFDTDRSGTICSSELPGAFEAAGFHLNEHLYNMIIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQEWLQLTMYS	chr19:36139953-36150353[+]	Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development (By similarity).	PDB: 1KFU; PDB: 1KFX; PDB: 4PHJ; PDB: 4PHK; PDB: 4PHM; PDB: 4WQ2; PDB: 4WQ3; PDB: 5D69; PDB: 6QLB	HGNC:1481	CPNS1_HUMAN	Reviewed	ENSG00000126247	.	.	.	.	.
Mol00304	Protein	Protein cereblon (CRBN)	AD-006	CRBN	51185	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000231948.9, CRBN-201, 2187; ENST00000432408.6, CRBN-203, 2203; ENST00000639284.1, CRBN-214, 2223; ENST00000424814.5, CRBN-202, 2038; ENST00000450014.1, CRBN-204, 878; ENST00000491834.5, CRBN-210, 5628; ENST00000488263.5, CRBN-209, 4528; ENST00000498700.5, CRBN-213, 1012; ENST00000459840.5, CRBN-205, 723; ENST00000482844.5, CRBN-208, 653; ENST00000478353.1, CRBN-206, 566; ENST00000480249.5, CRBN-207, 565; ENST00000492178.1, CRBN-211, 500; ENST00000498442.1, CRBN-212, 488"	MAGEGDQQDAAHNMGNHLPLLPAESEEEDEMEVEDQDSKEAKKPNIINFDTSLPTSHTYLGADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTFAVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQAKVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQKRKFHCANLTSWPRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLKIGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETLTVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRSALLPTIPDTEDEISPDKVILCL	chr3:3144628-3179727[-]	"Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large-conductance calcium-activated potassium (BK) channels in excitatory neurons. Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1. May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism."	PDB: 4M91; PDB: 4TZ4; PDB: 5FQD; PDB: 5HXB; PDB: 5V3O; PDB: 6BN7; PDB: 6BN8; PDB: 6BN9; PDB: 6BNB; PDB: 6BOY; PDB: 6H0F; PDB: 6H0G; PDB: 6UML; PDB: 6XK9; PDB: 7BQU; PDB: 7BQV; PDB: 7LPS	HGNC:30185	CRBN_HUMAN	Reviewed	ENSG00000113851	.	.	.	.	.
Mol00305	Protein	Cyclic AMP-responsive element-binding protein 1 (CREB1)	CREB-1; cAMP-responsive element-binding protein 1	CREB1	1385	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000353267.8, CREB1-201, 10095; ENST00000432329.6, CREB1-206, 7650; ENST00000430624.5, CREB1-205, 2005; ENST00000448277.5, CREB1-209, 829; ENST00000455757.1, CREB1-212, 730; ENST00000421139.5, CREB1-204, 713; ENST00000445803.5, CREB1-207, 651; ENST00000414681.1, CREB1-202, 580; ENST00000452474.5, CREB1-211, 518; ENST00000457101.5, CREB1-213, 430; ENST00000418081.5, CREB1-203, 893; ENST00000451164.1, CREB1-210, 813; ENST00000494983.1, CREB1-217, 754; ENST00000480189.5, CREB1-215, 569; ENST00000446449.1, CREB1-208, 265; ENST00000464407.1, CREB1-214, 920; ENST00000494094.5, CREB1-216, 580"	MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD	chr2:207529737-207605988[+]	"Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells."	PDB: 2LXT; PDB: 5ZK1; PDB: 5ZKO	HGNC:2345	CREB1_HUMAN	Reviewed	ENSG00000118260	.	.	.	.	.
Mol00307	Protein	Cysteine-rich motor neuron 1 protein (CRIM1)	CRIM-1; Cysteine-rich repeat-containing protein S52; S52; UNQ1886/PRO4330	CRIM1	51232	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000280527.7, CRIM1-201, 6060; ENST00000413985.1, CRIM1-202, 874; ENST00000428774.1, CRIM1-204, 700; ENST00000426856.1, CRIM1-203, 667; ENST00000473403.5, CRIM1-205, 386; ENST00000477491.5, CRIM1-206, 311; ENST00000497236.1, CRIM1-208, 240; ENST00000481321.1, CRIM1-207, 346"	MYLVAGDRGLAGCGHLLVSLLGLLLLLARSGTRALVCLPCDESKCEEPRNCPGSIVQGVCGCCYTCASQRNESCGGTFGIYGTCDRGLRCVIRPPLNGDSLTEYEAGVCEDENWTDDQLLGFKPCNENLIAGCNIINGKCECNTIRTCSNPFEFPSQDMCLSALKRIEEEKPDCSKARCEVQFSPRCPEDSVLIEGYAPPGECCPLPSRCVCNPAGCLRKVCQPGNLNILVSKASGKPGECCDLYECKPVFGVDCRTVECPPVQQTACPPDSYETQVRLTADGCCTLPTRCECLSGLCGFPVCEVGSTPRIVSRGDGTPGKCCDVFECVNDTKPACVFNNVEYYDGDMFRMDNCRFCRCQGGVAICFTAQCGEINCERYYVPEGECCPVCEDPVYPFNNPAGCYANGLILAHGDRWREDDCTFCQCVNGERHCVATVCGQTCTNPVKVPGECCPVCEEPTIITVDPPACGELSNCTLTGKDCINGFKRDHNGCRTCQCINTEELCSERKQGCTLNCPFGFLTDAQNCEICECRPRPKKCRPIICDKYCPLGLLKNKHGCDICRCKKCPELSCSKICPLGFQQDSHGCLICKCREASASAGPPILSGTCLTVDGHHHKNEESWHDGCRECYCLNGREMCALITCPVPACGNPTIHPGQCCPSCADDFVVQKPELSTPSICHAPGGEYFVEGETWNIDSCTQCTCHSGRVLCETEVCPPLLCQNPSRTQDSCCPQCTDQPFRPSLSRNNSVPNYCKNDEGDIFLAAESWKPDVCTSCICIDSVISCFSESCPSVSCERPVLRKGQCCPYCIEDTIPKKVVCHFSGKAYADEERWDLDSCTHCYCLQGQTLCSTVSCPPLPCVEPINVEGSCCPMCPEMYVPEPTNIPIEKTNHRGEVDLEVPLWPTPSENDIVHLPRDMGHLQVDYRDNRLHPSEDSSLDSIASVVVPIIICLSIIIAFLFINQKKQWIPLLCWYRTPTKPSSLNNQLVSVDCKKGTRVQVDSSQRMLRIAEPDARFSGFYSMQKQNHLQADNFYQTV	chr2:36355778-36551135[+]	May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface.	.	HGNC:2359	CRIM1_HUMAN	Reviewed	ENSG00000150938	.	.	.	.	.
Mol00308	Protein	Macrophage colony-stimulating factor 1 (MCSF)	CSF-1; M-CSF; MCSF; Lanimostim	CSF1	1435	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000329608.11, CSF1-201, 3994; ENST00000369802.7, CSF1-204, 2484; ENST00000369801.1, CSF1-203, 1364; ENST00000420111.6, CSF1-205, 1083; ENST00000488198.5, CSF1-206, 1009; ENST00000357302.8, CSF1-202, 597; ENST00000527192.5, CSF1-209, 577; ENST00000525659.5, CSF1-207, 551; ENST00000526001.1, CSF1-208, 573"	MTAPGAAGRCPPTTWLGSLLLLVCLLASRSITEEVSEYCSHMIGSGHLQSLQRLIDSQMETSCQITFEFVDQEQLKDPVCYLKKAFLLVQDIMEDTMRFRDNTPNAIAIVQLQELSLRLKSCFTKDYEEHDKACVRTFYETPLQLLEKVKNVFNETKNLLDKDWNIFSKNCNNSFAECSSQDVVTKPDCNCLYPKAIPSSDPASVSPHQPLAPSMAPVAGLTWEDSEGTEGSSLLPGEQPLHTVDPGSAKQRPPRSTCQSFEPPETPVVKDSTIGGSPQPRPSVGAFNPGMEDILDSAMGTNWVPEEASGEASEIPVPQGTELSPSRPGGGSMQTEPARPSNFLSASSPLPASAKGQQPADVTGTALPRVGPVRPTGQDWNHTPQKTDHPSALLRDPPEPGSPRISSLRPQGLSNPSTLSAQPQLSRSHSSGSVLPLGELEGRRSTRDRRSPAEPEGGPASEGAARPLPRFNSVPLTDTGHERQSEGSFSPQLQESVFHLLVPSVILVLLAVGGLLFYRWRRRSHQEPQRADSPLEQPEGSPLTQDDRQVELPV	chr1:109910242-109930992[+]	"Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of proinflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance."	PDB: 1HMC; PDB: 3UEZ; PDB: 3UF2; PDB: 4ADF; PDB: 4FA8; PDB: 4WRL; PDB: 4WRM; PDB: 5LXF	HGNC:2432	CSF1_HUMAN	Reviewed	ENSG00000184371	.	.	.	.	.
Mol00309	Protein	C-terminal-binding protein 1 (CTBP1)	CtBP1; CTBP	CTBP1	1487	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000382952.8, CTBP1-203, 2488; ENST00000290921.10, CTBP1-201, 2297; ENST00000510568.1, CTBP1-209, 4250; ENST00000503594.5, CTBP1-204, 1108; ENST00000515399.5, CTBP1-217, 985; ENST00000504092.5, CTBP1-205, 920; ENST00000514210.5, CTBP1-213, 856; ENST00000506180.5, CTBP1-208, 843; ENST00000513420.1, CTBP1-212, 704; ENST00000504784.1, CTBP1-206, 418; ENST00000629223.1, CTBP1-219, 210; ENST00000510739.1, CTBP1-210, 774; ENST00000515690.1, CTBP1-218, 858; ENST00000514669.5, CTBP1-216, 809; ENST00000505826.5, CTBP1-207, 657; ENST00000514495.1, CTBP1-214, 564; ENST00000511907.1, CTBP1-211, 900; ENST00000514596.1, CTBP1-215, 648; ENST00000382950.8, CTBP1-202, 547"	MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL	chr4:1211445-1249953[-]	Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.	PDB: 1MX3; PDB: 4LCE; PDB: 4U6Q; PDB: 4U6S; PDB: 6CDF; PDB: 6CDR; PDB: 6V89; PDB: 6V8A; PDB: 7KWM	HGNC:2494	CTBP1_HUMAN	Reviewed	ENSG00000159692	.	.	.	.	.
Mol00310	Protein	Catenin delta-1 (CTNND1)	Cadherin-associated Src substrate; CAS; p120 catenin; p120(ctn); p120(cas); KIAA0384	CTNND1	1500	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000399050.10, CTNND1-205, 6670; ENST00000524630.5, CTNND1-209, 6553; ENST00000361332.8, CTNND1-202, 6295; ENST00000361391.10, CTNND1-203, 6232; ENST00000361796.9, CTNND1-204, 6226; ENST00000358694.10, CTNND1-201, 6135; ENST00000529526.5, CTNND1-219, 6099; ENST00000532649.5, CTNND1-231, 6026; ENST00000534579.5, CTNND1-236, 6024; ENST00000428599.6, CTNND1-208, 6016; ENST00000532844.5, CTNND1-233, 6012; ENST00000526357.5, CTNND1-212, 5994; ENST00000529873.5, CTNND1-220, 5931; ENST00000530748.5, CTNND1-226, 5925; ENST00000528621.5, CTNND1-218, 5907; ENST00000415361.6, CTNND1-206, 5832; ENST00000530094.5, CTNND1-224, 5814; ENST00000426142.6, CTNND1-207, 5800; ENST00000532787.5, CTNND1-232, 5751; ENST00000532463.5, CTNND1-230, 5749; ENST00000528232.5, CTNND1-217, 5745; ENST00000529986.5, CTNND1-222, 5727; ENST00000532245.5, CTNND1-229, 5655; ENST00000673683.1, CTNND1-238, 5340; ENST00000531007.2, CTNND1-227, 6105; ENST00000674106.1, CTNND1-241, 5363; ENST00000673826.1, CTNND1-239, 5335; ENST00000527467.5, CTNND1-215, 5071; ENST00000531014.5, CTNND1-228, 5053; ENST00000533667.5, CTNND1-235, 4990; ENST00000525902.5, CTNND1-211, 4984; ENST00000526772.5, CTNND1-213, 4966; ENST00000674015.1, CTNND1-240, 4956; ENST00000529919.5, CTNND1-221, 4780; ENST00000683201.1, CTNND1-247, 3555; ENST00000683769.1, CTNND1-249, 3555; ENST00000526938.5, CTNND1-214, 3489; ENST00000530068.5, CTNND1-223, 579; ENST00000533189.1, CTNND1-234, 498; ENST00000682621.1, CTNND1-243, 3669; ENST00000673661.1, CTNND1-237, 4692; ENST00000682974.1, CTNND1-246, 7540; ENST00000682741.1, CTNND1-244, 7000; ENST00000683906.1, CTNND1-250, 6410; ENST00000681984.1, CTNND1-242, 5926; ENST00000684035.1, CTNND1-251, 4374; ENST00000683510.1, CTNND1-248, 3654; ENST00000684704.1, CTNND1-252, 3337; ENST00000525821.2, CTNND1-210, 3262; ENST00000530720.2, CTNND1-225, 3010; ENST00000682814.1, CTNND1-245, 1556; ENST00000527599.1, CTNND1-216, 572"	MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANPLMANGTLTRRHQNGRFVGDADLERQKFSDLKLNGPQDHSHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETSDDGTTRRTETTVKKVVKTVTTRTVQPVAMGPDGLPVDASSVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYSRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPSDQYYWAPLAQHERGSLASLDSLRKGGPPPPNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPVLVGLLDHPKKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEAAPNVANNTGPHAASCFGAKKGKDEWFSRGKKPIEDPANDTVDFPKRTSPARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIADLLTNEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVISILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDKKPDREEIQMSNMGSNTKSLDNNYSTPNERGDHNRTLDRSGDLGDMEPLKGTTPLMQDEGQESLEEELDVLVLDDEGGQVSYPSMQKI	chr11:57753243-57819546[+]	"Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability. Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors."	PDB: 3L6X; PDB: 3L6Y	HGNC:2515	CTND1_HUMAN	Reviewed	ENSG00000198561	.	.	.	.	.
Mol00311	Protein	Cullin-4A (CUL4A)	CUL-4A	CUL4A	8451	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375440.9, CUL4A-202, 5821; ENST00000617546.4, CUL4A-212, 5666; ENST00000375441.7, CUL4A-203, 4037; ENST00000451881.5, CUL4A-204, 3724; ENST00000326335.8, CUL4A-201, 3705; ENST00000488558.2, CUL4A-209, 1111; ENST00000463426.5, CUL4A-205, 893; ENST00000474116.5, CUL4A-208, 866; ENST00000470067.5, CUL4A-206, 794; ENST00000498562.2, CUL4A-211, 790; ENST00000472083.1, CUL4A-207, 574; ENST00000494985.5, CUL4A-210, 292"	MADEAPRKGSFSALVGRTNGLTKPAALAAAPAKPGGAGGSKKLVIKNFRDRPRLPDNYTQDTWRKLHEAVRAVQSSTSIRYNLEELYQAVENLCSHKVSPMLYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNSTLPSIWDMGLELFRTHIISDKMVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQEREVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQALLQHWSEYIKTFGTAIVINPEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINKRPNKPAELIAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQTTLGHAVLKAEFKEGKKEFQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNGEFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLKFPVKPGDLKKRIESLIDRDYMERDKDNPNQYHYVA	chr13:113208193-113267108[+]	"Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of p53/TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(DTL) directs autoubiquitination of DTL. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1. A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes. With CUL4B, contributes to ribosome biogenesis."	PDB: 2HYE; PDB: 4A0K; PDB: 7OKQ; PDB: 7OPC; PDB: 7OPD	HGNC:2554	CUL4A_HUMAN	Reviewed	ENSG00000139842	.	.	.	.	.
Mol00312	Protein	Cullin-4B (CUL4B)	CUL-4B; KIAA0695	CUL4B	8450	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371322.11, CUL4B-202, 5915; ENST00000680673.1, CUL4B-221, 24020; ENST00000681253.1, CUL4B-231, 5960; ENST00000681652.1, CUL4B-235, 5092; ENST00000336592.11, CUL4B-201, 4906; ENST00000679927.1, CUL4B-214, 5899; ENST00000674137.11, CUL4B-210, 5097; ENST00000681206.1, CUL4B-228, 4981; ENST00000681090.1, CUL4B-225, 4857; ENST00000371323.3, CUL4B-203, 4418; ENST00000679844.1, CUL4B-213, 3965; ENST00000404115.8, CUL4B-204, 2902; ENST00000680474.1, CUL4B-219, 2545; ENST00000486604.1, CUL4B-206, 1024; ENST00000680988.1, CUL4B-223, 479; ENST00000681869.1, CUL4B-239, 1969; ENST00000681333.1, CUL4B-233, 7377; ENST00000681189.1, CUL4B-227, 5097; ENST00000681080.1, CUL4B-224, 5081; ENST00000680918.1, CUL4B-222, 4872; ENST00000673919.1, CUL4B-208, 4836; ENST00000679405.1, CUL4B-211, 4599; ENST00000681908.1, CUL4B-240, 4215; ENST00000674073.2, CUL4B-209, 3897; ENST00000679432.1, CUL4B-212, 3234; ENST00000680457.1, CUL4B-218, 4082; ENST00000681706.1, CUL4B-237, 2656; ENST00000681148.1, CUL4B-226, 308; ENST00000680324.1, CUL4B-217, 6206; ENST00000681864.1, CUL4B-238, 5595; ENST00000680577.1, CUL4B-220, 5440; ENST00000680165.1, CUL4B-216, 5430; ENST00000681263.1, CUL4B-232, 3469; ENST00000679965.1, CUL4B-215, 3206; ENST00000681487.1, CUL4B-234, 2310; ENST00000681681.1, CUL4B-236, 1736; ENST00000681236.1, CUL4B-230, 1480; ENST00000497616.2, CUL4B-207, 1059; ENST00000467641.2, CUL4B-205, 1011; ENST00000681224.1, CUL4B-229, 812"	MMSQSSGSGDGNDDEATTSKDGGFSSPSPSAAAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSNSSNEREDFDSTSSSSSTPPLQPRDSASPSTSSFCLGVSVAASSHVPIQKKLRFEDTLEFVGFDAKMAEESSSSSSSSSPTAATSQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA	chrX:120505920-120604074[-]	"Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes. Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8. With CUL4A, contributes to ribosome biogenesis."	PDB: 2DO7; PDB: 4A0C; PDB: 4A0L; PDB: 4A64	HGNC:2555	CUL4B_HUMAN	Reviewed	ENSG00000158290	.	.	.	.	.
Mol00313	Protein	CX3C chemokine receptor 1 (CX3CR1)	C-X3-C CKR-1; CX3CR1; Beta chemokine receptor-like 1; CMK-BRL-1; CMK-BRL1; Fractalkine receptor; G-protein coupled receptor 13; V28; CMKBRL1; GPR13	CX3CR1	1524	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000399220.3, CX3CR1-202, 3106; ENST00000541347.5, CX3CR1-205, 3255; ENST00000542107.5, CX3CR1-206, 3215; ENST00000358309.3, CX3CR1-201, 3151; ENST00000435290.1, CX3CR1-204, 699; ENST00000412814.1, CX3CR1-203, 559"	MDQFPESVTENFEYDDLAEACYIGDIVVFGTVFLSIFYSVIFAIGLVGNLLVVFALTNSKKPKSVTDIYLLNLALSDLLFVATLPFWTHYLINEKGLHNAMCKFTTAFFFIGFFGSIFFITVISIDRYLAIVLAANSMNNRTVQHGVTISLGVWAAAILVAAPQFMFTKQKENECLGDYPEVLQEIWPVLRNVETNFLGFLLPLLIMSYCYFRIIQTLFSCKNHKKAKAIKLILLVVIVFFLFWTPYNVMIFLETLKLYDFFPSCDMRKDLRLALSVTETVAFSHCCLNPLIYAFAGEKFRRYLYHLYGKCLAVLCGRSVHVDFSSSESQRSRHGSVLSSNFTYHTSDGDALLLL	chr3:39263495-39281735[-]	"Receptor for the C-X3-C chemokine fractalkine (CX3CL1) present on many early leukocyte cells; CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. CX3CR1-CX3CL1 signaling mediates cell migratory functions. Responsible for the recruitment of natural killer (NK) cells to inflamed tissues. Acts as a regulator of inflammation process leading to atherogenesis by mediating macrophage and monocyte recruitment to inflamed atherosclerotic plaques, promoting cell survival. Involved in airway inflammation by promoting interleukin 2-producing T helper (Th2) cell survival in inflamed lung. Involved in the migration of circulating monocytes to non-inflamed tissues, where they differentiate into macrophages and dendritic cells. Acts as a negative regulator of angiogenesis, probably by promoting macrophage chemotaxis. Plays a key role in brain microglia by regulating inflammatory response in the central nervous system (CNS) and regulating synapse maturation. Required to restrain the microglial inflammatory response in the CNS and the resulting parenchymal damage in response to pathological stimuli. Involved in brain development by participating in synaptic pruning, a natural process during which brain microglia eliminates extra synapses during postnatal development. Synaptic pruning by microglia is required to promote the maturation of circuit connectivity during brain development. Acts as an important regulator of the gut microbiota by controlling immunity to intestinal bacteria and fungi. Expressed in lamina propria dendritic cells in the small intestine, which form transepithelial dendrites capable of taking up bacteria in order to provide defense against pathogenic bacteria. Required to initiate innate and adaptive immune responses against dissemination of commensal fungi (mycobiota) component of the gut: expressed in mononuclear phagocytes (MNPs) and acts by promoting induction of antifungal IgG antibodies response to confer protection against disseminated C.albicans or C.auris infection. Also acts as a receptor for C-C motif chemokine CCL26, inducing cell chemotaxis."	.	HGNC:2558	CX3C1_HUMAN	Reviewed	ENSG00000168329	.	.	.	.	.
Mol00314	Protein	CXC chemokine receptor type 4 (CXCR4)	.	CXCR4	7852	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000241393.4, CXCR4-201, 1668; ENST00000409817.1, CXCR4-202, 1895; ENST00000696137.1, CXCR4-205, 2170; ENST00000696228.1, CXCR4-207, 1787; ENST00000696152.1, CXCR4-206, 1666; ENST00000696136.1, CXCR4-204, 1638; ENST00000466288.1, CXCR4-203, 1485"	MEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSVSRGSSLKILSKGKRGGHSSVSTESESSSFHSS	chr2:136114349-136119177[-]	"Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Involved in the AKT signaling cascade. Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival."	PDB: 2K03; PDB: 2K04; PDB: 2K05; PDB: 2N55; PDB: 3ODU; PDB: 3OE0; PDB: 3OE6; PDB: 3OE8; PDB: 3OE9; PDB: 4RWS	HGNC:2561	CXCR4_HUMAN	Reviewed	ENSG00000121966	.	.	.	.	.
Mol00315	Protein	Ubiquitin carboxyl-terminal hydrolase CYLD (CYLD)	Deubiquitinating enzyme CYLD; Ubiquitin thioesterase CYLD; Ubiquitin-specific-processing protease CYLD; CYLD1; KIAA0849; HSPC057	CYLD	1540	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000427738.8, CYLD-203, 8540; ENST00000311559.13, CYLD-201, 5371; ENST00000398568.6, CYLD-202, 3536; ENST00000569418.5, CYLD-214, 3513; ENST00000564326.5, CYLD-207, 3259; ENST00000568704.2, CYLD-212, 3292; ENST00000566206.5, CYLD-210, 3104; ENST00000566679.6, CYLD-211, 1158; ENST00000562884.1, CYLD-204, 725; ENST00000564634.5, CYLD-208, 539; ENST00000566024.1, CYLD-209, 409; ENST00000569891.5, CYLD-215, 4665; ENST00000563629.1, CYLD-205, 2568; ENST00000563976.1, CYLD-206, 547; ENST00000568744.1, CYLD-213, 370"	MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKVGETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSPPLQPPPVNSLTTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK	chr16:50742050-50801935[+]	"Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis. Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors. Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation. Negative regulator of Wnt signaling. Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules. Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis. Required for normal cell cycle progress and normal cytokinesis. Inhibits nuclear translocation of NF-kappa-B. Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation. Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells. Negatively regulates TNFRSF11A signaling and osteoclastogenesis. Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation. Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins. Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation. Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1. Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome. Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades."	PDB: 1IXD; PDB: 1WHL; PDB: 1WHM; PDB: 2VHF; PDB: 7OWD	HGNC:2584	CYLD_HUMAN	Reviewed	ENSG00000083799	.	.	.	.	.
Mol00316	Protein	Death-associated protein kinase 2 (DAPK2)	DAP kinase 2; DAP-kinase-related protein 1; DRP-1	DAPK2	23604	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261891.7, DAPK2-201, 2603; ENST00000612884.4, DAPK2-213, 8086; ENST00000457488.5, DAPK2-202, 1741; ENST00000558069.5, DAPK2-205, 1473; ENST00000559306.1, DAPK2-209, 724; ENST00000559007.5, DAPK2-208, 4835; ENST00000558064.1, DAPK2-204, 584; ENST00000561162.5, DAPK2-212, 566; ENST00000558482.5, DAPK2-207, 909; ENST00000559897.1, DAPK2-211, 570; ENST00000559731.5, DAPK2-210, 539; ENST00000557867.1, DAPK2-203, 537; ENST00000558076.1, DAPK2-206, 484"	MFQASMRSPNMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRPDEDLRNCESDTEEDIARRKALHPRRRSSTS	chr15:63907036-64072033[-]	"Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell death signals, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation. Regulates granulocytic motility by controlling cell spreading and polarization."	PDB: 1WMK; PDB: 1WRZ; PDB: 1Z9X; PDB: 1ZUZ; PDB: 1ZWS; PDB: 2A27; PDB: 2A2A; PDB: 2CKE; PDB: 6PAW	HGNC:2675	DAPK2_HUMAN	Reviewed	ENSG00000035664	.	.	.	.	.
Mol00317	Protein	Deoxycytidine kinase (DCK)	dCK; Deoxyadenosine kinase; Deoxyguanosine kinase	DCK	1633	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000286648.10, DCK-201, 2506; ENST00000504952.1, DCK-204, 2614; ENST00000504730.5, DCK-203, 2401; ENST00000509617.1, DCK-205, 428; ENST00000503359.5, DCK-202, 2683; ENST00000509764.1, DCK-206, 183"	MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCNVQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAEKPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQATPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNEDFKDKYESLVEKVKEFLSTL	chr4:70992538-71030914[+]	"Phosphorylates the deoxyribonucleosides deoxycytidine, deoxyguanosine and deoxyadenosine. Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents."	PDB: 1P5Z; PDB: 1P60; PDB: 1P61; PDB: 1P62; PDB: 2A2Z; PDB: 2A30; PDB: 2A7Q; PDB: 2NO0; PDB: 2NO1; PDB: 2NO6; PDB: 2NO7; PDB: 2NO9; PDB: 2NOA; PDB: 2QRN; PDB: 2QRO; PDB: 2ZI3; PDB: 2ZI4; PDB: 2ZI5; PDB: 2ZI6; PDB: 2ZI7; PDB: 2ZI9; PDB: 2ZIA; PDB: 3HP1; PDB: 3IPX; PDB: 3IPY; PDB: 3KFX; PDB: 3MJR; PDB: 3QEJ; PDB: 3QEN; PDB: 3QEO; PDB: 4JLJ; PDB: 4JLK; PDB: 4JLM; PDB: 4JLN; PDB: 4KCG; PDB: 4L5B; PDB: 4Q18; PDB: 4Q19; PDB: 4Q1A; PDB: 4Q1B; PDB: 4Q1C; PDB: 4Q1D; PDB: 4Q1E; PDB: 4Q1F; PDB: 5MQJ; PDB: 5MQL; PDB: 5MQT	HGNC:2704	DCK_HUMAN	Reviewed	ENSG00000156136	.	.	.	.	.
Mol00319	Protein	Serine/threonine-protein kinase DCLK1 (DCLK1)	Doublecortin domain-containing protein 3A; Doublecortin-like and CAM kinase-like 1; Doublecortin-like kinase 1; DCAMKL1; DCDC3A; KIAA0369	DCLK1	9201	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000360631.8, DCLK1-202, 8394; ENST00000615680.4, DCLK1-208, 7592; ENST00000255448.8, DCLK1-201, 5703; ENST00000379893.5, DCLK1-204, 4612; ENST00000379892.4, DCLK1-203, 2101; ENST00000460982.1, DCLK1-205, 5247; ENST00000486239.1, DCLK1-207, 578; ENST00000477664.1, DCLK1-206, 542"	MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGSPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASSSRRSTTKSPGPSRRSKSPASTSSVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRSSQHGGSSTSLASTKVCSSMDENDGPGEEVSEEGFQIPATITERYKVGRTIGDGNFAVVKECVERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELITMMLLVDVDQRFSAVQVLEHPWVNDDGLPENEHQLSVAGKIKKHFNTGPKPNSTAAGVSVIATTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNSPF	chr13:35768652-36131382[-]	Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.	PDB: 1MFW; PDB: 1MG4; PDB: 1UF0; PDB: 5JZJ; PDB: 5JZN; PDB: 6KYQ; PDB: 6KYR; PDB: 7F3G; PDB: 7KX6; PDB: 7KX8; PDB: 7KXW	HGNC:2700	DCLK1_HUMAN	Reviewed	ENSG00000133083	.	.	.	.	.
Mol00320	Protein	m7GpppN-mRNA hydrolase (DCP2)	Nucleoside diphosphate-linked moiety X motif 20; Nudix motif 20; mRNA-decapping enzyme 2; hDpc; NUDT20	DCP2	167227	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000389063.3, DCP2-201, 10110; ENST00000515408.5, DCP2-208, 8029; ENST00000513585.6, DCP2-207, 1572; ENST00000674880.1, DCP2-209, 4679; ENST00000502635.2, DCP2-202, 1302; ENST00000504961.1, DCP2-203, 852; ENST00000512751.5, DCP2-206, 570; ENST00000508359.1, DCP2-204, 838; ENST00000510046.1, DCP2-205, 369"	METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKPYNNHSEMSDLLKGKNQSMRGNGRKQYQDSPNQKKRTNGLQPAKQQNSLMKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAEGQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL	chr5:112976702-113022195[+]	"Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Plays a role in replication-dependent histone mRNA degradation. Has higher activity towards mRNAs that lack a poly(A) tail. Has no activity towards a cap structure lacking an RNA moiety. The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping. Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts."	PDB: 5MP0; PDB: 5QOH; PDB: 5QOI; PDB: 5QOJ; PDB: 5QOK; PDB: 5QOL; PDB: 5QOM; PDB: 5QON; PDB: 5QOO; PDB: 5QOP; PDB: 5QOQ; PDB: 5QOR; PDB: 5QOS; PDB: 5QOT; PDB: 5QOU; PDB: 5QOV; PDB: 5QOW; PDB: 5QOX; PDB: 5QOY; PDB: 5QOZ; PDB: 5QP0; PDB: 5QP1; PDB: 5QP2; PDB: 5QP3; PDB: 5QP4; PDB: 5QP5; PDB: 5QP6; PDB: 5QP7; PDB: 5QP8; PDB: 5QP9; PDB: 5QPA; PDB: 5QPB; PDB: 5QPC	HGNC:24452	DCP2_HUMAN	Reviewed	ENSG00000172795	.	.	.	.	.
Mol00321	Protein	DNA damage-binding protein 1 (DDB1)	DDB p127 subunit; DNA damage-binding protein a; DDBa; Damage-specific DNA-binding protein 1; HBV X-associated protein 1; XAP-1; UV-damaged DNA-binding factor; UV-damaged DNA-binding protein 1; UV-DDB 1; XPE-binding factor; XPE-BF; Xeroderma pigmentosum group E-complementing protein; XPCe; XAP1	DDB1	1642	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000301764.12, DDB1-201, 4245; ENST00000680367.1, DDB1-233, 4426; ENST00000681803.1, DDB1-243, 4348; ENST00000679588.1, DDB1-225, 4184; ENST00000681935.1, DDB1-245, 4138; ENST00000679712.1, DDB1-226, 4033; ENST00000680602.1, DDB1-235, 4001; ENST00000680075.1, DDB1-228, 3981; ENST00000680717.1, DDB1-236, 3937; ENST00000539426.5, DDB1-214, 805; ENST00000543658.5, DDB1-222, 571; ENST00000542337.5, DDB1-220, 558; ENST00000535283.6, DDB1-206, 4920; ENST00000680357.1, DDB1-232, 4363; ENST00000681188.1, DDB1-240, 4329; ENST00000540166.5, DDB1-217, 3906; ENST00000545930.5, DDB1-224, 1278; ENST00000538280.1, DDB1-211, 227; ENST00000680250.1, DDB1-230, 4459; ENST00000680881.1, DDB1-237, 4335; ENST00000681067.1, DDB1-239, 4180; ENST00000679855.1, DDB1-227, 3902; ENST00000680959.1, DDB1-238, 3114; ENST00000680452.1, DDB1-234, 3110; ENST00000681368.1, DDB1-241, 3088; ENST00000680096.1, DDB1-229, 2873; ENST00000535147.5, DDB1-204, 2789; ENST00000680345.1, DDB1-231, 2623; ENST00000543162.2, DDB1-221, 2592; ENST00000545894.1, DDB1-223, 2282; ENST00000681815.1, DDB1-244, 2205; ENST00000414411.3, DDB1-202, 1904; ENST00000539332.2, DDB1-213, 1767; ENST00000681580.1, DDB1-242, 1629; ENST00000539739.5, DDB1-216, 1624; ENST00000535967.5, DDB1-207, 1404; ENST00000537877.5, DDB1-209, 1375; ENST00000451943.6, DDB1-203, 1224; ENST00000537120.5, DDB1-208, 1215; ENST00000540784.5, DDB1-218, 1119; ENST00000539712.5, DDB1-215, 1020; ENST00000541513.2, DDB1-219, 958; ENST00000535174.5, DDB1-205, 896; ENST00000538470.2, DDB1-212, 858; ENST00000538129.1, DDB1-210, 475"	MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLEIYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGIIGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLEELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYHNGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSDPNRETDDTLVLSFVGQTRVLMLNGEEVEETELMGFVDDQQTFFCGNVAHQQLIQITSASVRLVSQEPKALVSEWKEPQAKNISVASCNSSQVVVAVGRALYYLQIHPQELRQISHTEMEHEVACLDITPLGDSNGLSPLCAIGLWTDISARILKLPSFELLHKEMLGGEIIPRSILMTTFESSHYLLCALGDGALFYFGLNIETGLLSDRKKVTLGTQPTVLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSDGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPSASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIIDQHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAMVYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLKTKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMSAVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEVGLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNGMIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRSFHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYDDGSGMKREATADDLIKVVEELTRIH	chr11:61299451-61342596[-]	"Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively. Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1. DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver."	PDB: 2B5L; PDB: 2B5M; PDB: 2B5N; PDB: 2HYE; PDB: 3E0C; PDB: 3EI1; PDB: 3EI2; PDB: 3EI3; PDB: 3EI4; PDB: 3I7H; PDB: 3I7K; PDB: 3I7L; PDB: 3I7N; PDB: 3I7O; PDB: 3I7P; PDB: 3I89; PDB: 3I8C; PDB: 3I8E; PDB: 4A08; PDB: 4A09; PDB: 4A0A; PDB: 4A0B; PDB: 4A0K; PDB: 4A0L; PDB: 4A11; PDB: 4CI1; PDB: 4CI2; PDB: 4CI3; PDB: 4E54; PDB: 4E5Z; PDB: 4TZ4; PDB: 5FQD; PDB: 5HXB; PDB: 5JK7; PDB: 5V3O; PDB: 6BN7; PDB: 6BN8; PDB: 6BN9; PDB: 6BNB; PDB: 6BOY; PDB: 6DSZ; PDB: 6FCV; PDB: 6H0F; PDB: 6H0G; PDB: 6PAI; PDB: 6Q0R; PDB: 6Q0V; PDB: 6Q0W; PDB: 6R8Y; PDB: 6R8Z; PDB: 6R90; PDB: 6R91; PDB: 6R92; PDB: 6SJ7; PDB: 6TD3; PDB: 6UD7; PDB: 6UE5; PDB: 6UML; PDB: 6XK9; PDB: 6ZUE; PDB: 6ZX9; PDB: 7LPS; PDB: 7OKQ; PDB: 7OO3; PDB: 7OOB; PDB: 7OOP; PDB: 7OPC; PDB: 7OPD	HGNC:2717	DDB1_HUMAN	Reviewed	ENSG00000167986	.	.	.	.	.
Mol00322	Protein	DNA damage-inducible transcript 3 (DDIT3)	DDIT-3; C/EBP zeta; C/EBP-homologous protein; CHOP; C/EBP-homologous protein 10; CHOP-10; CCAAT/enhancer-binding protein homologous protein; Growth arrest and DNA damage-inducible protein GADD153; CHOP; CHOP10; GADD153	DDIT3	1649	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000346473.8, DDIT3-201, 903; ENST00000551116.5, DDIT3-204, 1067; ENST00000552740.5, DDIT3-205, 951; ENST00000623876.2, DDIT3-206, 940; ENST00000547303.5, DDIT3-202, 872; ENST00000547526.1, DDIT3-203, 644"	MAAESLPFSFGTLSSWELEAWYEDLQEVLSSDENGGTYVSPPGNEEEESKIFTTLDPASLAWLTEEEPEPAEVTSTSQSPHSPDSSQSSLAQEEEEEDQGRTRKRKQSGHSPARAGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVEATRRALIDRMVNLHQA	chr12:57516588-57521737[-]	"Multifunctional transcription factor in endoplasmic reticulum (ER) stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Together with ATF4, mediates ER-mediated cell death by promoting expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the unfolded protein response (UPR) in response to ER stress. Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response. Acts as a major regulator of postnatal neovascularization through regulation of endothelial nitric oxide synthase (NOS3)-related signaling."	.	HGNC:2726	DDIT3_HUMAN	Reviewed	ENSG00000175197	.	.	.	.	.
Mol00323	Protein	Epithelial discoidin domain-containing receptor 1 (DDR1)	.	DDR1	780	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000376568.8, DDR1-225, 3836; ENST00000324771.12, DDR1-223, 4148; ENST00000454612.6, DDR1-240, 3942; ENST00000452441.5, DDR1-239, 3857; ENST00000376567.6, DDR1-224, 3832; ENST00000376570.8, DDR1-227, 3820; ENST00000376569.7, DDR1-226, 3783; ENST00000418800.6, DDR1-232, 3588; ENST00000446312.5, DDR1-238, 3202; ENST00000508312.5, DDR1-262, 3073; ENST00000513240.5, DDR1-271, 2882; ENST00000417521.5, DDR1-231, 1479; ENST00000428153.6, DDR1-235, 1257; ENST00000460944.6, DDR1-241, 1248; ENST00000484556.1, DDR1-245, 1038; ENST00000515881.5, DDR1-280, 956; ENST00000421124.6, DDR1-233, 800; ENST00000376575.7, DDR1-228, 732; ENST00000396342.6, DDR1-229, 675; ENST00000505534.5, DDR1-257, 673; ENST00000503495.5, DDR1-249, 636; ENST00000512694.5, DDR1-268, 623; ENST00000509639.5, DDR1-265, 615; ENST00000513043.5, DDR1-270, 604; ENST00000437124.6, DDR1-237, 587; ENST00000424544.2, DDR1-234, 587; ENST00000515233.5, DDR1-278, 580; ENST00000502955.5, DDR1-247, 574; ENST00000507046.5, DDR1-259, 573; ENST00000512336.5, DDR1-267, 572; ENST00000503670.5, DDR1-251, 572; ENST00000504651.5, DDR1-253, 571; ENST00000507901.5, DDR1-261, 562; ENST00000505066.5, DDR1-256, 556; ENST00000511510.5, DDR1-266, 547; ENST00000504927.5, DDR1-255, 542; ENST00000512725.5, DDR1-269, 539; ENST00000508317.5, DDR1-263, 538; ENST00000503180.5, DDR1-248, 527; ENST00000514434.1, DDR1-275, 514; ENST00000412274.6, DDR1-230, 496; ENST00000515219.5, DDR1-277, 481; ENST00000504679.5, DDR1-254, 460; ENST00000482873.6, DDR1-244, 2673; ENST00000513749.5, DDR1-274, 584; ENST00000503628.5, DDR1-250, 570; ENST00000508472.5, DDR1-264, 836; ENST00000506573.1, DDR1-258, 585; ENST00000515529.4, DDR1-279, 340; ENST00000465966.4, DDR1-242, 268; ENST00000482050.1, DDR1-243, 246; ENST00000513514.2, DDR1-273, 186; ENST00000431373.1, DDR1-236, 886; ENST00000504152.5, DDR1-252, 695; ENST00000514534.1, DDR1-276, 566; ENST00000513243.5, DDR1-272, 549; ENST00000507533.1, DDR1-260, 545; ENST00000485023.1, DDR1-246, 515"	MGPEALSSLLLLLLVASGDADMKGHFDPAKCRYALGMQDRTIPDSDISASSSWSDSTAARHSRLESSDGDGAWCPAGSVFPKEEEYLQVDLQRLHLVALVGTQGRHAGGLGKEFSRSYRLRYSRDGRRWMGWKDRWGQEVISGNEDPEGVVLKDLGPPMVARLVRFYPRADRVMSVCLRVELYGCLWRDGLLSYTAPVGQTMYLSEAVYLNDSTYDGHTVGGLQYGGLGQLADGVVGLDDFRKSQELRVWPGYDYVGWSNHSFSSGYVEMEFEFDRLRAFQAMQVHCNNMHTLGARLPGGVECRFRRGPAMAWEGEPMRHNLGGNLGDPRARAVSVPLGGRVARFLQCRFLFAGPWLLFSEISFISDVVNNSSPALGGTFPPAPWWPPGPPPTNFSSLELEPRGQQPVAKAEGSPTAILIGCLVAIILLLLLIIALMLWRLHWRRLLSKAERRVLEEELTVHLSVPGDTILINNRPGPREPPPYQEPRPRGNPPHSAPCVPNGSALLLSNPAYRLLLATYARPPRGPGPPTPAWAKPTNTQAYSGDYMEPEKPGAPLLPPPPQNSVPHYAEADIVTLQGVTGGNTYAVPALPPGAVGDGPPRVDFPRSRLRFKEKLGEGQFGEVHLCEVDSPQDLVSLDFPLNVRKGHPLLVAVKILRPDATKNARNDFLKEVKIMSRLKDPNIIRLLGVCVQDDPLCMITDYMENGDLNQFLSAHQLEDKAAEGAPGDGQAAQGPTISYPMLLHVAAQIASGMRYLATLNFVHRDLATRNCLVGENFTIKIADFGMSRNLYAGDYYRVQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEVLMLCRAQPFGQLTDEQVIENAGEFFRDQGRQVYLSRPPACPQGLYELMLRCWSRESEQRPPFSQLHRFLAEDALNTV	chr6:30876421-30900156[+]	"Tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing (By similarity). Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11."	PDB: 3ZOS; PDB: 4AG4; PDB: 4BKJ; PDB: 4CKR; PDB: 5BVK; PDB: 5BVN; PDB: 5BVO; PDB: 5BVW; PDB: 5FDP; PDB: 5FDX; PDB: 6BRJ; PDB: 6BSD; PDB: 6FEW; PDB: 6FEX; PDB: 6FIL; PDB: 6FIN; PDB: 6FIO; PDB: 6FIQ; PDB: 6GWR; PDB: 6HP9; PDB: 6Y23; PDB: 7BCM; PDB: 7BE6	HGNC:2730	DDR1_HUMAN	Reviewed	ENSG00000204580	.	.	.	.	.
Mol00324	Protein	Death effector domain-containing protein (DEDD)	DEDPro1; Death effector domain-containing testicular molecule; FLDED-1; DEDPRO1; DEFT; KE05	DEDD	9191	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368006.8, DEDD-202, 2344; ENST00000545495.5, DEDD-212, 2329; ENST00000458050.6, DEDD-203, 2300; ENST00000490843.6, DEDD-210, 1527; ENST00000368005.5, DEDD-201, 1256; ENST00000464113.1, DEDD-205, 964; ENST00000489249.5, DEDD-209, 1116; ENST00000486041.5, DEDD-208, 1068; ENST00000463227.5, DEDD-204, 954; ENST00000496632.1, DEDD-211, 875; ENST00000473679.6, DEDD-207, 869; ENST00000472996.1, DEDD-206, 314"	MAGLKRRASQVWPEEHGEQEHGLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKRRRAVCPDLVDKYLEETSIRYVTPRALSDPEPRPPQPSKTVPPHYPVVCCPTSGPQMCSKRPARGRATLGSQRKRRKSVTPDPKEKQTCDIRLRVRAEYCQHETALQGNVFSNKQDPLERQFERFNQANTILKSRDLGSIICDIKFSELTYLDAFWRDYINGSLLEALKGVFITDSLKQAVGHEAIKLLVNVDEEDYELGRQKLLRNLMLQALP	chr1:161120974-161132688[-]	A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. Inhibits DNA transcription in vitro (By similarity).	.	HGNC:2755	DEDD_HUMAN	Reviewed	ENSG00000158796	.	.	.	.	.
Mol00325	Protein	Endoribonuclease Dicer (DICER1)	Helicase with RNase motif; Helicase MOI; DICER; HERNA; KIAA0928	DICER1	23405	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000343455.8, DICER1-201, 10384; ENST00000674628.2, DICER1-215, 10483; ENST00000531162.7, DICER1-209, 10453; ENST00000529720.2, DICER1-208, 10374; ENST00000526495.6, DICER1-203, 10315; ENST00000393063.6, DICER1-202, 7423; ENST00000527414.5, DICER1-204, 6179; ENST00000541352.5, DICER1-211, 5621; ENST00000696733.1, DICER1-218, 10006; ENST00000696736.1, DICER1-221, 6509; ENST00000532939.3, DICER1-210, 5989; ENST00000696737.1, DICER1-222, 5815; ENST00000696739.1, DICER1-224, 2025; ENST00000696740.1, DICER1-225, 1188; ENST00000675540.2, DICER1-216, 10356; ENST00000696734.1, DICER1-219, 10081; ENST00000675995.1, DICER1-217, 7157; ENST00000556045.6, DICER1-213, 6161; ENST00000696738.1, DICER1-223, 1967; ENST00000527416.2, DICER1-205, 691; ENST00000696735.1, DICER1-220, 2822; ENST00000529206.1, DICER1-207, 1286; ENST00000554367.1, DICER1-212, 897; ENST00000527554.2, DICER1-206, 665; ENST00000556681.1, DICER1-214, 310"	MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS	chr14:95086228-95158010[-]	"Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes."	PDB: 2EB1; PDB: 4NGB; PDB: 4NGC; PDB: 4NGD; PDB: 4NGF; PDB: 4NGG; PDB: 4NH3; PDB: 4NH5; PDB: 4NH6; PDB: 4NHA; PDB: 4WYQ; PDB: 5ZAK; PDB: 5ZAL; PDB: 5ZAM	HGNC:17098	DICER_HUMAN	Reviewed	ENSG00000100697	.	.	.	.	.
Mol00326	Protein	Dickkopf-related protein 1 (DKK1)	Dickkopf-1; Dkk-1; hDkk-1; SK; UNQ492/PRO1008	DKK1	22943	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373970.4, DKK1-201, 1805; ENST00000467359.5, DKK1-202, 547; ENST00000476752.1, DKK1-203, 544; ENST00000494277.5, DKK1-204, 465"	MMALGAAGATRVFVAMVAAALGGHPLLGVSATLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQPYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGNYCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHTKGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGLEIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH	chr10:52314281-52318042[+]	"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity."	PDB: 3S2K; PDB: 3S8V; PDB: 3SOQ; PDB: 5FWW; PDB: 5GJE	HGNC:2891	DKK1_HUMAN	Reviewed	ENSG00000107984	.	.	.	.	.
Mol00327	Protein	Dickkopf-related protein 2 (DKK2)	Dickkopf-2; Dkk-2; hDkk-2; UNQ682/PRO1316	DKK2	27123	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000285311.8, DKK2-201, 3654; ENST00000513208.5, DKK2-204, 925; ENST00000510463.1, DKK2-202, 908; ENST00000510534.1, DKK2-203, 1474"	MAALMRSKDSSCCLLLLAAVLMVESSQIGSSRAKLNSIKSSLGGETPGQAANRSAGMYQGLAFGGSKKGKNLGQAYPCSSDKECEVGRYCHSPHQGSSACMVCRRKKKRCHRDGMCCPSTRCNNGICIPVTESILTPHIPALDGTRHRDRNHGHYSNHDLGWQNLGRPHTKMSHIKGHEGDPCLRSSDCIEGFCCARHFWTKICKPVLHQGEVCTKQRKKGSHGLEIFQRCDCAKGLSCKVWKDATYSSKARLHVCQKI	chr4:106921802-107283806[-]	"Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity)."	.	HGNC:2892	DKK2_HUMAN	Reviewed	ENSG00000155011	.	.	.	.	.
Mol00328	Protein	DNA (cytosine-5)-methyltransferase 3A (DNMT3A)	Dnmt3a; Cysteine methyltransferase DNMT3A; DNA methyltransferase HsaIIIA; DNA MTase HsaIIIA; M.HsaIIIA	DNMT3A	1788	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000321117.10, DNMT3A-202, 9421; ENST00000264709.7, DNMT3A-201, 9501; ENST00000380746.8, DNMT3A-203, 3589; ENST00000406659.3, DNMT3A-206, 1775; ENST00000683760.1, DNMT3A-217, 3585; ENST00000402667.1, DNMT3A-205, 2300; ENST00000470983.5, DNMT3A-209, 589; ENST00000380756.7, DNMT3A-204, 4477; ENST00000683393.1, DNMT3A-216, 3149; ENST00000474887.6, DNMT3A-211, 988; ENST00000461228.1, DNMT3A-207, 581; ENST00000482935.5, DNMT3A-212, 519; ENST00000491288.5, DNMT3A-214, 472; ENST00000682842.1, DNMT3A-215, 1802; ENST00000474807.5, DNMT3A-210, 840; ENST00000466601.5, DNMT3A-208, 812; ENST00000484184.1, DNMT3A-213, 619"	MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEASPPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV	chr2:25227855-25342590[-]	Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. Also has weak auto-methylation activity on Cys-710 in absence of DNA.	PDB: 2QRV; PDB: 3A1A; PDB: 3A1B; PDB: 3LLR; PDB: 3SVM; PDB: 4QBQ; PDB: 4QBR; PDB: 4QBS; PDB: 4U7P; PDB: 4U7T; PDB: 5YX2; PDB: 6BRR; PDB: 6F57; PDB: 6PA7; PDB: 6W89; PDB: 6W8B; PDB: 6W8D; PDB: 6W8J	HGNC:2978	DNM3A_HUMAN	Reviewed	ENSG00000119772	.	.	.	.	.
Mol00329	Protein	DNA (cytosine-5)-methyltransferase 3B (DNMT3B)	Dnmt3b; DNA methyltransferase HsaIIIB; DNA MTase HsaIIIB; M.HsaIIIB	DNMT3B	1789	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000328111.6, DNMT3B-202, 4336; ENST00000201963.3, DNMT3B-201, 4255; ENST00000353855.6, DNMT3B-204, 4237; ENST00000348286.6, DNMT3B-203, 4048; ENST00000443239.7, DNMT3B-205, 2674; ENST00000456297.6, DNMT3B-206, 2315; ENST00000696232.1, DNMT3B-208, 4150; ENST00000696239.1, DNMT3B-215, 2343; ENST00000696231.1, DNMT3B-207, 4369; ENST00000696233.1, DNMT3B-209, 4271; ENST00000696238.1, DNMT3B-214, 4165; ENST00000696235.1, DNMT3B-211, 1709; ENST00000696236.1, DNMT3B-212, 1512; ENST00000696245.1, DNMT3B-221, 2039; ENST00000696237.1, DNMT3B-213, 766; ENST00000696234.1, DNMT3B-210, 1542; ENST00000696244.1, DNMT3B-220, 826; ENST00000696243.1, DNMT3B-219, 722; ENST00000696242.1, DNMT3B-218, 706; ENST00000696241.1, DNMT3B-217, 701; ENST00000696240.1, DNMT3B-216, 588"	MKGDTRHLNGEEDAGGREDSILVNGACSDQSSDSPPILEAIRTPEIRGRRSSSRLSKREVSSLLSYTQDLTGDGDGEDGDGSDTPVMPKLFRETRTRSESPAVRTRNNNSVSSRERHRPSPRSTRGRQGRNHVDESPVEFPATRSLRRRATASAGTPWPSPPSSYLTIDLTDDTEDTHGTPQSSSTPYARLAQDSQQGGMESPQVEADSGDGDSSEYQDGKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMSGMRWVQWFGDGKFSEVSADKLVALGLFSQHFNLATFNKLVSYRKAMYHALEKARVRAGKTFPSSPGDSLEDQLKPMLEWAHGGFKPTGIEGLKPNNTQPVVNKSKVRRAGSRKLESRKYENKTRRRTADDSATSDYCPAPKRLKTNCYNNGKDRGDEDQSREQMASDVANNKSSLEDGCLSCGRKNPVSFHPLFEGGLCQTCRDRFLELFYMYDDDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGTGTAAEAKLQEPWSCYMCLPQRCHGVLRRRKDWNVRLQAFFTSDTGLEYEAPKLYPAIPAARRRPIRVLSLFDGIATGYLVLKELGIKVGKYVASEVCEESIAVGTVKHEGNIKYVNDVRNITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYSRPKEGDDRPFFWMFENVVAMKVGDKRDISRFLECNPVMIDAIKVSAAHRARYFWGNLPGMNRPVIASKNDKLELQDCLEYNRIAKLKKVQTITTKSNSIKQGKNQLFPVVMNGKEDVLWCTELERIFGFPVHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE	chr20:32762385-32809359[+]	"Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Functions as a transcriptional corepressor by associating with ZHX1. Required for DUX4 silencing in somatic cells."	PDB: 3FLG; PDB: 3QKJ; PDB: 5CIU; PDB: 5NR3; PDB: 5NRR; PDB: 5NRS; PDB: 5NRV; PDB: 5NV0; PDB: 5NV2; PDB: 5NV7; PDB: 5NVO; PDB: 6KDA; PDB: 6KDB; PDB: 6KDL; PDB: 6KDP; PDB: 6KDT; PDB: 6PA7; PDB: 6R3E; PDB: 6U8P; PDB: 6U8V; PDB: 6U8W; PDB: 6U8X; PDB: 6U90; PDB: 6U91	HGNC:2979	DNM3B_HUMAN	Reviewed	ENSG00000088305	.	.	.	.	.
Mol00330	Protein	DNA polymerase theta (POLQ)	DNA polymerase eta; POLH	POLQ	10721	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264233.6, POLQ-201, 8757; ENST00000683498.1, POLQ-204, 501; ENST00000488282.1, POLQ-203, 839; ENST00000474243.1, POLQ-202, 613"	MNLLRRSGKRRRSESGSDSFSGSGGDSSASPQFLSGSVLSPPPGLGRCLKAAAAGECKPTVPDYERDKLLLANWGLPKAVLEKYHSFGVKKMFEWQAECLLLGQVLEGKNLVYSAPTSAGKTLVAELLILKRVLEMRKKALFILPFVSVAKEKKYYLQSLFQEVGIKVDGYMGSTSPSRHFSSLDIAVCTIERANGLINRLIEENKMDLLGMVVVDELHMLGDSHRGYLLELLLTKICYITRKSASCQADLASSLSNAVQIVGMSATLPNLELVASWLNAELYHTDFRPVPLLESVKVGNSIYDSSMKLVREFEPMLQVKGDEDHVVSLCYETICDNHSVLLFCPSKKWCEKLADIIAREFYNLHHQAEGLVKPSECPPVILEQKELLEVMDQLRRLPSGLDSVLQKTVPWGVAFHHAGLTFEERDIIEGAFRQGLIRVLAATSTLSSGVNLPARRVIIRTPIFGGRPLDILTYKQMVGRAGRKGVDTVGESILICKNSEKSKGIALLQGSLKPVRSCLQRREGEEVTGSMIRAILEIIVGGVASTSQDMHTYAACTFLAASMKEGKQGIQRNQESVQLGAIEACVMWLLENEFIQSTEASDGTEGKVYHPTHLGSATLSSSLSPADTLDIFADLQRAMKGFVLENDLHILYLVTPMFEDWTTIDWYRFFCLWEKLPTSMKRVAELVGVEEGFLARCVKGKVVARTERQHRQMAIHKRFFTSLVLLDLISEVPLREINQKYGCNRGQIQSLQQSAAVYAGMITVFSNRLGWHNMELLLSQFQKRLTFGIQRELCDLVRVSLLNAQRARVLYASGFHTVADLARANIVEVEVILKNAVPFKSARKAVDEEEEAVEERRNMRTIWVTGRKGLTEREAAALIVEEARMILQQDLVEMGVQWNPCALLHSSTCSLTHSESEVKEHTFISQTKSSYKKLTSKNKSNTIFSDSYIKHSPNIVQDLNKSREHTSSFNCNFQNGNQEHQTCSIFRARKRASLDINKEKPGASQNEGKTSDKKVVQTFSQKTKKAPLNFNSEKMSRSFRSWKRRKHLKRSRDSSPLKDSGACRIHLQGQTLSNPSLCEDPFTLDEKKTEFRNSGPFAKNVSLSGKEKDNKTSFPLQIKQNCSWNITLTNDNFVEHIVTGSQSKNVTCQATSVVSEKGRGVAVEAEKINEVLIQNGSKNQNVYMKHHDIHPINQYLRKQSHEQTSTITKQKNIIERQMPCEAVSSYINRDSNVTINCERIKLNTEENKPSHFQALGDDISRTVIPSEVLPSAGAFSKSEGQHENFLNISRLQEKTGTYTTNKTKNNHVSDLGLVLCDFEDSFYLDTQSEKIIQQMATENAKLGAKDTNLAAGIMQKSLVQQNSMNSFQKECHIPFPAEQHPLGATKIDHLDLKTVGTMKQSSDSHGVDILTPESPIFHSPILLEENGLFLKKNEVSVTDSQLNSFLQGYQTQETVKPVILLIPQKRTPTGVEGECLPVPETSLNMSDSLLFDSFSDDYLVKEQLPDMQMKEPLPSEVTSNHFSDSLCLQEDLIKKSNVNENQDTHQQLTCSNDESIIFSEMDSVQMVEALDNVDIFPVQEKNHTVVSPRALELSDPVLDEHHQGDQDGGDQDERAEKSKLTGTRQNHSFIWSGASFDLSPGLQRILDKVSSPLENEKLKSMTINFSSLNRKNTELNEEQEVISNLETKQVQGISFSSNNEVKSKIEMLENNANHDETSSLLPRKESNIVDDNGLIPPTPIPTSASKLTFPGILETPVNPWKTNNVLQPGESYLFGSPSDIKNHDLSPGSRNGFKDNSPISDTSFSLQLSQDGLQLTPASSSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV	chr3:121431431-121545988[-]	"DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA. MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation. POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends. POLQ-mediated MMEJ may be required to promote the survival of cells with a compromised HR repair pathway, thereby preventing genomic havoc by resolving unrepaired lesions. The polymerase acts by binding directly the 2 ends of resected double-strand breaks, allowing microhomologous sequences in the overhangs to form base pairs. It then extends each strand from the base-paired region using the opposing overhang as a template. Requires partially resected DNA containing 2 to 6 base pairs of microhomology to perform MMEJ. The polymerase activity is highly promiscuous: unlike most polymerases, promotes extension of ssDNA and partial ssDNA (pssDNA) substrates. Also exhibits low-fidelity DNA synthesis, translesion synthesis and lyase activity, and it is implicated in interstrand-cross-link repair, base excision repair and DNA end-joining. Involved in somatic hypermutation of immunoglobulin genes, a process that requires the activity of DNA polymerases to ultimately introduce mutations at both A/T and C/G base pairs."	PDB: 4X0P; PDB: 4X0Q; PDB: 5A9F; PDB: 5A9J; PDB: 5AGA	HGNC:9186	DPOLQ_HUMAN	Reviewed	ENSG00000051341	.	.	.	.	.
Mol00331	Protein	Dihydropyrimidine dehydrogenase [NADP(+)]	DHPDHase; DPD; Dihydrothymine dehydrogenase; Dihydrouracil dehydrogenase	DPYD	1806	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000370192.8, DPYD-202, 4423; ENST00000306031.5, DPYD-201, 1779; ENST00000646851.1, DPYD-205, 799; ENST00000460019.1, DPYD-203, 551; ENST00000474241.1, DPYD-204, 1036"	MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQDQGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQNVAFSPLKRNCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLSVNPVC	chr1:97077743-97995000[-]	Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.	.	HGNC:3012	DPYD_HUMAN	Reviewed	ENSG00000188641	.	.	.	.	.
Mol00332	Protein	Dual specificity protein phosphatase 1 (DUSP1)	Dual specificity protein phosphatase hVH1; Mitogen-activated protein kinase phosphatase 1; MAP kinase phosphatase 1; MKP-1; Protein-tyrosine phosphatase CL100; CL100; MKP1; PTPN10; VH1	DUSP1	1843	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000239223.4, DUSP1-201, 2013"	MVMEVGTLDAGGLRALLGERAAQCLLLDCRSFFAFNAGHIAGSVNVRFSTIVRRRAKGAMGLEHIVPNAELRGRLLAGAYHAVVLLDERSAALDGAKRDGTLALAAGALCREARAAQVFFLKGGYEAFSASCPELCSKQSTPMGLSLPLSTSVPDSAESGCSSCSTPLYDQGGPVEILPFLYLGSAYHASRKDMLDALGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSIKNAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPHCSAEAGSPAMAVLDRGTSTTTVFNFPVSIPVHSTNSALSYLQSPITTSPSC	chr5:172768096-172771195[-]	"Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle."	PDB: 6APX; PDB: 6D65; PDB: 6D66; PDB: 6D67	HGNC:3064	DUS1_HUMAN	Reviewed	ENSG00000120129	.	.	.	.	.
Mol00333	Protein	Dual specificity protein phosphatase 2 (DUSP2)	Dual specificity protein phosphatase PAC-1; PAC1	DUSP2	1844	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000288943.5, DUSP2-201, 1685; ENST00000488952.1, DUSP2-202, 773"	MGLEAARELECAALGTLLRDPREAERTLLLDCRPFLAFCRRHVRAARPVPWNALLRRRARGPPAAVLACLLPDRALRTRLVRGELARAVVLDEGSASVAELRPDSPAHVLLAALLHETRAGPTAVYFLRGGFDGFQGCCPDLCSEAPAPALPPTGDKTSRSDSRAPVYDQGGPVEILPYLFLGSCSHSSDLQGLQACGITAVLNVSASCPNHFEGLFRYKSIPVEDNQMVEISAWFQEAIGFIDWVKNSGGRVLVHCQAGISRSATICLAYLMQSRRVRLDEAFDFVKQRRGVISPNFSFMGQLLQFETQVLCH	chr2:96143169-96145440[-]	Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2.	PDB: 1M3G	HGNC:3068	DUS2_HUMAN	Reviewed	ENSG00000158050	.	.	.	.	.
Mol00334	Protein	Dynamin-3 (DNM3)	Dynamin; testicular; T-dynamin; KIAA0820	DNM3	26052	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000627582.3, DNM3-208, 7627; ENST00000367731.5, DNM3-202, 7613; ENST00000355305.9, DNM3-201, 3280; ENST00000367733.6, DNM3-203, 2322; ENST00000520906.5, DNM3-206, 4454; ENST00000485254.3, DNM3-204, 2911; ENST00000688173.1, DNM3-209, 2030; ENST00000523513.1, DNM3-207, 1554; ENST00000491124.1, DNM3-205, 822"	MGNREMEELIPLVNRLQDAFSALGQSCLLELPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVTSKAEYAEFLHCKGKKFTDFDEVRLEIEAETDRVTGMNKGISSIPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIREMIMQFITRENCLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYVGVVNRSQKDIDGKKDIKAAMLAERKFFLSHPAYRHIADRMGTPHLQKVLNQQLTNHIRDTLPNFRNKLQGQLLSIEHEVEAYKNFKPEDPTRKTKALLQMVQQFAVDFEKRIEGSGDQVDTLELSGGAKINRIFHERFPFEIVKMEFNEKELRREISYAIKNIHGIRTGLFTPDMAFEAIVKKQIVKLKGPSLKSVDLVIQELINTVKKCTKKLANFPRLCEETERIVANHIREREGKTKDQVLLLIDIQVSYINTNHEDFIGFANAQQRSSQVHKKTTVGNQGTNLPPSRQIVIRKGWLTISNIGIMKGGSKGYWFVLTAESLSWYKDDEEKEKKYMLPLDNLKVRDVEKSFMSSKHIFALFNTEQRNVYKDYRFLELACDSQEDVDSWKASLLRAGVYPDKSVAENDENGQAENFSMDPQLERQVETIRNLVDSYMSIINKCIRDLIPKTIMHLMINNVKDFINSELLAQLYSSEDQNTLMEESAEQAQRRDEMLRMYQALKEALGIIGDISTATVSTPAPPPVDDSWIQHSRRSPPPSPTTQRRPTLSAPLARPTSGRGPAPAIPSPGPHSGAPPVPFRPGPLPPFPSSSDSFGAPPQVPSRPTRAPPSVPSRRPPPSPTRPTIIRPLESSLLD	chr1:171817887-172418466[+]	"Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis (By similarity)."	PDB: 3L43; PDB: 5A3F	HGNC:29125	DYN3_HUMAN	Reviewed	ENSG00000197959	.	.	.	.	.
Mol00335	Protein	Dihydrofolate reductase (DHFR)	.	DHFR	1719	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000439211.7, DHFR-201, 3919; ENST00000505337.5, DHFR-203, 1719; ENST00000511032.5, DHFR-205, 1474; ENST00000504396.1, DHFR-202, 1447; ENST00000513048.5, DHFR-206, 994; ENST00000513314.1, DHFR-207, 582; ENST00000508282.1, DHFR-204, 545"	MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND	chr5:80626226-80654983[-]	"Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2."	PDB: 1BOZ; PDB: 1DHF; PDB: 1DLR; PDB: 1DLS; PDB: 1DRF; PDB: 1HFP; PDB: 1HFQ; PDB: 1HFR; PDB: 1KMS; PDB: 1KMV; PDB: 1MVS; PDB: 1MVT; PDB: 1OHJ; PDB: 1OHK; PDB: 1PD8; PDB: 1PD9; PDB: 1PDB; PDB: 1S3U; PDB: 1S3V; PDB: 1S3W; PDB: 1U71; PDB: 1U72; PDB: 1YHO; PDB: 2C2S; PDB: 2C2T; PDB: 2DHF; PDB: 2W3A; PDB: 2W3B; PDB: 2W3M; PDB: 3EIG; PDB: 3F8Y; PDB: 3F8Z; PDB: 3F91; PDB: 3FS6; PDB: 3GHC; PDB: 3GHV; PDB: 3GHW; PDB: 3GI2; PDB: 3GYF; PDB: 3L3R; PDB: 3N0H; PDB: 3NTZ; PDB: 3NU0; PDB: 3NXO; PDB: 3NXR; PDB: 3NXT; PDB: 3NXV; PDB: 3NXX; PDB: 3NXY; PDB: 3NZD; PDB: 3OAF; PDB: 3S3V; PDB: 3S7A; PDB: 4DDR; PDB: 4G95; PDB: 4KAK; PDB: 4KBN; PDB: 4KD7; PDB: 4KEB; PDB: 4KFJ; PDB: 4M6J; PDB: 4M6K; PDB: 4M6L; PDB: 4QHV; PDB: 4QJC; PDB: 5HPB; PDB: 5HQY; PDB: 5HQZ; PDB: 5HSR; PDB: 5HSU; PDB: 5HT4; PDB: 5HT5; PDB: 5HUI; PDB: 5HVB; PDB: 5HVE; PDB: 6A7C; PDB: 6A7E; PDB: 6DAV; PDB: 6DE4; PDB: 6VCJ; PDB: 7ESE	HGNC:2861	DYR_HUMAN	Reviewed	ENSG00000228716	.	.	.	.	.
Mol00336	Protein	Transcription factor E2F1 (E2F1)	E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1; Retinoblastoma-binding protein 3; RBBP-3; pRB-binding protein E2F-1; RBBP3	E2F1	1869	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000343380.6, E2F1-201, 2690"	.	chr20:33675477-33686385[-]	.	PDB: 1H24; PDB: 1O9K; PDB: 2AZE; PDB: 5M9N; PDB: 5M9O; PDB: 6G0P; PDB: 6ULS	HGNC:3113	E2F1_HUMAN	Reviewed	ENSG00000101412	.	.	.	.	.
Mol00337	Protein	Transcription factor E2F2 (E2F2)	E2F-2	E2F2	1870	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361729.3, E2F2-201, 5196; ENST00000487237.1, E2F2-202, 550"	MLQGPRALASAAGQTPKVVPAMSPTELWPSGLSSPQLCPATATYYTPLYPQTAPPAAAPGTCLDATPHGPEGQVVRCLPAGRLPAKRKLDLEGIGRPVVPEFPTPKGKCIRVDGLPSPKTPKSPGEKTRYDTSLGLLTKKFIYLLSESEDGVLDLNWAAEVLDVQKRRIYDITNVLEGIQLIRKKAKNNIQWVGRGMFEDPTRPGKQQQLGQELKELMNTEQALDQLIQSCSLSFKHLTEDKANKRLAYVTYQDIRAVGNFKEQTVIAVKAPPQTRLEVPDRTEDNLQIYLKSTQGPIEVYLCPEEVQEPDSPSEEPLPSTSTLCPSPDSAQPSSSTDPSIMEPTASSVPAPAPTPQQAPPPPSLVPLEATDSLLELPHPLLQQTEDQFLSPTLACSSPLISFSPSLDQDDYLWGLEAGEGISDLFDSYDLGDLLIN	chr1:23506438-23531233[-]	"Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner."	PDB: 1N4M	HGNC:3114	E2F2_HUMAN	Reviewed	ENSG00000007968	.	.	.	.	.
Mol00338	Protein	Transcription factor E2F3 (E2F3)	E2F-3; KIAA0075	E2F3	1871	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000346618.8, E2F3-201, 5036; ENST00000535432.2, E2F3-202, 4425"	MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEVPDSIESLQIHLASTQGPIEVYLCPEETETHSPMKTNNQDHNGNIPKPASKDLASTNSGHSDCSVSMGNLSPLASPANLLQQTEDQIPSNLEGPFVNLLPPLLQEDYLLSLGEEEGISDLFDAYDLEKLPLVEDFMCS	chr6:20401879-20493714[+]	"Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F3 binds specifically to RB1 in a cell-cycle dependent manner. Inhibits adipogenesis, probably through the repression of CEBPA binding to its target gene promoters (By similarity)."	.	HGNC:3115	E2F3_HUMAN	Reviewed	ENSG00000112242	.	.	.	.	.
Mol00339	Protein	Transcription factor E2F6 (E2F6)	E2F-6	E2F6	1876	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000381525.8, E2F6-202, 3230; ENST00000542100.5, E2F6-211, 3450; ENST00000307236.8, E2F6-201, 3317; ENST00000546212.2, E2F6-212, 3191; ENST00000444832.5, E2F6-206, 3296; ENST00000428221.5, E2F6-204, 3139; ENST00000455198.5, E2F6-207, 2227; ENST00000437573.5, E2F6-205, 1253; ENST00000421117.1, E2F6-203, 907; ENST00000468775.1, E2F6-208, 1061; ENST00000471343.5, E2F6-209, 970; ENST00000498701.1, E2F6-210, 610"	MSQQRPARKLPSLLLDPTEETVRRRCRDPINVEGLLPSKIRINLEDNVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIDLVEKKSKNHIRWIGSDLSNFGAVPQQKKLQEELSDLSAMEDALDELIKDCAQQLFELTDDKENERLAYVTYQDIHSIQAFHEQIVIAVKAPAETRLDVPAPREDSITVHIRSTNGPIDVYLCEVEQGQTSNKRSEGVGTSSSESTHPEGPEEEENPQQSEELLEVSN	chr2:11444375-11466177[-]	"Inhibitor of E2F-dependent transcription. Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and pocket protein binding domains. Appears to regulate a subset of E2F-dependent genes whose products are required for entry into the cell cycle but not for normal cell cycle progression. Represses expression of some meiosis-specific genes, including SLC25A31/ANT4. May silence expression via the recruitment of a chromatin remodeling complex containing histone H3-K9 methyltransferase activity. Overexpression delays the exit of cells from the S-phase."	.	HGNC:3120	E2F6_HUMAN	Reviewed	ENSG00000169016	.	.	.	.	.
Mol00340	Protein	Transcription factor E2F7 (E2F7)	E2F-7	E2F7	144455	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000322886.12, E2F7-201, 5725; ENST00000416496.6, E2F7-202, 5297; ENST00000550669.5, E2F7-204, 2302; ENST00000551058.1, E2F7-205, 724; ENST00000547316.1, E2F7-203, 570; ENST00000552907.5, E2F7-207, 812; ENST00000551558.1, E2F7-206, 1464"	MEVNCLTLKDLISPRQPRLDFAVEDGENAQKENIFVDRSRMAPKTPIKNEPIDLSKQKKFTPERNPITPVKFVDRQQAEPWTPTANLKMLISAASPDIRDREKKKGLFRPIENKDDAFTDSLQLDVVGDSAVDEFEKQRPSRKQKSLGLLCQKFLARYPSYPLSTEKTTISLDEVAVSLGVERRRIYDIVNVLESLHLVSRVAKNQYGWHGRHSLPKTLRNLQRLGEEQKYEEQMAYLQQKELDLIDYKFGERKKDGDPDSQEQQLLDFSEPDCPSSSANSRKDKSLRIMSQKFVMLFLVSKTKIVTLDVAAKILIEESQDAPDHSKFKTKVRRLYDIANVLTSLALIKKVHVTEERGRKPAFKWIGPVDFSSSDEELVDVSASVLPELKRETYGQIQVCAKQKLARHGSFNTVQASERIQRKVNSEPSSPYREEQGSGGYSLEIGSLAAVYRQKIEDNSQGKAFASKRVVPPSSSLDPVAPFPVLSVDPEYCVNPLAHPVFSVAQTDLQAFSMQNGLNGQVDVSLASAASAVESLKPALLAGQPLVYVPSASLFMLYGSLQEGPASGSGSERDDRSSEAPATVELSSAPSAQKRLCEERKPQEEDEPATKRQSREYEDGPLSLVMPKKPSDSTDLASPKTMGNRASIPLKDIHVNGQLPAAEEISGKATANSLVSSEWGNPSRNTDVEKPSKENESTKEPSLLQYLCVQSPAGLNGFNVLLSGSQTPPTVGPSSGQLPSFSVPCMVLPSPPLGPFPVLYSPAMPGPVSSTLGALPNTGPVNFSLPGLGSIAQLLVGPTAVVNPKSSTLPSADPQLQSQPSLNLSPVMSRSHSVVQQPESPVYVGHPVSVVKLHQSPVPVTPKSIQRTHRETFFKTPGSLGDPVLKRRERNQSRNTSSAQRRLEIPSGGAD	chr12:77021248-77065569[-]	"Atypical E2F transcription factor that participates in various processes such as angiogenesis, polyploidization of specialized cells and DNA damage response. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses transcription of classical E2F transcription factors such as E2F1. Acts as a regulator of S-phase by recognizing and binding the E2-related site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes. Plays a key role in polyploidization of cells in placenta and liver by regulating the endocycle, probably by repressing genes promoting cytokinesis and antagonizing action of classical E2F proteins (E2F1, E2F2 and/or E2F3). Required for placental development by promoting polyploidization of trophoblast giant cells. Also involved in DNA damage response: up-regulated by p53/TP53 following genotoxic stress and acts as a downstream effector of p53/TP53-dependent repression by mediating repression of indirect p53/TP53 target genes involved in DNA replication. Acts as a promoter of sprouting angiogenesis, possibly by acting as a transcription activator: associates with HIF1A, recognizes and binds the VEGFA promoter, which is different from canonical E2 recognition site, and activates expression of the VEGFA gene. Acts as a negative regulator of keratinocyte differentiation."	.	HGNC:23820	E2F7_HUMAN	Reviewed	ENSG00000165891	.	.	.	.	.
Mol00342	Protein	Endoglin (ENG)	.	ENG	2022	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373203.9, ENG-202, 2946; ENST00000344849.4, ENG-201, 3059; ENST00000480266.5, ENG-204, 2804; ENST00000486329.1, ENG-205, 663; ENST00000462196.1, ENG-203, 495"	MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTYTTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVLSVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPITSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLEGVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLIDANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPLASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKELVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNILSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSEFLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPIPKTGTLSCTVALRPKTGSQDQEVHRTVFMRLNIISPDLSGCTSKGLVLPAVLGITFGAFLIGALLTAALWYIYSHTRSPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA	chr9:127815013-127854658[-]	"Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature. Regulates the migration of vascular endothelial cells. Required for normal extraembryonic angiogenesis and for embryonic heart development. May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis. May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3."	PDB: 5HZV; PDB: 5HZW; PDB: 5I04	HGNC:3349	EGLN_HUMAN	Reviewed	ENSG00000106991	.	.	.	.	.
Mol00343	Protein	Early growth response protein 1 (EGR1)	EGR-1; AT225; Nerve growth factor-induced protein A; NGFI-A; Transcription factor ETR103; Transcription factor Zif268; Zinc finger protein 225; Zinc finger protein Krox-24; KROX24; ZNF225	EGR1	1958	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000239938.5, EGR1-201, 3137"	MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGAPEGSGSNSSSSSSGGGGGGGGGSNSSSSSSTFNPQADTGEQPYEHLTAESFPDISLNNEKVLVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPASSSSAPSPAASSASASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPAAKGGFQVPMIPDYLFPQQQGDLGLGTPDQKPFQGLESRTQQPSLTPLSTIKAFATQSGSQDLKALNTSYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKADKSVVASSATSSLSSYPSPVATSYPSPVTTSYPSPATTSYPSPVPTSFSSPGSSTYPSPVHSGFPSPSVATTYSSVPPAFPAQVSSFPSSAVTNSFSASTGLSDMTATFSPRTIEIC	chr5:138465479-138469303[+]	"Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Activates expression of p53/TP53 and TGFB1, and thereby helps prevent tumor formation. Required for normal progress through mitosis and normal proliferation of hepatocytes after partial hepatectomy. Mediates responses to ischemia and hypoxia; regulates the expression of proteins such as IL1B and CXCL2 that are involved in inflammatory processes and development of tissue damage after ischemia. Regulates biosynthesis of luteinizing hormone (LHB) in the pituitary. Regulates the amplitude of the expression rhythms of clock genes: ARNTL/BMAL1, PER2 and NR1D1 in the liver via the activation of PER1 (clock repressor) transcription. Regulates the rhythmic expression of core-clock gene ARNTL/BMAL1 in the suprachiasmatic nucleus (SCN)."	PDB: 4R2A; PDB: 4R2C; PDB: 4R2D; PDB: 4X9J; PDB: 5N14	HGNC:3238	EGR1_HUMAN	Reviewed	ENSG00000120738	.	.	.	.	.
Mol00344	Protein	E3 SUMO-protein ligase EGR2 (EGR2)	AT591; E3 SUMO-protein transferase ERG2; Early growth response protein 2; EGR-2; Zinc finger protein Krox-20; KROX20	EGR2	1959	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000242480.4, EGR2-201, 2979; ENST00000411732.4, EGR2-202, 2882; ENST00000637191.2, EGR2-204, 2796; ENST00000691610.1, EGR2-207, 1490; ENST00000439032.6, EGR2-203, 3155; ENST00000690143.1, EGR2-206, 1640; ENST00000639815.1, EGR2-205, 1075"	MMTAKAVDKIPVTLSGFVHQLSDNIYPVEDLAATSVTIFPNAELGGPFDQMNGVAGDGMINIDMTGEKRSLDLPYPSSFAPVSAPRNQTFTYMGKFSIDPQYPGASCYPEGIINIVSAGILQGVTSPASTTASSSVTSASPNPLATGPLGVCTMSQTQPDLDHLYSPPPPPPPYSGCAGDLYQDPSAFLSAATTSTSSSLAYPPPPSYPSPKPATDPGLFPMIPDYPGFFPSQCQRDLHGTAGPDRKPFPCPLDTLRVPPPLTPLSTIRNFTLGGPSAGVTGPGASGGSEGPRLPGSSSAAAAAAAAAAYNPHHLPLRPILRPRKYPNRPSKTPVHERPYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGRKFARSDERKRHTKIHLRQKERKSSAPSASVPAPSTASCSGGVQPGGTLCSSNSSSLGGGPLAPCSSRTRTP	chr10:62811996-62819167[-]	"Sequence-specific DNA-binding transcription factor. Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in the formation and maintenance of myelin. Binds to two EGR2-consensus sites EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in the HOXB3 enhancer and promotes HOXB3 transcriptional activation. Binds to specific DNA sites located in the promoter region of HOXA4, HOXB2 and ERBB2. Regulates hindbrain segmentation by controlling the expression of Hox genes, such as HOXA4, HOXB3 and HOXB2, and thereby specifying odd and even rhombomeres. Promotes the expression of HOXB3 in the rhombomere r5 in the hindbrain. Regulates myelination in the peripheral nervous system after birth, possibly by regulating the expression of myelin proteins, such as MPZ, and by promoting the differentiation of Schwann cells. Involved in the development of the jaw openener musculature, probably by playing a role in its innervation through trigeminal motor neurons. May play a role in adipogenesis, possibly by regulating the expression of CEBPB."	.	HGNC:3239	EGR2_HUMAN	Reviewed	ENSG00000122877	.	.	.	.	.
Mol00345	Protein	ETS homologous factor (EHF)	hEHF; ETS domain-containing transcription factor; Epithelium-specific Ets transcription factor 3; ESE-3; ESE3; ESE3B; ESEJ	EHF	26298	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000257831.8, EHF-201, 5399; ENST00000450654.6, EHF-202, 2519; ENST00000533754.5, EHF-212, 1501; ENST00000531794.5, EHF-210, 1481; ENST00000530286.5, EHF-208, 1280; ENST00000525253.5, EHF-203, 564; ENST00000529527.5, EHF-207, 560; ENST00000532302.1, EHF-211, 557; ENST00000527935.1, EHF-205, 557; ENST00000531728.5, EHF-209, 485; ENST00000527001.5, EHF-204, 507; ENST00000529161.1, EHF-206, 502"	MILEGGGVMNLNPGNNLLHQPPAWTDSYSTCNVSSGFFGGQWHEIHPQYWTKYQVWEWLQHLLDTNQLDANCIPFQEFDINGEHLCSMSLQEFTRAAGTAGQLLYSNLQHLKWNGQCSSDLFQSTHNVIVKTEQTEPSIMNTWKDENYLYDTNYGSTVDLLDSKTFCRAQISMTTTSHLPVAESPDMKKEQDPPAKCHTKKHNPRGTHLWEFIRDILLNPDKNPGLIKWEDRSEGVFRFLKSEAVAQLWGKKKNNSSMTYEKLSRAMRYYYKREILERVDGRRLVYKFGKNARGWRENEN	chr11:34621093-34663288[+]	Transcriptional activator that may play a role in regulating epithelial cell differentiation and proliferation. May act as a repressor for a specific subset of ETS/AP-1-responsive genes and as a modulator of the nuclear response to mitogen-activated protein kinase signaling cascades. Binds to DNA sequences containing the consensus nucleotide core sequence GGAA. Involved in regulation of TNFRSF10B/DR5 expression through Ets-binding sequences on the TNFRSF10B/DR5 promoter. May contribute to development and carcinogenesis by acting as a tumor suppressor gene or anti-oncogene.	.	HGNC:3246	EHF_HUMAN	Reviewed	ENSG00000135373	.	.	.	.	.
Mol00346	Protein	Eukaryotic translation initiation factor 3 subunit A (EIF3A)	eIF3a; Eukaryotic translation initiation factor 3 subunit 10; eIF-3-theta; eIF3 p167; eIF3 p180; eIF3 p185; EIF3S10; KIAA0139	EIF3A	8661	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369144.8, EIF3A-201, 6659; ENST00000541549.2, EIF3A-203, 4495; ENST00000462527.2, EIF3A-202, 1192"	MPAYFQRPENALKRANEFLEVGKKQPALDVLYDVMKSKKHRTWQKIHEPIMLKYLELCVDLRKSHLAKEGLYQYKNICQQVNIKSLEDVVRAYLKMAEEKTEAAKEESQQMVLDIEDLDNIQTPESVLLSAVSGEDTQDRTDRLLLTPWVKFLWESYRQCLDLLRNNSRVERLYHDIAQQAFKFCLQYTRKAEFRKLCDNLRMHLSQIQRHHNQSTAINLNNPESQSMHLETRLVQLDSAISMELWQEAFKAVEDIHGLFSLSKKPPKPQLMANYYNKVSTVFWKSGNALFHASTLHRLYHLSREMRKNLTQDEMQRMSTRVLLATLSIPITPERTDIARLLDMDGIIVEKQRRLATLLGLQAPPTRIGLINDMVRFNVLQYVVPEVKDLYNWLEVEFNPLKLCERVTKVLNWVREQPEKEPELQQYVPQLQNNTILRLLQQVSQIYQSIEFSRLTSLVPFVDAFQLERAIVDAARHCDLQVRIDHTSRTLSFGSDLNYATREDAPIGPHLQSMPSEQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYLKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEEQRIKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQRKEERRITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQRELEIEERERRREEERRLGDSSLSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRGEGRDEDRSHRRDEERPRRLGDDEDREPSLRPDDDRVPRRGMDDDRGPRRGPEEDRFSRRGADDDRPSWRNTDDDRPPRRIADEDRGNWRHADDDRPPRRGLDEDRGSWRTADEDRGPRRGMDDDRGPRRGGADDERSSWRNADDDRGPRRGLDDDRGPRRGMDDDRGPRRGMDDDRGPRRGMDDDRGPRRGLDDDRGPWRNADDDRIPRRGAEDDRGPWRNMDDDRLSRRADDDRFPRRGDDSRPGPWRPLVKPGGWREKEKAREESWGPPRESRPSEEREWDREKERDRDNQDREENDKDPERERDRERDVDREDRFRRPRDEGGWRRGPAEESSSWRDSSRRDDRDRDDRRRERDDRRDLRERRDLRDDRDRRGPPLRSEREEVSSWRRADDRKDDRVEERDPPRRVPPPALSRDRERDRDREREGEKEKASWRAEKDRESLRRTKNETDEDGWTTVRR	chr10:119033670-119080823[-]	"RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression."	PDB: 3J8B; PDB: 3J8C; PDB: 6YBD; PDB: 6YBT; PDB: 6ZMW; PDB: 6ZON; PDB: 6ZP4; PDB: 6ZVJ; PDB: 7A09	HGNC:3271	EIF3A_HUMAN	Reviewed	ENSG00000107581	.	.	.	.	.
Mol00347	Protein	Endoplasmin (HSP90B1)	94 kDa glucose-regulated protein; GRP-94; Heat shock protein 90 kDa beta member 1; Tumor rejection antigen 1; gp96 homolog; GRP94; TRA1	HSP90B1	7184	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000299767.10, HSP90B1-201, 2782; ENST00000550595.2, HSP90B1-207, 3112; ENST00000680762.1, HSP90B1-224, 2858; ENST00000681949.1, HSP90B1-235, 2850; ENST00000681861.1, HSP90B1-232, 2831; ENST00000679861.1, HSP90B1-215, 2740; ENST00000680316.1, HSP90B1-218, 2646; ENST00000614327.2, HSP90B1-210, 2610; ENST00000549334.5, HSP90B1-205, 581; ENST00000680391.1, HSP90B1-220, 3184; ENST00000680899.1, HSP90B1-225, 3049; ENST00000681174.1, HSP90B1-228, 2903; ENST00000680370.1, HSP90B1-219, 2816; ENST00000681172.1, HSP90B1-227, 2811; ENST00000681941.1, HSP90B1-234, 2808; ENST00000679538.1, HSP90B1-213, 2775; ENST00000680663.1, HSP90B1-223, 2713; ENST00000681698.1, HSP90B1-230, 2570; ENST00000681704.1, HSP90B1-231, 6609; ENST00000552051.2, HSP90B1-209, 5608; ENST00000680478.1, HSP90B1-221, 5223; ENST00000680653.1, HSP90B1-222, 3903; ENST00000679377.1, HSP90B1-212, 3858; ENST00000679779.1, HSP90B1-214, 3459; ENST00000681910.1, HSP90B1-233, 3458; ENST00000681245.1, HSP90B1-229, 3365; ENST00000680989.1, HSP90B1-226, 3327; ENST00000680281.1, HSP90B1-217, 3248; ENST00000540297.7, HSP90B1-202, 3128; ENST00000680242.1, HSP90B1-216, 3091; ENST00000548462.5, HSP90B1-203, 3032; ENST00000640977.2, HSP90B1-211, 1204; ENST00000548622.1, HSP90B1-204, 839; ENST00000551983.1, HSP90B1-208, 728; ENST00000550479.1, HSP90B1-206, 698"	MRALWVLGLCCVLLTFGSVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAEKDEL	chr12:103930107-103953931[+]	"Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10."	PDB: 4NH9	HGNC:12028	ENPL_HUMAN	Reviewed	ENSG00000166598	.	.	.	.	.
Mol00348	Protein	Histone acetyltransferase p300 (EP300)	p300 HAT; E1A-associated protein p300; Histone butyryltransferase p300; Histone crotonyltransferase p300; Protein 2-hydroxyisobutyryltransferase p300; Protein lactyltransferas p300; Protein propionyltransferase p300; P300	EP300	2033	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263253.9, EP300-201, 8779; ENST00000674155.1, EP300-212, 8288; ENST00000634690.1, EP300-203, 559; ENST00000635584.1, EP300-209, 544; ENST00000635552.1, EP300-208, 1952; ENST00000635083.1, EP300-206, 613; ENST00000634787.1, EP300-204, 496; ENST00000634422.1, EP300-202, 488; ENST00000634860.1, EP300-205, 428; ENST00000635691.1, EP300-210, 402; ENST00000635538.1, EP300-207, 318; ENST00000637592.1, EP300-211, 100"	MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH	chr22:41092592-41180077[+]	"Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1 or SIRT2. Acetylates 'Lys-131' of ALX1 and acts as its coactivator. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of p53/TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Following DNA damage, forms a stress-responsive p53/TP53 coactivator complex with JMY which mediates p53/TP53 acetylation, thereby increasing p53/TP53-dependent transcription and apoptosis. Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acetylates 'Lys-247' of EGR2. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity. Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity. Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER). Acetylates MEF2D. Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation. Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity. Acetylates PCK1 and promotes PCK1 anaplerotic activity. Acetylates RXRA and RXRG. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation or propionylation, respectively. Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low. Also acts as a histone butyryltransferase; butyrylation marks active promoters. Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription. Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes. Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway."	PDB: 1L3E; PDB: 1P4Q; PDB: 2K8F; PDB: 2MH0; PDB: 2MZD; PDB: 3BIY; PDB: 3I3J; PDB: 3IO2; PDB: 3P57; PDB: 3T92; PDB: 4BHW; PDB: 4PZR; PDB: 4PZS; PDB: 4PZT; PDB: 5BT3; PDB: 5KJ2; PDB: 5LKT; PDB: 5LKU; PDB: 5LKX; PDB: 5LKZ; PDB: 5LPK; PDB: 5LPM; PDB: 5NU5; PDB: 5XZC; PDB: 6DS6; PDB: 6FGN; PDB: 6FGS; PDB: 6GYR; PDB: 6GYT; PDB: 6K4N; PDB: 6PF1; PDB: 6PGU; PDB: 6V8B; PDB: 6V8K; PDB: 6V8N; PDB: 6V90; PDB: 7LJE	HGNC:3373	EP300_HUMAN	Reviewed	ENSG00000100393	.	.	.	.	.
Mol00349	Protein	Ephrin type-A receptor 2 (EPHA2)	Epithelial cell kinase; Tyrosine-protein kinase receptor ECK; ECK	EPHA2	1969	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000358432.8, EPHA2-201, 3946; ENST00000461614.1, EPHA2-202, 875; ENST00000480202.1, EPHA2-204, 795; ENST00000462805.1, EPHA2-203, 438"	MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI	chr1:16124337-16156069[-]	"Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis."	PDB: 1MQB; PDB: 2E8N; PDB: 2K9Y; PDB: 2KSO; PDB: 2X10; PDB: 2X11; PDB: 3C8X; PDB: 3CZU; PDB: 3FL7; PDB: 3HEI; PDB: 3HPN; PDB: 3KKA; PDB: 3MBW; PDB: 3MX0; PDB: 3SKJ; PDB: 4P2K; PDB: 4PDO; PDB: 4TRL; PDB: 5EK7; PDB: 5I9U; PDB: 5I9V; PDB: 5I9W; PDB: 5I9X; PDB: 5I9Y; PDB: 5I9Z; PDB: 5IA0; PDB: 5IA1; PDB: 5IA2; PDB: 5IA3; PDB: 5IA4; PDB: 5IA5; PDB: 5NJZ; PDB: 5NK0; PDB: 5NK1; PDB: 5NK2; PDB: 5NK3; PDB: 5NK4; PDB: 5NK5; PDB: 5NK6; PDB: 5NK7; PDB: 5NK8; PDB: 5NK9; PDB: 5NKA; PDB: 5NKB; PDB: 5NKC; PDB: 5NKD; PDB: 5NKE; PDB: 5NKF; PDB: 5NKG; PDB: 5NKH; PDB: 5NKI; PDB: 5NZ9; PDB: 6B9L; PDB: 6F7M; PDB: 6F7N; PDB: 6FNF; PDB: 6FNG; PDB: 6FNH; PDB: 6HES; PDB: 6HET; PDB: 6HEU; PDB: 6HEV; PDB: 6HEW; PDB: 6HEX; PDB: 6HEY; PDB: 6NJZ; PDB: 6NK0; PDB: 6NK1; PDB: 6NK2; PDB: 6NKP; PDB: 6Q7B; PDB: 6Q7C; PDB: 6Q7D; PDB: 6Q7E; PDB: 6Q7F; PDB: 6Q7G; PDB: 6RW2; PDB: 7B7N; PDB: 7CZE; PDB: 7CZF; PDB: 7KJA; PDB: 7KJB; PDB: 7KJC	HGNC:3386	EPHA2_HUMAN	Reviewed	ENSG00000142627	.	.	.	.	.
Mol00351	Protein	Receptor tyrosine-protein kinase erbB-4 (ERBB4)	Proto-oncogene-like protein c-ErbB-4; Tyrosine kinase-type cell surface receptor HER4; p180erbB4; 4ICD; E4ICD; s80HER4; HER4	ERBB4	2066	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000342788.9, ERBB4-202, 12097; ENST00000436443.5, ERBB4-205, 12084; ENST00000402597.6, ERBB4-203, 11699; ENST00000260943.10, ERBB4-201, 2194; ENST00000435846.1, ERBB4-204, 569; ENST00000484474.1, ERBB4-208, 582; ENST00000463121.1, ERBB4-207, 309; ENST00000484594.5, ERBB4-209, 2680; ENST00000459774.1, ERBB4-206, 444"	MKPATGLWVWVSLLVAAGTVQPSDSQSVCAGTENKLSSLSDLEQQYRALRKYYENCEVVMGNLEITSIEHNRDLSFLRSVREVTGYVLVALNQFRYLPLENLRIIRGTKLYEDRYALAIFLNYRKDGNFGLQELGLKNLTEILNGGVYVDQNKFLCYADTIHWQDIVRNPWPSNLTLVSTNGSSGCGRCHKSCTGRCWGPTENHCQTLTRTVCAEQCDGRCYGPYVSDCCHRECAGGCSGPKDTDCFACMNFNDSGACVTQCPQTFVYNPTTFQLEHNFNAKYTYGAFCVKKCPHNFVVDSSSCVRACPSSKMEVEENGIKMCKPCTDICPKACDGIGTGSLMSAQTVDSSNIDKFINCTKINGNLIFLVTGIHGDPYNAIEAIDPEKLNVFRTVREITGFLNIQSWPPNMTDFSVFSNLVTIGGRVLYSGLSLLILKQQGITSLQFQSLKEISAGNIYITDNSNLCYYHTINWTTLFSTINQRIVIRDNRKAENCTAEGMVCNHLCSSDGCWGPGPDQCLSCRRFSRGRICIESCNLYDGEFREFENGSICVECDPQCEKMEDGLLTCHGPGPDNCTKCSHFKDGPNCVEKCPDGLQGANSFIFKYADPDRECHPCHPNCTQGCNGPTSHDCIYYPWTGHSTLPQHARTPLIAAGVIGGLFILVIVGLTFAVYVRRKSIKKKRALRRFLETELVEPLTPSGTAPNQAQLRILKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHGCLLEYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQGDDRMKLPSPNDSKFFQNLLDEEDLEDMMDAEEYLVPQAFNIPPPIYTSRARIDSNRSEIGHSPPPAYTPMSGNQFVYRDGGFAAEQGVSVPYRAPTSTIPEAPVAQGATAEIFDDSCCNGTLRKPVAPHVQEDSSTQRYSADPTVFAPERSPRGELDEEGYMTPMRDKPKQEYLNPVEENPFVSRRKNGDLQALDNPEYHNASNGPPKAEDEYVNEPLYLNTFANTLGKAEYLKNNILSMPEKAKKAFDNPDYWNHSLPPRSTLQHPDYLQEYSTKYFYKQNGRIRPIVAENPEYLSEFSLKPGTVLPPPPYRHRNTVV	chr2:211375717-212538841[-]	"Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis."	PDB: 2AHX; PDB: 2L2T; PDB: 2LCX; PDB: 2R4B; PDB: 3BBT; PDB: 3BBW; PDB: 3BCE; PDB: 3U2P; PDB: 3U7U; PDB: 3U9U	HGNC:3432	ERBB4_HUMAN	Reviewed	ENSG00000178568	.	.	.	.	.
Mol00352	Protein	DNA excision repair protein ERCC-1 (ERCC1)	.	ERCC1	2067	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000300853.8, ERCC1-202, 3379; ENST00000589165.5, ERCC1-208, 1453; ENST00000013807.9, ERCC1-201, 1278; ENST00000340192.11, ERCC1-203, 949; ENST00000423698.6, ERCC1-204, 3119; ENST00000592083.5, ERCC1-214, 938; ENST00000591636.5, ERCC1-212, 836; ENST00000589381.5, ERCC1-210, 738; ENST00000592023.5, ERCC1-213, 738; ENST00000589214.1, ERCC1-209, 674; ENST00000592444.5, ERCC1-216, 449; ENST00000590701.5, ERCC1-211, 345; ENST00000587888.5, ERCC1-205, 556; ENST00000588738.5, ERCC1-207, 586; ENST00000592410.5, ERCC1-215, 508; ENST00000588300.1, ERCC1-206, 1055; ENST00000592905.5, ERCC1-217, 882"	MDPGKDKEGVPQPSGPPARKKFVIPLDEDEVPPGVAKPLFRSTQSLPTVDTSAQAAPQTYAEYAISQPLEGAGATCPTGSEPLAGETPNQALKPGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIHGRLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDLALCPGLGPQKARRLFDVLHEPFLKVP	chr19:45407334-45478828[-]	"[Isoform 1]: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4."	PDB: 1Z00; PDB: 2A1I; PDB: 2A1J; PDB: 2JNW; PDB: 2JPD; PDB: 2MUT; PDB: 6SXA; PDB: 6SXB	HGNC:3433	ERCC1_HUMAN	Reviewed	ENSG00000012061	.	.	.	.	.
Mol00353	Protein	General transcription and DNA repair factor IIH helicase subunit XPD (ERCC2)	TFIIH subunit XPD; Basic transcription factor 2 80 kDa subunit; BTF2 p80; CXPD; DNA excision repair protein ERCC-2; DNA repair protein complementing XP-D cells; TFIIH basal transcription factor complex 80 kDa subunit; TFIIH 80 kDa subunit; TFIIH p80; Xeroderma pigmentosum group D-complementing protein; XPD; XPDC	ERCC2	2068	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000391945.10, ERCC2-204, 4108; ENST00000485403.6, ERCC2-205, 1538; ENST00000684407.1, ERCC2-218, 4013; ENST00000391941.6, ERCC2-201, 2871; ENST00000391944.8, ERCC2-203, 2853; ENST00000586131.6, ERCC2-206, 1015; ENST00000586856.1, ERCC2-209, 690; ENST00000682414.1, ERCC2-214, 3110; ENST00000684218.1, ERCC2-216, 3989; ENST00000684458.1, ERCC2-219, 3979; ENST00000587376.6, ERCC2-210, 823; ENST00000591309.5, ERCC2-212, 557; ENST00000682508.1, ERCC2-215, 4094; ENST00000684468.1, ERCC2-220, 3777; ENST00000684264.1, ERCC2-217, 3621; ENST00000646507.1, ERCC2-213, 3119; ENST00000588652.5, ERCC2-211, 2405; ENST00000391942.6, ERCC2-202, 1488; ENST00000586441.1, ERCC2-207, 682; ENST00000586737.5, ERCC2-208, 481"	MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEITDLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLESEETLKRIEQIAQQL	chr19:45349837-45370918[-]	"ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers."	PDB: 5IVW; PDB: 5IY6; PDB: 5IY7; PDB: 5IY8; PDB: 5IY9; PDB: 5OF4; PDB: 6NMI; PDB: 6O9L; PDB: 6O9M; PDB: 6RO4; PDB: 6TUN; PDB: 7AD8; PDB: 7EGB; PDB: 7EGC; PDB: 7ENA; PDB: 7ENC; PDB: 7LBM; PDB: 7NVR; PDB: 7NVW; PDB: 7NVX; PDB: 7NVY; PDB: 7NVZ; PDB: 7NW0	HGNC:3434	ERCC2_HUMAN	Reviewed	ENSG00000104884	.	.	.	.	.
Mol00354	Protein	Proepiregulin (EREG)	EPR	EREG	2069	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000244869.3, EREG-201, 4615; ENST00000503689.1, EREG-202, 598; ENST00000507603.1, EREG-203, 1290"	MTAGRRMEMLCAGRVPALLLCLGFHLLQAVLSTTVIPSCIPGESSDNCTALVQTEDNPRVAQVSITKCSSDMNGYCLHGQCIYLVDMSQNYCRCEVGYTGVRCEHFFLTVHQPLSKEYVALTVILIILFLITVVGSTYYFCRWYRNRKSKEPKKEYERVTSGDPELPQV	chr4:74365145-74388749[+]	"Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation. Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation."	PDB: 1K36; PDB: 1K37; PDB: 5E8D; PDB: 5WB7	HGNC:3443	EREG_HUMAN	Reviewed	ENSG00000124882	.	.	.	.	.
Mol00355	Protein	ERBB receptor feedback inhibitor 1 (ERRFI1)	Mitogen-inducible gene 6 protein; MIG-6; MIG6	ERRFI1	54206	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377482.10, ERRFI1-201, 3097; ENST00000467067.1, ERRFI1-202, 2097; ENST00000469499.5, ERRFI1-203, 995; ENST00000474874.5, ERRFI1-204, 479; ENST00000487559.1, ERRFI1-205, 787"	MSIAGVAAQEIRVPLKTGFLHNGRAMGNMRKTYWSSRSEFKNNFLNIDPITMAYSLNSSAQERLIPLGHASKSAPMNGHCFAENGPSQKSSLPPLLIPPSENLGPHEEDQVVCGFKKLTVNGVCASTPPLTPIKNSPSLFPCAPLCERGSRPLPPLPISEALSLDDTDCEVEFLTSSDTDFLLEDSTLSDFKYDVPGRRSFRGCGQINYAYFDTPAVSAADLSYVSDQNGGVPDPNPPPPQTHRRLRRSHSGPAGSFNKPAIRISNCCIHRASPNSDEDKPEVPPRVPIPPRPVKPDYRRWSAEVTSSTYSDEDRPPKVPPREPLSPSNSRTPSPKSLPSYLNGVMPPTQSFAPDPKYVSSKALQRQNSEGSASKVPCILPIIENGKKVSSTHYYLLPERPPYLDKYEKFFREAEETNGGAQIQPLPADCGISSATEKPDSKTKMDLGGHVKRKHLSYVVSP	chr1:8004404-8026309[-]	"Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity)."	PDB: 2RF9; PDB: 2RFD; PDB: 2RFE; PDB: 4I21; PDB: 4R3P; PDB: 4R3R; PDB: 4ZJV	HGNC:18185	ERRFI_HUMAN	Reviewed	ENSG00000116285	.	.	.	.	.
Mol00356	Protein	Estrogen receptor alpha (ESR1)	ER; ER-alpha; Estradiol receptor; Nuclear receptor subfamily 3 group A member 1; ESR; NR3A1	ESR1	2099	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000206249.8, ESR1-201, 6327; ENST00000440973.5, ESR1-207, 6466; ENST00000443427.5, ESR1-208, 6357; ENST00000427531.6, ESR1-206, 5436; ENST00000338799.9, ESR1-202, 3335; ENST00000456483.3, ESR1-210, 1368; ENST00000406599.5, ESR1-204, 1251; ENST00000446550.1, ESR1-209, 731; ENST00000404742.5, ESR1-203, 624; ENST00000415488.1, ESR1-205, 323; ENST00000641399.1, ESR1-214, 1207; ENST00000482101.1, ESR1-212, 641; ENST00000488573.1, ESR1-213, 530; ENST00000473497.5, ESR1-211, 219"	MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV	chr6:151656691-152129619[+]	"Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3."	PDB: 1A52; PDB: 1ERE; PDB: 1ERR; PDB: 1G50; PDB: 1GWQ; PDB: 1GWR; PDB: 1HCP; PDB: 1HCQ; PDB: 1L2I; PDB: 1PCG; PDB: 1QKT; PDB: 1QKU; PDB: 1R5K; PDB: 1SJ0; PDB: 1UOM; PDB: 1X7E; PDB: 1X7R; PDB: 1XP1; PDB: 1XP6; PDB: 1XP9; PDB: 1XPC; PDB: 1XQC; PDB: 1YIM; PDB: 1YIN; PDB: 1ZKY; PDB: 2AYR; PDB: 2B1V; PDB: 2B1Z; PDB: 2B23; PDB: 2BJ4; PDB: 2FAI; PDB: 2G44; PDB: 2G5O; PDB: 2I0J; PDB: 2IOG; PDB: 2IOK; PDB: 2JF9; PDB: 2JFA; PDB: 2LLO; PDB: 2LLQ; PDB: 2OCF; PDB: 2OUZ; PDB: 2P15; PDB: 2POG; PDB: 2Q6J; PDB: 2Q70; PDB: 2QA6; PDB: 2QA8; PDB: 2QAB; PDB: 2QE4; PDB: 2QGT; PDB: 2QGW; PDB: 2QH6; PDB: 2QR9; PDB: 2QSE; PDB: 2QXM; PDB: 2QXS; PDB: 2QZO; PDB: 2R6W; PDB: 2R6Y; PDB: 2YAT; PDB: 2YJA; PDB: 3CBM; PDB: 3CBO; PDB: 3CBP; PDB: 3DT3; PDB: 3ERD; PDB: 3ERT; PDB: 3HLV; PDB: 3HM1; PDB: 3L03; PDB: 3OS8; PDB: 3OS9; PDB: 3OSA; PDB: 3Q95; PDB: 3UU7; PDB: 3UUA; PDB: 3UUC; PDB: 3UUD; PDB: 4AA6; PDB: 4DMA; PDB: 4IU7; PDB: 4IUI; PDB: 4IV2; PDB: 4IV4; PDB: 4IVW; PDB: 4IVY; PDB: 4IW6; PDB: 4IW8; PDB: 4IWC; PDB: 4IWF; PDB: 4JC3; PDB: 4JDD; PDB: 4MG5; PDB: 4MG6; PDB: 4MG7; PDB: 4MG8; PDB: 4MG9; PDB: 4MGA; PDB: 4MGB; PDB: 4MGC; PDB: 4MGD; PDB: 4O6F; PDB: 4PP6; PDB: 4PPP; PDB: 4PPS; PDB: 4PXM; PDB: 4Q13; PDB: 4Q50; PDB: 4TUZ; PDB: 4TV1; PDB: 4XI3; PDB: 4ZN7; PDB: 4ZN9; PDB: 4ZNH; PDB: 4ZNS; PDB: 4ZNT; PDB: 4ZNU; PDB: 4ZNV; PDB: 4ZNW; PDB: 5AAU; PDB: 5AAV; PDB: 5ACC; PDB: 5AK2; PDB: 5DI7; PDB: 5DID; PDB: 5DIE; PDB: 5DIG; PDB: 5DK9; PDB: 5DKB; PDB: 5DKE; PDB: 5DKG; PDB: 5DKS; PDB: 5DL4; PDB: 5DLR; PDB: 5DMC; PDB: 5DMF; PDB: 5DP0; PDB: 5DRJ; PDB: 5DRM; PDB: 5DTV; PDB: 5DU5; PDB: 5DUE; PDB: 5DUG; PDB: 5DUH; PDB: 5DVS; PDB: 5DVV; PDB: 5DWE; PDB: 5DWG; PDB: 5DWI; PDB: 5DWJ; PDB: 5DX3; PDB: 5DXB; PDB: 5DXE; PDB: 5DXG; PDB: 5DXK; PDB: 5DXM; PDB: 5DXP; PDB: 5DXQ; PDB: 5DXR; PDB: 5DY8; PDB: 5DYB; PDB: 5DYD; PDB: 5DZ0; PDB: 5DZ1; PDB: 5DZ3; PDB: 5DZH; PDB: 5DZI; PDB: 5E0W; PDB: 5E0X; PDB: 5E14; PDB: 5E15; PDB: 5E19; PDB: 5E1C; PDB: 5EGV; PDB: 5EHJ; PDB: 5EI1; PDB: 5EIT; PDB: 5FQP; PDB: 5FQR; PDB: 5FQS; PDB: 5FQT; PDB: 5FQV; PDB: 5GS4; PDB: 5GTR; PDB: 5HYR; PDB: 5JMM; PDB: 5KCC; PDB: 5KCD; PDB: 5KCE; PDB: 5KCF; PDB: 5KCT; PDB: 5KCU; PDB: 5KCW; PDB: 5KD9; PDB: 5KR9; PDB: 5KRA; PDB: 5KRC; PDB: 5KRF; PDB: 5KRH; PDB: 5KRI; PDB: 5KRJ; PDB: 5KRK; PDB: 5KRL; PDB: 5KRM; PDB: 5KRO; PDB: 5N10; PDB: 5T0X; PDB: 5T1Z; PDB: 5T92; PDB: 5T97; PDB: 5TLD; PDB: 5TLF; PDB: 5TLG; PDB: 5TLL; PDB: 5TLM; PDB: 5TLO; PDB: 5TLP; PDB: 5TLT; PDB: 5TLU; PDB: 5TLV; PDB: 5TLX; PDB: 5TLY; PDB: 5TM1; PDB: 5TM2; PDB: 5TM3; PDB: 5TM4; PDB: 5TM5; PDB: 5TM6; PDB: 5TM7; PDB: 5TM8; PDB: 5TM9; PDB: 5TML; PDB: 5TMM; PDB: 5TMO; PDB: 5TMQ; PDB: 5TMR; PDB: 5TMS; PDB: 5TMT; PDB: 5TMU; PDB: 5TMV; PDB: 5TMW; PDB: 5TMZ; PDB: 5TN1; PDB: 5TN3; PDB: 5TN4; PDB: 5TN5; PDB: 5TN6; PDB: 5TN7; PDB: 5TN8; PDB: 5TN9; PDB: 5TNB; PDB: 5U2B; PDB: 5U2D; PDB: 5UFW; PDB: 5UFX; PDB: 5W9C; PDB: 5W9D; PDB: 5WGD; PDB: 5WGQ; PDB: 6B0F; PDB: 6C42; PDB: 6CBZ; PDB: 6CHW; PDB: 6CHZ; PDB: 6CZN; PDB: 6D0F; PDB: 6DF6; PDB: 6DFN; PDB: 6HHP; PDB: 6HKB; PDB: 6HKF; PDB: 6HMU; PDB: 6IAR; PDB: 6OWC; PDB: 6PET; PDB: 6PFM; PDB: 6PIT; PDB: 6PSJ; PDB: 6SBO; PDB: 6SQ0; PDB: 6SUO; PDB: 6TJM; PDB: 6TL3; PDB: 6V87; PDB: 6V8T; PDB: 6VGH; PDB: 6VIG; PDB: 6VJ1; PDB: 6VJD; PDB: 6VMU; PDB: 6VPF; PDB: 6VPK; PDB: 6VVP; PDB: 6WOK; PDB: 6ZOQ; PDB: 6ZOR; PDB: 6ZOS; PDB: 7B9M; PDB: 7B9R; PDB: 7B9T; PDB: 7BA3; PDB: 7BA5; PDB: 7BA6; PDB: 7BA7; PDB: 7BA8; PDB: 7BA9; PDB: 7BAA; PDB: 7BAB; PDB: 7JHD; PDB: 7KBS; PDB: 7KCA; PDB: 7KCD; PDB: 7MSA; PDB: 7NDO; PDB: 7NEL; PDB: 7NFB; PDB: 7NFW; PDB: 7RRX; PDB: 7RRY; PDB: 7RRZ; PDB: 7RS0; PDB: 7RS1; PDB: 7RS2; PDB: 7RS3; PDB: 7RS4; PDB: 7RS7; PDB: 7RS8; PDB: 7RS9	HGNC:3467	ESR1_HUMAN	Reviewed	ENSG00000091831	.	.	.	.	.
Mol00357	Protein	Liver carboxylesterase 1 (CES1)	Acyl-coenzyme A:cholesterol acyltransferase; ACAT; Brain carboxylesterase hBr1; Carboxylesterase 1; CE-1; hCE-1; Cholesteryl ester hydrolase; CEH; Cocaine carboxylesterase; Egasyn; HMSE; Methylumbelliferyl-acetate deacetylase 1; Monocyte/macrophage serine esterase; Retinyl ester hydrolase; REH; Serine esterase 1; Triacylglycerol hydrolase; TGH; CES2; SES1	CES1	1066	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000360526.8, CES1-201, 1946; ENST00000422046.6, CES1-203, 2178; ENST00000361503.8, CES1-202, 1835; ENST00000563241.5, CES1-205, 509; ENST00000565568.1, CES1-207, 659; ENST00000569260.1, CES1-209, 499; ENST00000566555.1, CES1-208, 659; ENST00000563005.5, CES1-204, 1002; ENST00000565403.5, CES1-206, 540"	MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAKKAVEKPPQTEHIEL	chr16:55802851-55833337[-]	"Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins. Hydrolyzes cellular cholesteryl esters to free cholesterols and promotes reverse cholesterol transport (RCT) by facilitating both the initial and final steps in the process. First of all, allows free cholesterol efflux from macrophages to extracellular cholesterol acceptors and secondly, releases free cholesterol from lipoprotein-delivered cholesteryl esters in the liver for bile acid synthesis or direct secretion into the bile."	PDB: 1MX1; PDB: 1MX5; PDB: 1MX9; PDB: 1YA4; PDB: 1YA8; PDB: 1YAH; PDB: 1YAJ; PDB: 2DQY; PDB: 2DQZ; PDB: 2DR0; PDB: 2H7C; PDB: 2HRQ; PDB: 2HRR; PDB: 3K9B; PDB: 4AB1; PDB: 5A7F; PDB: 5A7G; PDB: 5A7H	HGNC:1863	EST1_HUMAN	Reviewed	ENSG00000198848	.	.	.	.	.
Mol00358	Protein	Cocaine esterase (CES2)	Carboxylesterase 2; CE-2; hCE-2; Methylumbelliferyl-acetate deacetylase 2; ICE	CES2	8824	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000317091.10, CES2-201, 2871; ENST00000417689.6, CES2-202, 3868; ENST00000561697.5, CES2-203, 918; ENST00000564420.1, CES2-206, 862; ENST00000568470.6, CES2-211, 3391; ENST00000570032.2, CES2-212, 739; ENST00000566182.1, CES2-207, 891; ENST00000568347.1, CES2-210, 832; ENST00000566359.1, CES2-208, 500; ENST00000561843.1, CES2-204, 454; ENST00000567128.1, CES2-209, 440; ENST00000563988.1, CES2-205, 371"	MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL	chr16:66934444-66945096[+]	"Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine. Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins."	.	HGNC:1864	EST2_HUMAN	Reviewed	ENSG00000172831	.	.	.	.	.
Mol00359	Protein	Carboxylesterase 4A (CES4A)	CES8; UNQ440/PRO873	CES4A	283848	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000648724.2, CES4A-212, 2476; ENST00000540947.6, CES4A-207, 2284; ENST00000540579.6, CES4A-206, 2124; ENST00000535696.1, CES4A-203, 1472; ENST00000538199.5, CES4A-205, 1958; ENST00000535543.5, CES4A-202, 2178; ENST00000567587.6, CES4A-211, 2062; ENST00000397205.2, CES4A-201, 952; ENST00000543561.1, CES4A-208, 3419; ENST00000535948.1, CES4A-204, 1220; ENST00000544986.1, CES4A-210, 877; ENST00000544478.1, CES4A-209, 740"	MRWILCWSLTLCLMAQTALGALHTKRPQVVTKYGTLQGKQMHVGKTPIQVFLGVPFSRPPLGILRFAPPEPPEPWKGIRDATTYPPGCLQESWGQLASMYVSTRERYKWLRFSEDCLYLNVYAPARAPGDPQLPVMVWFPGGAFIVGAASSYEGSDLAAREKVVLVFLQHRLGIFGFLSTDDSHARGNWGLLDQMAALRWVQENIAAFGGDPGNVTLFGQSAGAMSISGLMMSPLASGLFHRAISQSGTALFRLFITSNPLKVAKKVAHLAGCNHNSTQILVNCLRALSGTKVMRVSNKMRFLQLNFQRDPEEIIWSMSPVVDGVVIPDDPLVLLTQGKVSSVPYLLGVNNLEFNWLLPYIMKFPLNRQAMRKETITKMLWSTRTLLNITKEQVPLVVEEYLDNVNEHDWKMLRNRMMDIVQDATFVYATLQTAHYHRDAGLPVYLYEFEHHARGIIVKPRTDGADHGDEMYFLFGGPFATGLSMGKEKALSLQMMKYWANFARTGNPNDGNLPCWPRYNKDEKYLQLDFTTRVGMKLKEKKMAFWMSLYQSQRPEKQRQF	chr16:66988589-67009758[+]	Probable carboxylesterase.	.	HGNC:26741	EST4A_HUMAN	Reviewed	ENSG00000172824	.	.	.	.	.
Mol00360	Protein	Protein C-ets-1 (ETS1)	p54; EWSR2	ETS1	2113	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000392668.8, ETS1-202, 5139; ENST00000535549.5, ETS1-208, 4594; ENST00000526145.6, ETS1-204, 3389; ENST00000319397.6, ETS1-201, 2231; ENST00000531611.5, ETS1-207, 2134; ENST00000608978.1, ETS1-209, 545; ENST00000525404.5, ETS1-203, 655; ENST00000527676.2, ETS1-205, 628; ENST00000530924.2, ETS1-206, 475"	MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMNGAALCALGKDCFLELAPDFVGDILWEHLEILQKEDVKPYQVNGVNPAYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPLQTDTLQNDYFAIKQEVVTPDNMCMGRTSRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE	chr11:128458761-128587558[-]	"Transcription factor. Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion."	PDB: 1GVJ; PDB: 2NNY; PDB: 2STT; PDB: 2STW; PDB: 3MFK; PDB: 3RI4; PDB: 3WTS; PDB: 3WTT; PDB: 3WTU; PDB: 3WTV; PDB: 3WTW; PDB: 3WTX; PDB: 3WTY; PDB: 3WTZ; PDB: 3WU0; PDB: 3WU1; PDB: 4L0Y; PDB: 4L0Z; PDB: 4L18; PDB: 4LG0; PDB: 5ZMC	HGNC:3488	ETS1_HUMAN	Reviewed	ENSG00000134954	.	.	.	.	.
Mol00361	Protein	Histone-lysine N-methyltransferase EZH1 (EZH1)	ENX-2; Enhancer of zeste homolog 1; KIAA0388	EZH1	2145	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000428826.7, EZH1-202, 4633; ENST00000415827.6, EZH1-201, 4608; ENST00000592743.5, EZH1-222, 2501; ENST00000585893.5, EZH1-205, 2394; ENST00000590078.5, EZH1-217, 2392; ENST00000586382.5, EZH1-209, 1022; ENST00000593214.5, EZH1-224, 745; ENST00000586089.5, EZH1-207, 559; ENST00000592492.5, EZH1-221, 535; ENST00000588897.5, EZH1-215, 2283; ENST00000586867.5, EZH1-211, 1031; ENST00000588239.5, EZH1-214, 819; ENST00000586935.5, EZH1-212, 580; ENST00000590783.5, EZH1-219, 595; ENST00000590082.1, EZH1-218, 565; ENST00000586103.5, EZH1-208, 2752; ENST00000591330.5, EZH1-220, 2387; ENST00000585912.5, EZH1-206, 2295; ENST00000585550.5, EZH1-204, 1643; ENST00000587179.1, EZH1-213, 804; ENST00000589846.1, EZH1-216, 773; ENST00000586714.1, EZH1-210, 594; ENST00000593148.1, EZH1-223, 591; ENST00000585455.1, EZH1-203, 346"	MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGRRRRRHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL	chr17:42700275-42745049[-]	"Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation."	PDB: 7KSO; PDB: 7KSR; PDB: 7KTP	HGNC:3526	EZH1_HUMAN	Reviewed	ENSG00000108799	.	.	.	.	.
Mol00362	Protein	Histone-lysine N-methyltransferase EZH2 (EZH2)	ENX-1; Enhancer of zeste homolog 2; Lysine N-methyltransferase 6; KMT6	EZH2	2146	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000320356.7, EZH2-201, 2654; ENST00000460911.5, EZH2-203, 2591; ENST00000476773.5, EZH2-205, 2572; ENST00000478654.5, EZH2-206, 2522; ENST00000350995.6, EZH2-202, 2477; ENST00000483967.5, EZH2-208, 2466; ENST00000492143.5, EZH2-209, 3641; ENST00000684300.1, EZH2-217, 2961; ENST00000683292.1, EZH2-214, 2909; ENST00000683744.1, EZH2-216, 2707; ENST00000682317.1, EZH2-212, 2535; ENST00000483012.1, EZH2-207, 1491; ENST00000684400.1, EZH2-218, 4502; ENST00000682263.1, EZH2-211, 4367; ENST00000683293.1, EZH2-215, 4189; ENST00000684510.1, EZH2-220, 2860; ENST00000684436.1, EZH2-219, 2684; ENST00000498186.5, EZH2-210, 1876; ENST00000682401.1, EZH2-213, 1732; ENST00000469631.1, EZH2-204, 414"	MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP	chr7:148807257-148884321[-]	"Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription."	PDB: 4MI0; PDB: 4MI5; PDB: 5GSA; PDB: 5H14; PDB: 5H15; PDB: 5H17; PDB: 5H19; PDB: 5H24; PDB: 5H25; PDB: 5HYN; PDB: 5IJ7; PDB: 5IJ8; PDB: 5LS6; PDB: 5U5T; PDB: 5U62; PDB: 5WG6; PDB: 5WUK; PDB: 6C23; PDB: 6C24; PDB: 6LO2; PDB: 6P5L; PDB: 6U4Y; PDB: 6WKR; PDB: 7AT8	HGNC:3527	EZH2_HUMAN	Reviewed	ENSG00000106462	.	.	.	.	.
Mol00363	Protein	Ezrin (EZR)	Cytovillin; Villin-2; p81; VIL2	EZR	7430	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367075.4, EZR-202, 3052; ENST00000337147.11, EZR-201, 3068; ENST00000476189.1, EZR-203, 956"	MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL	chr6:158765741-158819368[-]	"Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis."	PDB: 1NI2; PDB: 4RM8; PDB: 4RM9; PDB: 4RMA	HGNC:12691	EZRI_HUMAN	Reviewed	ENSG00000092820	.	.	.	.	.
Mol00364	Protein	NUP98-DDX10 fusion protein type 1 (NUP98-DDX10 )	PTSG_00124; NUP98-DDX10 fusion protein type 1	PTSG_00124	16067821	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MGRKGNKKQHVADAADADVKEEEVESTPTPQPTPSALPLEATANAGEWERLTHSDGTPLKLDERILTRLRAWKFDQMTPVQAACVPLFLEYKDVAAEAVTGSGKTLAFLIPAVEMLLRTPPKSRMAVGCIVLSPTRELAQQTHHVLSDLLKDSPLTHVLITGGKDAETDIVSMEKHGTNIIVATPGRLNDLIKRVPSLATNIKLLEVFVMDEADRLLDMGFKTTLNEILAVLPKQRRTGLFSATQTKEVELLVRAGLRNPVRVTVAVEDPEMFVHRCGRTARNGLDGNALLYLMPTEDEYVEFLKIRQVPMEEMDAITAAPSQFSAVRTHAANDRDIYEKGRLAFVSYIRSYREHKCNFLLKLSRLDLGMVANGFGLLDLPVMPELKKSKAAANFVPSDVDTSAITFKDKNREKQRQENLKRRGDRTSDPAAKRSKERQKQKNEAWSKQKERKKKKLARATKKQQQEDRKRKKMLENLLETEQEWDELAREVRLRKQLKQGKITQDEFERLVGEDADPVMTM	.	.	.	.	F2TVL2_SALR5	Unreviewed	.	.	.	.	.	.
Mol00366	Protein	Fanconi anemia group D2 protein (FANCD2)	Protein FACD2; FACD	FANCD2	2177	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000675286.1, FANCD2-212, 5096; ENST00000287647.7, FANCD2-201, 5219; ENST00000419585.5, FANCD2-202, 5185; ENST00000676013.1, FANCD2-213, 4334; ENST00000431693.1, FANCD2-204, 2450; ENST00000625535.1, FANCD2-211, 117; ENST00000421731.5, FANCD2-203, 3425; ENST00000682647.1, FANCD2-215, 2145; ENST00000435522.5, FANCD2-205, 567; ENST00000681997.1, FANCD2-214, 3559; ENST00000683263.1, FANCD2-216, 3474; ENST00000438741.1, FANCD2-206, 558; ENST00000470757.5, FANCD2-209, 547; ENST00000470028.1, FANCD2-208, 449; ENST00000683312.1, FANCD2-217, 4010; ENST00000683933.1, FANCD2-218, 836; ENST00000480909.1, FANCD2-210, 603; ENST00000464934.1, FANCD2-207, 563"	MVSKRRLSKSEDKESLTEDASKTRKQPLSKKTKKSHIANEVEENDSIFVKLLKISGIILKTGESQNQLAVDQIAFQKKLFQTLRRHPSYPKIIEEFVSGLESYIEDEDSFRNCLLSCERLQDEEASMGASYSKSLIKLLLGIDILQPAIIKTLFEKLPEYFFENKNSDEINIPRLIVSQLKWLDRVVDGKDLTTKIMQLISIAPENLQHDIITSLPEILGDSQHADVGKELSDLLIENTSLTVPILDVLSSLRLDPNFLLKVRQLVMDKLSSIRLEDLPVIIKFILHSVTAMDTLEVISELREKLDLQHCVLPSRLQASQVKLKSKGRASSSGNQESSGQSCIILLFDVIKSAIRYEKTISEAWIKAIENTASVSEHKVFDLVMLFIIYSTNTQTKKYIDRVLRNKIRSGCIQEQLLQSTFSVHYLVLKDMCSSILSLAQSLLHSLDQSIISFGSLLYKYAFKFFDTYCQQEVVGALVTHICSGNEAEVDTALDVLLELVVLNPSAMMMNAVFVKGILDYLDNISPQQIRKLFYVLSTLAFSKQNEASSHIQDDMHLVIRKQLSSTVFKYKLIGIIGAVTMAGIMAADRSESPSLTQERANLSDEQCTQVTSLLQLVHSCSEQSPQASALYYDEFANLIQHEKLDPKALEWVGHTICNDFQDAFVVDSCVVPEGDFPFPVKALYGLEEYDTQDGIAINLLPLLFSQDFAKDGGPVTSQESGQKLVSPLCLAPYFRLLRLCVERQHNGNLEEIDGLLDCPIFLTDLEPGEKLESMSAKERSFMCSLIFLTLNWFREIVNAFCQETSPEMKGKVLTRLKHIVELQIILEKYLAVTPDYVPPLGNFDVETLDITPHTVTAISAKIRKKGKIERKQKTDGSKTSSSDTLSEEKNSECDPTPSHRGQLNKEFTGKEEKTSLLLHNSHAFFRELDIEVFSILHCGLVTKFILDTEMHTEATEVVQLGPPELLFLLEDLSQKLESMLTPPIARRVPFLKNKGSRNIGFSHLQQRSAQEIVHCVFQLLTPMCNHLENIHNYFQCLAAENHGVVDGPGVKVQEYHIMSSCYQRLLQIFHGLFAWSGFSQPENQNLLYSALHVLSSRLKQGEHSQPLEELLSQSVHYLQNFHQSIPSFQCALYLIRLLMVILEKSTASAQNKEKIASLARQFLCRVWPSGDKEKSNISNDQLHALLCIYLEHTESILKAIEEIAGVGVPELINSPKDASSSTFPTLTRHTFVVFFRVMMAELEKTVKKIEPGTAADSQQIHEEKLLYWNMAVRDFSILINLIKVFDSHPVLHVCLKYGRLFVEAFLKQCMPLLDFSFRKHREDVLSLLETFQLDTRLLHHLCGHSKIHQDTRLTQHVPLLKKTLELLVCRVKAMLTLNNCREAFWLGNLKNRDLQGEEIKSQNSQESTADESEDDMSSQASKSKATEDGEEDEVSAGEKEQDSDESYDDSD	chr3:10026370-10101932[+]	"Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress. Required for the targeting, or stabilization, of BLM to non-centromeric abnormal structures induced by replicative stress. Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be involved in B-cell immunoglobulin isotype switching."	PDB: 6VAA; PDB: 6VAD; PDB: 6VAE; PDB: 6VAF; PDB: 7AY1; PDB: 7KZQ; PDB: 7KZR; PDB: 7KZS; PDB: 7KZT; PDB: 7KZV	HGNC:3585	FACD2_HUMAN	Reviewed	ENSG00000144554	.	.	.	.	.
Mol00367	Protein	Focal adhesion kinase 1 (FAK1)	FADK 1; Focal adhesion kinase-related nonkinase; FRNK; Protein phosphatase 1 regulatory subunit 71; PPP1R71; Protein-tyrosine kinase 2; p125FAK; pp125FAK; FAK; FAK1	PTK2	5747	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000517887.5, PTK2-207, 4661; ENST00000522684.5, PTK2-240, 4955; ENST00000340930.7, PTK2-201, 4414; ENST00000521059.5, PTK2-228, 4405; ENST00000430260.6, PTK2-203, 1940; ENST00000696786.1, PTK2-258, 5136; ENST00000519419.5, PTK2-212, 4439; ENST00000395218.3, PTK2-202, 4415; ENST00000519654.5, PTK2-215, 4129; ENST00000517712.5, PTK2-206, 3351; ENST00000519465.5, PTK2-213, 3279; ENST00000523539.5, PTK2-246, 3236; ENST00000521986.5, PTK2-238, 2393; ENST00000519881.5, PTK2-216, 863; ENST00000523803.5, PTK2-252, 750; ENST00000521562.5, PTK2-233, 678; ENST00000521332.5, PTK2-231, 630; ENST00000523435.1, PTK2-244, 629; ENST00000520045.5, PTK2-219, 602; ENST00000523388.5, PTK2-243, 581; ENST00000519024.5, PTK2-210, 576; ENST00000520828.5, PTK2-223, 574; ENST00000520151.5, PTK2-220, 573; ENST00000520892.5, PTK2-225, 571; ENST00000517453.5, PTK2-205, 571; ENST00000520475.5, PTK2-222, 570; ENST00000522424.5, PTK2-239, 569; ENST00000522950.1, PTK2-241, 548; ENST00000521907.5, PTK2-235, 542; ENST00000521395.5, PTK2-232, 540; ENST00000524357.5, PTK2-257, 535; ENST00000523679.1, PTK2-249, 504; ENST00000524040.5, PTK2-254, 475; ENST00000524257.5, PTK2-256, 430; ENST00000519993.5, PTK2-218, 4388; ENST00000524202.5, PTK2-255, 3014; ENST00000521250.5, PTK2-230, 592; ENST00000521029.5, PTK2-227, 584; ENST00000521791.5, PTK2-234, 556; ENST00000521981.5, PTK2-236, 552; ENST00000523670.5, PTK2-247, 542; ENST00000523067.5, PTK2-242, 488; ENST00000519635.1, PTK2-214, 578; ENST00000523746.5, PTK2-250, 574; ENST00000520460.1, PTK2-221, 572; ENST00000518509.5, PTK2-209, 569; ENST00000523474.5, PTK2-245, 567; ENST00000519361.5, PTK2-211, 553; ENST00000521985.1, PTK2-237, 538; ENST00000521172.1, PTK2-229, 507; ENST00000523805.5, PTK2-253, 440; ENST00000520843.5, PTK2-224, 438; ENST00000523797.1, PTK2-251, 405; ENST00000519899.5, PTK2-217, 762; ENST00000520917.1, PTK2-226, 653; ENST00000523675.1, PTK2-248, 650; ENST00000510126.2, PTK2-204, 580; ENST00000518173.5, PTK2-208, 441"	MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH	chr8:140657900-141002216[-]	"Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription."	PDB: 1K04; PDB: 1K05; PDB: 1MP8; PDB: 1OW6; PDB: 1OW7; PDB: 1OW8; PDB: 2ETM; PDB: 2IJM; PDB: 3B71; PDB: 3BZ3; PDB: 3PXK; PDB: 3S9O; PDB: 4EBV; PDB: 4EBW; PDB: 4GU6; PDB: 4GU9; PDB: 4I4E; PDB: 4I4F; PDB: 4K8A; PDB: 4K9Y; PDB: 4KAB; PDB: 4KAO; PDB: 4NY0; PDB: 4Q9S; PDB: 6I8Z; PDB: 6LES; PDB: 6PW8; PDB: 6YOJ; PDB: 6YQ1; PDB: 6YR9; PDB: 6YT6; PDB: 6YVS; PDB: 6YVY; PDB: 6YXV; PDB: 7PI4	HGNC:9611	FAK1_HUMAN	Reviewed	ENSG00000169398	.	.	.	.	.
Mol00368	Protein	Fanconi anemia group A protein (FANCA)	Protein FACA; FAA; FACA; FANCH	FANCA	2175	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000389301.8, FANCA-202, 5452; ENST00000568369.6, FANCA-230, 5464; ENST00000389302.7, FANCA-203, 1641; ENST00000543736.5, FANCA-205, 1000; ENST00000564475.6, FANCA-215, 4686; ENST00000696287.1, FANCA-238, 4557; ENST00000563673.5, FANCA-213, 1694; ENST00000696294.1, FANCA-243, 1426; ENST00000696295.1, FANCA-244, 1423; ENST00000534992.5, FANCA-204, 1088; ENST00000567879.5, FANCA-226, 713; ENST00000561722.5, FANCA-208, 696; ENST00000564870.1, FANCA-216, 460; ENST00000696275.1, FANCA-234, 4815; ENST00000561667.2, FANCA-207, 6113; ENST00000696291.1, FANCA-240, 4969; ENST00000696286.1, FANCA-237, 4422; ENST00000567510.2, FANCA-224, 3025; ENST00000567205.2, FANCA-222, 2772; ENST00000696292.1, FANCA-241, 1818; ENST00000696288.1, FANCA-239, 1699; ENST00000696277.1, FANCA-236, 1596; ENST00000696293.1, FANCA-242, 1482; ENST00000567621.6, FANCA-225, 1184; ENST00000567988.5, FANCA-229, 915; ENST00000696296.1, FANCA-245, 909; ENST00000567943.1, FANCA-228, 860; ENST00000565582.5, FANCA-218, 812; ENST00000561660.1, FANCA-206, 762; ENST00000568626.1, FANCA-231, 727; ENST00000563510.5, FANCA-211, 633; ENST00000563318.1, FANCA-210, 605; ENST00000563513.1, FANCA-212, 571; ENST00000566409.1, FANCA-220, 395; ENST00000696276.1, FANCA-235, 3025; ENST00000567284.7, FANCA-223, 2499; ENST00000696274.1, FANCA-233, 4600; ENST00000566889.5, FANCA-221, 2201; ENST00000563767.2, FANCA-214, 1633; ENST00000305699.15, FANCA-201, 1430; ENST00000568983.6, FANCA-232, 917; ENST00000564969.5, FANCA-217, 850; ENST00000566133.1, FANCA-219, 761; ENST00000562424.1, FANCA-209, 745; ENST00000567883.5, FANCA-227, 650"	MSDSWVPNSASGQDPGGRRRAWAELLAGRVKREKYNPERAQKLKESAVRLLRSHQDLNALLLEVEGPLCKKLSLSKVIDCDSSEAYANHSSSFIGSALQDQASRLGVPVGILSAGMVASSVGQICTAPAETSHPVLLTVEQRKKLSSLLEFAQYLLAHSMFSRLSFCQELWKIQSSLLLEAVWHLHVQGIVSLQELLESHPDMHAVGSWLFRNLCCLCEQMEASCQHADVARAMLSDFVQMFVLRGFQKNSDLRRTVEPEKMPQVTVDVLQRMLIFALDALAAGVQEESSTHKIVRCWFGVFSGHTLGSVISTDPLKRFFSHTLTQILTHSPVLKASDAVQMQREWSFARTHPLLTSLYRRLFVMLSAEELVGHLQEVLETQEVHWQRVLSFVSALVVCFPEAQQLLEDWVARLMAQAFESCQLDSMVTAFLVVRQAALEGPSAFLSYADWFKASFGSTRGYHGCSKKALVFLFTFLSELVPFESPRYLQVHILHPPLVPGKYRSLLTDYISLAKTRLADLKVSIENMGLYEDLSSAGDITEPHSQALQDVEKAIMVFEHTGNIPVTVMEASIFRRPYYVSHFLPALLTPRVLPKVPDSRVAFIESLKRADKIPPSLYSTYCQACSAAEEKPEDAALGVRAEPNSAEEPLGQLTAALGELRASMTDPSQRDVISAQVAVISERLRAVLGHNEDDSSVEISKIQLSINTPRLEPREHMAVDLLLTSFCQNLMAASSVAPPERQGPWAALFVRTMCGRVLPAVLTRLCQLLRHQGPSLSAPHVLGLAALAVHLGESRSALPEVDVGPPAPGAGLPVPALFDSLLTCRTRDSLFFCLKFCTAAISYSLCKFSSQSRDTLCSCLSPGLIKKFQFLMFRLFSEARQPLSEEDVASLSWRPLHLPSADWQRAALSLWTHRTFREVLKEEDVHLTYQDWLHLELEIQPEADALSDTERQDFHQWAIHEHFLPESSASGGCDGDLQAACTILVNALMDFHQSSRSYDHSENSDLVFGGRTGNEDIISRLQEMVADLELQQDLIVPLGHTPSQEHFLFEIFRRRLQALTSGWSVAASLQRQRELLMYKRILLRLPSSVLCGSSFQAEQPITARCEQFFHLVNSEMRNFCSHGGALTQDITAHFFRGLLNACLRSRDPSLMVDFILAKCQTKCPLILTSALVWWPSLEPVLLCRWRRHCQSPLPRELQKLQEGRQFASDFLSPEAASPAPNPDWLSAAALHFAIQQVREENIRKQLKKLDCEREELLVFLFFFSLMGLLSSHLTSNSTTDLPKAFHVCAAILECLEKRKISWLALFQLTESDLRLGRLLLRVAPDQHTRLLPFAFYSLLSYFHEDAAIREEAFLHVAVDMYLKLVQLFVAGDTSTVSPPAGRSLELKGQGNPVELITKARLFLLQLIPRCPKKSFSHVAELLADRGDCDPEVSAALQSRQQAAPDADLSQEPHLF	chr16:89726683-89816977[-]	DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability.	PDB: 7KZP; PDB: 7KZQ; PDB: 7KZR; PDB: 7KZS; PDB: 7KZT; PDB: 7KZV	HGNC:3582	FANCA_HUMAN	Reviewed	ENSG00000187741	.	.	.	.	.
Mol00369	Protein	Protocadherin Fat 1 (FAT1)	Cadherin family member 7; Cadherin-related tumor suppressor homolog; Protein fat homolog; CDHF7; FAT	FAT1	2195	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000441802.7, FAT1-201, 14776; ENST00000509647.1, FAT1-208, 1852; ENST00000512772.5, FAT1-211, 1305; ENST00000507105.1, FAT1-204, 854; ENST00000509927.1, FAT1-209, 357; ENST00000509537.1, FAT1-207, 479; ENST00000512347.1, FAT1-210, 512; ENST00000507662.1, FAT1-205, 428; ENST00000500085.2, FAT1-202, 2224; ENST00000503253.1, FAT1-203, 462; ENST00000508035.1, FAT1-206, 341"	MGRHLALLLLLLLLFQHFGDSDGSQRLEQTPLQFTHLEYNVTVQENSAAKTYVGHPVKMGVYITHPAWEVRYKIVSGDSENLFKAEEYILGDFCFLRIRTKGGNTAILNREVKDHYTLIVKALEKNTNVEARTKVRVQVLDTNDLRPLFSPTSYSVSLPENTAIRTSIARVSATDADIGTNGEFYYSFKDRTDMFAIHPTSGVIVLTGRLDYLETKLYEMEILAADRGMKLYGSSGISSMAKLTVHIEQANECAPVITAVTLSPSELDRDPAYAIVTVDDCDQGANGDIASLSIVAGDLLQQFRTVRSFPGSKEYKVKAIGGIDWDSHPFGYNLTLQAKDKGTPPQFSSVKVIHVTSPQFKAGPVKFEKDVYRAEISEFAPPNTPVVMVKAIPAYSHLRYVFKSTPGKAKFSLNYNTGLISILEPVKRQQAAHFELEVTTSDRKASTKVLVKVLGANSNPPEFTQTAYKAAFDENVPIGTTVMSLSAVDPDEGENGYVTYSIANLNHVPFAIDHFTGAVSTSENLDYELMPRVYTLRIRASDWGLPYRREVEVLATITLNNLNDNTPLFEKINCEGTIPRDLGVGEQITTVSAIDADELQLVQYQIEAGNELDFFSLNPNSGVLSLKRSLMDGLGAKVSFHSLRITATDGENFATPLYINITVAASHKLVNLQCEETGVAKMLAEKLLQANKLHNQGEVEDIFFDSHSVNAHIPQFRSTLPTGIQVKENQPVGSSVIFMNSTDLDTGFNGKLVYAVSGGNEDSCFMIDMETGMLKILSPLDRETTDKYTLNITVYDLGIPQKAAWRLLHVVVVDANDNPPEFLQESYFVEVSEDKEVHSEIIQVEATDKDLGPNGHVTYSIVTDTDTFSIDSVTGVVNIARPLDRELQHEHSLKIEARDQAREEPQLFSTVVVKVSLEDVNDNPPTFIPPNYRVKVREDLPEGTVIMWLEAHDPDLGQSGQVRYSLLDHGEGNFDVDKLSGAVRIVQQLDFEKKQVYNLTVRAKDKGKPVSLSSTCYVEVEVVDVNENLHPPVFSSFVEKGTVKEDAPVGSLVMTVSAHDEDARRDGEIRYSIRDGSGVGVFKIGEETGVIETSDRLDRESTSHYWLTVFATDQGVVPLSSFIEIYIEVEDVNDNAPQTSEPVYYPEIMENSPKDVSVVQIEAFDPDSSSNDKLMYKITSGNPQGFFSIHPKTGLITTTSRKLDREQQDEHILEVTVTDNGSPPKSTIARVIVKILDENDNKPQFLQKFYKIRLPEREKPDRERNARREPLYHVIATDKDEGPNAEISYSIEDGNEHGKFFIEPKTGVVSSKRFSAAGEYDILSIKAVDNGRPQKSSTTRLHIEWISKPKPSLEPISFEESFFTFTVMESDPVAHMIGVISVEPPGIPLWFDITGGNYDSHFDVDKGTGTIIVAKPLDAEQKSNYNLTVEATDGTTTILTQVFIKVIDTNDHRPQFSTSKYEVVIPEDTAPETEILQISAVDQDEKNKLIYTLQSSRDPLSLKKFRLDPATGSLYTSEKLDHEAVHQHTLTVMVRDQDVPVKRNFARIVVNVSDTNDHAPWFTASSYKGRVYESAAVGSVVLQVTALDKDKGKNAEVLYSIESGNIGNSFMIDPVLGSIKTAKELDRSNQAEYDLMVKATDKGSPPMSEITSVRIFVTIADNASPKFTSKEYSVELSETVSIGSFVGMVTAHSQSSVVYEIKDGNTGDAFDINPHSGTIITQKALDFETLPIYTLIIQGTNMAGLSTNTTVLVHLQDENDNAPVFMQAEYTGLISESASINSVVLTDRNVPLVIRAADADKDSNALLVYHIVEPSVHTYFAIDSSTGAIHTVLSLDYEETSIFHFTVQVHDMGTPRLFAEYAANVTVHVIDINDCPPVFAKPLYEASLLLPTYKGVKVITVNATDADSSAFSQLIYSITEGNIGEKFSMDYKTGALTVQNTTQLRSRYELTVRASDGRFAGLTSVKINVKESKESHLKFTQDVYSAVVKENSTEAETLAVITAIGNPINEPLFYHILNPDRRFKISRTSGVLSTTGTPFDREQQEAFDVVVEVTEEHKPSAVAHVVVKVIVEDQNDNAPVFVNLPYYAVVKVDTEVGHVIRYVTAVDRDSGRNGEVHYYLKEHHEHFQIGPLGEISLKKQFELDTLNKEYLVTVVAKDGGNPAFSAEVIVPITVMNKAMPVFEKPFYSAEIAESIQVHSPVVHVQANSPEGLKVFYSITDGDPFSQFTINFNTGVINVIAPLDFEAHPAYKLSIRATDSLTGAHAEVFVDIIVDDINDNPPVFAQQSYAVTLSEASVIGTSVVQVRATDSDSEPNRGISYQMFGNHSKSHDHFHVDSSTGLISLLRTLDYEQSRQHTIFVRAVDGGMPTLSSDVIVTVDVTDLNDNPPLFEQQIYEARISEHAPHGHFVTCVKAYDADSSDIDKLQYSILSGNDHKHFVIDSATGIITLSNLHRHALKPFYSLNLSVSDGVFRSSTQVHVTVIGGNLHSPAFLQNEYEVELAENAPLHTLVMEVKTTDGDSGIYGHVTYHIVNDFAKDRFYINERGQIFTLEKLDRETPAEKVISVRLMAKDAGGKVAFCTVNVILTDDNDNAPQFRATKYEVNIGSSAAKGTSVVKVLASDADEGSNADITYAIEADSESVKENLEINKLSGVITTKESLIGLENEFFTFFVRAVDNGSPSKESVVLVYVKILPPEMQLPKFSEPFYTFTVSEDVPIGTEIDLIRAEHSGTVLYSLVKGNTPESNRDESFVIDRQSGRLKLEKSLDHETTKWYQFSILARCTQDDHEMVASVDVSIQVKDANDNSPVFESSPYEAFIVENLPGGSRVIQIRASDADSGTNGQVMYSLDQSQSVEVIESFAINMETGWITTLKELDHEKRDNYQIKVVASDHGEKIQLSSTAIVDVTVTDVNDSPPRFTAEIYKGTVSEDDPQGGVIAILSTTDADSEEINRQVTYFITGGDPLGQFAVETIQNEWKVYVKKPLDREKRDNYLLTITATDGTFSSKAIVEVKVLDANDNSPVCEKTLYSDTIPEDVLPGKLIMQISATDADIRSNAEITYTLLGSGAEKFKLNPDTGELKTSTPLDREEQAVYHLLVRATDGGGRFCQASIVLTLEDVNDNAPEFSADPYAITVFENTEPGTLLTRVQATDADAGLNRKILYSLIDSADGQFSINELSGIIQLEKPLDRELQAVYTLSLKAVDQGLPRRLTATGTVIVSVLDINDNPPVFEYREYGATVSEDILVGTEVLQVYAASRDIEANAEITYSIISGNEHGKFSIDSKTGAVFIIENLDYESSHEYYLTVEATDGGTPSLSDVATVNVNVTDINDNTPVFSQDTYTTVISEDAVLEQSVITVMADDADGPSNSHIHYSIIDGNQGSSFTIDPVRGEVKVTKLLDRETISGYTLTVQASDNGSPPRVNTTTVNIDVSDVNDNAPVFSRGNYSVIIQENKPVGFSVLQLVVTDEDSSHNGPPFFFTIVTGNDEKAFEVNPQGVLLTSSAIKRKEKDHYLLQVKVADNGKPQLSSLTYIDIRVIEESIYPPAILPLEIFITSSGEEYSGGVIGKIHATDQDVYDTLTYSLDPQMDNLFSVSSTGGKLIAHKKLDIGQYLLNVSVTDGKFTTVADITVHIRQVTQEMLNHTIAIRFANLTPEEFVGDYWRNFQRALRNILGVRRNDIQIVSLQSSEPHPHLDVLLFVEKPGSAQISTKQLLHKINSSVTDIEEIIGVRILNVFQKLCAGLDCPWKFCDEKVSVDESVMSTHSTARLSFVTPRHHRAAVCLCKEGRCPPVHHGCEDDPCPEGSECVSDPWEEKHTCVCPSGRFGQCPGSSSMTLTGNSYVKYRLTENENKLEMKLTMRLRTYSTHAVVMYARGTDYSILEIHHGRLQYKFDCGSGPGIVSVQSIQVNDGQWHAVALEVNGNYARLVLDQVHTASGTAPGTLKTLNLDNYVFFGGHIRQQGTRHGRSPQVGNGFRGCMDSIYLNGQELPLNSKPRSYAHIEESVDVSPGCFLTATEDCASNPCQNGGVCNPSPAGGYYCKCSALYIGTHCEISVNPCSSKPCLYGGTCVVDNGGFVCQCRGLYTGQRCQLSPYCKDEPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECSGNPCLHGALCENTHGSYHCNCSHEYRGRHCEDAAPNQYVSTPWNIGLAEGIGIVVFVAGIFLLVVVFVLCRKMISRKKKHQAEPKDKHLGPATAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESVHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDTKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEVIDEQTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAADELPPLPPEFSNQFESIHPPRDMPAAGSLGSSSRNRQRFNLNQYLPNFYPLDMSEPQTKGTGENSTCREPHAPYPPGYQRHFEAPAVESMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV	chr4:186587794-186726722[-]	"[Protocadherin Fat 1]: Plays an essential role for cellular polarization, directed cell migration and modulating cell-cell contact."	.	HGNC:3595	FAT1_HUMAN	Reviewed	ENSG00000083857	.	.	.	.	.
Mol00370	Protein	Fibroblast growth factor 2 (FGF1)	FGF-2; Basic fibroblast growth factor; bFGF; Heparin-binding growth factor 2; HBGF-2; FGFB	FGF2	2247	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000644866.2, FGF2-203, 6652; ENST00000264498.8, FGF2-201, 6775; ENST00000608478.1, FGF2-202, 3880"	MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRTEERPSGSRLGDRGRGRALPGGRLGGRGRGRAPERVGGRGRGRGTAAPRAAPAARGSRPGPAGTMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS	chr4:122826708-122898236[+]	"Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4. Also acts as an integrin ligand which is required for FGF2 signaling. Binds to integrin ITGAV:ITGB3. Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Can induce angiogenesis. Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation."	PDB: 1BAS; PDB: 1BFB; PDB: 1BFC; PDB: 1BFF; PDB: 1BFG; PDB: 1BLA; PDB: 1BLD; PDB: 1CVS; PDB: 1EV2; PDB: 1FGA; PDB: 1FQ9; PDB: 1II4; PDB: 1IIL; PDB: 2BFH; PDB: 2FGF; PDB: 2M49; PDB: 4FGF; PDB: 4OEE; PDB: 4OEF; PDB: 4OEG; PDB: 5X1O; PDB: 6L4O	HGNC:3676	FGF2_HUMAN	Reviewed	ENSG00000138685	.	.	.	.	.
Mol00371	Protein	Fibroblast growth factor receptor 1 (FGFR1)	.	FGFR1	2260	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000447712.7, FGFR1-214, 5697; ENST00000397091.9, FGFR1-206, 5702; ENST00000532791.5, FGFR1-238, 5590; ENST00000335922.9, FGFR1-202, 4157; ENST00000356207.9, FGFR1-204, 3824; ENST00000326324.10, FGFR1-201, 3816; ENST00000397113.6, FGFR1-209, 3680; ENST00000397108.8, FGFR1-208, 2870; ENST00000341462.9, FGFR1-203, 4442; ENST00000683765.1, FGFR1-253, 4135; ENST00000683815.1, FGFR1-255, 4094; ENST00000684654.1, FGFR1-257, 3827; ENST00000425967.8, FGFR1-211, 3352; ENST00000397103.5, FGFR1-207, 2953; ENST00000525001.5, FGFR1-226, 1155; ENST00000529552.5, FGFR1-233, 688; ENST00000526742.5, FGFR1-229, 657; ENST00000413133.6, FGFR1-210, 587; ENST00000533668.5, FGFR1-241, 571; ENST00000434187.5, FGFR1-212, 529; ENST00000530568.5, FGFR1-234, 467; ENST00000440174.1, FGFR1-213, 389; ENST00000649678.1, FGFR1-243, 6216; ENST00000619564.3, FGFR1-242, 5482; ENST00000674380.1, FGFR1-247, 5002; ENST00000674189.1, FGFR1-244, 3309; ENST00000487647.5, FGFR1-222, 1608; ENST00000674235.1, FGFR1-246, 1071; ENST00000531196.5, FGFR1-236, 842; ENST00000484370.5, FGFR1-221, 826; ENST00000496629.1, FGFR1-224, 584; ENST00000526688.1, FGFR1-228, 570; ENST00000527203.5, FGFR1-231, 556; ENST00000480571.1, FGFR1-220, 442; ENST00000533301.1, FGFR1-239, 377; ENST00000530701.1, FGFR1-235, 276; ENST00000526570.5, FGFR1-227, 5528; ENST00000674474.1, FGFR1-248, 4711; ENST00000683948.1, FGFR1-256, 4057; ENST00000524528.2, FGFR1-225, 4028; ENST00000683276.1, FGFR1-252, 2714; ENST00000683795.1, FGFR1-254, 2427; ENST00000682398.1, FGFR1-249, 2369; ENST00000470826.5, FGFR1-217, 2281; ENST00000674217.1, FGFR1-245, 2011; ENST00000683132.1, FGFR1-251, 1976; ENST00000496296.5, FGFR1-223, 1898; ENST00000527114.5, FGFR1-230, 1499; ENST00000682770.1, FGFR1-250, 947; ENST00000466021.5, FGFR1-216, 823; ENST00000527745.3, FGFR1-232, 790; ENST00000397090.4, FGFR1-205, 777; ENST00000474970.1, FGFR1-218, 764; ENST00000532386.5, FGFR1-237, 725; ENST00000464163.1, FGFR1-215, 545; ENST00000533619.5, FGFR1-240, 540; ENST00000475621.1, FGFR1-219, 485"	MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR	chr8:38400215-38468834[-]	"Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation."	PDB: 1AGW; PDB: 1CVS; PDB: 1EVT; PDB: 1FGI; PDB: 1FGK; PDB: 1FQ9; PDB: 1XR0; PDB: 2CR3; PDB: 2FGI; PDB: 3C4F; PDB: 3DPK; PDB: 3GQI; PDB: 3GQL; PDB: 3JS2; PDB: 3KRJ; PDB: 3KRL; PDB: 3KXX; PDB: 3KY2; PDB: 3OJV; PDB: 3RHX; PDB: 3TT0; PDB: 4F63; PDB: 4F64; PDB: 4F65; PDB: 4NK9; PDB: 4NKA; PDB: 4NKS; PDB: 4RWI; PDB: 4RWJ; PDB: 4RWK; PDB: 4RWL; PDB: 4UWB; PDB: 4UWC; PDB: 4UWY; PDB: 4V01; PDB: 4V04; PDB: 4V05; PDB: 4WUN; PDB: 4ZSA; PDB: 5A46; PDB: 5A4C; PDB: 5AM6; PDB: 5AM7; PDB: 5B7V; PDB: 5EW8; PDB: 5FLF; PDB: 5O49; PDB: 5O4A; PDB: 5UQ0; PDB: 5UR1; PDB: 5VND; PDB: 5W21; PDB: 5W59; PDB: 5Z0S; PDB: 5ZV2; PDB: 6C18; PDB: 6C19; PDB: 6C1B; PDB: 6C1C; PDB: 6C1O; PDB: 6ITJ; PDB: 6MZQ; PDB: 6MZW; PDB: 6NVL; PDB: 6P68; PDB: 6P69	HGNC:3688	FGFR1_HUMAN	Reviewed	ENSG00000077782	.	.	.	.	.
Mol00372	Protein	Fibroblast growth factor receptor 2 (FGFR2)	.	FGFR2	2263	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000358487.10, FGFR2-206, 4624; ENST00000683211.1, FGFR2-235, 6964; ENST00000351936.11, FGFR2-203, 4761; ENST00000613048.4, FGFR2-224, 4369; ENST00000478859.5, FGFR2-218, 3990; ENST00000682550.1, FGFR2-230, 3887; ENST00000369061.8, FGFR2-213, 3803; ENST00000357555.9, FGFR2-205, 3690; ENST00000356226.8, FGFR2-204, 3547; ENST00000369060.8, FGFR2-212, 3244; ENST00000457416.6, FGFR2-215, 3061; ENST00000360144.7, FGFR2-208, 3001; ENST00000369056.5, FGFR2-209, 2650; ENST00000346997.6, FGFR2-202, 2472; ENST00000684153.1, FGFR2-240, 4251; ENST00000682772.1, FGFR2-231, 3638; ENST00000683035.1, FGFR2-234, 3615; ENST00000638709.2, FGFR2-227, 3290; ENST00000369059.5, FGFR2-211, 3003; ENST00000369058.7, FGFR2-210, 2727; ENST00000336553.10, FGFR2-201, 2593; ENST00000359354.6, FGFR2-207, 1680; ENST00000429361.5, FGFR2-214, 1138; ENST00000613324.4, FGFR2-225, 579; ENST00000611527.1, FGFR2-223, 435; ENST00000636922.1, FGFR2-226, 587; ENST00000683250.1, FGFR2-236, 5108; ENST00000604236.5, FGFR2-222, 3501; ENST00000682904.1, FGFR2-232, 2796; ENST00000490349.5, FGFR2-219, 1478; ENST00000491111.1, FGFR2-220, 574; ENST00000467584.1, FGFR2-217, 497; ENST00000463870.5, FGFR2-216, 386; ENST00000683418.1, FGFR2-237, 6317; ENST00000684516.1, FGFR2-241, 4989; ENST00000683029.1, FGFR2-233, 3969; ENST00000682296.1, FGFR2-228, 3318; ENST00000683885.1, FGFR2-239, 1838; ENST00000683678.1, FGFR2-238, 1191; ENST00000682400.1, FGFR2-229, 846; ENST00000491475.1, FGFR2-221, 730"	MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT	chr10:121478332-121598458[-]	"Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1."	PDB: 1DJS; PDB: 1E0O; PDB: 1EV2; PDB: 1GJO; PDB: 1II4; PDB: 1IIL; PDB: 1NUN; PDB: 1OEC; PDB: 1WVZ; PDB: 2FDB; PDB: 2PSQ; PDB: 2PVF; PDB: 2PVY; PDB: 2PWL; PDB: 2PY3; PDB: 2PZ5; PDB: 2PZP; PDB: 2PZR; PDB: 2Q0B; PDB: 3B2T; PDB: 3CAF; PDB: 3CLY; PDB: 3CU1; PDB: 3DAR; PDB: 3EUU; PDB: 3OJ2; PDB: 3OJM; PDB: 3RI1; PDB: 4J23; PDB: 4J95; PDB: 4J96; PDB: 4J97; PDB: 4J98; PDB: 4J99; PDB: 4WV1; PDB: 5EG3; PDB: 5UGL; PDB: 5UGX; PDB: 5UHN; PDB: 5UI0; PDB: 6AGX; PDB: 6LVK; PDB: 6LVL; PDB: 6V6Q; PDB: 7KIA; PDB: 7KIE	HGNC:3689	FGFR2_HUMAN	Reviewed	ENSG00000066468	.	.	.	.	.
Mol00373	Protein	Fibronectin (FN1)	FN; Cold-insoluble globulin; CIG; FN	FN1	2335	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354785.11, FN1-203, 8390; ENST00000323926.10, FN1-201, 8708; ENST00000336916.8, FN1-202, 8435; ENST00000421182.5, FN1-207, 8103; ENST00000446046.5, FN1-212, 7952; ENST00000357867.8, FN1-205, 7898; ENST00000356005.8, FN1-204, 7846; ENST00000443816.5, FN1-211, 7762; ENST00000432072.6, FN1-209, 7759; ENST00000426059.1, FN1-208, 2388; ENST00000359671.5, FN1-206, 8524; ENST00000456923.5, FN1-213, 3720; ENST00000438981.1, FN1-210, 723; ENST00000490833.5, FN1-223, 699; ENST00000492816.6, FN1-224, 9171; ENST00000498719.1, FN1-227, 2433; ENST00000474036.1, FN1-219, 1058; ENST00000460217.1, FN1-214, 804; ENST00000496542.1, FN1-226, 695; ENST00000494446.1, FN1-225, 676; ENST00000469569.1, FN1-216, 629; ENST00000485567.1, FN1-222, 584; ENST00000480024.1, FN1-220, 576; ENST00000461974.1, FN1-215, 571; ENST00000473614.1, FN1-218, 568; ENST00000471193.1, FN1-217, 496; ENST00000480737.1, FN1-221, 384"	MLRGPGPGLLLLAVQCLGTAVPSTGASKSKRQAQQMVQPQSPVAVSQSKPGCYDNGKHYQINQQWERTYLGNALVCTCYGGSRGFNCESKPEAEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDHAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSVQTTSSGSGPFTDVRAAVYQPQPHPQPPPYGHCVTDSGVVYSVGMQWLKTQGNKQMLCTCLGNGVSCQETAVTQTYGGNSNGEPCVLPFTYNGRTFYSCTTEGRQDGHLWCSTTSNYEQDQKYSFCTDHTVLVQTRGGNSNGALCHFPFLYNNHNYTDCTSEGRRDNMKWCGTTQNYDADQKFGFCPMAAHEEICTTNEGVMYRIGDQWDKQHDMGHMMRCTCVGNGRGEWTCIAYSQLRDQCIVDDITYNVNDTFHKRHEEGHMLNCTCFGQGRGRWKCDPVDQCQDSETGTFYQIGDSWEKYVHGVRYQCYCYGRGIGEWHCQPLQTYPSSSGPVEVFITETPSQPNSHPIQWNAPQPSHISKYILRWRPKNSVGRWKEATIPGHLNSYTIKGLKPGVVYEGQLISIQQYGHQEVTRFDFTTTSTSTPVTSNTVTGETTPFSPLVATSESVTEITASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDTTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPRDLQFVEVTDVKVTIMWTPPESAVTGYRVDVIPVNLPGEHGQRLPISRNTFAEVTGLSPGVTYYFKVFAVSHGRESKPLTAQQTTKLDAPTNLQFVNETDSTVLVRWTPPRAQITGYRLTVGLTRRGQPRQYNVGPSVSKYPLRNLQPASEYTVSLVAIKGNQESPKATGVFTTLQPGSSIPPYNTEVTETTIVITWTPAPRIGFKLGVRPSQGGEAPREVTSDSGSIVVSGLTPGVEYVYTIQVLRDGQERDAPIVNKVVTPLSPPTNLHLEANPDTGVLTVSWERSTTPDITGYRITTTPTNGQQGNSLEEVVHADQSSCTFDNLSPGLEYNVSVYTVKDDKESVPISDTIIPEVPQLTDLSFVDITDSSIGLRWTPLNSSTIIGYRITVVAAGEGIPIFEDFVDSSVGYYTVTGLEPGIDYDISVITLINGGESAPTTLTQQTAVPPPTDLRFTNIGPDTMRVTWAPPPSIDLTNFLVRYSPVKNEEDVAELSISPSDNAVVLTNLLPGTEYVVSVSSVYEQHESTPLRGRQKTGLDSPTGIDFSDITANSFTVHWIAPRATITGYRIRHHPEHFSGRPREDRVPHSRNSITLTNLTPGTEYVVSIVALNGREESPLLIGQQSTVSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIDKPSQMQVTDVQDNSISVKWLPSSSPVTGYRVTTTPKNGPGPTKTKTAGPDQTEMTIEGLQPTVEYVVSVYAQNPSGESQPLVQTAVTNIDRPKGLAFTDVDVDSIKIAWESPQGQVSRYRVTYSSPEDGIHELFPAPDGEEDTAELQGLRPGSEYTVSVVALHDDMESQPLIGTQSTAIPAPTDLKFTQVTPTSLSAQWTPPNVQLTGYRVRVTPKEKTGPMKEINLAPDSSSVVVSGLMVATKYEVSVYALKDTLTSRPAQGVVTTLENVSPPRRARVTDATETTITISWRTKTETITGFQVDAVPANGQTPIQRTIKPDVRSYTITGLQPGTDYKIYLYTLNDNARSSPVVIDASTAIDAPSNLRFLATTPNSLLVSWQPPRARITGYIIKYEKPGSPPREVVPRPRPGVTEATITGLEPGTEYTIYVIALKNNQKSEPLIGRKKTDELPQLVTLPHPNLHGPEILDVPSTVQKTPFVTHPGYDTGNGIQLPGTSGQQPSVGQQMIFEEHGFRRTTPPTTATPIRHRPRPYPPNVGEEIQIGHIPREDVDYHLYPHGPGLNPNASTGQEALSQTTISWAPFQDTSEYIISCHPVGTDEEPLQFRVPGTSTSATLTGLTRGATYNVIVEALKDQQRHKVREEVVTVGNSVNEGLNQPTDDSCFDPYTVSHYAVGDEWERMSESGFKLLCQCLGFGSGHFRCDSSRWCHDNGVNYKIGEKWDRQGENGQMMSCTCLGNGKGEFKCDPHEATCYDDGKTYHVGEQWQKEYLGAICSCTCFGGQRGWRCDNCRRPGGEPSPEGTTGQSYNQYSQRYHQRTNTNVNCPIECFMPLDVQADREDSRE	chr2:215360440-215436073[-]	"Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. Acts as a ligand for the LILRB4 receptor, inhibiting FCGR1A/CD64-mediated monocyte activation."	PDB: 1E88; PDB: 1E8B; PDB: 1FBR; PDB: 1FNA; PDB: 1FNF; PDB: 1FNH; PDB: 1J8K; PDB: 1O9A; PDB: 1OWW; PDB: 1Q38; PDB: 1QGB; PDB: 1QO6; PDB: 1TTF; PDB: 1TTG; PDB: 2CG6; PDB: 2CG7; PDB: 2CK2; PDB: 2CKU; PDB: 2EC3; PDB: 2FN2; PDB: 2FNB; PDB: 2GEE; PDB: 2H41; PDB: 2H45; PDB: 2HA1; PDB: 2MNU; PDB: 2N1K; PDB: 2OCF; PDB: 2RKY; PDB: 2RKZ; PDB: 2RL0; PDB: 3CAL; PDB: 3EJH; PDB: 3GXE; PDB: 3M7P; PDB: 3MQL; PDB: 3R8Q; PDB: 3T1W; PDB: 3ZRZ; PDB: 4GH7; PDB: 4JE4; PDB: 4JEG; PDB: 4LXO; PDB: 4MMX; PDB: 4MMY; PDB: 4MMZ; PDB: 4PZ5; PDB: 5DC0; PDB: 5DC4; PDB: 5DC9; PDB: 5DFT; PDB: 5J6Z; PDB: 5J7C; PDB: 5M0A; PDB: 5N47; PDB: 5N48; PDB: 6HNF; PDB: 6MFA; PDB: 6MSV; PDB: 6NAJ; PDB: 6XAX; PDB: 6XAY; PDB: 7NWL	HGNC:3778	FINC_HUMAN	Reviewed	ENSG00000115414	.	.	.	.	.
Mol00374	Protein	Mitochondrial fission 1 protein (FIS1)	FIS1 homolog; hFis1; Tetratricopeptide repeat protein 11; TPR repeat protein 11; TTC11; CGI-135	FIS1	51024	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000223136.5, FIS1-201, 870; ENST00000474120.5, FIS1-207, 915; ENST00000435848.1, FIS1-202, 692; ENST00000442303.1, FIS1-203, 631; ENST00000473527.5, FIS1-206, 1005; ENST00000449367.5, FIS1-204, 745; ENST00000482199.5, FIS1-209, 731; ENST00000480497.1, FIS1-208, 530; ENST00000463406.5, FIS1-205, 527"	MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEYAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS	chr7:101239458-101252316[-]	"Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission."	PDB: 1NZN; PDB: 1PC2	HGNC:21689	FIS1_HUMAN	Reviewed	ENSG00000214253	.	.	.	.	.
Mol00375	Protein	Receptor-type tyrosine-protein kinase FLT3 (FLT3)	.	FLT3	2322	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000241453.12, FLT3-201, 3826; ENST00000380987.2, FLT3-202, 3634; ENST00000469894.1, FLT3-203, 474"	MPALARDGGQLPLLVVFSAMIFGTITNQDLPVIKCVLINHKNNDSSVGKSSSYPMVSESPEDLGCALRPQSSGTVYEAAAVEVDVSASITLQVLVDAPGNISCLWVFKHSSLNCQPHFDLQNRGVVSMVILKMTETQAGEYLLFIQSEATNYTILFTVSIRNTLLYTLRRPYFRKMENQDALVCISESVPEPIVEWVLCDSQGESCKEESPAVVKKEEKVLHELFGTDIRCCARNELGRECTRLFTIDLNQTPQTTLPQLFLKVGEPLWIRCKAVHVNHGFGLTWELENKALEEGNYFEMSTYSTNRTMIRILFAFVSSVARNDTGYYTCSSSKHPSQSALVTIVEKGFINATNSSEDYEIDQYEEFCFSVRFKAYPQIRCTWTFSRKSFPCEQKGLDNGYSISKFCNHKHQPGEYIFHAENDDAQFTKMFTLNIRRKPQVLAEASASQASCFSDGYPLPSWTWKKCSDKSPNCTEEITEGVWNRKANRKVFGQWVSSSTLNMSEAIKGFLVKCCAYNSLGTSCETILLNSPGPFPFIQDNISFYATIGVCLLFIVVLTLLICHKYKKQFRYESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQSHPNSSMPGSREVQIHPDSDQISGLHGNSFHSEDEIEYENQKRLEEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQLADAEEAMYQNVDGRVSECPHTYQNRRPFSREMDLGLLSPQAQVEDS	chr13:28003274-28100592[-]	"Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways."	PDB: 1RJB; PDB: 3QS7; PDB: 3QS9; PDB: 4RT7; PDB: 4XUF; PDB: 5X02; PDB: 6IL3; PDB: 6JQR	HGNC:3765	FLT3_HUMAN	Reviewed	ENSG00000122025	.	.	.	.	.
Mol00376	Protein	Hepatocyte nuclear factor 3-alpha (FOXA1)	HNF-3-alpha; HNF-3A; Forkhead box protein A1; Transcription factor 3A; TCF-3A; HNF3A; TCF3A	FOXA1	3169	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000250448.5, FOXA1-201, 3509; ENST00000553751.1, FOXA1-203, 507; ENST00000545425.2, FOXA1-202, 1806; ENST00000554607.1, FOXA1-204, 789; ENST00000557418.1, FOXA1-205, 392"	MLGTVKMEGHETSDWNSYYADTQEAYSSVPVSNMNSGLGSMNSMNTYMTMNTMTTSGNMTPASFNMSYANPGLGAGLSPGAVAGMPGGSAGAMNSMTAAGVTAMGTALSPSGMGAMGAQQAASMNGLGPYAAAMNPCMSPMAYAPSNLGRSRAGGGGDAKTFKRSYPHAKPPYSYISLITMAIQQAPSKMLTLSEIYQWIMDLFPYYRQNQQRWQNSIRHSLSFNDCFVKVARSPDKPGKGSYWTLHPDSGNMFENGCYLRRQKRFKCEKQPGAGGGGGSGSGGSGAKGGPESRKDPSGASNPSADSPLHRGVHGKTGQLEGAPAPGPAASPQTLDHSGATATGGASELKTPASSTAPPISSGPGALASVPASHPAHGLAPHESQLHLKGDPHYSFNHPFSINNLMSSSEQQHKLDFKAYEQALQYSPYGSTLPASLPLGSASVTTRSPIEPSALEPAYYQGVYSRPVLNTS	chr14:37589552-37596059[-]	"Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play a role in translating the epigenetic signatures into cell type-specific enhancer-driven transcriptional programs. Its differential recruitment to chromatin is dependent on distribution of histone H3 methylated at 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the development of multiple endoderm-derived organ systems such as liver, pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in part redundant roles (By similarity). Modulates the transcriptional activity of nuclear hormone receptors. Is involved in ESR1-mediated transcription; required for ESR1 binding to the NKX2-1 promoter in breast cancer cells; binds to the RPRM promoter and is required for the estrogen-induced repression of RPRM. Involved in regulation of apoptosis by inhibiting the expression of BCL2. Involved in cell cycle regulation by activating expression of CDKN1B, alone or in conjunction with BRCA1. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis."	.	HGNC:5021	FOXA1_HUMAN	Reviewed	ENSG00000129514	.	.	.	.	.
Mol00377	Protein	Forkhead box protein M1 (FOXM1)	Forkhead-related protein FKHL16; Hepatocyte nuclear factor 3 forkhead homolog 11; HFH-11; HNF-3/fork-head homolog 11; M-phase phosphoprotein 2; MPM-2 reactive phosphoprotein 2; Transcription factor Trident; Winged-helix factor from INS-1 cells; FKHL16; HFH11; MPP2; WIN	FOXM1	2305	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359843.8, FOXM1-202, 3552; ENST00000627656.2, FOXM1-210, 3487; ENST00000342628.6, FOXM1-201, 3475; ENST00000361953.7, FOXM1-203, 3370; ENST00000535350.1, FOXM1-205, 618; ENST00000538564.5, FOXM1-208, 693; ENST00000537018.5, FOXM1-207, 740; ENST00000536066.1, FOXM1-206, 2518; ENST00000545049.1, FOXM1-209, 900; ENST00000366362.3, FOXM1-204, 775"	MKTSPRRPLILKRRRLPLPVQNAPSETSEEEPKRSPAQQESNQAEASKEVAESNSCKFPAGIKIINHPTMPNTQVVAIPNNANIHSIITALTAKGKESGSSGPNKFILISCGGAPTQPPGLRPQTQTSYDAKRTEVTLETLGPKPAARDVNLPRPPGALCEQKRETCADGEAAGCTINNSLSNIQWLRKMSSDGLGSRSIKQEMEEKENCHLEQRQVKVEEPSRPSASWQNSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRYLTLDQVFKPLDPGSPQLPEHLESQQKRPNPELRRNMTIKTELPLGARRKMKPLLPRVSSYLVPIQFPVNQSLVLQPSVKVPLPLAASLMSSELARHSKRVRIAPKVLLAEEGIAPLSSAGPGKEEKLLFGEGFSPLLPVQTIKEEEIQPGEEMPHLARPIKVESPPLEEWPSPAPSFKEESSHSWEDSSQSPTPRPKKSYSGLRSPTRCVSEMLVIQHRERRERSRSRRKQHLLPPCVDEPELLFSEGPSTSRWAAELPFPADSSDPASQLSYSQEVGGPFKTPIKETLPISSTPSKSVLPRTPESWRLTPPAKVGGLDFSPVQTSQGASDPLPDPLGLMDLSTTPLQSAPPLESPQRLLSSEPLDLISVPFGNSSPSDIDVPKPGSPEPQVSGLAANRSLTEGLVLDTMNDSLSKILLDISFPGLDEDPLGPDNINWSQFIPELQ	chr12:2857680-2877174[-]	"Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis. Plays a role in the control of cell proliferation. Also plays a role in DNA break repair, participating in the DNA damage checkpoint response. Promotes transcription of PHB2."	PDB: 3G73	HGNC:3818	FOXM1_HUMAN	Reviewed	ENSG00000111206	.	.	.	.	.
Mol00378	Protein	Forkhead box protein O1 (FOXO1)	Forkhead box protein O1A; Forkhead in rhabdomyosarcoma; FKHR; FOXO1A	FOXO1	2308	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000379561.6, FOXO1-201, 5779; ENST00000655267.1, FOXO1-203, 509; ENST00000660760.1, FOXO1-204, 491; ENST00000473775.1, FOXO1-202, 178"	MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG	chr13:40555667-40666641[-]	"Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner. Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling. Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis."	PDB: 3CO6; PDB: 3CO7; PDB: 3COA; PDB: 4LG0; PDB: 5DUI; PDB: 6LBI; PDB: 6QVW; PDB: 6QZR; PDB: 6QZS	HGNC:3819	FOXO1_HUMAN	Reviewed	ENSG00000150907	.	.	.	.	.
Mol00379	Protein	Forkhead box protein O3 (FOXO3)	AF6q21 protein; Forkhead in rhabdomyosarcoma-like 1; FKHRL1; FOXO3A	FOXO3	2309	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000406360.2, FOXO3-202, 7296; ENST00000343882.10, FOXO3-201, 7308; ENST00000540898.1, FOXO3-203, 2553"	MAEAPASPAPLSPLEVELDPEFEPQSRPRSCTWPLQRPELQASPAKPSGETAADSMIPEEEDDEDDEDGGGRAGSAMAIGGGGGSGTLGSGLLLEDSARVLAPGGQDPGSGPATAAGGLSGGTQALLQPQQPLPPPQPGAAGGSGQPRKCSSRRNAWGNLSYADLITRAIESSPDKRLTLSQIYEWMVRCVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFMRVQNEGTGKSSWWIINPDGGKSGKAPRRRAVSMDNSNKYTKSRGRAAKKKAALQTAPESADDSPSQLSKWPGSPTSRSSDELDAWTDFRSRTNSNASTVSGRLSPIMASTELDEVQDDDAPLSPMLYSSSASLSPSVSKPCTVELPRLTDMAGTMNLNDGLTENLMDDLLDNITLPPSQPSPTGGLMQRSSSFPYTTKGSGLGSPTSSFNSTVFGPSSLNSLRQSPMQTIQENKPATFSSMSHYGNQTLQDLLTSDSLSHSDVMMTQSDPLMSQASTAVSAQNSRRNVMLRNDPMMSFAAQPNQGSLVNQNLLHHQHQTQGALGGSRALSNSVSNMGLSESSSLGSAKHQQQSPVSQSMQTLSDSLSGSSLYSTSANLPVMGHEKFPSDLDLDMFNGSLECDMESIIRSELMDADGLDFNFDSLISTQNVVGLNVGNFTGAKQASSQSWVPG	chr6:108559835-108684774[+]	"Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy. Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins. Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress. Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation. In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3."	PDB: 2K86; PDB: 2LQH; PDB: 2LQI; PDB: 2UZK; PDB: 6MNL	HGNC:3821	FOXO3_HUMAN	Reviewed	ENSG00000118689	.	.	.	.	.
Mol00380	Protein	Ferritin light chain (FTL)	Ferritin L subunit	FTL	2512	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331825.11, FTL-201, 871"	MSSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD	chr19:48965309-48966879[+]	"Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity)."	PDB: 2FFX; PDB: 2FG4; PDB: 2FG8; PDB: 3KXU; PDB: 4V6B; PDB: 5LG8; PDB: 6TR9; PDB: 6TS0; PDB: 6TS1; PDB: 6TSA; PDB: 6TSF; PDB: 6TSJ; PDB: 6WX6	HGNC:3999	FRIL_HUMAN	Reviewed	ENSG00000087086	.	.	.	.	.
Mol00381	Protein	RNA-binding protein FUS (FUS)	75 kDa DNA-pairing protein; Oncogene FUS; Oncogene TLS; POMp75; Translocated in liposarcoma protein; TLS	FUS	2521	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000254108.12, FUS-201, 1824; ENST00000380244.7, FUS-202, 1818; ENST00000568685.1, FUS-210, 1785; ENST00000566605.5, FUS-209, 1787; ENST00000474990.5, FUS-203, 827; ENST00000487509.6, FUS-206, 4920; ENST00000487045.6, FUS-205, 952; ENST00000564766.1, FUS-208, 791; ENST00000483853.1, FUS-204, 778; ENST00000487974.1, FUS-207, 643; ENST00000569760.5, FUS-212, 639; ENST00000570090.1, FUS-213, 544; ENST00000568901.2, FUS-211, 521"	MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY	chr16:31180138-31191605[+]	"DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response. Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing. Binds also its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay. Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair. In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis."	PDB: 2LA6; PDB: 2LCW; PDB: 4FDD; PDB: 4FQ3; PDB: 5W3N; PDB: 5XRR; PDB: 5XSG; PDB: 5YVG; PDB: 5YVH; PDB: 5YVI; PDB: 6BWZ; PDB: 6BXV; PDB: 6BZP; PDB: 6G99; PDB: 6GBM; PDB: 6KJ1; PDB: 6KJ2; PDB: 6KJ3; PDB: 6KJ4; PDB: 6SNJ; PDB: 6XFM; PDB: 7CYL	HGNC:4010	FUS_HUMAN	Reviewed	ENSG00000089280	.	.	.	.	.
Mol00382	Protein	"Alpha-(1,3)-fucosyltransferase 4 (FUT4)"	4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase; ELAM-1 ligand fucosyltransferase; Fucosyltransferase 4; Fucosyltransferase IV; Fuc-TIV; FucT-IV; Galactoside 3-L-fucosyltransferase; ELFT; FCT3A	FUT4	2526	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000358752.4, FUT4-201, 5975"	MRRLWGAARKPSGAGWEKEWAEAPQEAPGAWSGRLGPGRSGRKGRAVPGWASWPAHLALAARPARHLGGAGQGPRPLHSGTAPFHSRASGERQRRLEPQLQHESRCRSSTPADAWRAEAALPVRAMGAPWGSPTAAAGGRRGWRRGRGLPWTVCVLAAAGLTCTALITYACWGQLPPLPWASPTPSRPVGVLLWWEPFGGRDSAPRPPPDCRLRFNISGCRLLTDRASYGEAQAVLFHHRDLVKGPPDWPPPWGIQAHTAEEVDLRVLDYEEAAAAAEALATSSPRPPGQRWVWMNFESPSHSPGLRSLASNLFNWTLSYRADSDVFVPYGYLYPRSHPGDPPSGLAPPLSRKQGLVAWVVSHWDERQARVRYYHQLSQHVTVDVFGRGGPGQPVPEIGLLHTVARYKFYLAFENSQHLDYITEKLWRNALLAGAVPVVLGPDRANYERFVPRGAFIHVDDFPSASSLASYLLFLDRNPAVYRRYFHWRRSYAVHITSFWDEPWCRVCQAVQRAGDRPKSIRNLASWFER	chr11:94543921-94549895[+]	"[Isoform Short]: Catalyzes alpha(1->3) linkage of fucosyl moiety transferred from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2 lactosamine (LacNAc, Gal-beta(1->4)GlcNAc) glycan attached to N- or O-linked glycoproteins. Robustly fucosylates nonsialylated distal LacNAc unit of the polylactosamine chain to form Lewis X antigen (CD15), a glycan determinant known to mediate important cellular functions in development and immunity. Fucosylates with lower efficiency sialylated LacNAc acceptors to form sialyl Lewis X and 6-sulfo sialyl Lewis X determinants that serve as recognition epitopes for C-type lectins. Together with FUT7 contributes to SELE, SELL and SELP selectin ligand biosynthesis and selectin-dependent lymphocyte homing, leukocyte migration and blood leukocyte homeostasis. In a cell type specific manner, may also fucosylate the internal LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE."	.	HGNC:4015	FUT4_HUMAN	Reviewed	ENSG00000196371	.	.	.	.	.
Mol00383	Protein	Tyrosine-protein kinase Fyn (FYN)	Proto-oncogene Syn; Proto-oncogene c-Fyn; Src-like kinase; SLK; p59-Fyn	FYN	2534	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354650.7, FYN-202, 3628; ENST00000368682.7, FYN-205, 3234; ENST00000538466.5, FYN-229, 3023; ENST00000368678.8, FYN-204, 2573; ENST00000368667.6, FYN-203, 2416; ENST00000229471.8, FYN-201, 2009; ENST00000518295.5, FYN-219, 1012; ENST00000523238.5, FYN-224, 1012; ENST00000462856.6, FYN-207, 989; ENST00000520518.5, FYN-221, 864; ENST00000462598.7, FYN-206, 825; ENST00000484067.6, FYN-212, 712; ENST00000517419.5, FYN-218, 610; ENST00000521062.5, FYN-222, 609; ENST00000523570.5, FYN-226, 597; ENST00000518630.5, FYN-220, 571; ENST00000523574.5, FYN-227, 569; ENST00000524310.5, FYN-228, 541; ENST00000487824.2, FYN-213, 518; ENST00000476769.6, FYN-211, 793; ENST00000491885.6, FYN-214, 649; ENST00000471959.2, FYN-210, 932; ENST00000523322.5, FYN-225, 909; ENST00000496864.6, FYN-217, 839; ENST00000467921.6, FYN-209, 799; ENST00000495927.5, FYN-215, 755; ENST00000521361.5, FYN-223, 723; ENST00000467899.5, FYN-208, 642; ENST00000495935.1, FYN-216, 436"	MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL	chr6:111660332-111873452[-]	"Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity)."	PDB: 1A0N; PDB: 1AOT; PDB: 1AOU; PDB: 1AVZ; PDB: 1AZG; PDB: 1EFN; PDB: 1FYN; PDB: 1G83; PDB: 1M27; PDB: 1NYF; PDB: 1NYG; PDB: 1SHF; PDB: 1ZBJ; PDB: 2DQ7; PDB: 2MQI; PDB: 2MRJ; PDB: 2MRK; PDB: 3H0F; PDB: 3H0H; PDB: 3H0I; PDB: 3UA6; PDB: 3UA7; PDB: 4D8D; PDB: 4EIK; PDB: 4U17; PDB: 4U1P; PDB: 4ZNX; PDB: 5ZAU; PDB: 6EDF; PDB: 6IPY; PDB: 6IPZ; PDB: 7A2J; PDB: 7A2K; PDB: 7A2L; PDB: 7A2M; PDB: 7A2N; PDB: 7A2O; PDB: 7A2P; PDB: 7A2Q; PDB: 7A2R; PDB: 7A2S; PDB: 7A2T; PDB: 7A2U; PDB: 7A2V; PDB: 7A2W; PDB: 7A2X; PDB: 7A2Y; PDB: 7A2Z	HGNC:4037	FYN_HUMAN	Reviewed	ENSG00000010810	.	.	.	.	.
Mol00384	Protein	Frizzled-1 (FZD1)	Fz-1; hFz1; FzE1	FZD1	8321	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000287934.4, FZD1-201, 6894"	MAEEEAPKKSRAAGGGASWELCAGALSARLAEEGSGDAGGRRRPPVDPRRLARQLLLLLWLLEAPLLLGVRAQAAGQGPGQGPGPGQQPPPPPQQQQSGQQYNGERGISVPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGHRGGFPGGAGASERGKFSCPRALKVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTWIGIWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYTAVAVAYIAGFLLEDRVVCNDKFAEDGARTVAQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAIKTITILALGQVDGDVLSGVCFVGLNNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVIACYFYEQAFRDQWERSWVAQSCKSYAIPCPHLQAGGGAPPHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETTV	chr7:91264433-91271326[+]	"Receptor for Wnt proteins. Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B. Contradictory results showing activation by WNT7B have been described for mouse. Functions in the canonical Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable)."	.	HGNC:4038	FZD1_HUMAN	Reviewed	ENSG00000157240	.	.	.	.	.
Mol00385	Protein	Glyceraldehyde-3-phosphate dehydrogenase 1 (GAPDH)	GAPDH; Peptidyl-cysteine S-nitrosylase GAPDH; GAPD; CDABP0047; OK/SW-cl.12	GAPDH	2597	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000229239.10, GAPDH-201, 1285; ENST00000396861.5, GAPDH-205, 1348; ENST00000396858.5, GAPDH-203, 1292; ENST00000396859.5, GAPDH-204, 1256; ENST00000396856.5, GAPDH-202, 1266; ENST00000619601.1, GAPDH-211, 1086; ENST00000466525.1, GAPDH-206, 1720; ENST00000466588.5, GAPDH-207, 1363; ENST00000474249.5, GAPDH-208, 1333; ENST00000492719.5, GAPDH-209, 930; ENST00000496049.1, GAPDH-210, 390"	MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSNRVVDLMAHMASKE	chr12:6534512-6538374[+]	"Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC."	PDB: 1U8F; PDB: 1ZNQ; PDB: 3GPD; PDB: 4WNC; PDB: 4WNI; PDB: 6ADE; PDB: 6IQ6; PDB: 6M61; PDB: 6YND; PDB: 6YNE; PDB: 6YNF; PDB: 6YNH	HGNC:4141	G3P_HUMAN	Reviewed	ENSG00000111640	.	.	.	.	.
Mol00386	Protein	Glucose-6-phosphate dehydrogenase (G6PD)	G6PD	G6PD	2539	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393562.10, G6PD-202, 2223; ENST00000696430.1, G6PD-223, 2417; ENST00000696429.1, G6PD-222, 2359; ENST00000393564.7, G6PD-203, 2271; ENST00000439227.6, G6PD-205, 2336; ENST00000696421.1, G6PD-214, 2142; ENST00000696423.1, G6PD-216, 2023; ENST00000696422.1, G6PD-215, 2020; ENST00000696420.1, G6PD-213, 1995; ENST00000369620.6, G6PD-201, 1799; ENST00000440967.5, G6PD-206, 1056; ENST00000433845.1, G6PD-204, 817; ENST00000696431.1, G6PD-224, 484; ENST00000696426.1, G6PD-219, 2638; ENST00000696428.1, G6PD-221, 2335; ENST00000696427.1, G6PD-220, 2209; ENST00000696425.1, G6PD-218, 2034; ENST00000696424.1, G6PD-217, 2009; ENST00000567614.1, G6PD-211, 792; ENST00000490651.1, G6PD-209, 783; ENST00000497281.5, G6PD-210, 532; ENST00000489497.1, G6PD-208, 512; ENST00000647501.1, G6PD-212, 471; ENST00000488434.1, G6PD-207, 432"	MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL	chrX:154517825-154547572[-]	"Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis."	PDB: 1QKI; PDB: 2BH9; PDB: 2BHL; PDB: 5UKW; PDB: 6E07; PDB: 6E08; PDB: 6JYU; PDB: 6VA0; PDB: 6VA7; PDB: 6VA8; PDB: 6VA9; PDB: 6VAQ	HGNC:4057	G6PD_HUMAN	Reviewed	ENSG00000160211	.	.	.	.	.
Mol00387	Protein	Growth arrest-specific protein 6 (GAS6)	GAS-6; AXL receptor tyrosine kinase ligand; AXLLG	GAS6	2621	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000327773.7, GAS6-201, 2508; ENST00000476291.1, GAS6-202, 537; ENST00000608763.1, GAS6-204, 2646; ENST00000480426.5, GAS6-203, 2507; ENST00000610073.1, GAS6-205, 2169"	MAPSLSPGPAALRRAPQLLLLLLAAECALAALLPAREATQFLRPRQRRAFQVFEEAKQGHLERECVEELCSREEAREVFENDPETDYFYPRYLDCINKYGSPYTKNSGFATCVQNLPDQCTPNPCDRKGTQACQDLMGNFFCLCKAGWGGRLCDKDVNECSQENGGCLQICHNKPGSFHCSCHSGFELSSDGRTCQDIDECADSEACGEARCKNLPGSYSCLCDEGFAYSSQEKACRDVDECLQGRCEQVCVNSPGSYTCHCDGRGGLKLSQDMDTCEDILPCVPFSVAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLVAEFDFRTFDPEGILLFAGGHQDSTWIVLALRAGRLELQLRYNGVGRVTSSGPVINHGMWQTISVEELARNLVIKVNRDAVMKIAVAGDLFQPERGLYHLNLTVGGIPFHEKDLVQPINPRLDGCMRSWNWLNGEDTTIQETVKVNTRMQCFSVTERGSFYPGSGFAFYSLDYMRTPLDVGTESTWEVEVVAHIRPAADTGVLFALWAPDLRAVPLSVALVDYHSTKKLKKQLVVLAVEHTALALMEIKVCDGQEHVVTVSLRDGEATLEVDGTRGQSEVSAAQLQERLAVLERHLRSPVLTFAGGLPDVPVTSAPVTAFYRGCMTLEVNRRLLDLDEAAYKHSDITAHSCPPVEPAAA	chr13:113820549-113864076[-]	"Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses."	PDB: 1H30; PDB: 2C5D; PDB: 4RA0; PDB: 5VXZ	HGNC:4168	GAS6_HUMAN	Reviewed	ENSG00000183087	.	.	.	.	.
Mol00388	Protein	Trans-acting T-cell-specific transcription factor GATA-3 (GATA3)	GATA-binding factor 3	GATA3	2625	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000379328.9, GATA3-202, 3083; ENST00000346208.4, GATA3-201, 2650; ENST00000481743.2, GATA3-204, 975; ENST00000643001.1, GATA3-205, 748; ENST00000461472.1, GATA3-203, 895"	MEVTADQPRWVSHHHPAVLNGQHPDTHHPGLSHSYMDAAQYPLPEEVDVLFNIDGQGNHVPPYYGNSVRATVQRYPPTHHGSQVCRPPLLHGSLPWLDGGKALGSHHTASPWNLSPFSKTSIHHGSPGPLSVYPPASSSSLSGGHASPHLFTFPPTPPKDVSPDPSLSTPGSAGSARQDEKECLKYQVPLPDSMKLESSHSRGSMTALGGASSSTHHPITTYPPYVPEYSSGLFPPSSLLGGSPTGFGCKSRPKARSSTGRECVNCGATSTPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTSCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNINRPLTMKKEGIQTRNRKMSSKSKKCKKVHDSLEDFPKNSSFNPAALSRHMSSLSHISPFSHSSHMLTTPTPMHPPSSLSFGPHHPSSMVTAMG	chr10:8045378-8075198[+]	Transcriptional activator which binds to the enhancer of the T-cell receptor alpha and delta genes. Binds to the consensus sequence 5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process following immune and inflammatory responses. Positively regulates ASB2 expression (By similarity).	PDB: 4HC7; PDB: 4HC9; PDB: 4HCA	HGNC:4172	GATA3_HUMAN	Reviewed	ENSG00000107485	.	.	.	.	.
Mol00389	Protein	Transcription factor GATA6 (GATA6)	GATA-binding factor 6	GATA6	2627	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000269216.10, GATA6-201, 3624; ENST00000581694.1, GATA6-202, 2057"	MALTDGGWCLPKRFGAAGADASDSRAFPAREPSTPPSPISSSSSSCSRGGERGPGGASNCGTPQLDTEAAAGPPARSLLLSSYASHPFGAPHGPSAPGVAGPGGNLSSWEDLLLFTDLDQAATASKLLWSSRGAKLSPFAPEQPEEMYQTLAALSSQGPAAYDGAPGGFVHSAAAAAAAAAAASSPVYVPTTRVGSMLPGLPYHLQGSGSGPANHAGGAGAHPGWPQASADSPPYGSGGGAAGGGAAGPGGAGSAAAHVSARFPYSPSPPMANGAAREPGGYAAAGSGGAGGVSGGGSSLAAMGGREPQYSSLSAARPLNGTYHHHHHHHHHHPSPYSPYVGAPLTPAWPAGPFETPVLHSLQSRAGAPLPVPRGPSADLLEDLSESRECVNCGSIQTPLWRRDGTGHYLCNACGLYSKMNGLSRPLIKPQKRVPSSRRLGLSCANCHTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMKKEGIQTRKRKPKNINKSKTCSGNSNNSIPMTPTSTSSNSDDCSKNTSPTTQPTASGAGAPVMTGAGESTNPENSELKYSGQDGLYIGVSLASPAEVTSSVRPDSWCALALA	chr18:22169589-22202528[+]	"Transcriptional activator. Regulates SEMA3C and PLXNA2. Involved in gene regulation specifically in the gastric epithelium. May regulate genes that protect epithelial cells from bacterial infection. Involved in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions. In human skin, controls several physiological processes contributing to homeostasis of the upper pilosebaceous unit. Triggers ductal and sebaceous differentiation as well as limits cell proliferation and lipid production to prevent hyperseborrhoea. Mediates the effects of retinoic acid on sebocyte proliferation, differentiation and lipid production. Also contributes to immune regulation of sebocytes and antimicrobial responses by modulating the expression of anti-inflammatory genes such as IL10 and pro-inflammatory genes such as IL6, TLR2, TLR4, and IFNG. Activates TGFB1 signaling which controls the interfollicular epidermis fate."	.	HGNC:4174	GATA6_HUMAN	Reviewed	ENSG00000141448	.	.	.	.	.
Mol00390	Protein	Glucocorticoid receptor (NR3C1)	GR; Nuclear receptor subfamily 3 group C member 1; GRL	NR3C1	2908	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000394464.7, NR3C1-203, 6778; ENST00000343796.6, NR3C1-202, 7286; ENST00000415690.6, NR3C1-205, 3789; ENST00000231509.7, NR3C1-201, 3556; ENST00000504572.5, NR3C1-212, 3389; ENST00000394466.6, NR3C1-204, 3245; ENST00000503201.1, NR3C1-209, 2594; ENST00000424646.6, NR3C1-206, 4591; ENST00000652686.1, NR3C1-217, 2961; ENST00000514699.1, NR3C1-216, 623; ENST00000510170.5, NR3C1-215, 585; ENST00000502500.1, NR3C1-207, 585; ENST00000508760.5, NR3C1-214, 547; ENST00000502892.5, NR3C1-208, 498; ENST00000504336.1, NR3C1-211, 611; ENST00000503701.1, NR3C1-210, 602; ENST00000505058.5, NR3C1-213, 491"	MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK	chr5:143277931-143435512[-]	"Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth."	PDB: 1M2Z; PDB: 1NHZ; PDB: 1P93; PDB: 3BQD; PDB: 3CLD; PDB: 3E7C; PDB: 3H52; PDB: 3K22; PDB: 3K23; PDB: 4CSJ; PDB: 4HN5; PDB: 4HN6; PDB: 4LSJ; PDB: 4MDD; PDB: 4P6W; PDB: 4P6X; PDB: 4UDC; PDB: 4UDD; PDB: 5CBX; PDB: 5CBY; PDB: 5CBZ; PDB: 5CC1; PDB: 5E69; PDB: 5E6A; PDB: 5E6B; PDB: 5E6C; PDB: 5E6D; PDB: 5EMC; PDB: 5EMP; PDB: 5EMQ; PDB: 5G3J; PDB: 5G5W; PDB: 5NFP; PDB: 5NFT; PDB: 5UC3; PDB: 5VA0; PDB: 5VA7; PDB: 6BQU; PDB: 6CFN; PDB: 6DXK; PDB: 6EL6; PDB: 6EL7; PDB: 6EL9; PDB: 6X6D; PDB: 6X6E; PDB: 6YMO; PDB: 6YO8; PDB: 6YOS	HGNC:7978	GCR_HUMAN	Reviewed	ENSG00000113580	.	.	.	.	.
Mol00391	Protein	Gem-associated protein 2 (SIP1)	Gemin-2; Component of gems 2; Survival of motor neuron protein-interacting protein 1; SMN-interacting protein 1; SIP1	GEMIN2	8487	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308317.12, GEMIN2-202, 1320; ENST00000250379.13, GEMIN2-201, 1094; ENST00000396249.7, GEMIN2-203, 801; ENST00000534684.7, GEMIN2-212, 658; ENST00000524781.1, GEMIN2-205, 649; ENST00000527381.2, GEMIN2-209, 592; ENST00000525153.6, GEMIN2-207, 1476; ENST00000650481.1, GEMIN2-213, 1202; ENST00000412033.7, GEMIN2-204, 825; ENST00000531684.6, GEMIN2-211, 630; ENST00000524980.1, GEMIN2-206, 662; ENST00000525430.1, GEMIN2-208, 659; ENST00000529365.1, GEMIN2-210, 583"	MRRAELAGLKTMAWVPAESAVEELMPRLLPVEPCDLTEGFDPSVPPRTPQEYLRRVQIEAAQCPDVVVAQIDPKKLKRKQSVNISLSGCQPAPEGYSPTLQWQQQQVAQFSTVRQNVNKHRSHWKSQQLDSNVTMPKSEDEEGWKKFCLGEKLCADGAVGPATNESPGIDYVQIGFPPLLSIVSRMNQATVTSVLEYLSNWFGERDFTPELGRWLYALLACLEKPLLPEAHSLIRQLARRCSEVRLLVDSKDDERVPALNLLICLVSRYFDQRDLADEPS	chr14:39114285-39136973[+]	"The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A. Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound."	PDB: 2LEH; PDB: 5XJL; PDB: 5XJQ; PDB: 5XJR; PDB: 5XJS; PDB: 5XJT; PDB: 5XJU	HGNC:10884	GEMI2_HUMAN	Reviewed	ENSG00000092208	.	.	.	.	.
Mol00392	Protein	Zinc finger protein GLI1 (GLI1)	Glioma-associated oncogene; Oncogene GLI; GLI	GLI1	2735	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000228682.7, GLI1-201, 3972; ENST00000546141.5, GLI1-208, 3475; ENST00000543426.5, GLI1-207, 3394; ENST00000528467.1, GLI1-204, 3196; ENST00000532291.5, GLI1-206, 784; ENST00000528432.1, GLI1-203, 480; ENST00000527742.1, GLI1-202, 676; ENST00000530789.1, GLI1-205, 314"	MFNSMTPPPISSYGEPCCLRPLPSQGAPSVGTEGLSGPPFCHQANLMSGPHSYGPARETNSCTEGPLFSSPRSAVKLTKKRALSISPLSDASLDLQTVIRTSPSSLVAFINSRCTSPGGSYGHLSIGTMSPSLGFPAQMNHQKGPSPSFGVQPCGPHDSARGGMIPHPQSRGPFPTCQLKSELDMLVGKCREEPLEGDMSSPNSTGIQDPLLGMLDGREDLEREEKREPESVYETDCRWDGCSQEFDSQEQLVHHINSEHIHGERKEFVCHWGGCSRELRPFKAQYMLVVHMRRHTGEKPHKCTFEGCRKSYSRLENLKTHLRSHTGEKPYMCEHEGCSKAFSNASDRAKHQNRTHSNEKPYVCKLPGCTKRYTDPSSLRKHVKTVHGPDAHVTKRHRGDGPLPRAPSISTVEPKREREGGPIREESRLTVPEGAMKPQPSPGAQSSCSSDHSPAGSAANTDSGVEMTGNAGGSTEDLSSLDEGPCIAGTGLSTLRRLENLRLDQLHQLRPIGTRGLKLPSLSHTGTTVSRRVGPPVSLERRSSSSSSISSAYTVSRRSSLASPFPPGSPPENGASSLPGLMPAQHYLLRARYASARGGGTSPTAASSLDRIGGLPMPPWRSRAEYPGYNPNAGVTRRASDPAQAADRPAPARVQRFKSLGCVHTPPTVAGGGQNFDPYLPTSVYSPQPPSITENAAMDARGLQEEPEVGTSMVGSGLNPYMDFPPTDTLGYGGPEGAAAEPYGARGPGSLPLGPGPPTNYGPNPCPQQASYPDPTQETWGEFPSHSGLYPGPKALGGTYSQCPRLEHYGQVQVKPEQGCPVGSDSTGLAPCLNAHPSEGPPHPQPLFSHYPQPSPPQYLQSGPYTQPPPDYLPSEPRPCLDFDSPTHSTGQLKAQLVCNYVQSQQELLWEGGGREDAPAQEPSYQSPKFLGGSQVSPSRAKAPVNTYGPGFGPNLPNHKSGSYPTPSPCHENFVVGANRASHRAAAPPRLLPPLPTCYGPLKVGGTNPSCGHPEVGRLGGGPALYPPPEGQVCNPLDSLDLDNTQLDFVAILDEPQGLSPPPSHDQRGSSGHTPPPSGPPNMAVGNMSVLLRSLPGETEFLNSSA	chr12:57459785-57472268[+]	"Acts as a transcriptional activator. Binds to the DNA consensus sequence 5'-GACCACCCA-3'. Regulates the transcription of specific genes during normal development. Plays a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling. Plays a role in cell proliferation and differentiation via its role in SHH signaling."	PDB: 2GLI; PDB: 4BLB; PDB: 4KMD; PDB: 5OM0	HGNC:4317	GLI1_HUMAN	Reviewed	ENSG00000111087	.	.	.	.	.
Mol00393	Protein	Golgi phosphoprotein 3 (GOLPH3)	Coat protein GPP34; Mitochondrial DNA absence factor; MIDAS; GPP34	GOLPH3	64083	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265070.7, GOLPH3-201, 2678; ENST00000503610.5, GOLPH3-202, 1074; ENST00000512668.1, GOLPH3-203, 665"	MTSLTQRSSGLVQRRTEASRNAADKERAAGGGAGSSEDDAQSRRDEQDDDDKGDSKETRLTLMEEVLLLGLKDREGYTSFWNDCISSGLRGCMLIELALRGRLQLEACGMRRKSLLTRKVICKSDAPTGDVLLDEALKHVKETQPPETVQNWIELLSGETWNPLKLHYQLRNVRERLAKNLVEKGVLTTEKQNFLLFDMTTHPLTNNNIKQRLIKKVQEAVLDKWVNDPHRMDRRLLALIYLAHASDVLENAFAPLLDEQYDLATKRVRQLLDLDPEVECLKANTNEVLWAVVAAFTK	chr5:32124716-32174319[-]	"Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis."	PDB: 3KN1	HGNC:15452	GOLP3_HUMAN	Reviewed	ENSG00000113384	.	.	.	.	.
Mol00394	Protein	G-protein coupled estrogen receptor 1 (GPER1)	Chemoattractant receptor-like 2; Flow-induced endothelial G-protein coupled receptor 1; FEG-1; G protein-coupled estrogen receptor 1; G-protein coupled receptor 30; GPCR-Br; IL8-related receptor DRY12; Lymphocyte-derived G-protein coupled receptor; LYGPR; Membrane estrogen receptor; mER; CEPR; CMKRL2; DRY12; GPER; GPR30	GPER1	2852	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000397088.4, GPER1-202, 2613; ENST00000397092.5, GPER1-203, 2971; ENST00000297469.3, GPER1-201, 2778; ENST00000401670.1, GPER1-204, 1542; ENST00000413368.5, GPER1-205, 1105"	MDVTSQARGVGLEMYPGTAQPAAPNTTSPELNLSHPLLGTALANGTGELSEHQQYVIGLFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAVADLILVADSLIEVFNLHERYYDIAVLCTFMSLFLQVNMYSSVFFLTWMSFDRYIALARAMRCSLFRTKHHARLSCGLIWMASVSATLVPFTAVHLQHTDEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRVLVRAHRHRGLRPRRQKALRMILAVVLVFFVCWLPENVFISVHLLQRTQPGAAPCKQSFRHAHPLTGHIVNLAAFSNSCLNPLIYSFLGETFRDKLRLYIEQKTNLPALNRFCHAALKAVIPDSTEQSDVRFSSAV	chr7:1082208-1093815[+]	"G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Functions also as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells."	.	HGNC:4485	GPER1_HUMAN	Reviewed	ENSG00000164850	.	.	.	.	.
Mol00395	Protein	Growth factor receptor-bound protein 2 (GRB2)	Adapter protein GRB2; Protein Ash; SH2/SH3 adapter GRB2; ASH	GRB2	2885	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000316804.10, GRB2-202, 3273; ENST00000392562.5, GRB2-203, 3729; ENST00000392564.5, GRB2-205, 3182; ENST00000316615.9, GRB2-201, 3181; ENST00000392563.5, GRB2-204, 2851; ENST00000578961.5, GRB2-208, 687; ENST00000582582.1, GRB2-210, 584; ENST00000581959.1, GRB2-209, 359; ENST00000648046.1, GRB2-212, 1711; ENST00000462266.1, GRB2-206, 601; ENST00000583912.1, GRB2-211, 561; ENST00000577711.1, GRB2-207, 555"	MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIEMKPHPWFFGKIPRAKAEEMLSKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEDGELGFRRGDFIHVMDNSDPNWWKGACHGQTGMFPRNYVTPVNRNV	chr17:75318076-75405709[-]	Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.	PDB: 1AZE; PDB: 1BM2; PDB: 1BMB; PDB: 1CJ1; PDB: 1FHS; PDB: 1FYR; PDB: 1GCQ; PDB: 1GFC; PDB: 1GFD; PDB: 1GHU; PDB: 1GRI; PDB: 1IO6; PDB: 1JYQ; PDB: 1JYR; PDB: 1JYU; PDB: 1QG1; PDB: 1TZE; PDB: 1X0N; PDB: 1ZFP; PDB: 2AOA; PDB: 2AOB; PDB: 2H46; PDB: 2H5K; PDB: 2HUW; PDB: 2VVK; PDB: 2VWF; PDB: 2W0Z; PDB: 3C7I; PDB: 3IMD; PDB: 3IMJ; PDB: 3IN7; PDB: 3IN8; PDB: 3KFJ; PDB: 3MXC; PDB: 3MXY; PDB: 3N7Y; PDB: 3N84; PDB: 3N8M; PDB: 3OV1; PDB: 3OVE; PDB: 3S8L; PDB: 3S8N; PDB: 3S8O; PDB: 3WA4; PDB: 4P9V; PDB: 4P9Z; PDB: 5CDW; PDB: 6ICG; PDB: 6ICH; PDB: 6SDF; PDB: 6VK2; PDB: 6WM1; PDB: 6WO2; PDB: 7MPH	HGNC:4566	GRB2_HUMAN	Reviewed	ENSG00000177885	.	.	.	.	.
Mol00396	Protein	Glutamate--cysteine ligase regulatory subunit (GCLM)	GCS light chain; Gamma-ECS regulatory subunit; Gamma-glutamylcysteine synthetase regulatory subunit; Glutamate--cysteine ligase modifier subunit; GLCLR	GCLM	2730	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000370238.8, GCLM-201, 4883; ENST00000615724.1, GCLM-204, 3008; ENST00000467772.1, GCLM-203, 625; ENST00000462183.1, GCLM-202, 583"	MGTDSRAAKALLARARTLHLQTGNLLNWGRLRKKCPSTHSEELHDCIQKTLNEWSSQINPDLVREFPDVLECTVSHAVEKINPDEREEMKVSAKLFIVESNSSSSTRSAVDMACSVLGVAQLDSVIIASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIQAHEWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS	chr1:93885199-93909456[-]	.	.	HGNC:4312	GSH0_HUMAN	Reviewed	ENSG00000023909	.	.	.	.	.
Mol00397	Protein	Glutamate--cysteine ligase catalytic subunit (GCLC)	GCS heavy chain; Gamma-ECS; Gamma-glutamylcysteine synthetase; GLCL; GLCLC	GCLC	2729	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650454.1, GCLC-214, 3785; ENST00000513939.6, GCLC-207, 1800; ENST00000509541.5, GCLC-205, 3774; ENST00000616923.5, GCLC-212, 3287; ENST00000514004.5, GCLC-208, 2356; ENST00000643939.1, GCLC-213, 2289; ENST00000505197.1, GCLC-203, 592; ENST00000504525.1, GCLC-202, 1011; ENST00000514933.2, GCLC-210, 553; ENST00000515580.1, GCLC-211, 2132; ENST00000505294.5, GCLC-204, 847; ENST00000510837.5, GCLC-206, 776; ENST00000504353.1, GCLC-201, 597; ENST00000514373.3, GCLC-209, 332"	MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDHENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTVEANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAINKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDIGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVLQGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN	chr6:53497341-53616970[-]	Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis.	.	HGNC:4311	GSH1_HUMAN	Reviewed	ENSG00000001084	.	.	.	.	.
Mol00398	Protein	Glutathione synthetase (GSH)	GSH synthetase; GSH-S; Glutathione synthase	GSS	2937	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000651619.1, GSS-228, 1909; ENST00000644793.1, GSS-217, 2702; ENST00000643188.1, GSS-205, 1940; ENST00000642498.1, GSS-203, 2131; ENST00000646735.1, GSS-226, 1554; ENST00000643502.1, GSS-209, 1310; ENST00000451957.2, GSS-201, 1092; ENST00000645328.1, GSS-219, 870; ENST00000643271.1, GSS-207, 587; ENST00000645102.1, GSS-218, 512; ENST00000644608.1, GSS-215, 450; ENST00000646405.1, GSS-222, 1667; ENST00000642538.1, GSS-204, 1540; ENST00000643443.1, GSS-208, 1437; ENST00000645408.1, GSS-220, 830; ENST00000642493.1, GSS-202, 767; ENST00000646766.1, GSS-227, 732; ENST00000646502.1, GSS-224, 1870; ENST00000643628.1, GSS-210, 920; ENST00000646497.1, GSS-223, 900; ENST00000645723.1, GSS-221, 3019; ENST00000643908.1, GSS-212, 1998; ENST00000646512.1, GSS-225, 1907; ENST00000644538.1, GSS-214, 1780; ENST00000644694.1, GSS-216, 747; ENST00000644197.1, GSS-213, 728; ENST00000643690.1, GSS-211, 573; ENST00000643203.1, GSS-206, 461"	MATNWGSLLQDKQQLEELARQAVDRALAEGVLLRTSQEPTSSEVVSYAPFTLFPSLVPSALLEQAYAVQMDFNLLVDAVSQNAAFLEQTLSSTIKQDDFTARLFDIHKQVLKEGIAQTVFLGLNRSDYMFQRSADGSPALKQIEINTISASFGGLASRTPAVHRHVLSVLSKTKEAGKILSNNPSKGLALGIAKAWELYGSPNALVLLIAQEKERNIFDQRAIENELLARNIHVIRRTFEDISEKGSLDQDRRLFVDGQEIAVVYFRDGYMPRQYSLQNWEARLLLERSHAAKCPDIATQLAGTKKVQQELSRPGMLEMLLPGQPEAVARLRATFAGLYSLDVGEEGDQAIAEALAAPSRFVLKPQREGGGNNLYGEEMVQALKQLKDSEERASYILMEKIEPEPFENCLLRPGSPARVVQCISELGIFGVYVRQEKTLVMNKHVGHLLRTKAIEHADGGVAAGVAVLDNPYPV	chr20:34928432-34956027[-]	"Catalyzes the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner. Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes."	PDB: 2HGS	HGNC:4624	GSHB_HUMAN	Reviewed	ENSG00000100983	.	.	.	.	.
Mol00399	Protein	Glutathione reductase (GSR)	GR; GRase; GLUR; GRD1	GSR	2936	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000221130.11, GSR-201, 3034; ENST00000546342.5, GSR-206, 1482; ENST00000541648.5, GSR-205, 1410; ENST00000537535.5, GSR-204, 1323; ENST00000643653.1, GSR-208, 2804; ENST00000523295.5, GSR-203, 913; ENST00000643525.1, GSR-207, 1802; ENST00000521479.1, GSR-202, 582"	MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR	chr8:30678066-30727846[-]	Maintains high levels of reduced glutathione in the cytosol.	PDB: 1ALG; PDB: 1BWC; PDB: 1DNC; PDB: 1GRA; PDB: 1GRB; PDB: 1GRE; PDB: 1GRF; PDB: 1GRG; PDB: 1GRH; PDB: 1GRT; PDB: 1GSN; PDB: 1K4Q; PDB: 1XAN; PDB: 2AAQ; PDB: 2GH5; PDB: 2GRT; PDB: 3DJG; PDB: 3DJJ; PDB: 3DK4; PDB: 3DK8; PDB: 3DK9; PDB: 3GRS; PDB: 3GRT; PDB: 3SQP; PDB: 4GR1; PDB: 4GRT; PDB: 5GRT	HGNC:4623	GSHR_HUMAN	Reviewed	ENSG00000104687	.	.	.	.	.
Mol00401	Protein	Solute carrier family 16 member 3 (SLC16A3)	MCT 4; Solute carrier family 16 member 3; MCT4	SLC16A3	9123	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000582743.6, SLC16A3-213, 2599; ENST00000581287.5, SLC16A3-210, 4830; ENST00000580189.6, SLC16A3-209, 2711; ENST00000584689.6, SLC16A3-216, 2667; ENST00000392339.6, SLC16A3-201, 2662; ENST00000392341.6, SLC16A3-202, 2659; ENST00000617373.5, SLC16A3-218, 2636; ENST00000619321.2, SLC16A3-219, 2603; ENST00000580098.6, SLC16A3-208, 2676; ENST00000577650.6, SLC16A3-203, 2503; ENST00000578684.6, SLC16A3-205, 2439; ENST00000583025.1, SLC16A3-214, 955; ENST00000582715.1, SLC16A3-212, 279; ENST00000584781.5, SLC16A3-217, 562; ENST00000583444.1, SLC16A3-215, 2882; ENST00000578574.1, SLC16A3-204, 958; ENST00000579572.1, SLC16A3-207, 863; ENST00000578810.1, SLC16A3-206, 678; ENST00000581642.1, SLC16A3-211, 557"	MGGAVVDEGPTGVKAPDGGWGWAVLFGCFVITGFSYAFPKAVSVFFKELIQEFGIGYSDTAWISSILLAMLYGTGPLCSVCVNRFGCRPVMLVGGLFASLGMVAASFCRSIIQVYLTTGVITGLGLALNFQPSLIMLNRYFSKRRPMANGLAAAGSPVFLCALSPLGQLLQDRYGWRGGFLILGGLLLNCCVCAALMRPLVVTAQPGSGPPRPSRRLLDLSVFRDRGFVLYAVAASVMVLGLFVPPVFVVSYAKDLGVPDTKAAFLLTILGFIDIFARPAAGFVAGLGKVRPYSVYLFSFSMFFNGLADLAGSTAGDYGGLVVFCIFFGISYGMVGALQFEVLMAIVGTHKFSSAIGLVLLMEAVAVLVGPPSGGKLLDATHVYMYVFILAGAEVLTSSLILLLGNFFCIRKKPKEPQPEVAAAEEEKLHKPPADSGVDLREVEHFLKAEPEKNGEVVHTPETSV	chr17:82217934-82261129[+]	"Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity)."	.	HGNC:10924	MOT4_HUMAN	Reviewed	ENSG00000141526	.	.	.	.	.
Mol00402	Protein	HCLS1-associated protein X-1 (HAX1)	HS1-associating protein X-1; HAX-1; HS1-binding protein 1; HSP1BP-1; HS1BP1	HAX1	10456	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000328703.12, HAX1-201, 1109; ENST00000457918.6, HAX1-204, 914; ENST00000483970.6, HAX1-208, 1151; ENST00000435087.2, HAX1-202, 908; ENST00000532105.1, HAX1-211, 771; ENST00000447768.6, HAX1-203, 842; ENST00000531435.5, HAX1-210, 1284; ENST00000471326.5, HAX1-206, 1170; ENST00000477780.2, HAX1-207, 1089; ENST00000492550.1, HAX1-209, 733; ENST00000459914.1, HAX1-205, 726"	MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR	chr1:154272589-154275875[+]	Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools.	.	HGNC:16915	HAX1_HUMAN	Reviewed	ENSG00000143575	.	.	.	.	.
Mol00403	Protein	Proheparin-binding EGF-like growth factor (HBEGF)	HB-EGF; HBEGF; Diphtheria toxin receptor; DT-R; DTR; DTS; HEGFL	HBEGF	1839	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000230990.7, HBEGF-201, 2358; ENST00000482211.2, HBEGF-202, 1230; ENST00000498452.1, HBEGF-203, 565"	MKLLPSVVLKLFLAAVLSALVTGESLERLRRGLAAGTSNPDPPTVSTDQLLPLGGGRDRKVRDLQEADLDLLRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLSLPVENRLYTYDHTTILAVVAVVLSSVCLLVIVGLLMFRYHRRGGYDVENEEKVKLGMTNSH	chr5:140332843-140346603[-]	"Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor."	PDB: 1XDT; PDB: 2M8S	HGNC:3059	HBEGF_HUMAN	Reviewed	ENSG00000113070	.	.	.	.	.
Mol00404	Protein	Histone deacetylase 1 (HDAC1)	HD1; Protein deacetylase HDAC1; Protein decrotonylase HDAC1; RPD3L1	HDAC1	3065	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373548.8, HDAC1-201, 2118; ENST00000428704.1, HDAC1-202, 664; ENST00000490081.5, HDAC1-210, 1047; ENST00000463172.5, HDAC1-203, 895; ENST00000482310.5, HDAC1-208, 779; ENST00000481281.5, HDAC1-207, 721; ENST00000472928.5, HDAC1-205, 532; ENST00000476391.5, HDAC1-206, 2409; ENST00000471488.1, HDAC1-204, 726; ENST00000484305.1, HDAC1-209, 561"	MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA	chr1:32292083-32333635[+]	"Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also functions as deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and TSHZ3. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones."	PDB: 4BKX; PDB: 5ICN; PDB: 6Z2J; PDB: 6Z2K; PDB: 7AO8; PDB: 7AO9; PDB: 7AOA	HGNC:4852	HDAC1_HUMAN	Reviewed	ENSG00000116478	.	.	.	.	.
Mol00405	Protein	Histone deacetylase 3 (HDAC3)	HD3; Protein deacetylase HDAC3; Protein deacylase HDAC3; RPD3-2; SMAP45	HDAC3	8841	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305264.8, HDAC3-201, 1933; ENST00000523088.5, HDAC3-216, 699; ENST00000519474.5, HDAC3-215, 736; ENST00000469207.5, HDAC3-204, 829; ENST00000459727.5, HDAC3-202, 524; ENST00000469550.6, HDAC3-205, 1952; ENST00000492506.1, HDAC3-213, 830; ENST00000495485.1, HDAC3-214, 797; ENST00000492407.1, HDAC3-212, 782; ENST00000491581.5, HDAC3-211, 777; ENST00000486618.1, HDAC3-209, 711; ENST00000467533.5, HDAC3-203, 663; ENST00000490808.1, HDAC3-210, 605; ENST00000471968.1, HDAC3-206, 529; ENST00000476739.5, HDAC3-208, 422; ENST00000475549.1, HDAC3-207, 297"	MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI	chr5:141620876-141636849[-]	"Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation. Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress. Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner. During the activation phase, promotes the accumulation of ubiquitinated ARNTL/BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and ARNTL/BMAL1. The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene ARTNL/BMAL1 and the genes involved in lipid metabolism in the liver. Also functions as deacetylase for non-histone targets, such as KAT5, MEF2D, MAPK14 and RARA. Serves as a corepressor of RARA, mediating its deacetylation and repression, leading to inhibition of RARE DNA element binding. In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response. In addition to protein deacetylase activity, also acts as protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation and de-2-hydroxyisobutyrylation, respectively. Catalyzes decrotonylation of MAPRE1/EB1."	PDB: 4A69	HGNC:4854	HDAC3_HUMAN	Reviewed	ENSG00000171720	.	.	.	.	.
Mol00406	Protein	Histone deacetylase 4 (HDAC4)	HD4; KIAA0288	HDAC4	9759	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000543185.6, HDAC4-215, 8461; ENST00000345617.7, HDAC4-201, 8976; ENST00000430200.1, HDAC4-202, 578; ENST00000454542.5, HDAC4-205, 565; ENST00000446876.1, HDAC4-204, 554; ENST00000445704.1, HDAC4-203, 445; ENST00000685474.1, HDAC4-217, 637; ENST00000553145.1, HDAC4-216, 552; ENST00000494800.1, HDAC4-211, 451; ENST00000690129.1, HDAC4-218, 6209; ENST00000493582.5, HDAC4-210, 3188; ENST00000463007.5, HDAC4-208, 3158; ENST00000535493.5, HDAC4-214, 2743; ENST00000461113.5, HDAC4-207, 1019; ENST00000496347.1, HDAC4-213, 995; ENST00000495497.1, HDAC4-212, 849; ENST00000487617.5, HDAC4-209, 819; ENST00000460235.1, HDAC4-206, 343"	MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL	chr2:239048168-239401654[-]	"Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1."	PDB: 2H8N; PDB: 2O94; PDB: 2VQJ; PDB: 2VQM; PDB: 2VQO; PDB: 2VQQ; PDB: 2VQV; PDB: 2VQW; PDB: 3UXG; PDB: 3UZD; PDB: 3V31; PDB: 4CBT; PDB: 4CBY; PDB: 5A2S; PDB: 5ZOO; PDB: 5ZOP; PDB: 6FYZ	HGNC:14063	HDAC4_HUMAN	Reviewed	ENSG00000068024	.	.	.	.	.
Mol00407	Protein	Hypermethylated in cancer 2 protein (HIC2)	Hic-2; HIC1-related gene on chromosome 22 protein; Hic-3; Zinc finger and BTB domain-containing protein 30; HRG22; KIAA1020; ZBTB30	HIC2	23119	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000407464.7, HIC2-201, 6831; ENST00000443632.2, HIC2-203, 6940; ENST00000407598.2, HIC2-202, 4734"	MVSGPLALRWCAWAGRGDMGPDMELPSHSKQLLLQLNQQRTKGFLCDVIIMVENSIFRAHKNVLAASSIYFKSLVLHDNLINLDTDMVSSTVFQQILDFIYTGKLLPSDQPAEPNFSTLLTAASYLQLPELAALCRRKLKRAGKPFGSGRAGSTGMGRPPRSQRLSTASVIQARYQGLVDGRKGAHAPQELPQAKGSDDELFLGGSNQDSVQGLGRAVCPAGGEAGLGGCSSSTNGSSGGCEQELGLDLSKKSPPLPPATPGPHLTPDDAAQLSDSQHGSPPAASAPPVANSASYSELGGTPDEPMDLEGAEDNHLSLLEAPGGQPRKSLRHSTRKKEWGKKEPVAGSPFERREAGPKGPCPGEEGEGVGDRVPNGILASGAGPSGPYGEPPYPCKEEEENGKDASEDSAQSGSEGGSGHASAHYMYRQEGYETVSYGDNLYVCIPCAKGFPSSEQLNAHVETHTEEELFIKEEGAYETGSGGAEEEAEDLSAPSAAYTAEPRPFKCSVCEKTYKDPATLRQHEKTHWLTRPFPCNICGKMFTQRGTMTRHMRSHLGLKPFACDECGMRFTRQYRLTEHMRVHSGEKPYECQLCGGKFTQQRNLISHLRMHTSPS	chr22:21417371-21451463[+]	Transcriptional repressor.	.	HGNC:18595	HIC2_HUMAN	Reviewed	ENSG00000169635	.	.	.	.	.
Mol00408	Protein	Homeodomain-interacting protein kinase 2 (HIPK2)	hHIPk2	HIPK2	28996	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000406875.8, HIPK2-202, 15329; ENST00000428878.6, HIPK2-203, 3969; ENST00000342645.7, HIPK2-201, 2937"	MAPVYEGMASHVQVFSPHTLQSSAFCSVKKLKIEPSSNWDMTGYGSHSKVYSQSKNIPLSQPATTTVSTSLPVPNPSLPYEQTIVFPGSTGHIVVTSASSTSVTGQVLGGPHNLMRRSTVSLLDTYQKCGLKRKSEEIENTSSVQIIEEHPPMIQNNASGATVATATTSTATSKNSGSNSEGDYQLVQHEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPVLQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDTDSPYPLWRLKTPDDHEAETGIKSKEARKYIFNCLDDMAQVNMTTDLEGSDMLVEKADRREFIDLLKKMLTIDADKRITPIETLNHPFVTMTHLLDFPHSTHVKSCFQNMEICKRRVNMYDTVNQSKTPFITHVAPSTSTNLTMTFNNQLTTVHNQAPSSTSATISLANPEVSILNYPSTLYQPSAASMAAVAQRSMPLQTGTAQICARPDPFQQALIVCPPGFQGLQASPSKHAGYSVRMENAVPIVTQAPGAQPLQIQPGLLAQQAWPSGTQQILLPPAWQQLTGVATHTSVQHATVIPETMAGTQQLADWRNTHAHGSHYNPIMQQPALLTGHVTLPAAQPLNVGVAHVMRQQPTSTTSSRKSKQHQSSVRNVSTCEVSSSQAISSPQRSKRVKENTPPRCAMVHSSPACSTSVTCGWGDVASSTTRERQRQTIVIPDTPSPTVSVITISSDTDEEEEQKHAPTSTVSKQRKNVISCVTVHDSPYSDSSSNTSPYSVQQRAGHNNANAFDTKGSLENHCTGNPRTIIVPPLKTQASEVLVECDSLVPVNTSHHSSSYKSKSSSNVTSTSGHSSGSSSGAITYRQQRPGPHFQQQQPLNLSQAQQHITTDRTGSHRRQQAYITPTMAQAPYSFPHNSPSHGTVHPHLAAAAAAAHLPTQPHLYTYTAPAALGSTGTVAHLVASQGSARHTVQHTAYPASIVHQVPVSMGPRVLPSPTIHPSQYPAQFAHQTYISASPASTVYTGYPLSPAKVNQYPYI	chr7:139561570-139777998[-]	"Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1 and ZBTB4. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis."	PDB: 6P5S; PDB: 7NCF	HGNC:14402	HIPK2_HUMAN	Reviewed	ENSG00000064393	.	.	.	.	.
Mol00409	Protein	Homeodomain-interacting protein kinase 3 (HIPK3)	Androgen receptor-interacting nuclear protein kinase; ANPK; Fas-interacting serine/threonine-protein kinase; FIST; Homolog of protein kinase YAK1; DYRK6; FIST3; PKY	HIPK3	10114	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000303296.9, HIPK3-201, 7614; ENST00000456517.2, HIPK3-203, 7399; ENST00000379016.7, HIPK3-202, 7345; ENST00000525975.5, HIPK3-204, 3668; ENST00000531504.5, HIPK3-205, 591; ENST00000534262.1, HIPK3-206, 349"	MASQVLVYPPYVYQTQSSAFCSVKKLKVEPSSCVFQERNYPRTYVNGRNFGNSHPPTKGSAFQTKIPFNRPRGHNFSLQTSAVVLKNTAGATKVIAAQAQQAHVQAPQIGAWRNRLHFLEGPQRCGLKRKSEELDNHSSAMQIVDELSILPAMLQTNMGNPVTVVTATTGSKQNCTTGEGDYQLVQHEVLCSMKNTYEVLDFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTENADEYNFVRAYECFQHRNHTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKSTRFFCKETDMSHSGWRLKTLEEHEAETGMKSKEARKYIFNSLDDVAHVNTVMDLEGSDLLAEKADRREFVSLLKKMLLIDADLRITPAETLNHPFVNMKHLLDFPHSNHVKSCFHIMDICKSHLNSCDTNNHNKTSLLRPVASSSTATLTANFTKIGTLRSQALTTSAHSVVHHGIPLQAGTAQFGCGDAFQQTLIICPPAIQGIPATHGKPTSYSIRVDNTVPLVTQAPAVQPLQIRPGVLSQTWSGRTQQMLVPAWQQVTPLAPATTTLTSESVAGSHRLGDWGKMISCSNHYNSVMPQPLLTNQITLSAPQPVSVGIAHVVWPQPATTKKNKQCQNRGILVKLMEWEPGREEINAFSWSNSLQNTNIPHSAFISPKIINGKDVEEVSCIETQDNQNSEGEARNCCETSIRQDSDSSVSDKQRQTIIIADSPSPAVSVITISSDTDEEETSQRHSLRECKGSLDCEACQSTLNIDRMCSLSSPDSTLSTSSSGQSSPSPCKRPNSMSDEEQESSCDTVDGSPTSDSSGHDSPFAESTFVEDTHENTELVSSADTETKPAVCSVVVPPVELENGLNADEHMANTDSICQPLIKGRSAPGRLNQPSAVGTRQQKLTSAFQQQHLNFSQVQHFGSGHQEWNGNFGHRRQQAYIPTSVTSNPFTLSHGSPNHTAVHAHLAGNTHLGGQPTLLPYPSSATLSSAAPVAHLLASPCTSRPMLQHPTYNISHPSGIVHQVPVGLNPRLLPSPTIHQTQYKPIFPPHSYIAASPAYTGFPLSPTKLSQYPYM	chr11:33256672-33357023[+]	"Serine/threonine-protein kinase involved in transcription regulation, apoptosis and steroidogenic gene expression. Phosphorylates JUN and RUNX2. Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. The phosphorylation of NR5A1 activates SF1 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. In osteoblasts, supports transcription activation: phosphorylates RUNX2 that synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE)."	.	HGNC:4915	HIPK3_HUMAN	Reviewed	ENSG00000110422	.	.	.	.	.
Mol00410	Protein	High mobility group protein B2 (HMGB2)	High mobility group protein 2; HMG-2; HMG2	HMGB2	3148	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000296503.10, HMGB2-201, 1441; ENST00000446922.6, HMGB2-203, 1175; ENST00000438704.6, HMGB2-202, 1032; ENST00000506267.1, HMGB2-204, 629; ENST00000511316.1, HMGB2-205, 1841"	MGKGDPNKPRGKMSSYAFFVQTCREEHKKKHPDSSVNFAEFSKKCSERWKTMSAKEKSKFEDMAKSDKARYDREMKNYVPPKGDKKGKKKDPNAPKRPPSAFFLFCSEHRPKIKSEHPGLSIGDTAKKLGEMWSEQSAKDKQPYEQKAAKLKEKYEKDIAAYRAKGKSEAGKKGPGRPTGSKKKNEPEDEEEEEEEEDEDEEEEDEDEE	chr4:173331376-173334432[-]	"Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity. Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS). Proposed to be involved in the innate immune response to nucleic acids by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors. In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE. Has antimicrobial activity in gastrointestinal epithelial tissues. Involved in inflammatory response to antigenic stimulus coupled with proinflammatory activity. Involved in modulation of neurogenesis probably by regulation of neural stem proliferation. Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway."	.	HGNC:5000	HMGB2_HUMAN	Reviewed	ENSG00000164104	.	.	.	.	.
Mol00411	Protein	High mobility group protein B3 (HMGB3)	High mobility group protein 2a; HMG-2a; High mobility group protein 4; HMG-4; HMG2A; HMG4	HMGB3	3149	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000325307.12, HMGB3-201, 3507; ENST00000448905.6, HMGB3-204, 812; ENST00000455596.5, HMGB3-205, 793; ENST00000419110.5, HMGB3-202, 707; ENST00000430118.1, HMGB3-203, 529"	MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSGKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLNDSEKQPYITKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEDEEEEEEEEEEEEEEDE	chrX:150980509-150990771[+]	Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters (By similarity). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor (By similarity). Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (By similarity).	PDB: 2EQZ; PDB: 2YQI	HGNC:5004	HMGB3_HUMAN	Reviewed	ENSG00000029993	.	.	.	.	.
Mol00412	Protein	Nucleosome-binding protein 1 (NSBP1)	Nucleosome-binding protein 1; NSBP1	HMGN5	79366	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000358130.7, HMGN5-201, 2099; ENST00000436386.5, HMGN5-204, 859; ENST00000447319.5, HMGN5-205, 742; ENST00000451455.1, HMGN5-206, 720; ENST00000430960.5, HMGN5-203, 578; ENST00000373250.7, HMGN5-202, 572; ENST00000491275.1, HMGN5-207, 547"	MPKRKAAGQGDMRQEPKRRSARLSAMLVPVTPEVKPKRTSSSRKMKTKSDMMEENIDTSAQAVAETKQEAVVEEDYNENAKNGEAKITEAPASEKEIVEVKEENIEDATEKGGEKKEAVAAEVKNEEEDQKEDEEDQNEEKGEAGKEDKDEKGEEDGKEDKNGNEKGEDAKEKEDGKKGEDGKGNGEDGKEKGEDEKEEEDRKETGDGKENEDGKEKGDKKEGKDVKVKEDEKEREDGKEDEGGNEEEAGKEKEDLKEEEEGKEEDEIKEDDGKKEEPQSIV	chrX:81113699-81201913[-]	Preferentially binds to euchromatin and modulates cellular transcription by counteracting linker histone-mediated chromatin compaction.	.	HGNC:8013	HMGN5_HUMAN	Reviewed	ENSG00000198157	.	.	.	.	.
Mol00413	Protein	Heterogeneous nuclear ribonucleoprotein U (HNRNPU)	hnRNP U; GRIP120; Nuclear p120 ribonucleoprotein; Scaffold-attachment factor A; SAF-A; p120; pp120; C1orf199; HNRPU; SAFA; U21.1	HNRNPU	3192	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000640218.2, HNRNPU-226, 6867; ENST00000444376.7, HNRNPU-205, 6827; ENST00000639628.2, HNRNPU-219, 7674; ENST00000640001.1, HNRNPU-223, 4227; ENST00000440865.2, HNRNPU-204, 3207; ENST00000283179.14, HNRNPU-201, 3120; ENST00000638475.1, HNRNPU-214, 2698; ENST00000638716.1, HNRNPU-216, 2640; ENST00000639824.1, HNRNPU-221, 1450; ENST00000483966.3, HNRNPU-210, 1069; ENST00000475997.6, HNRNPU-208, 5290; ENST00000639880.1, HNRNPU-222, 4239; ENST00000638301.1, HNRNPU-213, 3650; ENST00000640306.1, HNRNPU-228, 2917; ENST00000640056.1, HNRNPU-224, 2045; ENST00000638230.1, HNRNPU-212, 1922; ENST00000640440.1, HNRNPU-229, 871; ENST00000640119.1, HNRNPU-225, 461; ENST00000489705.2, HNRNPU-211, 451; ENST00000465881.2, HNRNPU-206, 883; ENST00000640264.1, HNRNPU-227, 328; ENST00000649899.1, HNRNPU-231, 13084; ENST00000366527.4, HNRNPU-203, 12852; ENST00000638952.1, HNRNPU-217, 5678; ENST00000468690.2, HNRNPU-207, 5273; ENST00000476241.2, HNRNPU-209, 4844; ENST00000640657.1, HNRNPU-230, 4323; ENST00000639667.1, HNRNPU-220, 3940; ENST00000366525.8, HNRNPU-202, 2851; ENST00000639064.1, HNRNPU-218, 2625; ENST00000638589.1, HNRNPU-215, 2225"	MSSSPVNVKKLKVSELKEELKKRRLSDKGLKAELMERLQAALDDEEAGGRPAMEPGNGSLDLGGDSAGRSGAGLEQEAAAGGDEEEEEEEEEEEGISALDGDQMELGEENGAAGAADSGPMEEEEAASEDENGDDQGFQEGEDELGDEEEGAGDENGHGEQQPQPPATQQQQPQQQRGAAKEAAGKSSGPTSLFAVTVAPPGARQGQQQAGGKKKAEGGGGGGRPGAPAAGDGKTEQKGGDKKRGVKRPREDHGRGYFEYIEENKYSRAKSPQPPVEEEDEHFDDTVVCLDTYNCDLHFKISRDRLSASSLTMESFAFLWAGGRASYGVSKGKVCFEMKVTEKIPVRHLYTKDIDIHEVRIGWSLTTSGMLLGEEEFSYGYSLKGIKTCNCETEDYGEKFDENDVITCFANFESDEVELSYAKNGQDLGVAFKISKEVLAGRPLFPHVLCHNCAVEFNFGQKEKPYFPIPEEYTFIQNVPLEDRVRGPKGPEEKKDCEVVMMIGLPGAGKTTWVTKHAAENPGKYNILGTNTIMDKMMVAGFKKQMADTGKLNTLLQRAPQCLGKFIEIAARKKRNFILDQTNVSAAAQRRKMCLFAGFQRKAVVVCPKDEDYKQRTQKKAEVEGKDLPEHAVLKMKGNFTLPEVAECFDEITYVELQKEEAQKLLEQYKEESKKALPPEKKQNTGSKKSNKNKSGKNQFNRGGGHRGRGGFNMRGGNFRGGAPGNRGGYNRRGNMPQRGGGGGGSGGIGYPYPRAPVFPGRGSYSNRGNYNRGGMPNRGNYNQNFRGRGNNRGYKNQSQGYNQWQQGQFWGQKPWSQHYHQGYY	chr1:244840638-244864560[-]	"DNA- and RNA-binding protein involved in several cellular processes such as nuclear chromatin organization, telomere-length regulation, transcription, mRNA alternative splicing and stability, Xist-mediated transcriptional silencing and mitotic cell progression. Plays a role in the regulation of interphase large-scale gene-rich chromatin organization through chromatin-associated RNAs (caRNAs) in a transcription-dependent manner, and thereby maintains genomic stability. Required for the localization of the long non-coding Xist RNA on the inactive chromosome X (Xi) and the subsequent initiation and maintenance of X-linked transcriptional gene silencing during X-inactivation. Plays a role as a RNA polymerase II (Pol II) holoenzyme transcription regulator. Promotes transcription initiation by direct association with the core-TFIIH basal transcription factor complex for the assembly of a functional pre-initiation complex with Pol II in a actin-dependent manner. Blocks Pol II transcription elongation activity by inhibiting the C-terminal domain (CTD) phosphorylation of Pol II and dissociates from Pol II pre-initiation complex prior to productive transcription elongation. Positively regulates CBX5-induced transcriptional gene silencing and retention of CBX5 in the nucleus. Negatively regulates glucocorticoid-mediated transcriptional activation. Key regulator of transcription initiation and elongation in embryonic stem cells upon leukemia inhibitory factor (LIF) signaling. Involved in the long non-coding RNA H19-mediated Pol II transcriptional repression. Participates in the circadian regulation of the core clock component ARNTL/BMAL1 transcription. Plays a role in the regulation of telomere length. Plays a role as a global pre-mRNA alternative splicing modulator by regulating U2 small nuclear ribonucleoprotein (snRNP) biogenesis. Plays a role in mRNA stability. Component of the CRD-mediated complex that promotes MYC mRNA stabilization. Enhances the expression of specific genes, such as tumor necrosis factor TNFA, by regulating mRNA stability, possibly through binding to the 3'-untranslated region (UTR). Plays a role in mitotic cell cycle regulation. Involved in the formation of stable mitotic spindle microtubules (MTs) attachment to kinetochore, spindle organization and chromosome congression. Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement and segregation and progression through mitosis. Contributes also to the targeting of AURKA to mitotic spindle MTs. Binds to double- and single-stranded DNA and RNA, poly(A), poly(C) and poly(G) oligoribonucleotides. Binds to chromatin-associated RNAs (caRNAs). Associates with chromatin to scaffold/matrix attachment region (S/MAR) elements in a chromatin-associated RNAs (caRNAs)-dependent manner. Binds to the Xist RNA. Binds the long non-coding H19 RNA. Binds to SMN1/2 pre-mRNAs at G/U-rich regions. Binds to small nuclear RNAs (snRNAs). Binds to the 3'-UTR of TNFA mRNA. Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA; this binding is direct and bridges the Xist RNA and the inactive chromosome X (Xi). Also negatively regulates embryonic stem cell differentiation upon LIF signaling. Required for embryonic development. Binds to brown fat long non-coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B required to drive brown and beige fat development and thermogenesis."	PDB: 1ZRJ	HGNC:5048	HNRPU_HUMAN	Reviewed	ENSG00000153187	.	.	.	.	.
Mol00414	Protein	Heat shock cognate 71 kDa protein (HSPA8)	Heat shock 70 kDa protein 8; Lipopolysaccharide-associated protein 1; LAP-1; LPS-associated protein 1; HSC70; HSP73; HSPA10	HSPA8	3312	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000534624.6, HSPA8-224, 2264; ENST00000532636.5, HSPA8-218, 2306; ENST00000227378.7, HSPA8-201, 2186; ENST00000453788.6, HSPA8-202, 2004; ENST00000526110.5, HSPA8-207, 1924; ENST00000534319.5, HSPA8-222, 1884; ENST00000533540.5, HSPA8-221, 1826; ENST00000528292.5, HSPA8-212, 1112; ENST00000525624.5, HSPA8-206, 1048; ENST00000524552.5, HSPA8-203, 963; ENST00000526686.1, HSPA8-208, 740; ENST00000532182.5, HSPA8-217, 674; ENST00000530391.1, HSPA8-213, 648; ENST00000534567.5, HSPA8-223, 588; ENST00000525463.5, HSPA8-205, 583; ENST00000527387.5, HSPA8-210, 579; ENST00000524590.5, HSPA8-204, 536; ENST00000526862.1, HSPA8-209, 504; ENST00000533238.5, HSPA8-220, 465; ENST00000532091.1, HSPA8-215, 2301; ENST00000527983.5, HSPA8-211, 1509; ENST00000532780.5, HSPA8-219, 1194; ENST00000531063.1, HSPA8-214, 578; ENST00000532167.5, HSPA8-216, 570"	MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD	chr11:123057489-123063230[-]	"Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21."	PDB: 3AGY; PDB: 3AGZ; PDB: 3ESK; PDB: 3FZF; PDB: 3FZH; PDB: 3FZK; PDB: 3FZL; PDB: 3FZM; PDB: 3LDQ; PDB: 3M3Z; PDB: 4H5N; PDB: 4H5R; PDB: 4H5T; PDB: 4H5V; PDB: 4H5W; PDB: 4HWI; PDB: 4KBQ; PDB: 5AQF; PDB: 5AQG; PDB: 5AQH; PDB: 5AQI; PDB: 5AQJ; PDB: 5AQK; PDB: 5AQL; PDB: 5AQM; PDB: 5AQN; PDB: 5AQO; PDB: 5AQP; PDB: 5AQQ; PDB: 5AQR; PDB: 5AQS; PDB: 5AQT; PDB: 5AQU; PDB: 5AQV; PDB: 6B1I; PDB: 6B1M; PDB: 6B1N; PDB: 6ZYJ	HGNC:5241	HSP7C_HUMAN	Reviewed	ENSG00000109971	.	.	.	.	.
Mol00415	Protein	Heat shock protein beta-1 (HSPB1)	HspB1; 28 kDa heat shock protein; Estrogen-regulated 24 kDa protein; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; HSP27; HSP28	HSPB1	3315	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000248553.7, HSPB1-201, 777; ENST00000675538.1, HSPB1-213, 812; ENST00000676231.1, HSPB1-218, 807; ENST00000674547.1, HSPB1-204, 800; ENST00000675906.1, HSPB1-216, 794; ENST00000675226.1, HSPB1-210, 776; ENST00000674638.1, HSPB1-206, 772; ENST00000675134.1, HSPB1-209, 756; ENST00000674650.1, HSPB1-207, 687; ENST00000429938.1, HSPB1-202, 527; ENST00000674965.1, HSPB1-208, 802; ENST00000674560.1, HSPB1-205, 436; ENST00000675488.1, HSPB1-212, 435; ENST00000675733.1, HSPB1-215, 435; ENST00000676398.1, HSPB1-219, 434; ENST00000675624.1, HSPB1-214, 434; ENST00000676195.1, HSPB1-217, 144; ENST00000447574.1, HSPB1-203, 1455; ENST00000675417.1, HSPB1-211, 1089"	MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK	chr7:76302673-76304295[+]	Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.	PDB: 2N3J; PDB: 3Q9P; PDB: 3Q9Q; PDB: 4MJH; PDB: 6DV5; PDB: 6GJH	HGNC:5246	HSPB1_HUMAN	Reviewed	ENSG00000106211	.	.	.	.	.
Mol00416	Protein	Homeobox protein Hox-A1 (HOXA1)	Homeobox protein Hox-1F; HOX1F	HOXA1	3198	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000643460.2, HOXA1-202, 2543; ENST00000355633.5, HOXA1-201, 2016"	MDNARMNSFLEYPILSSGDSGTCSARAYPSDHRITTFQSCAVSANSCGGDDRFLVGRGVQIGSPHHHHHHHHHHPQPATYQTSGNLGVSYSHSSCGPSYGSQNFSAPYSPYALNQEADVSGGYPQCAPAVYSGNLSSPMVQHHHHHQGYAGGAVGSPQYIHHSYGQEHQSLALATYNNSLSPLHASHQEACRSPASETSSPAQTFDWMKVKRNPPKTGKVGEYGYLGQPNAVRTNFTTKQLTELEKEFHFNKYLTRARRVEIAASLQLNETQVKIWFQNRRMKQKKREKEGLLPISPATPPGNDEKAEESSEKSSSSPCVPSPGSSTSDTLTTSH	chr7:27092993-27096000[-]	"Sequence-specific transcription factor. Regulates multiple developmental processes including brainstem, inner and outer ear, abducens nerve and cardiovascular development and morphogenesis as well as cognition and behavior. Also part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Seems to act in the maintenance and/or generation of hindbrain segments. Activates transcription in the presence of PBX1A and PKNOX1."	.	HGNC:5099	HXA1_HUMAN	Reviewed	ENSG00000105991	.	.	.	.	.
Mol00417	Protein	Homeobox protein Hox-A3 (HOXA3)	Homeobox protein Hox-1E; HOX1E	HOXA3	3200	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000612286.5, HOXA3-206, 3026; ENST00000396352.8, HOXA3-202, 3263; ENST00000317201.7, HOXA3-201, 2763; ENST00000522788.5, HOXA3-205, 581; ENST00000522456.1, HOXA3-204, 503; ENST00000521401.1, HOXA3-203, 598"	MQKATYYDSSAIYGGYPYQAANGFAYNANQQPYPASAALGADGEYHRPACSLQSPSSAGGHPKAHELSEACLRTLSAPPSQPPSLGEPPLHPPPPQAAPPAPQPPQPAPQPPAPTPAAPPPPSSASPPQNASNNPTPANAAKSPLLNSPTVAKQIFPWMKESRQNTKQKTSSSSSGESCAGDKSPPGQASSKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLTERQIKIWFQNRRMKYKKDQKGKGMLTSSGGQSPSRSPVPPGAGGYLNSMHSLVNSVPYEPQSPPPFSKPPQGTYGLPPASYPASLPSCAPPPPPQKRYTAAGAGAGGTPDYDPHAHGLQGNGSYGTPHIQGSPVFVGGSYVEPMSNSGPALFGLTHLPHAASGAMDYGGAGPLGSGHHHGPGPGEPHPTYTDLTGHHPSQGRIQEAPKLTHL	chr7:27106184-27152583[-]	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	.	HGNC:5104	HXA3_HUMAN	Reviewed	ENSG00000105997	.	.	.	.	.
Mol00418	Protein	Homeobox protein Hox-A5 (HOXA5)	Homeobox protein Hox-1C; HOX1C	HOXA5	3202	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000222726.4, HOXA5-201, 1670; ENST00000520854.1, HOXA5-202, 329"	MSSYFVNSFCGRYPNGPDYQLHNYGDHSSVSEQFRDSASMHSGRYGYGYNGMDLSVGRSGSGHFGSGERARSYAASASAAPAEPRYSQPATSTHSPQPDPLPCSAVAPSPGSDSHHGGKNSLSNSSGASADAGSTHISSREGVGTASGAEEDAPASSEQASAQSEPSPAPPAQPQIYPWMRKLHISHDNIGGPEGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMSMAAAGGAFRP	chr7:27141052-27143681[-]	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Also binds to its own promoter. Binds specifically to the motif 5'-CYYNATTA[TG]Y-3'.	.	HGNC:5106	HXA5_HUMAN	Reviewed	ENSG00000106004	.	.	.	.	.
Mol00419	Protein	Homeobox protein Hox-C9 (HOXC9)	Homeobox protein Hox-3B; HOX3B	HOXC9	3225	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000303450.5, HOXC9-201, 1474; ENST00000508190.1, HOXC9-203, 1505; ENST00000504557.1, HOXC9-202, 581"	MSATGPISNYYVDSLISHDNEDLLASRFPATGAHPAAARPSGLVPDCSDFPSCSFAPKPAVFSTSWAPVPSQSSVVYHPYGPQPHLGADTRYMRTWLEPLSGAVSFPSFPAGGRHYALKPDAYPGRRADCGPGEGRSYPDYMYGSPGELRDRAPQTLPSPEADALAGSKHKEEKADLDPSNPVANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARVLNLTERQVKIWFQNRRMKMKKMNKEKTDKEQS	chr12:53994895-54003337[+]	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	PDB: 2LP0; PDB: 2MSY	HGNC:5130	HXC9_HUMAN	Reviewed	ENSG00000180806	.	.	.	.	.
Mol00420	Protein	Homeobox protein Hox-D8 (HOXD8)	Homeobox protein Hox-4E; Homeobox protein Hox-5.4; HOX4E	HOXD8	3234	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000313173.6, HOXD8-201, 2618; ENST00000429017.2, HOXD8-202, 1608; ENST00000450510.2, HOXD8-203, 1268; ENST00000544999.2, HOXD8-204, 1235"	MSSYFVNPLYSKYKAAAAAAAAAGEAINPTYYDCHFAPEVGGRHAAAAAALQLYGNSAAGFPHAPPQAHAHPHPSPPPSGTGCGGREGRGQEYFHPGGGSPAAAYQAAPPPPPHPPPPPPPPPCGGIACHGEPAKFYGYDNLQRQPIFTTQQEAELVQYPDCKSSSGNIGEDPDHLNQSSSPSQMFPWMRPQAAPGRRRGRQTYSRFQTLELEKEFLFNPYLTRKRRIEVSHALALTERQVKIWFQNRRMKWKKENNKDKFPVSRQEVKDGETKKEAQELEEDRAEGLTN	chr2:176129694-176132695[+]	Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.	.	HGNC:5139	HXD8_HUMAN	Reviewed	ENSG00000175879	.	.	.	.	.
Mol00421	Protein	Hexokinase-1 (HK1)	Brain form hexokinase; Hexokinase type I; HK I; Hexokinase-A	HK1	3098	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359426.7, HK1-202, 3602; ENST00000643399.2, HK1-218, 3998; ENST00000448642.6, HK1-206, 3868; ENST00000436817.6, HK1-205, 3835; ENST00000298649.8, HK1-201, 3229; ENST00000360289.6, HK1-203, 3961; ENST00000421088.5, HK1-204, 707; ENST00000464803.6, HK1-208, 567; ENST00000476368.6, HK1-210, 456; ENST00000450646.6, HK1-207, 449; ENST00000493591.6, HK1-216, 3745; ENST00000483077.5, HK1-214, 750; ENST00000479594.5, HK1-211, 680; ENST00000488644.5, HK1-215, 593; ENST00000483054.5, HK1-213, 592; ENST00000480047.5, HK1-212, 575; ENST00000470050.1, HK1-209, 314; ENST00000494253.1, HK1-217, 2848"	MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRLRTEASS	chr10:69269984-69401884[+]	"Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively). Does not phosphorylate N-acetyl-D-glucosamine. Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate. Involved in innate immunity and inflammation by acting as a pattern recognition receptor for bacterial peptidoglycan. When released in the cytosol, N-acetyl-D-glucosamine component of bacterial peptidoglycan inhibits the hexokinase activity of HK1 and causes its dissociation from mitochondrial outer membrane, thereby activating the NLRP3 inflammasome."	PDB: 1CZA; PDB: 1DGK; PDB: 1HKB; PDB: 1HKC; PDB: 1QHA; PDB: 4F9O; PDB: 4FOE; PDB: 4FOI; PDB: 4FPA; PDB: 4FPB	HGNC:4922	HXK1_HUMAN	Reviewed	ENSG00000156515	.	.	.	.	.
Mol00422	Protein	Hexokinase-2 (HK2)	Hexokinase type II; HK II; Hexokinase-B; Muscle form hexokinase	HK2	3099	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000290573.7, HK2-201, 5626; ENST00000409174.1, HK2-202, 5278; ENST00000472302.1, HK2-203, 395"	MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDDFRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKGAALITAVACRIREAGQR	chr2:74834127-74893359[+]	"Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate. Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis."	PDB: 2NZT; PDB: 5HEX; PDB: 5HFU; PDB: 5HG1	HGNC:4923	HXK2_HUMAN	Reviewed	ENSG00000159399	.	.	.	.	.
Mol00423	Protein	Oxalosuccinate decarboxylase (IDH1)	IDH; Cytosolic NADP-isocitrate dehydrogenase; IDP; NADP(+)-specific ICDH; Oxalosuccinate decarboxylase; PICD	IDH1	3417	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000345146.7, IDH1-201, 2318; ENST00000415913.5, IDH1-203, 2441; ENST00000446179.5, IDH1-205, 2298; ENST00000415282.5, IDH1-202, 942; ENST00000417583.5, IDH1-204, 702; ENST00000451391.5, IDH1-206, 563; ENST00000462386.5, IDH1-207, 1614; ENST00000484575.1, IDH1-209, 1044; ENST00000481557.1, IDH1-208, 556"	MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL	chr2:208236229-208266074[-]	.	PDB: 1T09; PDB: 1T0L; PDB: 3INM; PDB: 3MAP; PDB: 3MAR; PDB: 3MAS; PDB: 4I3K; PDB: 4I3L; PDB: 4KZO; PDB: 4L03; PDB: 4L04; PDB: 4L06; PDB: 4UMX; PDB: 4UMY; PDB: 4XRX; PDB: 4XS3; PDB: 5DE1; PDB: 5GIR; PDB: 5K10; PDB: 5K11; PDB: 5L57; PDB: 5L58; PDB: 5LGE; PDB: 5SUN; PDB: 5SVF; PDB: 5TQH; PDB: 5YFM; PDB: 5YFN; PDB: 6ADG; PDB: 6B0Z; PDB: 6BKX; PDB: 6BKY; PDB: 6BKZ; PDB: 6BL0; PDB: 6BL1; PDB: 6BL2; PDB: 6IO0; PDB: 6O2Y; PDB: 6O2Z; PDB: 6PAY; PDB: 6Q6F; PDB: 6U4J; PDB: 6VEI; PDB: 6VG0	HGNC:5382	IDHC_HUMAN	Reviewed	ENSG00000138413	.	.	.	.	.
Mol00424	Protein	Eukaryotic initiation factor 4A-I (EIF4A1)	eIF-4A-I; eIF4A-I; ATP-dependent RNA helicase eIF4A-1; DDX2A; EIF4A	EIF4A1	1973	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000293831.13, EIF4A1-201, 1758; ENST00000577269.5, EIF4A1-203, 1319; ENST00000582746.5, EIF4A1-224, 1645; ENST00000584860.5, EIF4A1-234, 1109; ENST00000583389.5, EIF4A1-227, 951; ENST00000578495.5, EIF4A1-209, 916; ENST00000584784.5, EIF4A1-232, 818; ENST00000577929.1, EIF4A1-206, 696; ENST00000581384.5, EIF4A1-216, 642; ENST00000585024.5, EIF4A1-236, 577; ENST00000583802.5, EIF4A1-228, 563; ENST00000582169.5, EIF4A1-222, 552; ENST00000578754.5, EIF4A1-211, 547; ENST00000581770.5, EIF4A1-218, 447; ENST00000581544.5, EIF4A1-217, 1444; ENST00000580461.5, EIF4A1-214, 909; ENST00000582050.1, EIF4A1-221, 576; ENST00000578476.5, EIF4A1-208, 573; ENST00000579139.1, EIF4A1-213, 568; ENST00000581808.1, EIF4A1-219, 205; ENST00000578324.5, EIF4A1-207, 1577; ENST00000584798.1, EIF4A1-233, 1440; ENST00000396527.7, EIF4A1-202, 1169; ENST00000584901.5, EIF4A1-235, 1021; ENST00000584712.5, EIF4A1-231, 782; ENST00000584054.5, EIF4A1-230, 716; ENST00000583899.5, EIF4A1-229, 665; ENST00000581841.1, EIF4A1-220, 621; ENST00000583217.1, EIF4A1-226, 599; ENST00000582848.5, EIF4A1-225, 591; ENST00000578569.1, EIF4A1-210, 583; ENST00000577731.1, EIF4A1-204, 574; ENST00000579085.5, EIF4A1-212, 569; ENST00000580886.5, EIF4A1-215, 562; ENST00000582213.5, EIF4A1-223, 560; ENST00000577738.5, EIF4A1-205, 531"	MSASQDSRSRDNGPDGMEPEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI	chr17:7572824-7579006[+]	"ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon."	.	HGNC:3282	IF4A1_HUMAN	Reviewed	ENSG00000161960	.	.	.	.	.
Mol00425	Protein	Eukaryotic initiation factor 4A-III (EIF4A3)	eIF-4A-III; eIF4A-III; ATP-dependent RNA helicase DDX48; ATP-dependent RNA helicase eIF4A-3; DEAD box protein 48; Eukaryotic initiation factor 4A-like NUK-34; Eukaryotic translation initiation factor 4A isoform 3; Nuclear matrix protein 265; NMP 265; hNMP 265; DDX48; KIAA0111	EIF4A3	9775	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649764.2, EIF4A3-209, 2524; ENST00000647795.1, EIF4A3-208, 1579; ENST00000576547.2, EIF4A3-206, 1492; ENST00000575978.1, EIF4A3-205, 3593; ENST00000575668.1, EIF4A3-203, 831; ENST00000576573.1, EIF4A3-207, 697; ENST00000575957.1, EIF4A3-204, 574; ENST00000570625.5, EIF4A3-201, 562; ENST00000570837.1, EIF4A3-202, 534"	MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI	chr17:80134369-80147151[-]	"ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. Involved in craniofacial development."	PDB: 2HXY; PDB: 2HYI; PDB: 2J0Q; PDB: 2J0S; PDB: 2J0U; PDB: 2XB2; PDB: 3EX7; PDB: 4C9B; PDB: 5MQF; PDB: 5XJC; PDB: 5YZG; PDB: 6ICZ; PDB: 6QDV; PDB: 6YVH; PDB: 7A5P	HGNC:18683	IF4A3_HUMAN	Reviewed	ENSG00000141543	.	.	.	.	.
Mol00426	Protein	Eukaryotic translation initiation factor 4E (EIF4E)	eIF-4E; eIF4E; eIF-4F 25 kDa subunit; mRNA cap-binding protein; EIF4EL1; EIF4F	EIF4E	1977	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000450253.7, EIF4E-203, 2427; ENST00000504432.5, EIF4E-204, 1132; ENST00000280892.10, EIF4E-201, 1097; ENST00000505992.1, EIF4E-208, 898; ENST00000511644.5, EIF4E-210, 686; ENST00000515638.5, EIF4E-211, 738; ENST00000504472.1, EIF4E-205, 588; ENST00000418385.2, EIF4E-202, 574; ENST00000505194.5, EIF4E-206, 563; ENST00000507665.5, EIF4E-209, 1143; ENST00000505829.1, EIF4E-207, 429"	MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV	chr4:98879276-98929133[-]	"Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm. Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression: in the complex, EIF4E mediates the binding to the mRNA cap. Component of a multiprotein complex that sequesters and represses translation of proneurogenic factors during neurogenesis. In P-bodies, component of a complex that mediates the storage of translationally inactive mRNAs in the cytoplasm and prevents their degradation. May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development."	PDB: 1IPB; PDB: 1IPC; PDB: 1WKW; PDB: 2GPQ; PDB: 2V8W; PDB: 2V8X; PDB: 2V8Y; PDB: 2W97; PDB: 3AM7; PDB: 3TF2; PDB: 3U7X; PDB: 4AZA; PDB: 4BEA; PDB: 4DT6; PDB: 4DUM; PDB: 4TPW; PDB: 4TQB; PDB: 4TQC; PDB: 4UED; PDB: 5EHC; PDB: 5EI3; PDB: 5EIR; PDB: 5EKV; PDB: 5GW6; PDB: 5T46; PDB: 5ZJY; PDB: 5ZJZ; PDB: 5ZK5; PDB: 5ZK7; PDB: 5ZK9; PDB: 5ZML; PDB: 7D6Y; PDB: 7D8B; PDB: 7MEU	HGNC:3287	IF4E_HUMAN	Reviewed	ENSG00000151247	.	.	.	.	.
Mol00427	Protein	Eukaryotic translation initiation factor 5A-2 (EIF5A2)	eIF-5A-2; eIF-5A2; Eukaryotic initiation factor 5A isoform 2	EIF5A2	56648	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000295822.7, EIF5A2-201, 5534; ENST00000474096.5, EIF5A2-203, 570; ENST00000487522.5, EIF5A2-205, 565; ENST00000474417.1, EIF5A2-204, 457; ENST00000460117.5, EIF5A2-202, 518"	MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK	chr3:170888418-170908644[-]	"MRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity)."	.	HGNC:3301	IF5A2_HUMAN	Reviewed	ENSG00000163577	.	.	.	.	.
Mol00428	Protein	Interferon-induced protein with tetratricopeptide repeats 2 (IFIT2)	IFIT-2; ISG-54 K; Interferon-induced 54 kDa protein; IFI-54K; P54; CIG-42; G10P2; IFI54; ISG54	IFIT2	3433	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371826.4, IFIT2-201, 3393; ENST00000638108.1, IFIT2-203, 3703; ENST00000680954.1, IFIT2-212, 3643; ENST00000680809.1, IFIT2-211, 3373; ENST00000679755.1, IFIT2-208, 3418; ENST00000679734.1, IFIT2-207, 3382; ENST00000680381.1, IFIT2-209, 3337; ENST00000611722.2, IFIT2-202, 2497; ENST00000679619.1, IFIT2-206, 651; ENST00000681843.1, IFIT2-214, 1774; ENST00000679608.1, IFIT2-205, 484; ENST00000681850.1, IFIT2-215, 383; ENST00000679606.1, IFIT2-204, 382; ENST00000680558.1, IFIT2-210, 282; ENST00000681150.1, IFIT2-213, 263"	MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE	chr10:89283694-89309271[+]	"IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis."	PDB: 4G1T	HGNC:5409	IFIT2_HUMAN	Reviewed	ENSG00000119922	.	.	.	.	.
Mol00429	Protein	NF-kappa-B inhibitor alpha (NFKBIA)	I-kappa-B-alpha; IkB-alpha; IkappaBalpha; Major histocompatibility complex enhancer-binding protein MAD3; IKBA; MAD3; NFKBI	NFKBIA	4792	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000216797.10, NFKBIA-201, 1559; ENST00000557389.1, NFKBIA-209, 1537; ENST00000557140.5, NFKBIA-208, 1400; ENST00000553342.1, NFKBIA-202, 212; ENST00000554001.5, NFKBIA-203, 1396; ENST00000557100.5, NFKBIA-207, 825; ENST00000557459.1, NFKBIA-210, 780; ENST00000555371.1, NFKBIA-204, 690; ENST00000555629.1, NFKBIA-205, 599; ENST00000556664.1, NFKBIA-206, 381"	MFQAAERPQEWAMEGPRDGLKKERLLDDRHDSGLDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEFTEDELPYDDCVFGGQRLTL	chr14:35401513-35404749[-]	"Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription."	PDB: 1IKN; PDB: 1NFI; PDB: 6TTU; PDB: 6Y1J	HGNC:7797	IKBA_HUMAN	Reviewed	ENSG00000100906	.	.	.	.	.
Mol00430	Protein	I-kappa-B-kinase beta (IKKB)	I-kappa-B-kinase beta; IKK-B; IKK-beta; IkBKB; I-kappa-B kinase 2; IKK2; Nuclear factor NF-kappa-B inhibitor kinase beta; NFKBIKB; Serine/threonine protein kinase IKBKB; IKKB	IKBKB	3551	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000520810.6, IKBKB-216, 3938; ENST00000520835.7, IKBKB-217, 2406; ENST00000522147.4, IKBKB-222, 954; ENST00000518983.1, IKBKB-210, 447; ENST00000342222.6, IKBKB-201, 3952; ENST00000629753.2, IKBKB-229, 3868; ENST00000520655.5, IKBKB-215, 3777; ENST00000416505.7, IKBKB-202, 3330; ENST00000676525.1, IKBKB-233, 3116; ENST00000518679.5, IKBKB-209, 2784; ENST00000649612.3, IKBKB-231, 2783; ENST00000517890.5, IKBKB-206, 2501; ENST00000523517.5, IKBKB-227, 2378; ENST00000521661.5, IKBKB-219, 2196; ENST00000523105.5, IKBKB-226, 1966; ENST00000517388.5, IKBKB-203, 577; ENST00000519733.5, IKBKB-211, 527; ENST00000517812.5, IKBKB-205, 523; ENST00000519735.5, IKBKB-212, 1166; ENST00000522785.1, IKBKB-224, 527; ENST00000517502.5, IKBKB-204, 498; ENST00000521225.3, IKBKB-218, 260; ENST00000520201.5, IKBKB-214, 5002; ENST00000523599.2, IKBKB-228, 4188; ENST00000648136.2, IKBKB-230, 3913; ENST00000519938.5, IKBKB-213, 2403; ENST00000517917.5, IKBKB-207, 1731; ENST00000522103.3, IKBKB-220, 1575; ENST00000518647.5, IKBKB-208, 1543; ENST00000522133.1, IKBKB-221, 576; ENST00000649751.1, IKBKB-232, 466; ENST00000522545.1, IKBKB-223, 452; ENST00000523018.5, IKBKB-225, 373"	MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMRRLTHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGTVKFSSSLPYPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPTYGPNGCFKALDDILNLKLVHILNMVTGTIHTYPVTEDESLQSLKARIQQDTGIPEEDQELLQEAGLALIPDKPATQCISDGKLNEGHTLDMDLVFLFDNSKITYETQISPRPQPESVSCILQEPKRNLAFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMNLLRNNSCLSKMKNSMASMSQQLKAKLDFFKTSIQIDLEKYSEQTEFGITSDKLLLAWREMEQAVELCGRENEVKLLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRRLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDEKTVVRLQEKRQKELWNLLKIACSKVRGPVSGSPDSMNASRLSQPGQLMSQPSTASNSLPEPAKKSEELVAEAHNLCTLLENAIQDTVREQDQSFTALDWSWLQTEEEEHSCLEQAS	chr8:42271302-42332460[+]	"Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation. Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation. Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death. Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus."	PDB: 3BRT; PDB: 3BRV; PDB: 4E3C; PDB: 4KIK	HGNC:5960	IKKB_HUMAN	Reviewed	ENSG00000104365	.	.	.	.	.
Mol00431	Protein	DNA-binding protein Ikaros (IKZF1)	Ikaros family zinc finger protein 1; Lymphoid transcription factor LyF-1; IK1; IKAROS; LYF1; ZNFN1A1	IKZF1	10320	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331340.8, IKZF1-201, 6255; ENST00000343574.9, IKZF1-202, 5925; ENST00000357364.8, IKZF1-205, 5925; ENST00000349824.8, IKZF1-204, 5757; ENST00000439701.2, IKZF1-210, 3614; ENST00000359197.9, IKZF1-206, 3487; ENST00000413698.5, IKZF1-207, 1808; ENST00000438033.5, IKZF1-209, 1748; ENST00000492782.6, IKZF1-216, 571; ENST00000646110.1, IKZF1-221, 559; ENST00000615491.4, IKZF1-217, 5637; ENST00000440768.6, IKZF1-211, 5511; ENST00000346667.8, IKZF1-203, 5376; ENST00000645066.1, IKZF1-220, 558; ENST00000642219.1, IKZF1-219, 509; ENST00000426121.1, IKZF1-208, 201; ENST00000471793.1, IKZF1-213, 1779; ENST00000641948.1, IKZF1-218, 1527; ENST00000462201.1, IKZF1-212, 1122; ENST00000484847.6, IKZF1-214, 908; ENST00000492119.1, IKZF1-215, 584"	MDADEGQDMSQVSGKESPPVSDTPDEGDEPMPIPEDLSTTSGGQQSSKSDRVVASNVKVETQSDEENGRACEMNGEECAEDLRMLDASGEKMNGSHRDQGSSALSGVGGIRLPNGKLKCDICGIICIGPNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHSGEKPFKCHLCNYACRRRDALTGHLRTHSVGKPHKCGYCGRSYKQRSSLEEHKERCHNYLESMGLPGTLYPVIKEETNHSEMAEDLCKIGSERSLVLDRLASNVAKRKSSMPQKFLGDKGLSDTPYDSSASYEKENEMMKSHVMDQAINNAINYLGAESLRPLVQTPPGGSEVVPVISPMYQLHKPLAEGTPRSNHSAQDSAVENLLLLSKAKLVPSEREASPSNSCQDSTDTESNNEEQRSGLIYLTNHIAPHARNGLSLKEEHRAYDLLRAASENSQDALRVVSTSGEQMKVYKCEHCRVLFLDHVMYTIHMGCHGFRDPFECNMCGYHSQDRYEFSSHITRGEHRFHMS	chr7:50304068-50405101[+]	"Transcription regulator of hematopoietic cell differentiation. Binds gamma-satellite DNA. Plays a role in the development of lymphocytes, B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (fikzfterminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), to the beta-globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells. Confers early temporal competence to retinal progenitor cells (RPCs). Function is isoform-specific and is modulated by dominant-negative inactive isoforms."	PDB: 6H0F	HGNC:13176	IKZF1_HUMAN	Reviewed	ENSG00000185811	.	.	.	.	.
Mol00432	Protein	Zinc finger protein Helios (IKZF2)	Ikaros family zinc finger protein 2; HELIOS; ZNFN1A2	IKZF2	22807	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000434687.6, IKZF2-207, 9562; ENST00000374319.8, IKZF2-202, 2001; ENST00000457361.5, IKZF2-213, 9350; ENST00000451136.6, IKZF2-210, 9344; ENST00000342002.6, IKZF2-201, 3747; ENST00000433134.5, IKZF2-206, 602; ENST00000452786.2, IKZF2-211, 567; ENST00000442445.1, IKZF2-209, 551; ENST00000431520.5, IKZF2-205, 1780; ENST00000439848.5, IKZF2-208, 1763; ENST00000412444.5, IKZF2-204, 1737; ENST00000453575.5, IKZF2-212, 1594; ENST00000374326.7, IKZF2-203, 1401; ENST00000484040.1, IKZF2-214, 3534"	METEAIDGYITCDNELSPEREHSNMAIDLTSSTPNGQHASPSHMTSTNSVKLEMQSDEECDRKPLSREDEIRGHDEGSSLEEPLIESSEVADNRKVQELQGEGGIRLPNGKLKCDVCGMVCIGPNVLMVHKRSHTGERPFHCNQCGASFTQKGNLLRHIKLHSGEKPFKCPFCSYACRRRDALTGHLRTHSVGKPHKCNYCGRSYKQRSSLEEHKERCHNYLQNVSMEAAGQVMSHHVPPMEDCKEQEPIMDNNISLVPFERPAVIEKLTGNMGKRKSSTPQKFVGEKLMRFSYPDIHFDMNLTYEKEAELMQSHMMDQAINNAITYLGAEALHPLMQHPPSTIAEVAPVISSAYSQVYHPNRIERPISRETADSHENNMDGPISLIRPKSRPQEREASPSNSCLDSTDSESSHDDHQSYQGHPALNPKRKQSPAYMKEDVKALDTTKAPKGSLKDIYKVFNGEGEQIRAFKCEHCRVLFLDHVMYTIHMGCHGYRDPLECNICGYRSQDRYEFSSHIVRGEHTFH	chr2:212999691-213152427[-]	Associates with Ikaros at centromeric heterochromatin.	PDB: 7LPS	HGNC:13177	IKZF2_HUMAN	Reviewed	ENSG00000030419	.	.	.	.	.
Mol00433	Protein	Zinc finger protein Aiolos (IKZF3)	Ikaros family zinc finger protein 3; ZNFN1A3	IKZF3	22806	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000346872.8, IKZF3-203, 9788; ENST00000623724.3, IKZF3-217, 9787; ENST00000535189.5, IKZF3-215, 1996; ENST00000439167.6, IKZF3-213, 1879; ENST00000377958.6, IKZF3-210, 1837; ENST00000377945.7, IKZF3-208, 1696; ENST00000377944.7, IKZF3-207, 1669; ENST00000394189.6, IKZF3-211, 1552; ENST00000583368.1, IKZF3-216, 1456; ENST00000377952.6, IKZF3-209, 1435; ENST00000351680.7, IKZF3-206, 1413; ENST00000350532.7, IKZF3-205, 1413; ENST00000467757.5, IKZF3-214, 1362; ENST00000346243.7, IKZF3-202, 1296; ENST00000439016.2, IKZF3-212, 1246; ENST00000293068.9, IKZF3-201, 2224; ENST00000348427.7, IKZF3-204, 2056"	MEDIQTNAELKSTQEQSVPAESAAVLNDYSLTKSHEMENVDSGEGPANEDEDIGDDSMKVKDEYSERDENVLKSEPMGNAEEPEIPYSYSREYNEYENIKLERHVVSFDSSRPTSGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRTFLQSTDPGDTASAEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDVNYNSSYMYEKESELIQTRMMDQAINNAISYLGAEALRPLVQTPPAPTSEMVPVISSMYPIALTRAEMSNGAPQELEKKSIHLPEKSVPSERGLSPNNSGHDSTDTDSNHEERQNHIYQQNHMVLSRARNGMPLLKEVPRSYELLKPPPICPRDSVKVINKEGEVMDVYRCDHCRVLFLDYVMFTIHMGCHGFRDPFECNMCGYRSHDRYEFSSHIARGEHRALLK	chr17:39757718-39864312[-]	"Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in an IL2-dependent manner."	.	HGNC:13178	IKZF3_HUMAN	Reviewed	ENSG00000161405	.	.	.	.	.
Mol00434	Protein	Interleukin-11 (IL11)	.	IL11	3589	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264563.7, IL11-201, 2378; ENST00000585513.1, IL11-202, 1201; ENST00000590625.5, IL11-204, 1028; ENST00000587093.1, IL11-203, 650"	MNCVCRLVLVVLSLWPDTAVAPGPPPGPPRVSPDPRAELDSTVLLTRSLLADTRQLAAQLRDKFPADGDHNLDSLPTLAMSAGALGALQLPGVLTRLRADLLSYLRHVQWLRRAGGSSLKTLEPELGTLQARLDRLLRRLQLLMSRLALPQPPPDPPAPPLAPPSSAWGGIRAAHAILGGLHLTLDWAVRGLLLLKTRL	chr19:55364382-55370463[-]	"Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production. Also promotes the proliferation of hepatocytes in response to liver damage. Binding to its receptor formed by IL6ST and IL11RA activates a signaling cascade that promotes cell proliferation. Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3. The interaction with the membrane-bound IL11RA and IL6ST stimulates 'classic signaling', whereas the binding of IL11 and soluble IL11RA to IL6ST stimulates 'trans-signaling'."	PDB: 4MHL; PDB: 6O4O	HGNC:5966	IL11_HUMAN	Reviewed	ENSG00000095752	.	.	.	.	.
Mol00435	Protein	Interleukin-18 (IL18)	IL-18; Iboctadekin; Interferon gamma-inducing factor; IFN-gamma-inducing factor; Interleukin-1 gamma; IL-1 gamma; IGIF; IL1F4	IL18	3606	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000280357.12, IL18-201, 1115; ENST00000524595.5, IL18-202, 1090; ENST00000528832.1, IL18-204, 795; ENST00000533858.5, IL18-205, 758; ENST00000525547.5, IL18-203, 1697; ENST00000534225.1, IL18-206, 880"	MAAEPVEDNCINFVAMKFIDNTLYFIAEDDENLESDYFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED	chr11:112143253-112164096[-]	"Proinflammatory cytokine primarily involved in epithelial barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses. Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore."	PDB: 1J0S; PDB: 2VXT; PDB: 3F62; PDB: 3WO2; PDB: 3WO3; PDB: 3WO4; PDB: 4EEE; PDB: 4EKX; PDB: 4HJJ; PDB: 4R6U; PDB: 4XFS; PDB: 4XFT; PDB: 4XFU	HGNC:5986	IL18_HUMAN	Reviewed	ENSG00000150782	.	.	.	.	.
Mol00436	Protein	Interleukin-1 beta (IL1B)	IL-1 beta; Catabolin; IL1F2	IL1B	3553	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263341.7, IL1B-201, 1507; ENST00000418817.5, IL1B-203, 581; ENST00000432018.5, IL1B-204, 581; ENST00000416750.1, IL1B-202, 580; ENST00000491056.5, IL1B-207, 1617; ENST00000496280.5, IL1B-208, 849; ENST00000487639.1, IL1B-206, 654; ENST00000477398.1, IL1B-205, 571"	MAEVPELASEMMAYYSGNEDDLFFEADGPKQMKCSFQDLDLCPLDGGIQLRISDHHYSKGFRQAASVVVAMDKLRKMLVPCPQTFQENDLSTFFPFIFEEEPIFFDTWDNEAYVHDAPVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFVQGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKMEKRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS	chr2:112829751-112836816[-]	"Potent proinflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore."	PDB: 1HIB; PDB: 1I1B; PDB: 1IOB; PDB: 1ITB; PDB: 1L2H; PDB: 1S0L; PDB: 1T4Q; PDB: 1TOO; PDB: 1TP0; PDB: 1TWE; PDB: 1TWM; PDB: 21BI; PDB: 2I1B; PDB: 2KH2; PDB: 2NVH; PDB: 31BI; PDB: 3LTQ; PDB: 3O4O; PDB: 3POK; PDB: 41BI; PDB: 4DEP; PDB: 4G6J; PDB: 4G6M; PDB: 4GAF; PDB: 4GAI; PDB: 4I1B; PDB: 5BVP; PDB: 5I1B; PDB: 5MVZ; PDB: 5R7W; PDB: 5R85; PDB: 5R86; PDB: 5R87; PDB: 5R88; PDB: 5R89; PDB: 5R8A; PDB: 5R8B; PDB: 5R8C; PDB: 5R8D; PDB: 5R8E; PDB: 5R8F; PDB: 5R8G; PDB: 5R8H; PDB: 5R8I; PDB: 5R8J; PDB: 5R8K; PDB: 5R8L; PDB: 5R8M; PDB: 5R8N; PDB: 5R8O; PDB: 5R8P; PDB: 5R8Q; PDB: 6I1B; PDB: 6Y8I; PDB: 6Y8M; PDB: 7CHY; PDB: 7CHZ; PDB: 7I1B; PDB: 9ILB	HGNC:5992	IL1B_HUMAN	Reviewed	ENSG00000125538	.	.	.	.	.
Mol00437	Protein	Interleukin-24 (IL24)	IL-24; Melanoma differentiation-associated gene 7 protein; MDA-7; Suppression of tumorigenicity 16 protein; MDA7; ST16	IL24	11009	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000294984.7, IL24-201, 1976; ENST00000367093.3, IL24-202, 1819; ENST00000611909.4, IL24-207, 1621; ENST00000391929.7, IL24-204, 1320; ENST00000480741.1, IL24-205, 182; ENST00000367095.7, IL24-203, 1779; ENST00000491169.1, IL24-206, 623"	MNFQQRLQSLWTLARPFCPPLLATASQMQMVVLPCLGFTLLLWSQVSGAQGQEFHFGPCQVKGVVPQKLWEAFWAVKDTMQAQDNITSARLLQQEVLQNVSDAESCYLVHTLLEFYLKTVFKNYHNRTVEVRTLKSFSTLANNFVLIVSQLQPSQENEMFSIRDSAHRRFLLFRRAFKQLDVEAALTKALGEVDILLTWMQKFYKL	chr1:206897443-206904139[+]	Has antiproliferative properties on melanoma cells and may contribute to terminal cell differentiation.	PDB: 6DF3; PDB: 6GG1	HGNC:11346	IL24_HUMAN	Reviewed	ENSG00000162892	.	.	.	.	.
Mol00438	Protein	Interleukin-8 (IL8)	IL-8; C-X-C motif chemokine 8; Chemokine (C-X-C motif) ligand 8; Emoctakin; Granulocyte chemotactic protein 1; GCP-1; Monocyte-derived neutrophil chemotactic factor; MDNCF; Monocyte-derived neutrophil-activating peptide; MONAP; Neutrophil-activating protein 1; NAP-1; Protein 3-10C; T-cell chemotactic factor; GCP/IL-8 protein IV; IL8/NAP1 form I; (Ala-IL-8)77; GCP/IL-8 protein II; IL-8(1-77); IL8/NAP1 form II; MDNCF-b; (Ser-IL-8)72; GCP/IL-8 protein I; IL8/NAP1 form III; Lymphocyte-derived neutrophil-activating factor; LYNAP; MDNCF-c; Neutrophil-activating factor; NAF; GCP/IL-8 protein V; IL8/NAP1 form IV; GCP/IL-8 protein VI; IL8/NAP1 form V; GCP/IL-8 protein III; IL8/NAP1 form VI; IL8	CXCL8	3576	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000307407.8, CXCL8-201, 1642; ENST00000401931.1, CXCL8-202, 700; ENST00000696131.1, CXCL8-204, 2018; ENST00000696132.1, CXCL8-205, 1742; ENST00000483500.1, CXCL8-203, 599"	MTSKLAVALLAAFLISAALCEGAVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS	chr4:73740519-73743716[+]	"IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively."	PDB: 1ICW; PDB: 1IKL; PDB: 1IKM; PDB: 1IL8; PDB: 1ILP; PDB: 1ILQ; PDB: 1QE6; PDB: 1ROD; PDB: 2IL8; PDB: 3IL8; PDB: 4XDX; PDB: 5D14; PDB: 5WDZ; PDB: 6LFM; PDB: 6LFO; PDB: 6N2U; PDB: 6WZM; PDB: 6XMN	HGNC:6025	IL8_HUMAN	Reviewed	ENSG00000169429	.	.	.	.	.
Mol00439	Protein	Inositol monophosphatase 1 (IMPA1)	IMP 1; IMPase 1; D-galactose 1-phosphate phosphatase; Inositol-1(or 4)-monophosphatase 1; Lithium-sensitive myo-inositol monophosphatase A1; IMPA	IMPA1	3612	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256108.10, IMPA1-201, 3369; ENST00000449740.6, IMPA1-203, 1180; ENST00000311489.8, IMPA1-202, 1106; ENST00000523942.5, IMPA1-213, 793; ENST00000522997.5, IMPA1-211, 770; ENST00000519964.5, IMPA1-207, 653; ENST00000518202.5, IMPA1-205, 627; ENST00000521360.5, IMPA1-209, 543; ENST00000518188.5, IMPA1-204, 773; ENST00000519816.1, IMPA1-206, 617; ENST00000521979.5, IMPA1-210, 566; ENST00000523710.5, IMPA1-212, 731; ENST00000520065.1, IMPA1-208, 651"	MADPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPETVRMVLSNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLMSRRVIAANNRILAERIAKEIQVIPLQRDDED	chr8:81656914-81686331[-]	"Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates."	PDB: 1AWB; PDB: 1IMA; PDB: 1IMB; PDB: 1IMC; PDB: 1IMD; PDB: 1IME; PDB: 1IMF; PDB: 2HHM; PDB: 4AS4; PDB: 6GIU; PDB: 6GJ0; PDB: 6ZK0	HGNC:6050	IMPA1_HUMAN	Reviewed	ENSG00000133731	.	.	.	.	.
Mol00440	Protein	Growth protein 4 inhibitor (ING4)	p29ING4; My036	ING4	51147	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000341550.9, ING4-201, 1659; ENST00000396807.8, ING4-202, 1393; ENST00000446105.6, ING4-207, 1348; ENST00000412586.6, ING4-203, 741; ENST00000444704.5, ING4-206, 678; ENST00000423703.6, ING4-204, 602; ENST00000619641.4, ING4-218, 1280; ENST00000467678.5, ING4-208, 529; ENST00000493873.1, ING4-217, 397; ENST00000488381.5, ING4-215, 1150; ENST00000479301.5, ING4-211, 911; ENST00000469749.5, ING4-209, 776; ENST00000482489.5, ING4-212, 659; ENST00000486287.5, ING4-214, 797; ENST00000437149.6, ING4-205, 727; ENST00000484795.5, ING4-213, 1256; ENST00000472002.5, ING4-210, 942; ENST00000493267.1, ING4-216, 401"	MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEEKLALLKQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSDYDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKTAQKKLKLVRTSPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQERKKK	chr12:6650301-6663142[-]	"Component of HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced activity toward histone H4. Through chromatin acetylation it may function in DNA replication. May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation. Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA. May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC. Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11."	PDB: 2K1J; PDB: 2M1R; PDB: 2PNX; PDB: 2VNF; PDB: 4AFL	HGNC:19423	ING4_HUMAN	Reviewed	ENSG00000111653	.	.	.	.	.
Mol00441	Protein	Growth protein 5 inhibitor (ING5)	p28ING5	ING5	84289	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000313552.11, ING5-201, 5197; ENST00000636051.1, ING5-213, 4199"	MATAMYLEHYLDSIENLPCELQRNFQLMRELDQRTEDKKAEIDILAAEYISTVKTLSPDQRVERLQKIQNAYSKCKEYSDDKVQLAMQTYEMVDKHIRRLDADLARFEADLKDKMEGSDFESSGGRGLKKGRGQKEKRGSRGRGRRTSEEDTPKKKKHKGGSEFTDTILSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKGKWFCPRCVQEKRKKK	chr2:241687085-241729478[+]	"Component of the HBO1 complex, which specifically mediates acetylation of histone H3 at 'Lys-14' (H3K14ac) and, to a lower extent, acetylation of histone H4. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Through chromatin acetylation it may regulate DNA replication and may function as a transcriptional coactivator. Inhibits cell growth, induces a delay in S-phase progression and enhances Fas-induced apoptosis in an INCA1-dependent manner."	PDB: 3C6W; PDB: 5ME8; PDB: 5MTO	HGNC:19421	ING5_HUMAN	Reviewed	ENSG00000168395	.	.	.	.	.
Mol00442	Protein	Inositol polyphosphate-4-phosphatase type I A (INPP4A)	Inositol polyphosphate 4-phosphatase type I; Type I inositol 3;4-bisphosphate 4-phosphatase	INPP4A	3631	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000409851.8, INPP4A-205, 10096; ENST00000409016.8, INPP4A-202, 9996; ENST00000074304.9, INPP4A-201, 6752; ENST00000409540.7, INPP4A-204, 3231; ENST00000523221.1, INPP4A-210, 2934; ENST00000409463.5, INPP4A-203, 1565; ENST00000467042.1, INPP4A-207, 869; ENST00000498026.1, INPP4A-209, 499; ENST00000463367.1, INPP4A-206, 2005; ENST00000468638.1, INPP4A-208, 635"	MTAREHSPRHGARARAMQRASTIDVAADMLGLSLAGNIQDPDEPILEFSLACSELHTPSLDRKPNSFVAVSVTTPPQAFWTKHAQTEIIEGTNNPIFLSSIAFFQDSLINQMTQVKLSVYDVKDRSQGTMYLLGSGTFIVKDLLQDRHHRLHLTLRSAESDRVGNITVIGWQMEEKSDQRPPVTRSVDTVNGRMVLPVDESLTEALGIRSKYASLRKDTLLKSVFGGAICRMYRFPTTDGNHLRILEQMAESVLSLHVPRQFVKLLLEEDAARVCELEELGELSPCWESLRRQIVTQYQTIILTYQENLTDLHQYRGPSFKASSLKADKKLEFVPTNLHIQRMRVQDDGGSDQNYDIVTIGAPAAHCQGFKSGGLRKKLHKFEETKKHFEECCTSSGCQSIIYIPQDVVRAKEIIAQINTLKTQVSYYAERLSRAAKDRSATGLERTLAILADKTRQLVTVCDCKLLANSIHGLNAARPDYIASKASPTSTEEEQVMLRNDQDTLMARWTGRNSRSSLQVDWHEEEWEKVWLNVDKSLECIIQRVDKLLQKERLHGEGCEDVFPCAGSCTSKKGNPDSHAYWIRPEDPFCDVPSSPCPSTMPSTACHPHLTTHCSPPPEESSPGEWSEALYPLLTTLTDCVAMMSDKAKKAMVFLLMQDSAPTIATYLSLQYRRDVVFCQTLTALICGFIIKLRNCLHDDGFLRQLYTIGLLAQFESLLSTYGEELAMLEDMSLGIMDLRNVTFKVTQATSSASADMLPVITGNRDGFNVRVPLPGPLFDALPREIQSGMLLRVQPVLFNVGINEQQTLAERFGDTSLQEVINVESLVRLNSYFEQFKEVLPEDCLPRSRSQTCLPELLRFLGQNVHARKNKNVDILWQAAEICRRLNGVRFTSCKSAKDRTAMSVTLEQCLILQHEHGMAPQVFTQALECMRSEGCRRENTMKNVGSRKYAFNSLQLKAFPKHYRPPEGTYGKVET	chr2:98444854-98594392[+]	"Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2). Catalyzes also inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. May protect neurons from excitotoxic cell death by regulating the synaptic localization of cell surface N-methyl-D-aspartate-type glutamate receptors (NMDARs) and NMDAR-mediated excitatory postsynaptic current."	.	HGNC:6074	INP4A_HUMAN	Reviewed	ENSG00000040933	.	.	.	.	.
Mol00443	Protein	Integrin alpha-5 (ITGA5)	.	ITGA5	3678	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000293379.9, ITGA5-201, 4250; ENST00000547197.1, ITGA5-203, 757; ENST00000435631.6, ITGA5-202, 1240; ENST00000553071.1, ITGA5-213, 1013; ENST00000547744.1, ITGA5-204, 547; ENST00000552564.5, ITGA5-211, 4996; ENST00000552387.1, ITGA5-209, 1333; ENST00000552431.5, ITGA5-210, 588; ENST00000550141.1, ITGA5-206, 582; ENST00000552583.1, ITGA5-212, 568; ENST00000551861.1, ITGA5-208, 536; ENST00000549601.1, ITGA5-205, 505; ENST00000551564.1, ITGA5-207, 354"	MGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLDDLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGRFGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQVLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRPIVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIGFTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYLRNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQILLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEAELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGASLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQVTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSISQGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQQKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVWAKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKAEGSYGVPLWIIILAILFGLLLLGLLIYILYKLGFFKRSLPYGTAMEKAQLKPPATSDA	chr12:54395261-54419266[-]	Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling. ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling.	PDB: 3VI3; PDB: 3VI4; PDB: 4WJK; PDB: 4WK0; PDB: 4WK2; PDB: 4WK4; PDB: 7NWL; PDB: 7NXD	HGNC:6141	ITA5_HUMAN	Reviewed	ENSG00000161638	.	.	.	.	.
Mol00444	Protein	Integrin beta-1 (ITGB1)	.	ITGB1	3688	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000302278.8, ITGB1-201, 3735; ENST00000437302.6, ITGB1-206, 4274; ENST00000678701.1, ITGB1-231, 4090; ENST00000678943.1, ITGB1-233, 4001; ENST00000417122.7, ITGB1-204, 3982; ENST00000677999.1, ITGB1-227, 3918; ENST00000678952.1, ITGB1-234, 3815; ENST00000396033.6, ITGB1-202, 3784; ENST00000677363.1, ITGB1-226, 4809; ENST00000676460.1, ITGB1-220, 4489; ENST00000609742.3, ITGB1-219, 4170; ENST00000678591.1, ITGB1-230, 4097; ENST00000474568.6, ITGB1-210, 4021; ENST00000677310.1, ITGB1-225, 4010; ENST00000676964.1, ITGB1-224, 3955; ENST00000679187.1, ITGB1-236, 3839; ENST00000678766.1, ITGB1-232, 3780; ENST00000676659.1, ITGB1-222, 3779; ENST00000423113.5, ITGB1-205, 3729; ENST00000488494.6, ITGB1-215, 3726; ENST00000488427.2, ITGB1-214, 3707; ENST00000472147.1, ITGB1-209, 668; ENST00000480226.5, ITGB1-212, 585; ENST00000534049.5, ITGB1-218, 562; ENST00000528877.5, ITGB1-217, 546; ENST00000414670.2, ITGB1-203, 500; ENST00000678989.1, ITGB1-235, 4307; ENST00000676895.1, ITGB1-223, 3875; ENST00000678120.1, ITGB1-228, 3755; ENST00000678479.1, ITGB1-229, 3741; ENST00000494395.1, ITGB1-216, 562; ENST00000484088.5, ITGB1-213, 580; ENST00000676623.1, ITGB1-221, 5614; ENST00000475184.6, ITGB1-211, 1927; ENST00000439974.3, ITGB1-207, 580; ENST00000464001.1, ITGB1-208, 316"	MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK	chr10:32887273-33005792[-]	"Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling. ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling. Plays an important role in myoblast differentiation and fusion during skeletal myogenesis."	PDB: 3G9W; PDB: 3T9K; PDB: 3VI3; PDB: 3VI4; PDB: 4DX9; PDB: 4WJK; PDB: 4WK0; PDB: 4WK2; PDB: 4WK4; PDB: 7CEB; PDB: 7CEC; PDB: 7NWL; PDB: 7NXD	HGNC:6153	ITB1_HUMAN	Reviewed	ENSG00000150093	.	.	.	.	.
Mol00445	Protein	Integrin beta-8 (ITGB8)	.	ITGB8	3696	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000222573.5, ITGB8-201, 8974; ENST00000537992.5, ITGB8-205, 3420; ENST00000460204.1, ITGB8-202, 1090; ENST00000477859.1, ITGB8-203, 5573; ENST00000478974.1, ITGB8-204, 2054"	MCGSALAFFTAAFVCLQNDRRGPASFLWAAWVFSLVLGLGQGEDNRCASSNAASCARCLALGPECGWCVQEDFISGGSRSERCDIVSNLISKGCSVDSIEYPSVHVIIPTENEINTQVTPGEVSIQLRPGAEANFMLKVHPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSRKMAFFSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGTIAGEIESKAANLNNLVVEAYQKLISEVKVQVENQVQGIYFNITAICPDGSRKPGMEGCRNVTSNDEVLFNVTVTMKKCDVTGGKNYAIIKPIGFNETAKIHIHRNCSCQCEDNRGPKGKCVDETFLDSKCFQCDENKCHFDEDQFSSESCKSHKDQPVCSGRGVCVCGKCSCHKIKLGKVYGKYCEKDDFSCPYHHGNLCAGHGECEAGRCQCFSGWEGDRCQCPSAAAQHCVNSKGQVCSGRGTCVCGRCECTDPRSIGRFCEHCPTCYTACKENWNCMQCLHPHNLSQAILDQCKTSCALMEQQHYVDQTSECFSSPSYLRIFFIIFIVTFLIGLLKVLIIRQVILQWNSNKIKSSSDYRVSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAHETFRCNF	chr7:20330702-20415754[+]	"Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligands. Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs) (Probable). Required during vasculogenesis."	PDB: 6DJP; PDB: 6OM1; PDB: 6OM2; PDB: 6UJA; PDB: 6UJB; PDB: 6UJC	HGNC:6163	ITB8_HUMAN	Reviewed	ENSG00000105855	.	.	.	.	.
Mol00446	Protein	Transcription factor 4 (TCF4)	TCF-4; Class B basic helix-loop-helix protein 19; bHLHb19; Immunoglobulin transcription factor 2; ITF-2; SL3-3 enhancer factor 2; SEF-2; BHLHB19; ITF2; SEF2	TCF4	6925	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354452.8, TCF4-201, 8041; ENST00000636400.2, TCF4-277, 8343; ENST00000356073.8, TCF4-202, 8317; ENST00000636822.2, TCF4-280, 7640; ENST00000643689.1, TCF4-290, 7577; ENST00000637169.2, TCF4-283, 7553; ENST00000629387.2, TCF4-267, 3789; ENST00000564999.5, TCF4-225, 3590; ENST00000570287.6, TCF4-246, 3163; ENST00000537578.5, TCF4-205, 2767; ENST00000564403.6, TCF4-224, 2696; ENST00000568740.5, TCF4-241, 2628; ENST00000540999.5, TCF4-207, 2572; ENST00000398339.5, TCF4-203, 2551; ENST00000543082.5, TCF4-208, 2399; ENST00000568673.5, TCF4-240, 2398; ENST00000457482.7, TCF4-204, 2372; ENST00000544241.6, TCF4-209, 2264; ENST00000561992.5, TCF4-211, 2184; ENST00000566286.5, TCF4-232, 2119; ENST00000537856.7, TCF4-206, 1996; ENST00000675707.1, TCF4-293, 1935; ENST00000564228.5, TCF4-222, 1915; ENST00000570177.6, TCF4-245, 1872; ENST00000561831.7, TCF4-210, 1823; ENST00000616053.4, TCF4-248, 8140; ENST00000638154.3, TCF4-289, 7946; ENST00000635822.2, TCF4-275, 7805; ENST00000565018.6, TCF4-226, 2357; ENST00000566279.5, TCF4-231, 2128; ENST00000567880.5, TCF4-236, 1948; ENST00000626584.2, TCF4-253, 1701; ENST00000630720.3, TCF4-272, 1552; ENST00000628078.2, TCF4-261, 1277; ENST00000562030.3, TCF4-212, 1084; ENST00000566514.5, TCF4-234, 969; ENST00000563824.5, TCF4-220, 897; ENST00000627685.2, TCF4-259, 882; ENST00000568169.5, TCF4-238, 870; ENST00000626595.2, TCF4-254, 833; ENST00000630712.2, TCF4-271, 831; ENST00000628636.2, TCF4-264, 826; ENST00000629343.2, TCF4-266, 807; ENST00000565908.6, TCF4-230, 805; ENST00000630319.2, TCF4-270, 737; ENST00000630828.2, TCF4-273, 735; ENST00000570146.3, TCF4-244, 661; ENST00000566777.5, TCF4-235, 653; ENST00000630268.2, TCF4-269, 635; ENST00000626631.1, TCF4-255, 622; ENST00000625925.2, TCF4-250, 606; ENST00000562607.5, TCF4-214, 602; ENST00000627784.2, TCF4-260, 601; ENST00000562543.5, TCF4-213, 598; ENST00000562847.5, TCF4-217, 597; ENST00000568186.5, TCF4-239, 583; ENST00000626425.2, TCF4-251, 579; ENST00000563888.6, TCF4-221, 570; ENST00000564343.5, TCF4-223, 568; ENST00000569012.5, TCF4-242, 561; ENST00000565124.4, TCF4-227, 555; ENST00000568147.5, TCF4-237, 550; ENST00000562638.5, TCF4-215, 401; ENST00000590810.5, TCF4-247, 362; ENST00000636751.2, TCF4-279, 8283; ENST00000637115.2, TCF4-282, 7883; ENST00000637923.2, TCF4-287, 7314; ENST00000674764.1, TCF4-292, 2057; ENST00000628689.2, TCF4-265, 721; ENST00000627320.2, TCF4-257, 699; ENST00000569357.4, TCF4-243, 585; ENST00000630224.2, TCF4-268, 501; ENST00000565393.2, TCF4-228, 314; ENST00000637239.2, TCF4-284, 7771; ENST00000637250.2, TCF4-285, 7410; ENST00000635990.2, TCF4-276, 7396; ENST00000637941.1, TCF4-288, 2115; ENST00000563760.5, TCF4-219, 856; ENST00000627568.2, TCF4-258, 806; ENST00000627136.2, TCF4-256, 624; ENST00000565580.3, TCF4-229, 530; ENST00000631043.2, TCF4-274, 510; ENST00000566376.3, TCF4-233, 462; ENST00000625716.2, TCF4-249, 359; ENST00000628391.1, TCF4-263, 201; ENST00000636710.1, TCF4-278, 161; ENST00000637068.1, TCF4-281, 142; ENST00000637500.1, TCF4-286, 100; ENST00000563686.5, TCF4-218, 6012; ENST00000562680.5, TCF4-216, 5733; ENST00000674598.1, TCF4-291, 1842; ENST00000626466.1, TCF4-252, 1004; ENST00000628360.1, TCF4-262, 463"	MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAMPGGHGDMHGIIGPSHNGAMGGLGSGYGTGLLSANRHSLMVGTHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDASNHMGQM	chr18:55222185-55664787[-]	Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-CCANNTGG-3'.	PDB: 2KWF; PDB: 6OD3; PDB: 6OD4; PDB: 6OD5	HGNC:11634	ITF2_HUMAN	Reviewed	ENSG00000196628	.	.	.	.	.
Mol00447	Protein	Tyrosine-protein kinase ITK/TSK (ITK)	Interleukin-2-inducible T-cell kinase; IL-2-inducible T-cell kinase; Kinase EMT; T-cell-specific kinase; Tyrosine-protein kinase Lyk; EMT; LYK	ITK	3702	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000422843.8, ITK-201, 4508; ENST00000521769.5, ITK-208, 571; ENST00000517779.1, ITK-202, 587; ENST00000519749.1, ITK-204, 3375; ENST00000522616.1, ITK-209, 1102; ENST00000519402.5, ITK-203, 5869; ENST00000523926.1, ITK-210, 996; ENST00000520173.1, ITK-206, 831; ENST00000520555.5, ITK-207, 606; ENST00000519759.1, ITK-205, 540"	MNNFILLEEQLIKKSQQKRRTSPSNFKVRFFVLTKASLAYFEDRHGKKRTLKGSIELSRIKCVEIVKSDISIPCHYKYPFQVVHDNYLLYVFAPDRESRQRWVLALKEETRNNNSLVPKYHPNFWMDGKWRCCSQLEKLATGCAQYDPTKNASKKPLPPTPEDNRRPLWEPEETVVIALYDYQTNDPQELALRRNEEYCLLDSSEIHWWRVQDRNGHEGYVPSSYLVEKSPNNLETYEWYNKSISRDKAEKLLLDTGKEGAFMVRDSRTAGTYTVSVFTKAVVSENNPCIKHYHIKETNDNPKRYYVAEKYVFDSIPLLINYHQHNGGGLVTRLRYPVCFGRQKAPVTAGLRYGKWVIDPSELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRGLFAAETLLGMCLDVCEGMAYLEEACVIHRDLAARNCLVGENQVIKVSDFGMTRFVLDDQYTSSTGTKFPVKWASPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDISTGFRLYKPRLASTHVYQIMNHCWKERPEDRPAFSRLLRQLAEIAESGL	chr5:157142933-157255185[+]	"Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. When antigen presenting cells (APC) activate T-cell receptor (TCR), a series of phosphorylation lead to the recruitment of ITK to the cell membrane, in the vicinity of the stimulated TCR receptor, where it is phosphorylated by LCK. Phosphorylation leads to ITK autophosphorylation and full activation. Once activated, phosphorylates PLCG1, leading to the activation of this lipase and subsequent cleavage of its substrates. In turn, the endoplasmic reticulum releases calcium in the cytoplasm and the nuclear activator of activated T-cells (NFAT) translocates into the nucleus to perform its transcriptional duty. Phosphorylates 2 essential adapter proteins: the linker for activation of T-cells/LAT protein and LCP2. Then, a large number of signaling molecules such as VAV1 are recruited and ultimately lead to lymphokine production, T-cell proliferation and differentiation. Required for TCR-mediated calcium response in gamma-delta T-cells, may also be involved in the modulation of the transcriptomic signature in the Vgamma2-positive subset of immature gamma-delta T-cells. Phosphorylates TBX21 at 'Tyr-530' and mediates its interaction with GATA3."	PDB: 1SM2; PDB: 1SNU; PDB: 1SNX; PDB: 2E6I; PDB: 2LMJ; PDB: 2YUQ; PDB: 3MIY; PDB: 3MJ1; PDB: 3MJ2; PDB: 3QGW; PDB: 3QGY; PDB: 3T9T; PDB: 3V5J; PDB: 3V5L; PDB: 3V8T; PDB: 3V8W; PDB: 4HCT; PDB: 4HCU; PDB: 4HCV; PDB: 4KIO; PDB: 4L7S; PDB: 4M0Y; PDB: 4M0Z; PDB: 4M12; PDB: 4M13; PDB: 4M14; PDB: 4M15; PDB: 4MF0; PDB: 4MF1; PDB: 4PP9; PDB: 4PPA; PDB: 4PPB; PDB: 4PPC; PDB: 4PQN; PDB: 4QD6; PDB: 4RFM	HGNC:6171	ITK_HUMAN	Reviewed	ENSG00000113263	.	.	.	.	.
Mol00448	Protein	"Inositol 1,4,5-trisphosphate receptor type 1 (ITPR1)"	IP3 receptor isoform 1; IP3R 1; InsP3R1; Type 1 inositol 1;4;5-trisphosphate receptor; Type 1 InsP3 receptor; INSP3R1	ITPR1	3708	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649015.2, ITPR1-237, 9908; ENST00000357086.10, ITPR1-203, 9767; ENST00000443694.5, ITPR1-204, 9647; ENST00000456211.8, ITPR1-205, 9506; ENST00000354582.12, ITPR1-202, 9876; ENST00000648266.1, ITPR1-230, 9767; ENST00000650294.1, ITPR1-254, 9353; ENST00000648309.1, ITPR1-231, 9311; ENST00000648038.1, ITPR1-227, 6998; ENST00000648431.1, ITPR1-233, 6517; ENST00000648212.1, ITPR1-229, 6373; ENST00000648016.1, ITPR1-226, 5773; ENST00000467056.6, ITPR1-207, 2845; ENST00000544951.6, ITPR1-219, 2799; ENST00000649414.1, ITPR1-243, 2266; ENST00000649139.1, ITPR1-239, 2229; ENST00000647685.1, ITPR1-222, 1650; ENST00000649908.1, ITPR1-249, 1626; ENST00000648390.1, ITPR1-232, 1601; ENST00000648564.1, ITPR1-235, 745; ENST00000478515.2, ITPR1-211, 565; ENST00000649051.1, ITPR1-238, 2142; ENST00000302640.13, ITPR1-201, 9305; ENST00000650552.1, ITPR1-255, 2831; ENST00000493491.6, ITPR1-217, 2678; ENST00000650074.1, ITPR1-250, 2666; ENST00000463980.6, ITPR1-206, 2639; ENST00000648770.1, ITPR1-236, 2526; ENST00000648208.1, ITPR1-228, 2444; ENST00000649314.1, ITPR1-242, 2400; ENST00000647997.1, ITPR1-225, 2328; ENST00000487016.1, ITPR1-214, 697; ENST00000649272.1, ITPR1-241, 663; ENST00000490572.1, ITPR1-215, 632; ENST00000491868.2, ITPR1-216, 187; ENST00000649694.1, ITPR1-247, 6907; ENST00000647717.1, ITPR1-223, 6659; ENST00000650079.1, ITPR1-251, 4740; ENST00000649144.1, ITPR1-240, 4370; ENST00000650139.1, ITPR1-252, 4188; ENST00000648510.1, ITPR1-234, 3368; ENST00000647624.1, ITPR1-220, 3172; ENST00000647673.1, ITPR1-221, 3058; ENST00000649767.1, ITPR1-248, 2632; ENST00000477577.2, ITPR1-210, 2628; ENST00000649430.1, ITPR1-245, 2042; ENST00000467545.6, ITPR1-208, 1652; ENST00000650146.1, ITPR1-253, 1364; ENST00000647900.1, ITPR1-224, 1358; ENST00000481415.2, ITPR1-213, 1019; ENST00000649425.1, ITPR1-244, 1013; ENST00000472205.1, ITPR1-209, 652; ENST00000479831.1, ITPR1-212, 591; ENST00000649669.1, ITPR1-246, 586; ENST00000494681.5, ITPR1-218, 580"	MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPETGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMAKGEENKGNNDVEKLKSSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQTSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDETMDGASGENEHKKTEEGNNKPQKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHSIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKLISIDELDNAELPPAPDSENATEELEPSPPLRQLEDHKRGEALRQVLVNRYYGNVRPSGRRESLTSFGNGPLSAGGPGKPGGGGGGSGSSSMSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQPGEGTQATADKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQSMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLVICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLASEFLFSDVCRVESGENCSSPAPREELVPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIKERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA	chr3:4493345-4847506[+]	"Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways."	.	HGNC:6180	ITPR1_HUMAN	Reviewed	ENSG00000150995	.	.	.	.	.
Mol00449	Protein	Protein jagged-1 (JAG1)	.	JAG1	182	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000254958.10, JAG1-201, 5940; ENST00000613518.1, JAG1-205, 597; ENST00000622545.1, JAG1-209, 507; ENST00000423891.6, JAG1-202, 3758; ENST00000617965.2, JAG1-207, 3385; ENST00000488480.2, JAG1-203, 1161; ENST00000620743.1, JAG1-208, 756; ENST00000612857.1, JAG1-204, 586; ENST00000617357.1, JAG1-206, 580"	MRSPRTRGRSGRPLSLLLALLCALRAKVCGASGQFELEILSMQNVNGELQNGNCCGGARNPGDRKCTRDECDTYFKVCLKEYQSRVTAGGPCSFGSGSTPVIGGNTFNLKASRGNDRNRIVLPFSFAWPRSYTLLVEAWDSSNDTVQPDSIIEKASHSGMINPSRQWQTLKQNTGVAHFEYQIRVTCDDYYYGFGCNKFCRPRDDFFGHYACDQNGNKTCMEGWMGPECNRAICRQGCSPKHGSCKLPGDCRCQYGWQGLYCDKCIPHPGCVHGICNEPWQCLCETNWGGQLCDKDLNYCGTHQPCLNGGTCSNTGPDKYQCSCPEGYSGPNCEIAEHACLSDPCHNRGSCKETSLGFECECSPGWTGPTCSTNIDDCSPNNCSHGGTCQDLVNGFKCVCPPQWTGKTCQLDANECEAKPCVNAKSCKNLIASYYCDCLPGWMGQNCDININDCLGQCQNDASCRDLVNGYRCICPPGYAGDHCERDIDECASNPCLNGGHCQNEINRFQCLCPTGFSGNLCQLDIDYCEPNPCQNGAQCYNRASDYFCKCPEDYEGKNCSHLKDHCRTTPCEVIDSCTVAMASNDTPEGVRYISSNVCGPHGKCKSQSGGKFTCDCNKGFTGTYCHENINDCESNPCRNGGTCIDGVNSYKCICSDGWEGAYCETNINDCSQNPCHNGGTCRDLVNDFYCDCKNGWKGKTCHSRDSQCDEATCNNGGTCYDEGDAFKCMCPGGWEGTTCNIARNSSCLPNPCHNGGTCVVNGESFTCVCKEGWEGPICAQNTNDCSPHPCYNSGTCVDGDNWYRCECAPGFAGPDCRININECQSSPCAFGATCVDEINGYRCVCPPGHSGAKCQEVSGRPCITMGSVIPDGAKWDDDCNTCQCLNGRIACSKVWCGPRPCLLHKGHSECPSGQSCIPILDDQCFVHPCTGVGECRSSSLQPVKTKCTSDSYYQDNCANITFTFNKEMMSPGLTTEHICSELRNLNILKNVSAEYSIYIACEPSPSANNEIHVAISAEDIRDDGNPIKEITDKIIDLVSKRDGNSSLIAAVAEVRVQRRPLKNRTDFLVPLLSSVLTVAWICCLVTAFYWCLRKRRKPGSHTHSASEDNTTNNVREQLNQIKNPIEKHGANTVPIKDYENKNSKMSKIRTHNSEVEEDDMDKHQQKARFAKQPAYTLVDREEKPPNGTPTKHPNWTNKQDNRDLESAQSLNRMEYIV	chr20:10637684-10673999[-]	Ligand for multiple Notch receptors and involved in the mediation of Notch signaling. May be involved in cell-fate decisions during hematopoiesis. Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation. Enhances fibroblast growth factor-induced angiogenesis (in vitro).	PDB: 2KB9; PDB: 2VJ2; PDB: 4CBZ; PDB: 4CC0; PDB: 4CC1; PDB: 4XI7; PDB: 5BO1	HGNC:6188	JAG1_HUMAN	Reviewed	ENSG00000101384	.	.	.	.	.
Mol00450	Protein	Tyrosine-protein kinase JAK3 (JAK3)	Janus kinase 3; JAK-3; Leukocyte janus kinase; L-JAK	JAK3	3718	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000458235.7, JAK3-201, 5386; ENST00000527670.5, JAK3-204, 3996; ENST00000534444.1, JAK3-207, 3612; ENST00000526008.5, JAK3-202, 1776; ENST00000527031.5, JAK3-203, 2809; ENST00000528293.1, JAK3-205, 1173; ENST00000528705.1, JAK3-206, 843"	MAPPSEETPLIPQRSCSLLSTEAGALHVLLPARGPGPPQRLSFSFGDHLAEDLCVQAAKASGILPVYHSLFALATEDLSCWFPPSHIFSVEDASTQVLLYRIRFYFPNWFGLEKCHRFGLRKDLASAILDLPVLEHLFAQHRSDLVSGRLPVGLSLKEQGECLSLAVLDLARMAREQAQRPGELLKTVSYKACLPPSLRDLIQGLSFVTRRRIRRTVRRALRRVAACQADRHSLMAKYIMDLERLDPAGAAETFHVGLPGALGGHDGLGLLRVAGDGGIAWTQGEQEVLQPFCDFPEIVDISIKQAPRVGPAGEHRLVTVTRTDNQILEAEFPGLPEALSFVALVDGYFRLTTDSQHFFCKEVAPPRLLEEVAEQCHGPITLDFAINKLKTGGSRPGSYVLRRSPQDFDSFLLTVCVQNPLGPDYKGCLIRRSPTGTFLLVGLSRPHSSLRELLATCWDGGLHVDGVAVTLTSCCIPRPKEKSNLIVVQRGHSPPTSSLVQPQSQYQLSQMTFHKIPADSLEWHENLGHGSFTKIYRGCRHEVVDGEARKTEVLLKVMDAKHKNCMESFLEAASLMSQVSYRHLVLLHGVCMAGDSTMVQEFVHLGAIDMYLRKRGHLVPASWKLQVVKQLAYALNYLEDKGLPHGNVSARKVLLAREGADGSPPFIKLSDPGVSPAVLSLEMLTDRIPWVAPECLREAQTLSLEADKWGFGATVWEVFSGVTMPISALDPAKKLQFYEDRQQLPAPKWTELALLIQQCMAYEPVQRPSFRAVIRDLNSLISSDYELLSDPTPGALAPRDGLWNGAQLYACQDPTIFEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRQSLRLVMEYLPSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLWSGSRGCETHAFTAHPEGKHHSLSFS	chr19:17824780-17848071[-]	"Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A AND STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion."	PDB: 1YVJ; PDB: 3LXK; PDB: 3LXL; PDB: 3PJC; PDB: 3ZC6; PDB: 3ZEP; PDB: 4HVD; PDB: 4HVG; PDB: 4HVH; PDB: 4HVI; PDB: 4I6Q; PDB: 4QPS; PDB: 4QT1; PDB: 4RIO; PDB: 4V0G; PDB: 4Z16; PDB: 5LWM; PDB: 5LWN; PDB: 5TOZ; PDB: 5TTS; PDB: 5TTU; PDB: 5TTV; PDB: 5VO6; PDB: 5W86; PDB: 5WFJ; PDB: 6AAK; PDB: 6DA4; PDB: 6DB3; PDB: 6DB4; PDB: 6DUD; PDB: 6GL9; PDB: 6GLA; PDB: 6GLB; PDB: 6HZV; PDB: 6NY4; PDB: 7APF; PDB: 7APG; PDB: 7C3N	HGNC:6193	JAK3_HUMAN	Reviewed	ENSG00000105639	.	.	.	.	.
Mol00451	Protein	Adenylate kinase 4 (AK4)	AK 4; Adenylate kinase 3-like; GTP:AMP phosphotransferase AK4; AK3; AK3L1	AK4	205	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000327299.8, AK4-201, 6845; ENST00000395334.6, AK4-202, 6998; ENST00000545314.5, AK4-207, 6887; ENST00000546702.5, AK4-208, 1335; ENST00000470888.6, AK4-203, 1043; ENST00000474968.5, AK4-204, 928; ENST00000479060.1, AK4-205, 867; ENST00000497030.5, AK4-206, 834"	MASKLLRAVILGPPGSGKGTVCQRIAQNFGLQHLSSGHFLRENIKASTEVGEMAKQYIEKSLLVPDHVITRLMMSELENRRGQHWLLDGFPRTLGQAEALDKICEVDLVISLNIPFETLKDRLSRRWIHPPSGRVYNLDFNPPHVHGIDDVTGEPLVQQEDDKPEAVAARLRQYKDVAKPVIELYKSRGVLHQFSGTETNKIWPYVYTLFSNKITPIQSKEAY	chr1:65147549-65232145[+]	"Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity. Plays a role in controlling cellular ATP levels by regulating phosphorylation and activation of the energy sensor protein kinase AMPK. Plays a protective role in the cellular response to oxidative stress."	PDB: 2AR7; PDB: 2BBW; PDB: 3NDP	HGNC:363	KAD4_HUMAN	Reviewed	ENSG00000162433	.	.	.	.	.
Mol00452	Protein	Histone acetyltransferase KAT6A (KAT6A)	MOZ; YBF2/SAS3; SAS2 and TIP60 protein 3; MYST-3; Monocytic leukemia zinc finger protein; Runt-related transcription factor-binding protein 2; Zinc finger protein 220; MOZ; MYST3; RUNXBP2; ZNF220	KAT6A	7994	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265713.8, KAT6A-201, 9153; ENST00000396930.4, KAT6A-202, 8006; ENST00000485568.5, KAT6A-208, 3592; ENST00000406337.6, KAT6A-203, 9254; ENST00000649817.1, KAT6A-214, 6139; ENST00000648335.1, KAT6A-213, 5532; ENST00000426524.6, KAT6A-205, 3917; ENST00000647746.1, KAT6A-209, 521; ENST00000649827.1, KAT6A-215, 4385; ENST00000650495.1, KAT6A-217, 6799; ENST00000647809.1, KAT6A-210, 3681; ENST00000648224.1, KAT6A-212, 3532; ENST00000648030.1, KAT6A-211, 3326; ENST00000418721.5, KAT6A-204, 3279; ENST00000650356.1, KAT6A-216, 3271; ENST00000470574.2, KAT6A-207, 3100; ENST00000463961.1, KAT6A-206, 506"	MVKLANPLYTEWILEAIKKVKKQKQRPSEERICNAVSSSHGLDRKTVLEQLELSVKDGTILKVSNKGLNSYKDPDNPGRIALPKPRNHGKLDNKQNVDWNKLIKRAVEGLAESGGSTLKSIERFLKGQKDVSALFGGSAASGFHQQLRLAIKRAIGHGRLLKDGPLYRLNTKATNVDGKESCESLSCLPPVSLLPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRPRKKGRKLLQKKAAQIKRRYTNPIGRPKNRLKKQNTVSKGPFSKVRTGPGRGRKRKITLSSQSASSSSEEGYLERIDGLDFCRDSNVSLKFNKKTKGLIDGLTKFFTPSPDGRKARGEVVDYSEQYRIRKRGNRKSSTSDWPTDNQDGWDGKQENEERLFGSQEIMTEKDMELFRDIQEQALQKVGVTGPPDPQVRCPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLCEFCLKYMKSRTILQQHMKKCGWFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQNDVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEKPLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGICPQDITSTLHHLRMLDFRSDQFVIIRREKLIQDHMAKLQLNLRPVDVDPECLRWTPVIVSNSVVSEEEEEEAEEGENEEPQCQERELEISVGKSVSHENKEQDSYSVESEKKPEVMAPVSSTRLSKQVLPHDSLPANSQPSRRGRWGRKNRKTQERFGDKDSKLLLEETSSAPQEQYGECGEKSEATQEQYTESEEQLVASEEQPSQDGKPDLPKRRLSEGVEPWRGQLKKSPEALKCRLTEGSERLPRRYSEGDRAVLRGFSESSEEEEEPESPRSSSPPILTKPTLKRKKPFLHRRRRVRKRKHHNSSVVTETISETTEVLDEPFEDSDSERPMPRLEPTFEIDEEEEEEDENELFPREYFRRLSSQDVLRCQSSSKRKSKDEEEDEESDDADDTPILKPVSLLRKRDVKNSPLEPDTSTPLKKKKGWPKGKSRKPIHWKKRPGRKPGFKLSREIMPVSTQACVIEPIVSIPKAGRKPKIQESEETVEPKEDMPLPEERKEEEEMQAEAEEAEEGEEEDAASSEVPAASPADSSNSPETETKEPEVEEEEEKPRVSEEQRQSEEEQQELEEPEPEEEEDAAAETAQNDDHDADDEDDGHLESTKKKELEEQPTREDVKEEPGVQESFLDANMQKSREKIKDKEETELDSEEEQPSHDTSVVSEQMAGSEDDHEEDSHTKEELIELKEEEEIPHSELDLETVQAVQSLTQEESSEHEGAYQDCEETLAACQTLQSYTQADEDPQMSMVEDCHASEHNSPISSVQSHPSQSVRSVSSPNVPALESGYTQISPEQGSLSAPSMQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNSSSQSSCSYGGLSSSSSLTQSSCVVTQQMASMGSSCSMMQQSSVQPAANCSIKSPQSCVVERPPSNQQQQPPPPPPQQPQPPPPQPQPAPQPPPPQQQPQQQPQPQPQQPPPPPPPQQQPPLSQCSMNNSFTPAPMIMEIPESGSTGNISIYERIPGDFGAGSYSQPSATFSLAKLQQLTNTIMDPHAMPYSHSPAVTSYATSVSLSNTGLAQLAPSHPLAGTPQAQATMTPPPNLASTTMNLTSPLLQCNMSATNIGIPHTQRLQGQMPVKGHISIRSKSAPLPSAAAHQQQLYGRSPSAVAMQAGPRALAVQRGMNMGVNLMPTPAYNVNSMNMNTLNAMNSYRMTQPMMNSSYHSNPAYMNQTAQYPMQMQMGMMGSQAYTQQPMQPNPHGNMMYTGPSHHSYMNAAGVPKQSLNGPYMRR	chr8:41929479-42051994[-]	Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML.	PDB: 1M36; PDB: 2LN0; PDB: 2OZU; PDB: 2RC4; PDB: 3V43; PDB: 4LJN; PDB: 4LK9; PDB: 4LKA; PDB: 4LLB; PDB: 5B75; PDB: 5B76; PDB: 5B77; PDB: 5B78; PDB: 6LSB	HGNC:13013	KAT6A_HUMAN	Reviewed	ENSG00000083168	.	.	.	.	.
Mol00453	Protein	NF-kappa-B inhibitor-interacting Ras-like protein 2 (NKIRAS2)	I-kappa-B-interacting Ras-like protein 2; Kappa B-Ras protein 2; KappaB-Ras2; KBRAS2	NKIRAS2	28511	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393885.9, NKIRAS2-206, 2453; ENST00000307641.9, NKIRAS2-201, 2948; ENST00000393880.5, NKIRAS2-204, 1644; ENST00000393881.7, NKIRAS2-205, 1598; ENST00000449471.8, NKIRAS2-207, 1461; ENST00000479407.5, NKIRAS2-209, 992; ENST00000316082.4, NKIRAS2-202, 833; ENST00000462043.6, NKIRAS2-208, 585; ENST00000585955.5, NKIRAS2-212, 564; ENST00000587337.1, NKIRAS2-214, 563; ENST00000491638.5, NKIRAS2-211, 1041; ENST00000485789.5, NKIRAS2-210, 997; ENST00000393879.3, NKIRAS2-203, 4213; ENST00000587028.1, NKIRAS2-213, 535"	MGKSCKVVVCGQASVGKTSILEQLLYGNHVVGSEMIETQEDIYVGSIETDRGVREQVRFYDTRGLRDGAELPRHCFSCTDGYVLVYSTDSRESFQRVELLKKEIDKSKDKKEVTIVVLGNKCDLQEQRRVDPDVAQHWAKSEKVKLWEVSVADRRSLLEPFVYLASKMTQPQSKSAFPLSRKNKGSGSLDG	chr17:42011382-42025644[+]	"Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity)."	.	HGNC:17898	KBRS2_HUMAN	Reviewed	ENSG00000168256	.	.	.	.	.
Mol00454	Protein	Potassium voltage-gated channel subfamily H member 1 (KCNH1)	Ether-a-go-go potassium channel 1; EAG channel 1; h-eag; hEAG1; Voltage-gated potassium channel subunit Kv10.1; EAG; EAG1	KCNH1	3756	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000271751.10, KCNH1-201, 8140; ENST00000639952.1, KCNH1-209, 8075; ENST00000638357.1, KCNH1-204, 3740; ENST00000638498.1, KCNH1-205, 3479; ENST00000367007.5, KCNH1-202, 3445; ENST00000640044.1, KCNH1-210, 1818; ENST00000640566.1, KCNH1-214, 1365; ENST00000640625.1, KCNH1-215, 1214; ENST00000638960.1, KCNH1-206, 4592; ENST00000640528.1, KCNH1-213, 4173; ENST00000640710.1, KCNH1-216, 3831; ENST00000640243.1, KCNH1-211, 3027; ENST00000640522.1, KCNH1-212, 1817; ENST00000639385.1, KCNH1-207, 711; ENST00000624583.2, KCNH1-203, 614; ENST00000639754.1, KCNH1-208, 2401; ENST00000640890.1, KCNH1-217, 1948"	MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSFQAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS	chr1:210676823-211134165[-]	"Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel. Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs)."	PDB: 5J7E	HGNC:6250	KCNH1_HUMAN	Reviewed	ENSG00000143473	.	.	.	.	.
Mol00455	Protein	Lysine-specific demethylase 5B (KDM5B)	Cancer/testis antigen 31; CT31; Histone demethylase JARID1B; Jumonji/ARID domain-containing protein 1B; PLU-1; Retinoblastoma-binding protein 2 homolog 1; RBP2-H1; [histone H3]-trimethyl-L-lysine(4) demethylase 5B; JARID1B; PLU1; RBBP2H1	KDM5B	10765	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367265.9, KDM5B-203, 9292; ENST00000367264.7, KDM5B-202, 6520; ENST00000648338.1, KDM5B-217, 9485; ENST00000648473.1, KDM5B-220, 6703; ENST00000648056.1, KDM5B-215, 6390; ENST00000650569.1, KDM5B-240, 6202; ENST00000649770.1, KDM5B-233, 5919; ENST00000648469.1, KDM5B-219, 5422; ENST00000235790.9, KDM5B-201, 4467; ENST00000650368.1, KDM5B-235, 3779; ENST00000649200.1, KDM5B-226, 2667; ENST00000648676.1, KDM5B-221, 1799; ENST00000649929.1, KDM5B-234, 1188; ENST00000648738.1, KDM5B-222, 948; ENST00000648354.1, KDM5B-218, 787; ENST00000650493.1, KDM5B-238, 571; ENST00000650417.1, KDM5B-236, 5362; ENST00000649089.1, KDM5B-225, 3550; ENST00000602511.1, KDM5B-210, 542; ENST00000647757.1, KDM5B-214, 6678; ENST00000649542.1, KDM5B-232, 6149; ENST00000456180.2, KDM5B-204, 574; ENST00000470573.5, KDM5B-206, 535; ENST00000467487.3, KDM5B-205, 529; ENST00000650506.1, KDM5B-239, 5725; ENST00000649230.1, KDM5B-227, 5403; ENST00000649400.1, KDM5B-231, 4750; ENST00000472822.6, KDM5B-207, 3806; ENST00000648958.1, KDM5B-224, 3691; ENST00000650422.1, KDM5B-237, 3630; ENST00000498276.2, KDM5B-209, 3309; ENST00000647747.1, KDM5B-212, 3243; ENST00000649339.1, KDM5B-229, 3141; ENST00000491153.2, KDM5B-208, 2972; ENST00000647754.1, KDM5B-213, 2301; ENST00000647657.1, KDM5B-211, 2019; ENST00000649321.1, KDM5B-228, 1141; ENST00000648744.1, KDM5B-223, 535; ENST00000649388.1, KDM5B-230, 444; ENST00000648099.1, KDM5B-216, 351"	MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK	chr1:202724495-202808487[-]	"Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2."	PDB: 2MA5; PDB: 2MNY; PDB: 2MNZ; PDB: 5A1F; PDB: 5A3N; PDB: 5A3P; PDB: 5A3T; PDB: 5A3W; PDB: 5FPL; PDB: 5FPU; PDB: 5FUN; PDB: 5FUP; PDB: 5FV3; PDB: 5FY4; PDB: 5FY5; PDB: 5FY9; PDB: 5FYB; PDB: 5FYS; PDB: 5FYT; PDB: 5FYU; PDB: 5FYV; PDB: 5FYY; PDB: 5FYZ; PDB: 5FZ0; PDB: 5FZ1; PDB: 5FZ3; PDB: 5FZ4; PDB: 5FZ6; PDB: 5FZ7; PDB: 5FZ8; PDB: 5FZ9; PDB: 5FZA; PDB: 5FZB; PDB: 5FZC; PDB: 5FZD; PDB: 5FZE; PDB: 5FZF; PDB: 5FZG; PDB: 5FZH; PDB: 5FZI; PDB: 5FZK; PDB: 5FZL; PDB: 5FZM; PDB: 5LW9; PDB: 5LWB; PDB: 6EIN; PDB: 6EIU; PDB: 6EIY; PDB: 6EJ0; PDB: 6EJ1; PDB: 6EK6; PDB: 6H4Z; PDB: 6H50; PDB: 6H51; PDB: 6H52; PDB: 6RBI	HGNC:18039	KDM5B_HUMAN	Reviewed	ENSG00000117139	.	.	.	.	.
Mol00456	Protein	Kelch-like ECH-associated protein 1 (KEAP1)	Cytosolic inhibitor of Nrf2; INrf2; Kelch-like protein 19; INRF2; KIAA0132; KLHL19	KEAP1	9817	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000171111.10, KEAP1-201, 2565; ENST00000393623.6, KEAP1-202, 2648; ENST00000592478.5, KEAP1-210, 1044; ENST00000591419.2, KEAP1-208, 986; ENST00000592055.2, KEAP1-209, 979; ENST00000591039.1, KEAP1-207, 960; ENST00000585845.1, KEAP1-203, 774; ENST00000590593.1, KEAP1-206, 582; ENST00000588024.1, KEAP1-204, 576; ENST00000590237.1, KEAP1-205, 451"	MQPDPRPSGAGACCRFLPLQSQCPEGAGDAVMYASTECKAEVTPSQHGNRTFSYTLEDHTKQAFGIMNELRLSQQLCDVTLQVKYQDAPAAQFMAHKVVLASSSPVFKAMFTNGLREQGMEVVSIEGIHPKVMERLIEFAYTASISMGEKCVLHVMNGAVMYQIDSVVRACSDFLVQQLDPSNAIGIANFAEQIGCVELHQRAREYIYMHFGEVAKQEEFFNLSHCQLVTLISRDDLNVRCESEVFHACINWVKYDCEQRRFYVQALLRAVRCHSLTPNFLQMQLQKCEILQSDSRCKDYLVKIFEELTLHKPTQVMPCRAPKVGRLIYTAGGYFRQSLSYLEAYNPSDGTWLRLADLQVPRSGLAGCVVGGLLYAVGGRNNSPDGNTDSSALDCYNPMTNQWSPCAPMSVPRNRIGVGVIDGHIYAVGGSHGCIHHNSVERYEPERDEWHLVAPMLTRRIGVGVAVLNRLLYAVGGFDGTNRLNSAECYYPERNEWRMITAMNTIRSGAGVCVLHNCIYAAGGYDGQDQLNSVERYDVETETWTFVAPMKHRRSALGITVHQGRIYVLGGYDGHTFLDSVECYDPDTDTWSEVTRMTSGRSGVGVAVTMEPCRKQIDQQNCTC	chr19:10486125-10503558[-]	"Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination. KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes. In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes. In response to selective autophagy, KEAP1 is sequestered in inclusion bodies following its interaction with SQSTM1/p62, leading to inactivation of the BCR(KEAP1) complex and activation of NFE2L2/NRF2. The BCR(KEAP1) complex also mediates ubiquitination of SQSTM1/p62, increasing SQSTM1/p62 sequestering activity and degradation. The BCR(KEAP1) complex also targets BPTF and PGAM5 for ubiquitination and degradation by the proteasome."	PDB: 1U6D; PDB: 1ZGK; PDB: 2FLU; PDB: 3VNG; PDB: 3VNH; PDB: 3ZGC; PDB: 3ZGD; PDB: 4CXI; PDB: 4CXJ; PDB: 4CXT; PDB: 4IFJ; PDB: 4IFL; PDB: 4IFN; PDB: 4IN4; PDB: 4IQK; PDB: 4L7B; PDB: 4L7C; PDB: 4L7D; PDB: 4N1B; PDB: 4XMB; PDB: 5DAD; PDB: 5DAF; PDB: 5F72; PDB: 5GIT; PDB: 5NLB; PDB: 5WFL; PDB: 5WFV; PDB: 5WG1; PDB: 5WHL; PDB: 5WHO; PDB: 5WIY; PDB: 5X54; PDB: 6FFM; PDB: 6FMP; PDB: 6FMQ; PDB: 6HWS; PDB: 6LRZ; PDB: 6ROG; PDB: 6SP1; PDB: 6SP4; PDB: 6T7V; PDB: 6T7Z; PDB: 6TG8; PDB: 6TYM; PDB: 6TYP; PDB: 6UF0; PDB: 6V6Z; PDB: 6W66; PDB: 6W67; PDB: 6W68; PDB: 6W69; PDB: 6WCQ; PDB: 6Z6A; PDB: 7K28; PDB: 7K29; PDB: 7K2A; PDB: 7K2B; PDB: 7K2C; PDB: 7K2D; PDB: 7K2E; PDB: 7K2F; PDB: 7K2G; PDB: 7K2H; PDB: 7K2I; PDB: 7K2J; PDB: 7K2K; PDB: 7K2L; PDB: 7K2M; PDB: 7K2N; PDB: 7K2O; PDB: 7K2P; PDB: 7K2Q; PDB: 7K2R; PDB: 7K2S	HGNC:23177	KEAP1_HUMAN	Reviewed	ENSG00000079999	.	.	.	.	.
Mol00457	Protein	Kinesin-like protein KIF11 (KIF11)	Kinesin-like protein 1; Kinesin-like spindle protein HKSP; Kinesin-related motor protein Eg5; Thyroid receptor-interacting protein 5; TR-interacting protein 5; TRIP-5; EG5; KNSL1; TRIP5	KIF11	3832	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000260731.5, KIF11-201, 5016; ENST00000676647.1, KIF11-203, 4788; ENST00000676757.1, KIF11-204, 4780; ENST00000676621.1, KIF11-202, 5134; ENST00000677720.1, KIF11-205, 5010"	MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL	chr10:92574105-92655395[+]	Motor protein required for establishing a bipolar spindle during mitosis. Required in non-mitotic cells for transport of secretory proteins from the Golgi complex to the cell surface.	PDB: 1II6; PDB: 1Q0B; PDB: 1X88; PDB: 1YRS; PDB: 2FKY; PDB: 2FL2; PDB: 2FL6; PDB: 2FME; PDB: 2G1Q; PDB: 2GM1; PDB: 2IEH; PDB: 2PG2; PDB: 2Q2Y; PDB: 2Q2Z; PDB: 2UYI; PDB: 2UYM; PDB: 2WOG; PDB: 2X2R; PDB: 2X7C; PDB: 2X7D; PDB: 2X7E; PDB: 2XAE; PDB: 3CJO; PDB: 3HQD; PDB: 3K3B; PDB: 3K5E; PDB: 3KEN; PDB: 3L9H; PDB: 3WPN; PDB: 3ZCW; PDB: 4A1Z; PDB: 4A28; PDB: 4A50; PDB: 4A51; PDB: 4A5Y; PDB: 4AP0; PDB: 4AQV; PDB: 4AQW; PDB: 4AS7; PDB: 4B7B; PDB: 4BBG; PDB: 4BXN; PDB: 4CK5; PDB: 4CK6; PDB: 4CK7; PDB: 4ZCA; PDB: 4ZHI; PDB: 5JV3; PDB: 5ZO7; PDB: 5ZO8; PDB: 5ZO9; PDB: 6G6Y; PDB: 6G6Z; PDB: 6HKX; PDB: 6HKY; PDB: 6TA3; PDB: 6TA4; PDB: 6TIW; PDB: 6TLE; PDB: 6TRL; PDB: 6Y1I	HGNC:6388	KIF11_HUMAN	Reviewed	ENSG00000138160	.	.	.	.	.
Mol00458	Protein	Mast/stem cell growth factor receptor Kit (KIT)	.	KIT	3815	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000288135.6, KIT-201, 5147; ENST00000687295.1, KIT-213, 5271; ENST00000687109.1, KIT-209, 5249; ENST00000692783.1, KIT-223, 5230; ENST00000686011.1, KIT-208, 5135; ENST00000412167.7, KIT-202, 5126; ENST00000690543.1, KIT-219, 5121; ENST00000689832.1, KIT-216, 5098; ENST00000689994.1, KIT-217, 5091; ENST00000687246.1, KIT-211, 5022; ENST00000685816.1, KIT-207, 466; ENST00000690519.1, KIT-218, 1418; ENST00000687208.1, KIT-210, 5483; ENST00000690917.1, KIT-220, 5266; ENST00000687265.1, KIT-212, 5226; ENST00000685269.1, KIT-206, 5116; ENST00000692991.1, KIT-224, 4977; ENST00000691361.1, KIT-221, 3937; ENST00000688060.1, KIT-214, 2883; ENST00000684818.1, KIT-205, 3777; ENST00000688704.1, KIT-215, 3426; ENST00000692301.1, KIT-222, 1806; ENST00000512959.1, KIT-203, 746; ENST00000514582.1, KIT-204, 538"	MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV	chr4:54657267-54740783[+]	"Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1."	PDB: 1PKG; PDB: 1T45; PDB: 1T46; PDB: 2E9W; PDB: 2EC8; PDB: 2IUH; PDB: 2VIF; PDB: 3G0E; PDB: 3G0F; PDB: 4HVS; PDB: 4K94; PDB: 4K9E; PDB: 4PGZ; PDB: 4U0I; PDB: 6GQJ; PDB: 6GQK; PDB: 6GQL; PDB: 6GQM; PDB: 6HH1; PDB: 6ITT; PDB: 6ITV; PDB: 6KLA; PDB: 6MOB; PDB: 6XV9; PDB: 6XVA; PDB: 6XVB	HGNC:6342	KIT_HUMAN	Reviewed	ENSG00000157404	.	.	.	.	.
Mol00459	Protein	Krueppel-like factor 12 (KLF12)	Transcriptional repressor AP-2rep; AP2REP; HSPC122	KLF12	11278	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377669.7, KLF12-201, 10832; ENST00000472022.1, KLF12-202, 1119"	MNIHMKRKTIKNINTFENRMLMLDGMPAVRVKTELLESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLSVDHFQTQTEPVDLSINKARTSPTAVSSSPVSMTASASSPSSTSTSSSSSSRLASSPTVITSVSSASSSSTVLTPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRIPVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRGHGKAQMDPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQKFPCSISPFSIESTRRQRRSESPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHYRKHTGVKPFKCADCDRSFSRSDHLALHRRRHMLV	chr13:73686089-74133929[-]	Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter.	.	HGNC:6346	KLF12_HUMAN	Reviewed	ENSG00000118922	.	.	.	.	.
Mol00460	Protein	Krueppel-like factor 4 (KLF4)	Epithelial zinc finger protein EZF; Gut-enriched krueppel-like factor; EZF; GKLF	KLF4	9314	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374672.5, KLF4-201, 2936; ENST00000610832.1, KLF4-206, 1956; ENST00000420475.1, KLF4-203, 822; ENST00000493306.1, KLF4-204, 2706; ENST00000497048.5, KLF4-205, 2393; ENST00000411706.1, KLF4-202, 800"	MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLGLEEVLSSRDCHPALPLPPGFHPHPGPNYPSFLPDQMQPQVPPLHYQGQSRGFVARAGEPCVCWPHFGTHGMMLTPPSSPLELMPPGSCMPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF	chr9:107484852-107490482[-]	"Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription."	PDB: 6VTX	HGNC:6348	KLF4_HUMAN	Reviewed	ENSG00000136826	.	.	.	.	.
Mol00461	Protein	Klotho (KL)	.	KL	9365	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000380099.4, KL-201, 5014; ENST00000487852.1, KL-202, 3214"	MPASAPPRRPRPPPPSLSLLLVLLGLGGRRLRAEPGDGAQTWARFSRPPAPEAAGLFQGTFPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRNASLPLGAPSPLQPATGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERLRELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNPYVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSSHWINPRRMTDHSIKECQKSLDFVLGWFAKPVFIDGDYPESMKNNLSSILPDFTESEKKFIKGTADFFALCFGPTLSFQLLDPHMKFRQLESPNLRQLLSWIDLEFNHPQIFIVENGWFVSGTTKRDDAKYMYYLKKFIMETLKAIKLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVDFLSQDKMLLPKSSALFYQKLIEKNGFPPLPENQPLEGTFPCDFAWGVVDNYIQVDTTLSQFTDLNVYLWDVHHSKRLIKVDGVVTKKRKSYCVDFAAIQPQIALLQEMHVTHFRFSLDWALILPLGNQSQVNHTILQYYRCMASELVRVNITPVVALWQPMAPNQGLPRLLARQGAWENPYTALAFAEYARLCFQELGHHVKLWITMNEPYTRNMTYSAGHNLLKAHALAWHVYNEKFRHAQNGKISIALQADWIEPACPFSQKDKEVAERVLEFDIGWLAEPIFGSGDYPWVMRDWLNQRNNFLLPYFTEDEKKLIQGTFDFLALSHYTTILVDSEKEDPIKYNDYLEVQEMTDITWLNSPSQVAVVPWGLRKVLNWLKFKYGDLPMYIISNGIDDGLHAEDDQLRVYYMQNYINEALKAHILDGINLCGYFAYSFNDRTAPRFGLYRYAADQFEPKASMKHYRKIIDSNGFPGPETLERFCPEEFTVCTECSFFHTRKSLLAFIAFLFFASIISLSLIFYYSKKGRRSYK	chr13:33016423-33066143[+]	"May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 239 and 872, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D (By similarity). Essential factor for the specific interaction between FGF23 and FGFR1 (By similarity)."	PDB: 5W21	HGNC:6344	KLOT_HUMAN	Reviewed	ENSG00000133116	.	.	.	.	.
Mol00462	Protein	Protein kinase C delta type (PRKCD)	Tyrosine-protein kinase PRKCD; nPKC-delta; Sphingosine-dependent protein kinase-1; SDK1; PKCD	PRKCD	5580	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000330452.8, PRKCD-201, 2833; ENST00000394729.6, PRKCD-202, 2810; ENST00000652449.1, PRKCD-210, 2711; ENST00000650739.1, PRKCD-207, 2531; ENST00000654719.1, PRKCD-211, 2262; ENST00000650940.1, PRKCD-208, 975; ENST00000464818.1, PRKCD-203, 777; ENST00000478843.5, PRKCD-205, 589; ENST00000487897.5, PRKCD-206, 562; ENST00000477794.2, PRKCD-204, 404; ENST00000651505.1, PRKCD-209, 2083"	MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED	chr3:53156009-53192717[+]	"Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment. Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis. Phosphorylates SMPD1 which induces SMPD1 secretion."	PDB: 1YRK; PDB: 2YUU	HGNC:9399	KPCD_HUMAN	Reviewed	ENSG00000163932	.	.	.	.	.
Mol00463	Protein	Ribosomal protein S6 kinase alpha-3 (RPS6KA3)	S6K-alpha-3; 90 kDa ribosomal protein S6 kinase 3; p90-RSK 3; p90RSK3; Insulin-stimulated protein kinase 1; ISPK-1; MAP kinase-activated protein kinase 1b; MAPK-activated protein kinase 1b; MAPKAP kinase 1b; MAPKAPK-1b; Ribosomal S6 kinase 2; RSK-2; pp90RSK2; ISPK1; MAPKAPK1B; RSK2	RPS6KA3	6197	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000379565.9, RPS6KA3-201, 7987; ENST00000643085.1, RPS6KA3-208, 4064; ENST00000645270.1, RPS6KA3-214, 3961; ENST00000643402.1, RPS6KA3-210, 3294; ENST00000643337.1, RPS6KA3-209, 3054; ENST00000647265.1, RPS6KA3-216, 3015; ENST00000644368.1, RPS6KA3-211, 2991; ENST00000642835.1, RPS6KA3-206, 2841; ENST00000457145.6, RPS6KA3-203, 2820; ENST00000646610.1, RPS6KA3-215, 2682; ENST00000644893.1, RPS6KA3-212, 2451; ENST00000479809.1, RPS6KA3-205, 847; ENST00000438357.2, RPS6KA3-202, 585; ENST00000645268.1, RPS6KA3-213, 2552; ENST00000643073.1, RPS6KA3-207, 2393; ENST00000474266.1, RPS6KA3-204, 930"	MPLAQLADPWQKMAVESPSDSAENGQQIMDEPMGEEEINPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL	chrX:20149911-20267519[-]	"Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration. Acts as a regulator of osteoblast differentiation by mediating phosphorylation of ATF4, thereby promoting ATF4 transactivation activity."	PDB: 4D9T; PDB: 4D9U; PDB: 4JG6; PDB: 4JG7; PDB: 4JG8; PDB: 4NUS; PDB: 4NW5; PDB: 4NW6; PDB: 5D9K; PDB: 5D9L	HGNC:10432	KS6A3_HUMAN	Reviewed	ENSG00000177189	.	.	.	.	.
Mol00464	Protein	Ribosomal protein S6 kinase beta-1 (RPS6KB1)	S6K-beta-1; S6K1; 70 kDa ribosomal protein S6 kinase 1; P70S6K1; p70-S6K 1; Ribosomal protein S6 kinase I; Serine/threonine-protein kinase 14A; p70 ribosomal S6 kinase alpha; p70 S6 kinase alpha; p70 S6K-alpha; p70 S6KA; STK14A	RPS6KB1	6198	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000225577.9, RPS6KB1-201, 5428; ENST00000393021.7, RPS6KB1-202, 5479; ENST00000406116.7, RPS6KB1-203, 1982; ENST00000443572.6, RPS6KB1-204, 1913; ENST00000592726.1, RPS6KB1-212, 622; ENST00000472940.5, RPS6KB1-205, 2808; ENST00000489824.1, RPS6KB1-208, 909; ENST00000587061.1, RPS6KB1-209, 564; ENST00000477179.5, RPS6KB1-207, 431; ENST00000590928.1, RPS6KB1-211, 720; ENST00000475155.1, RPS6KB1-206, 719; ENST00000587622.1, RPS6KB1-210, 583"	MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL	chr17:59893046-59950574[+]	"Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR. Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition."	PDB: 3A60; PDB: 3A61; PDB: 3A62; PDB: 3WE4; PDB: 3WF5; PDB: 3WF6; PDB: 3WF7; PDB: 3WF8; PDB: 3WF9; PDB: 4L3J; PDB: 4L3L; PDB: 4L42; PDB: 4L43; PDB: 4L44; PDB: 4L45; PDB: 4L46; PDB: 4RLO; PDB: 4RLP; PDB: 5WBH; PDB: 5WBK	HGNC:10436	KS6B1_HUMAN	Reviewed	ENSG00000108443	.	.	.	.	.
Mol00465	Protein	Kinase suppressor of Ras 1 (KSR1)	KSR	KSR1	8844	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000644974.2, KSR1-220, 6026; ENST00000398988.7, KSR1-204, 7237; ENST00000644418.1, KSR1-219, 5599; ENST00000268763.10, KSR1-201, 2806; ENST00000509603.6, KSR1-205, 2731; ENST00000582410.5, KSR1-215, 2392; ENST00000398982.6, KSR1-202, 2048; ENST00000583370.5, KSR1-216, 1041; ENST00000580430.1, KSR1-211, 483; ENST00000577823.5, KSR1-206, 685; ENST00000581975.5, KSR1-213, 737; ENST00000582311.1, KSR1-214, 693; ENST00000580822.1, KSR1-212, 669; ENST00000579961.5, KSR1-210, 384; ENST00000579309.1, KSR1-208, 343; ENST00000583998.1, KSR1-218, 339; ENST00000398985.1, KSR1-203, 2527; ENST00000579399.1, KSR1-209, 948; ENST00000578981.1, KSR1-207, 748; ENST00000583525.1, KSR1-217, 428"	MDRAALRAAAMGEKKEGGGGGDAAAAEGGAGAAASRALQQCGQLQKLIDISIGSLRGLRTKCAVSNDLTQQEIRTLEAKLVRYICKQRQCKLSVAPGERTPELNSYPRFSDWLYTFNVRPEVVQEIPRDLTLDALLEMNEAKVKETLRRCGASGDECGRLQYALTCLRKVTGLGGEHKEDSSWSSLDARRESGSGPSTDTLSAASLPWPPGSSQLGRAGNSAQGPRSISVSALPASDSPTPSFSEGLSDTCIPLHASGRLTPRALHSFITPPTTPQLRRHTKLKPPRTPPPPSRKVFQLLPSFPTLTRSKSHESQLGNRIDDVSSMRFDLSHGSPQMVRRDIGLSVTHRFSTKSWLSQVCHVCQKSMIFGVKCKHCRLKCHNKCTKEAPACRISFLPLTRLRRTESVPSDINNPVDRAAEPHFGTLPKALTKKEHPPAMNHLDSSSNPSSTTSSTPSSPAPFPTSSNPSSATTPPNPSPGQRDSRFNFPAAYFIHHRQQFIFPVPSAGHCWKCLLIAESLKENAFNISAFAHAAPLPEAADGTRLDDQPKADVLEAHEAEAEEPEAGKSEAEDDEDEVDDLPSSRRPWRGPISRKASQTSVYLQEWDIPFEQVELGEPIGQGRWGRVHRGRWHGEVAIRLLEMDGHNQDHLKLFKKEVMNYRQTRHENVVLFMGACMNPPHLAIITSFCKGRTLHSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDFGLFGISGVVREGRRENQLKLSHDWLCYLAPEIVREMTPGKDEDQLPFSKAADVYAFGTVWYELQARDWPLKNQAAEASIWQIGSGEGMKRVLTSVSLGKEVSEILSACWAFDLQERPSFSLLMDMLEKLPKLNRRLSHPGHFWKSADINSSKVVPRFERFGLGVLESSNPKM	chr17:27456448-27626438[+]	"Part of a multiprotein signaling complex which promotes phosphorylation of Raf family members and activation of downstream MAP kinases. Independently of its kinase activity, acts as MAP2K1/MEK1 and MAP2K2/MEK2-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1 or MAP2K2/MEK2, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 and/or MAP2K2/MEK2. Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP. Its kinase activity is unsure. Some protein kinase activity has been detected in vitro, however the physiological relevance of this activity is unknown."	PDB: 5VYK; PDB: 7JUW; PDB: 7JUX; PDB: 7JUY; PDB: 7JUZ; PDB: 7JV0; PDB: 7JV1	HGNC:6465	KSR1_HUMAN	Reviewed	ENSG00000141068	.	.	.	.	.
Mol00466	Protein	Lysosome-associated membrane glycoprotein 2 (LAMP2)	.	LAMP2	3920	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000200639.9, LAMP2-201, 6535; ENST00000371335.4, LAMP2-202, 4030; ENST00000434600.6, LAMP2-203, 2089; ENST00000486593.5, LAMP2-204, 1069"	MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSYWDAPLGSSYMCNKEQTVSVSGAFQINTFDLRVQPFNVTQGKYSTAQDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF	chrX:120426148-120469365[-]	"Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation. Plays a role in lysosomal protein degradation in response to starvation. Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes. Required for normal degradation of the contents of autophagosomes. Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens."	PDB: 2MOF; PDB: 2MOM	HGNC:6501	LAMP2_HUMAN	Reviewed	ENSG00000005893	.	.	.	.	.
Mol00467	Protein	Lysosome-associated membrane glycoprotein 3 (LAMP3)	.	LAMP3	27074	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265598.8, LAMP3-201, 3196; ENST00000466939.1, LAMP3-202, 1453; ENST00000476015.1, LAMP3-204, 835; ENST00000470251.1, LAMP3-203, 829; ENST00000486686.1, LAMP3-205, 469"	MPRQLSAAAALFASLAVILHDGSQMRAKAFPETRDYSQPTAAATVQDIKKPVQQPAKQAPHQTLAARFMDGHITFQTAATVKIPTTTPATTKNTATTSPITYTLVTTQATPNNSHTAPPVTEVTVGPSLAPYSLPPTITPPAHTTGTSSSTVSHTTGNTTQPSNQTTLPATLSIALHKSTTGQKPVQPTHAPGTTAAAHNTTRTAAPASTVPGPTLAPQPSSVKTGIYQVLNGSRLCIKAEMGIQLIVQDKESVFSPRRYFNIDPNATQASGNCGTRKSNLLLNFQGGFVNLTFTKDEESYYISEVGAYLTVSDPETIYQGIKHAVVMFQTAVGHSFKCVSEQSLQLSAHLQVKTTDVQLQAFDFEDDHFGNVDECSSDYTIVLPVIGAIVVGLCLMGMGVYKIRLRCQSSGYQRI	chr3:183122215-183163839[-]	"Lysosomal membrane glycoprotein which plays a role in the unfolded protein response (UPR) that contributes to protein degradation and cell survival during proteasomal dysfunction. Plays a role in the process of fusion of the lysosome with the autophagosome, thereby modulating the autophagic process. Promotes hepatocellular lipogenesis through activation of the PI3K/Akt pathway. May also play a role in dendritic cell function and in adaptive immunity."	PDB: 4AKM	HGNC:14582	LAMP3_HUMAN	Reviewed	ENSG00000078081	.	.	.	.	.
Mol00468	Protein	LIM and SH3 domain protein 1 (LASP1)	LASP-1; Metastatic lymph node gene 50 protein; MLN 50; MLN50	LASP1	3927	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000318008.11, LASP1-201, 3910; ENST00000433206.6, LASP1-203, 4023; ENST00000435347.7, LASP1-204, 3492; ENST00000579123.1, LASP1-206, 1874; ENST00000419929.1, LASP1-202, 762; ENST00000443937.7, LASP1-205, 1482; ENST00000585841.5, LASP1-209, 1408; ENST00000584106.1, LASP1-208, 1167; ENST00000581485.1, LASP1-207, 617"	MNPNCARCGKIVYPTEKVNCLDKFWHKACFHCETCKMTLNMKNYKGYEKKPYCNAHYPKQSFTMVADTPENLRLKQQSELQSQVRYKEEFEKNKGKGFSVVADTPELQRIKKTQDQISNIKYHEEFEKSRMGPSGGEGMEPERRDSQDGSSYRRPLEQQQPHHIPTSAPVYQQPQQQPVAQSYGGYKEPAAPVSIQRSAPGGGGKRYRAVYDYSAADEDEVSFQDGDTIVNVQQIDDGWMYGTVERTGDTGMLPANYVEAI	chr17:38869859-38921770[+]	"Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity)."	PDB: 3I35	HGNC:6513	LASP1_HUMAN	Reviewed	ENSG00000002834	.	.	.	.	.
Mol00469	Protein	Solute carrier family 7 member 5 (SLC7A5)	4F2 light chain; 4F2 LC; 4F2LC; CD98 light chain; Integral membrane protein E16; E16; L-type amino acid transporter 1; hLAT1; Solute carrier family 7 member 5; y+ system cationic amino acid transporter; CD98LC; LAT1; MPE16	SLC7A5	8140	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261622.5, SLC7A5-201, 4556; ENST00000565644.5, SLC7A5-203, 3983; ENST00000563489.1, SLC7A5-202, 780"	MAGAGPKRRALAAPAAEEKEEAREKMLAAKSADGSAPAGEGEGVTLQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLALVVWAACGVFSIVGALCYAELGTTISKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPLFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGDVSNLDPNFSFEGTKLDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPIVTLVYVLTNLAYFTTLSTEQMLSSEAVAVDFGNYHLGVMSWIIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSILSMIHPQLLTPVPSLVFTCVMTLLYAFSKDIFSVINFFSFFNWLCVALAIIGMIWLRHRKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSTTVLCQKLMQVVPQET	chr16:87830023-87869507[-]	"The heterodimer with SLC3A2 functions as sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as phenylalanine, tyrosine, L-DOPA, leucine, histidine, methionine and tryptophan. Functions as an amino acid exchanger. May play a role in the transport of L-DOPA across the blood-brain barrier. May act as the major transporter of tyrosine in fibroblasts (Probable). May mediate blood-to-retina L-leucine transport across the inner blood-retinal barrier. Can mediate the transport of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane. When associated with LAPTM4B, the heterodimer formed by SLC3A2 and SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation. Involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the membrane."	PDB: 6IRS; PDB: 6IRT; PDB: 6JMQ; PDB: 7DSK; PDB: 7DSL; PDB: 7DSN; PDB: 7DSQ	HGNC:11063	LAT1_HUMAN	Reviewed	ENSG00000103257	.	.	.	.	.
Mol00470	Protein	Serine/threonine-protein kinase LATS2 (LATS2)	Kinase phosphorylated during mitosis protein; Large tumor suppressor homolog 2; Serine/threonine-protein kinase kpm; Warts-like kinase; KPM	LATS2	26524	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000382592.5, LATS2-201, 5546; ENST00000472754.1, LATS2-202, 495"	MRPKTFPATTYSGNSRQRLQEIREGLKQPSKSSVQGLPAGPNSDTSLDAKVLGSKDATRQQQQMRATPKFGPYQKALREIRYSLLPFANESGTSAAAEVNRQMLQELVNAGCDQEMAGRALKQTGSRSIEAALEYISKMGYLDPRNEQIVRVIKQTSPGKGLMPTPVTRRPSFEGTGDSFASYHQLSGTPYEGPSFGADGPTALEEMPRPYVDYLFPGVGPHGPGHQHQHPPKGYGASVEAAGAHFPLQGAHYGRPHLLVPGEPLGYGVQRSPSFQSKTPPETGGYASLPTKGQGGPPGAGLAFPPPAAGLYVPHPHHKQAGPAAHQLHVLGSRSQVFASDSPPQSLLTPSRNSLNVDLYELGSTSVQQWPAATLARRDSLQKPGLEAPPRAHVAFRPDCPVPSRTNSFNSHQPRPGPPGKAEPSLPAPNTVTAVTAAHILHPVKSVRVLRPEPQTAVGPSHPAWVPAPAPAPAPAPAPAAEGLDAKEEHALALGGAGAFPLDVEYGGPDRRCPPPPYPKHLLLRSKSEQYDLDSLCAGMEQSLRAGPNEPEGGDKSRKSAKGDKGGKDKKQIQTSPVPVRKNSRDEEKRESRIKSYSPYAFKFFMEQHVENVIKTYQQKVNRRLQLEQEMAKAGLCEAEQEQMRKILYQKESNYNRLKRAKMDKSMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDSLYFVMDYIPGGDMMSLLIRMEVFPEHLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNSKYYQKGSHVRQDSMEPSDLWDDVSNCRCGDRLKTLEQRARKQHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPAQVKLSPEARDLITKLCCSADHRLGRNGADDLKAHPFFSAIDFSSDIRKQPAPYVPTISHPMDTSNFDPVDEESPWNDASEGSTKAWDTLTSPNNKHPEHAFYEFTFRRFFDDNGYPFRCPKPSGAEASQAESSDLESSDLVDQTEGCQPVYV	chr13:20973036-21061586[-]	"Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in centrosome duplication, maintenance of mitotic fidelity and genomic stability. Negatively regulates G1/S transition by down-regulating cyclin E/CDK2 kinase activity. Negative regulator of the androgen receptor. Phosphorylates SNAI1 in the nucleus leading to its nuclear retention and stabilization, which enhances its epithelial-mesenchymal transition and tumor cell invasion/migration activities. This tumor-promoting activity is independent of its effects upon YAP1 or WWTR1/TAZ."	.	HGNC:6515	LATS2_HUMAN	Reviewed	ENSG00000150457	.	.	.	.	.
Mol00471	Protein	Lactate dehydrogenase A (LDHA)	LDH-A; Cell proliferation-inducing gene 19 protein; LDH muscle subunit; LDH-M; Renal carcinoma antigen NY-REN-59; PIG19	LDHA	3939	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000422447.8, LDHA-205, 2241; ENST00000540430.5, LDHA-218, 2305; ENST00000379412.9, LDHA-203, 1922; ENST00000227157.8, LDHA-201, 1887; ENST00000396222.6, LDHA-204, 1766; ENST00000430553.6, LDHA-206, 1310; ENST00000542179.1, LDHA-220, 1288; ENST00000478970.6, LDHA-209, 732; ENST00000495052.5, LDHA-212, 682; ENST00000543445.5, LDHA-221, 576; ENST00000535451.5, LDHA-213, 465; ENST00000625635.1, LDHA-225, 141; ENST00000545215.5, LDHA-223, 1340; ENST00000486690.6, LDHA-210, 664; ENST00000541097.5, LDHA-219, 582; ENST00000545467.5, LDHA-224, 570; ENST00000539814.5, LDHA-217, 556; ENST00000543695.5, LDHA-222, 554; ENST00000536528.5, LDHA-214, 516; ENST00000375710.7, LDHA-202, 2169; ENST00000537296.5, LDHA-215, 1511; ENST00000538451.1, LDHA-216, 1345; ENST00000494573.6, LDHA-211, 1154; ENST00000460405.5, LDHA-207, 680; ENST00000469976.2, LDHA-208, 656"	MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF	chr11:18394560-18408425[+]	.	PDB: 1I10; PDB: 4AJP; PDB: 4JNK; PDB: 4L4R; PDB: 4L4S; PDB: 4M49; PDB: 4OJN; PDB: 4OKN; PDB: 4QO7; PDB: 4QO8; PDB: 4QSM; PDB: 4QT0; PDB: 4R68; PDB: 4R69; PDB: 4RLS; PDB: 4ZVV; PDB: 5IXS; PDB: 5IXY; PDB: 5W8H; PDB: 5W8I; PDB: 5W8J; PDB: 5W8K; PDB: 5W8L; PDB: 5ZJD; PDB: 5ZJE; PDB: 5ZJF; PDB: 6BAD; PDB: 6BAG; PDB: 6BAX; PDB: 6BAZ; PDB: 6BB0; PDB: 6BB1; PDB: 6BB2; PDB: 6BB3; PDB: 6MV8; PDB: 6MVA; PDB: 6Q0D; PDB: 6Q13; PDB: 6SBU; PDB: 6SBV; PDB: 6ZZR; PDB: 7M2N	HGNC:6535	LDHA_HUMAN	Reviewed	ENSG00000134333	.	.	.	.	.
Mol00472	Protein	Lymphoid enhancer-binding factor 1 (LEF1)	LEF-1; T cell-specific transcription factor 1-alpha; TCF1-alpha	LEF1	51176	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265165.6, LEF1-201, 3575; ENST00000379951.6, LEF1-202, 3477; ENST00000438313.6, LEF1-203, 1488; ENST00000510624.5, LEF1-216, 1472; ENST00000515500.5, LEF1-221, 1037; ENST00000512172.1, LEF1-218, 598; ENST00000506680.5, LEF1-212, 1280; ENST00000504950.5, LEF1-207, 572; ENST00000503879.5, LEF1-204, 1492; ENST00000504426.5, LEF1-205, 1479; ENST00000510135.5, LEF1-215, 1376; ENST00000509428.5, LEF1-214, 1090; ENST00000505379.5, LEF1-211, 1084; ENST00000514444.5, LEF1-220, 916; ENST00000505297.5, LEF1-209, 873; ENST00000504775.5, LEF1-206, 860; ENST00000510717.5, LEF1-217, 568; ENST00000512407.5, LEF1-219, 564; ENST00000505293.1, LEF1-208, 552; ENST00000507470.5, LEF1-213, 548; ENST00000505328.1, LEF1-210, 527"	MPQLSGGGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVARQAQTSQEPYHDKAREHPDDGKHPDGGLYNKGPSYSSYSGYIMMPNMNNDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSDVNSKQGMSRHPPAPDIPTFYPLSPGGVGQITPPLGWQGQPVYPITGGFRQPYPSSLSVDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPQHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESASGTGPRMTAAYI	chr4:108047545-108168956[-]	"Transcription factor that binds DNA in a sequence-specific manner. Participates in the Wnt signaling pathway. Activates transcription of target genes in the presence of CTNNB1 and EP300. PIAG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1. Regulates T-cell receptor alpha enhancer function. Required for IL17A expressing gamma-delta T-cell maturation and development, via binding to regulator loci of BLK to modulate expression. May play a role in hair cell differentiation and follicle morphogenesis."	.	HGNC:6551	LEF1_HUMAN	Reviewed	ENSG00000138795	.	.	.	.	.
Mol00473	Protein	Galectin-related protein (GRP)	Galectin-like protein; Lectin galactoside-binding-like protein; GRP; HSPC159	LGALSL	29094	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000238875.10, LGALSL-201, 3856; ENST00000409537.2, LGALSL-202, 3298; ENST00000464281.5, LGALSL-205, 607; ENST00000420552.5, LGALSL-203, 548; ENST00000462737.1, LGALSL-204, 469"	MAGSVADSDAVVKLDDGHLNNSLSSPVQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDSEDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRVEILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG	chr2:64453969-64461381[+]	"Does not bind lactose, and may not bind carbohydrates."	PDB: 2JJ6; PDB: 3B9C	HGNC:25012	LEGL_HUMAN	Reviewed	ENSG00000119862	.	.	.	.	.
Mol00474	Protein	Leucine-rich repeat-containing G-protein coupled receptor 5 (LGR5)	G-protein coupled receptor 49; G-protein coupled receptor 67; G-protein coupled receptor HG38; GPR49; GPR67	LGR5	8549	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000266674.10, LGR5-201, 4583; ENST00000540815.2, LGR5-203, 2800; ENST00000536515.5, LGR5-202, 2664; ENST00000550851.5, LGR5-206, 4095; ENST00000547310.1, LGR5-204, 576; ENST00000549015.1, LGR5-205, 298"	MDTSRLGVLLSLPVLLQLATGGSSPRSGVLLRGCPTHCHCEPDGRMLLRVDCSDLGLSELPSNLSVFTSYLDLSMNNISQLLPNPLPSLRFLEELRLAGNALTYIPKGAFTGLYSLKVLMLQNNQLRHVPTEALQNLRSLQSLRLDANHISYVPPSCFSGLHSLRHLWLDDNALTEIPVQAFRSLSALQAMTLALNKIHHIPDYAFGNLSSLVVLHLHNNRIHSLGKKCFDGLHSLETLDLNYNNLDEFPTAIRTLSNLKELGFHSNNIRSIPEKAFVGNPSLITIHFYDNPIQFVGRSAFQHLPELRTLTLNGASQITEFPDLTGTANLESLTLTGAQISSLPQTVCNQLPNLQVLDLSYNLLEDLPSFSVCQKLQKIDLRHNEIYEIKVDTFQQLLSLRSLNLAWNKIAIIHPNAFSTLPSLIKLDLSSNLLSSFPITGLHGLTHLKLTGNHALQSLISSENFPELKVIEMPYAYQCCAFGVCENAYKISNQWNKGDNSSMDDLHKKDAGMFQAQDERDLEDFLLDFEEDLKALHSVQCSPSPGPFKPCEHLLDGWLIRIGVWTIAVLALTCNALVTSTVFRSPLYISPIKLLIGVIAAVNMLTGVSSAVLAGVDAFTFGSFARHGAWWENGVGCHVIGFLSIFASESSVFLLTLAALERGFSVKYSAKFETKAPFSSLKVIILLCALLALTMAAVPLLGGSKYGASPLCLPLPFGEPSTMGYMVALILLNSLCFLMMTIAYTKLYCNLDKGDLENIWDCSMVKHIALLLFTNCILNCPVAFLSFSSLINLTFISPEVIKFILLVVVPLPACLNPLLYILFNPHFKEDLVSLRKQTYVWTRSKHPSLMSINSDDVEKQSCDSTQALVTFTSSSITYDLPPSSVPSPAYPVTESCHLSSVAFVPCL	chr12:71439798-71586310[+]	"Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development."	PDB: 4BSR; PDB: 4BSS; PDB: 4BST; PDB: 4BSU; PDB: 4KNG; PDB: 4UFR; PDB: 4UFS	HGNC:4504	LGR5_HUMAN	Reviewed	ENSG00000139292	.	.	.	.	.
Mol00475	Protein	LIM/homeobox protein Lhx6 (LHX6)	LIM homeobox protein 6; LIM/homeobox protein Lhx6.1; LHX6.1	LHX6	26468	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000394319.9, LHX6-204, 3574; ENST00000559895.5, LHX6-210, 3587; ENST00000340587.7, LHX6-201, 3457; ENST00000373755.6, LHX6-203, 3384; ENST00000373754.6, LHX6-202, 3278; ENST00000541397.2, LHX6-207, 2942; ENST00000482062.1, LHX6-206, 918; ENST00000560485.1, LHX6-212, 736; ENST00000464484.3, LHX6-205, 666; ENST00000559529.1, LHX6-209, 550; ENST00000558672.1, LHX6-208, 592; ENST00000560152.1, LHX6-211, 582"	MAQPGSGCKATTRCLEGTAPPAMAQSDAEALAGALDKDEGQASPCTPSTPSVCSPPSAASSVPSAGKNICSSCGLEILDRYLLKVNNLIWHVRCLECSVCRTSLRQQNSCYIKNKEIFCKMDYFSRFGTKCARCGRQIYASDWVRRARGNAYHLACFACFSCKRQLSTGEEFGLVEEKVLCRIHYDTMIENLKRAAENGNGLTLEGAVPSEQDSQPKPAKRARTSFTAEQLQVMQAQFAQDNNPDAQTLQKLADMTGLSRRVIQVWFQNCRARHKKHTPQHPVPPSGAPPSRLPSALSDDIHYTPFSSPERARMVTLHGYIESQVQCGQVHCRLPYTAPPVHLKADMDGPLSNRGEKVILFQY	chr9:122202577-122229626[-]	Probable transcription factor required for the expression of a subset of genes involved in interneurons migration and development. Functions in the specification of cortical interneuron subtypes and in the migration of GABAergic interneuron precursors from the subpallium to the cerebral cortex (By similarity).	.	HGNC:21735	LHX6_HUMAN	Reviewed	ENSG00000106852	.	.	.	.	.
Mol00476	Protein	Lysyl oxidase homolog 4 (LOXL4)	Lysyl oxidase-like protein 4; Lysyl oxidase-related protein C; LOXC	LOXL4	84171	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000260702.4, LOXL4-201, 3597"	MAWSPPATLFLFLLLLGQPPPSRPQSLGTTKLRLVGPESKPEEGRLEVLHQGQWGTVCDDNFAIQEATVACRQLGFEAALTWAHSAKYGQGEGPIWLDNVRCVGTESSLDQCGSNGWGVSDCSHSEDVGVICHPRRHRGYLSETVSNALGPQGRRLEEVRLKPILASAKQHSPVTEGAVEVKYEGHWRQVCDQGWTMNNSRVVCGMLGFPSEVPVDSHYYRKVWDLKMRDPKSRLKSLTNKNSFWIHQVTCLGTEPHMANCQVQVAPARGKLRPACPGGMHAVVSCVAGPHFRPPKTKPQRKGSWAEEPRVRLRSGAQVGEGRVEVLMNRQWGTVCDHRWNLISASVVCRQLGFGSAREALFGARLGQGLGPIHLSEVRCRGYERTLSDCPALEGSQNGCQHENDAAVRCNVPNMGFQNQVRLAGGRIPEEGLLEVQVEVNGVPRWGSVCSENWGLTEAMVACRQLGLGFAIHAYKETWFWSGTPRAQEVVMSGVRCSGTELALQQCQRHGPVHCSHGGGRFLAGVSCMDSAPDLVMNAQLVQETAYLEDRPLSQLYCAHEENCLSKSADHMDWPYGYRRLLRFSTQIYNLGRTDFRPKTGRDSWVWHQCHRHYHSIEVFTHYDLLTLNGSKVAEGHKASFCLEDTNCPTGLQRRYACANFGEQGVTVGCWDTYRHDIDCQWVDITDVGPGNYIFQVIVNPHYEVAESDFSNNMLQCRCKYDGHRVWLHNCHTGNSYPANAELSLEQEQRLRNNLI	chr10:98247690-98268194[-]	May modulate the formation of a collagenous extracellular matrix.	.	HGNC:17171	LOXL4_HUMAN	Reviewed	ENSG00000138131	.	.	.	.	.
Mol00477	Protein	Protein LRATD2 (LRATD2)	Breast cancer membrane protein 101; LRAT domain-containing 2; Protein FAM84B; Protein NSE2; BCMP101; FAM84B; NSE2	LRATD2	157638	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000304916.4, LRATD2-201, 5488; ENST00000652209.1, LRATD2-203, 4831; ENST00000517458.1, LRATD2-202, 844"	MGNQVEKLTHLSYKEVPTADPTGVDRDDGPRIGVSYIFSNDDEDVEPQPPPQGPDGGGLPDGGDGPPPPQPQPYDPRLHEVECSVFYRDECIYQKSFAPGSAALSTYTPENLLNKCKPGDLVEFVSQAQYPHWAVYVGNFQVVHLHRLEVINSFLTDASQGRRGRVVNDLYRYKPLSSSAVVRNALAHVGAKERELSWRNSESFAAWCRYGKREFKIGGELRIGKQPYRLQIQLSAQRSHTLEFQSLEDLIMEKRRNDQIGRAAVLQELATHLHPAEPEEGDSNVARTTPPPGRPPAPSSEEEDGEAVAH	chr8:126552443-126558478[-]	.	.	HGNC:24166	LRAT2_HUMAN	Reviewed	ENSG00000168672	.	.	.	.	.
Mol00478	Protein	Leucine-rich repeats and immunoglobulin-like domains protein 1 (LRIG1)	LIG-1; LIG1	LRIG1	26018	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000273261.8, LRIG1-201, 5363; ENST00000383703.3, LRIG1-202, 5283; ENST00000496559.6, LRIG1-207, 4129; ENST00000495037.1, LRIG1-205, 2336; ENST00000498287.5, LRIG1-209, 689; ENST00000497721.5, LRIG1-208, 598; ENST00000475366.5, LRIG1-203, 504; ENST00000495671.1, LRIG1-206, 409; ENST00000491821.1, LRIG1-204, 580"	MARPVRGGLGAPRRSPCLLLLWLLLLRLEPVTAAAGPRAPCAAACTCAGDSLDCGGRGLAALPGDLPSWTRSLNLSYNKLSEIDPAGFEDLPNLQEVYLNNNELTAVPSLGAASSHVVSLFLQHNKIRSVEGSQLKAYLSLEVLDLSLNNITEVRNTCFPHGPPIKELNLAGNRIGTLELGAFDGLSRSLLTLRLSKNRITQLPVRAFKLPRLTQLDLNRNRIRLIEGLTFQGLNSLEVLKLQRNNISKLTDGAFWGLSKMHVLHLEYNSLVEVNSGSLYGLTALHQLHLSNNSIARIHRKGWSFCQKLHELVLSFNNLTRLDEESLAELSSLSVLRLSHNSISHIAEGAFKGLRSLRVLDLDHNEISGTIEDTSGAFSGLDSLSKLTLFGNKIKSVAKRAFSGLEGLEHLNLGGNAIRSVQFDAFVKMKNLKELHISSDSFLCDCQLKWLPPWLIGRMLQAFVTATCAHPESLKGQSIFSVPPESFVCDDFLKPQIITQPETTMAMVGKDIRFTCSAASSSSSPMTFAWKKDNEVLTNADMENFVHVHAQDGEVMEYTTILHLRQVTFGHEGRYQCVITNHFGSTYSHKARLTVNVLPSFTKTPHDITIRTTTMARLECAATGHPNPQIAWQKDGGTDFPAARERRMHVMPDDDVFFITDVKIDDAGVYSCTAQNSAGSISANATLTVLETPSLVVPLEDRVVSVGETVALQCKATGNPPPRITWFKGDRPLSLTERHHLTPDNQLLVVQNVVAEDAGRYTCEMSNTLGTERAHSQLSVLPAAGCRKDGTTVGIFTIAVVSSIVLTSLVWVCIIYQTRKKSEEYSVTNTDETVVPPDVPSYLSSQGTLSDRQETVVRTEGGPQANGHIESNGVCPRDASHFPEPDTHSVACRQPKLCAGSAYHKEPWKAMEKAEGTPGPHKMEHGGRVVCSDCNTEVDCYSRGQAFHPQPVSRDSAQPSAPNGPEPGGSDQEHSPHHQCSRTAAGSCPECQGSLYPSNHDRMLTAVKKKPMASLDGKGDSSWTLARLYHPDSTELQPASSLTSGSPERAEAQYLLVSNGHLPKACDASPESTPLTGQLPGKQRVPLLLAPKS	chr3:66378797-66501263[-]	"Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation."	PDB: 4U7L; PDB: 4U7M	HGNC:17360	LRIG1_HUMAN	Reviewed	ENSG00000144749	.	.	.	.	.
Mol00479	Protein	Low-density lipoprotein receptor-related protein 1B (LRP1B)	LRP-1B; Low-density lipoprotein receptor-related protein-deleted in tumor; LRP-DIT; LRPDIT	LRP1B	53353	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000389484.8, LRP1B-201, 15850; ENST00000437977.5, LRP1B-203, 3810; ENST00000434794.1, LRP1B-202, 2621; ENST00000442974.1, LRP1B-204, 839; ENST00000486364.1, LRP1B-205, 514"	MSEFLLALLTLSGLLPIARVLTVGADRDQQLCDPGEFLCHDHVTCVSQSWLCDGDPDCPDDSDESLDTCPEEVEIKCPLNHIACLGTNKCVHLSQLCNGVLDCPDGYDEGVHCQELLSNCQQLNCQYKCTMVRNSTRCYCEDGFEITEDGRSCKDQDECAVYGTCSQTCRNTHGSYTCSCVEGYLMQPDNRSCKAKIEPTDRPPILLIANFETIEVFYLNGSKMATLSSVNGNEIHTLDFIYNEDMICWIESRESSNQLKCIQITKAGGLTDEWTINILQSFHNVQQMAIDWLTRNLYFVDHVGDRIFVCNSNGSVCVTLIDLELHNPKAIAVDPIAGKLFFTDYGNVAKVERCDMDGMNRTRIIDSKTEQPAALALDLVNKLVYWVDLYLDYVGVVDYQGKNRHTVIQGRQVRHLYGITVFEDYLYATNSDNYNIVRINRFNGTDIHSLIKIENAWGIRIYQKRTQPTVRSHACEVDPYGMPGGCSHICLLSSSYKTRTCRCRTGFNLGSDGRSCKRPKNELFLFYGKGRPGIVRGMDLNTKIADEYMIPIENLVNPRALDFHAETNYIYFADTTSFLIGRQKIDGTERETILKDDLDNVEGIAVDWIGNNLYWTNDGHRKTINVARLEKASQSRKTLLEGEMSHPRGIVVDPVNGWMYWTDWEEDEIDDSVGRIEKAWMDGFNRQIFVTSKMLWPNGLTLDFHTNTLYWCDAYYDHIEKVFLNGTHRKIVYSGRELNHPFGLSHHGNYVFWTDYMNGSIFQLDLITSEVTLLRHERPPLFGLQIYDPRKQQGDNMCRVNNGGCSTLCLAIPGGRVCACADNQLLDENGTTCTFNPGEALPHICKAGEFRCKNRHCIQARWKCDGDDDCLDGSDEDSVNCFNHSCPDDQFKCQNNRCIPKRWLCDGANDCGSNEDESNQTCTARTCQVDQFSCGNGRCIPRAWLCDREDDCGDQTDEMASCEFPTCEPLTQFVCKSGRCISSKWHCDSDDDCGDGSDEVGCVHSCFDNQFRCSSGRCIPGHWACDGDNDCGDFSDEAQINCTKEEIHSPAGCNGNEFQCHPDGNCVPDLWRCDGEKDCEDGSDEKGCNGTIRLCDHKTKFSCWSTGRCINKAWVCDGDIDCEDQSDEDDCDSFLCGPPKHPCANDTSVCLQPEKLCNGKKDCPDGSDEGYLCDECSLNNGGCSNHCSVVPGRGIVCSCPEGLQLNKDNKTCEIVDYCSNHLKCSQVCEQHKHTVKCSCYEGWKLDVDGESCTSVDPFEAFIIFSIRHEIRRIDLHKRDYSLLVPGLRNTIALDFHFNQSLLYWTDVVEDRIYRGKLSESGGVSAIEVVVEHGLATPEGLTVDWIAGNIYWIDSNLDQIEVAKLDGSLRTTLIAGAMEHPRAIALDPRYGILFWTDWDANFPRIESASMSGAGRKTIYKDMKTGAWPNGLTVDHFEKRIVWTDARSDAIYSALYDGTNMIEIIRGHEYLSHPFAVSLYGSEVYWTDWRTNTLSKANKWTGQNVSVIQKTSAQPFDLQIYHPSRQPQAPNPCAANDGKGPCSHMCLINHNRSAACACPHLMKLSSDKKTCYEMKKFLLYARRSEIRGVDIDNPYFNFITAFTVPDIDDVTVIDFDASEERLYWTDIKTQTIKRAFINGTGLETVISRDIQSIRGLAVDWVSRNLYWISSEFDETQINVARLDGSLKTSIIHGIDKPQCLAAHPVRGKLYWTDGNTINMANMDGSNSKILFQNQKEPVGLSIDYVENKLYWISSGNGTINRCNLDGGNLEVIESMKEELTKATALTIMDKKLWWADQNLAQLGTCSKRDGRNPTILRNKTSGVVHMKVYDKEAQQGSNSCQLNNGGCSQLCLPTSETTRTCMCTVGYYLQKNRMSCQGIESFLMYSVHEGIRGIPLEPSDKMDALMPISGTSFAVGIDFHAENDTIYWTDMGFNKISRAKRDQTWKEDIITNGLGRVEGIAVDWIAGNIYWTDHGFNLIEVARLNGSFRYVIISQGLDQPRSIAVHPEKGLLFWTEWGQMPCIGKARLDGSEKVVLVSMGIAWPNGISIDYEENKLYWCDARTDKIERIDLETGGNREMVLSGSNVDMFSVAVFGAYIYWSDRAHANGSVRRGHKNDATETITMRTGLGVNLKEVKIFNRVREKGTNVCARDNGGCKQLCLYRGNSRRTCACAHGYLAEDGVTCLRHEGYLLYSGRTILKSIHLSDETNLNSPIRPYENPRYFKNVIALAFDYNQRRKGTNRIFYSDAHFGNIQLIKDNWEDRQVIVENVGSVEGLAYHRAWDTLYWTSSTTSSITRHTVDQTRPGAFDREAVITMSEDDHPHVLALDECQNLMFWTNWNEQHPSIMRSTLTGKNAQVVVSTDILTPNGLTIDYRAEKLYFSDGSLGKIERCEYDGSQRHVIVKSGPGTFLSLAVYDNYIFWSDWGRRAILRSNKYTGGDTKILRSDIPHQPMGIIAVANDTNSCELSPCALLNGGCHDLCLLTPNGRVNCSCRGDRILLEDNRCVTKNSSCNAYSEFECGNGECIDYQLTCDGIPHCKDKSDEKLLYCENRSCRRGFKPCYNRRCIPHGKLCDGENDCGDNSDELDCKVSTCATVEFRCADGTCIPRSARCNQNIDCADASDEKNCNNTDCTHFYKLGVKTTGFIRCNSTSLCVLPTWICDGSNDCGDYSDELKCPVQNKHKCEENYFSCPSGRCILNTWICDGQKDCEDGRDEFHCDSSCSWNQFACSAQKCISKHWICDGEDDCGDGLDESDSICGAITCAADMFSCQGSRACVPRHWLCDGERDCPDGSDELSTAGCAPNNTCDENAFMCHNKVCIPKQFVCDHDDDCGDGSDESPQCGYRQCGTEEFSCADGRCLLNTQWQCDGDFDCPDHSDEAPLNPKCKSAEQSCNSSFFMCKNGRCIPSGGLCDNKDDCGDGSDERNCHINECLSKKVSGCSQDCQDLPVSYKCKCWPGFQLKDDGKTCVDIDECSSGFPCSQQCINTYGTYKCLCTDGYEIQPDNPNGCKSLSDEEPFLILADHHEIRKISTDGSNYTLLKQGLNNVIAIDFDYREEFIYWIDSSRPNGSRINRMCLNGSDIKVVHNTAVPNALAVDWIGKNLYWSDTEKRIIEVSKLNGLYPTILVSKRLKFPRDLSLDPQAGYLYWIDCCEYPHIGRVGMDGTNQSVVIETKISRPMALTIDYVNRRLYWADENHIEFSNMDGSHRHKVPNQDIPGVIALTLFEDYIYWTDGKTKSLSRAHKTSGADRLSLIYSWHAITDIQVYHSYRQPDVSKHLCMINNGGCSHLCLLAPGKTHTCACPTNFYLAADNRTCLSNCTASQFRCKTDKCIPFWWKCDTVDDCGDGSDEPDDCPEFRCQPGRFQCGTGLCALPAFICDGENDCGDNSDELNCDTHVCLSGQFKCTKNQKCIPVNLRCNGQDDCGDEEDERDCPENSCSPDYFQCKTTKHCISKLWVCDEDPDCADASDEANCDKKTCGPHEFQCKNNNCIPDHWRCDSQNDCSDNSDEENCKPQTCTLKDFLCANGDCVSSRFWCDGDFDCADGSDERNCETSCSKDQFRCSNGQCIPAKWKCDGHEDCKYGEDEKSCEPASPTCSSREYICASDGCISASLKCNGEYDCADGSDEMDCVTECKEDQFRCKNKAHCIPIRWLCDGIHDCVDGSDEENCERGGNICRADEFLCNNSLCKLHFWVCDGEDDCGDNSDEAPDMCVKFLCPSTRPHRCRNNRICLQSEQMCNGIDECGDNSDEDHCGGKLTYKARPCKKDEFACSNKKCIPMDLQCDRLDDCGDGSDEQGCRIAPTEYTCEDNVNPCGDDAYCNQIKTSVFCRCKPGFQRNMKNRQCEDLNECLVFGTCSHQCINVEGSYKCVCDQNFQERNNTCIAEGSEDQVLYIANDTDILGFIYPFNYSGDHQQISHIEHNSRITGMDVYYQRDMIIWSTQFNPGGIFYKRIHGREKRQANSGLICPEFKRPRDIAVDWVAGNIYWTDHSRMHWFSYYTTHWTSLRYSINVGQLNGPNCTRLLTNMAGEPYAIAVNPKRGMMYWTVVGDHSHIEEAAMDGTLRRILVQKNLQRPTGLAVDYFSERIYWADFELSIIGSVLYDGSNSVVSVSSKQGLLHPHRIDIFEDYIYGAGPKNGVFRVQKFGHGSVEYLALNIDKTKGVLISHRYKQLDLPNPCLDLACEFLCLLNPSGATCVCPEGKYLINGTCNDDSLLDDSCKLTCENGGRCILNEKGDLRCHCWPSYSGERCEVNHCSNYCQNGGTCVPSVLGRPTCSCALGFTGPNCGKTVCEDFCQNGGTCIVTAGNQPYCHCQPEYTGDRCQYYVCHHYCVNSESCTIGDDGSVECVCPTRYEGPKCEVDKCVRCHGGHCIINKDSEDIFCNCTNGKIASSCQLCDGYCYNGGTCQLDPETNVPVCLCSTNWSGTQCERPAPKSSKSDHISTRSIAIIVPLVLLVTLITTLVIGLVLCKRKRRTKTIRRQPIINGGINVEIGNPSYNMYEVDHDHNDGGLLDPGFMIDPTKARYIGGGPSAFKLPHTAPPIYLNSDLKGPLTAGPTNYSNPVYAKLYMDGQNCRNSLGSVDERKELLPKKIEIGIRETVA	chr2:140231423-142131016[-]	Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis.	.	HGNC:6693	LRP1B_HUMAN	Reviewed	ENSG00000168702	.	.	.	.	.
Mol00480	Protein	Leucine-rich repeat-containing protein 4 (LRRC4)	Brain tumor-associated protein BAG; Nasopharyngeal carcinoma-associated gene 14 protein; Netrin-G2 ligand; NGL-2; BAG; NAG14; UNQ554/PRO1111	LRRC4	64101	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000249363.4, LRRC4-201, 4195; ENST00000476782.5, LRRC4-202, 561; ENST00000494115.1, LRRC4-204, 557; ENST00000478726.1, LRRC4-203, 451"	MKLLWQVTVHHHTWNAILLPFVYLTAQVWILCAAIAAAASAGPQNCPSVCSCSNQFSKVVCTRRGLSEVPQGIPSNTRYLNLMENNIQMIQADTFRHLHHLEVLQLGRNSIRQIEVGAFNGLASLNTLELFDNWLTVIPSGAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLMRLDLGELKKLEYISEGAFEGLFNLKYLNLGMCNIKDMPNLTPLVGLEELEMSGNHFPEIRPGSFHGLSSLKKLWVMNSQVSLIERNAFDGLASLVELNLAHNNLSSLPHDLFTPLRYLVELHLHHNPWNCDCDILWLAWWLREYIPTNSTCCGRCHAPMHMRGRYLVEVDQASFQCSAPFIMDAPRDLNISEGRMAELKCRTPPMSSVKWLLPNGTVLSHASRHPRISVLNDGTLNFSHVLLSDTGVYTCMVTNVAGNSNASAYLNVSTAELNTSNYSFFTTVTVETTEISPEDTTRKYKPVPTTSTGYQPAYTTSTTVLIQTTRVPKQVAVPATDTTDKMQTSLDEVMKTTKIIIGCFVAVTLLAAAMLIVFYKLRKRHQQRSTVTAARTVEIIQVDEDIPAATSAAATAAPSGVSGEGAVVLPTIHDHINYNTYKPAHGAHWTENSLGNSLHPTVTTISEPYIIQTHTKDKVQETQI	chr7:128027071-128032107[-]	Synaptic adhesion protein. Regulates the formation of exitatory synapses through the recruitment of pre-and-postsynaptic proteins. Organize the lamina/pathway-specific differentiation of dendrites. Plays an important role for auditory synaptic responses. Involved in the suppression of glioma (By similarity).	PDB: 2DL9; PDB: 3ZYI	HGNC:15586	LRRC4_HUMAN	Reviewed	ENSG00000128594	.	.	.	.	.
Mol00481	Protein	Leucine-rich repeat flightless-interacting protein 1 (LRRFIP1)	LRR FLII-interacting protein 1; GC-binding factor 2; TAR RNA-interacting protein; GCF2; TRIP	LRRFIP1	9208	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308482.14, LRRFIP1-203, 4092; ENST00000244815.9, LRRFIP1-201, 4370; ENST00000289175.10, LRRFIP1-202, 3709; ENST00000392000.4, LRRFIP1-204, 3365; ENST00000420665.5, LRRFIP1-205, 570; ENST00000468950.5, LRRFIP1-208, 815; ENST00000498053.5, LRRFIP1-215, 593; ENST00000489603.5, LRRFIP1-214, 531; ENST00000473815.1, LRRFIP1-209, 476; ENST00000489295.5, LRRFIP1-213, 364; ENST00000478958.5, LRRFIP1-211, 2869; ENST00000474195.1, LRRFIP1-210, 1957; ENST00000465870.5, LRRFIP1-207, 1626; ENST00000483443.1, LRRFIP1-212, 1069; ENST00000464608.5, LRRFIP1-206, 564"	MTSPAAAQSREIDCLSPEAQKLAEARLAAKRAARAEAREIRMKELERQQKEEDSERYSRRSRRNTSASDEDERMSVGSRGSLRVEERPEKDFTEKGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEKHGIILNSEIATNGETSDTLNNVGYQGPTKMTKEELNALKSTGDGTLGRASEVEVKNEIVANVGKREILHNTEKEQHTEDTVKDCVDIEVFPAGENTEDQKSSEDTAPFLGTLAGATYEEQVQSQILESSSLPENTVQVESNEVMGAPDDRTRTPLEPSNCWSDLDGGNHTENVGEAAVTQVEEQAGTVASCPLGHSDDTVYHDDKCMVEVPQELETSTGHSLEKEFTNQEAAEPKEVPAHSTEVGRDHNEEEGEETGLRDEKPIKTEVPGSPAGTEGNCQEATGPSTVDTQNEPLDMKEPDEEKSDQQGEALDSSQKKTKNKKKKNKKKKSPVPVETLKDVKKELTYQNTDLSEIKEEEQVKSTDRKSAVEAQNEVTENPKQKIAAESSENVDCPENPKIKLDGKLDQEGDDVQTAAEEVLADGDTLDFEDDTVQSSGPRAGGEELDEGVAKDNAKIDGATQSSPAEPKSEDADRCTLPEHESPSQDISDACEAESTERCEMSEHPSQTVRKALDSNSLENDDLSAPGREPGHFNPESREDTRGGNEKGKSKEDCTMS	chr2:237627587-237813682[+]	"Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding."	PDB: 4H22	HGNC:6702	LRRF1_HUMAN	Reviewed	ENSG00000124831	.	.	.	.	.
Mol00482	Protein	Protein LYRIC (MTDH)	3D3/LYRIC; Astrocyte elevated gene-1 protein; AEG-1; Lysine-rich CEACAM1 co-isolated protein; Metadherin; Metastasis adhesion protein; AEG1; LYRIC	MTDH	92140	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000336273.8, MTDH-201, 7662; ENST00000519934.5, MTDH-203, 2184; ENST00000522313.1, MTDH-206, 672; ENST00000521933.1, MTDH-204, 565; ENST00000519293.1, MTDH-202, 629; ENST00000522104.1, MTDH-205, 486"	MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET	chr8:97644184-97730260[+]	"Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance."	PDB: 4QMG	HGNC:29608	LYRIC_HUMAN	Reviewed	ENSG00000147649	.	.	.	.	.
Mol00483	Protein	Leucine zipper putative tumor suppressor 1 (LZTS1)	F37/esophageal cancer-related gene-coding leucine-zipper motif; Fez1; FEZ1	LZTS1	11178	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000381569.5, LZTS1-202, 5706; ENST00000265801.6, LZTS1-201, 5459; ENST00000522290.5, LZTS1-203, 1614; ENST00000616228.1, LZTS1-204, 231"	MGSVSSLISGHSFHSKHCRASQYKLRKSSHLKKLNRYSDGLLRFGFSQDSGHGKSSSKMGKSEDFFYIKVSQKARGSHHPDYTALSSGDLGGQAGVDFDPSTPPKLMPFSNQLEMGSEKGAVRPTAFKPVLPRSGAILHSSPESASHQLHPAPPDKPKEQELKPGLCSGALSDSGRNSMSSLPTHSTSSSYQLDPLVTPVGPTSRFGGSAHNITQGIVLQDSNMMSLKALSFSDGGSKLGHSNKADKGPSCVRSPISTDECSIQELEQKLLEREGALQKLQRSFEEKELASSLAYEERPRRCRDELEGPEPKGGNKLKQASQKSQRAQQVLHLQVLQLQQEKRQLRQELESLMKEQDLLETKLRSYEREKTSFGPALEETQWEVCQKSGEISLLKQQLKESQTEVNAKASEILGLKAQLKDTRGKLEGLELRTQDLEGALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELQELRAQAALARDMGPPTFPEDVPALQRELERLRAELREERQGHDQMSSGFQHERLVWKEEKEKVIQYQKQLQQSYVAMYQRNQRLEKALQQLARGDSAGEPLEVDLEGADIPYEDIIATEI	chr8:20246165-20303963[-]	Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as a tumor suppressor.	.	HGNC:13861	LZTS1_HUMAN	Reviewed	ENSG00000061337	.	.	.	.	.
Mol00484	Protein	Mitogen-activated protein kinase kinase kinase 1 (MAP3K1)	MAPK/ERK kinase kinase 1; MEK kinase 1; MEKK 1; MAPKKK1; MEKK; MEKK1	MAP3K1	4214	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000399503.4, MAP3K1-201, 7036; ENST00000469188.1, MAP3K1-202, 3713"	MAAAAGNRASSSGFPGARATSPEAGGGGGALKASSAPAAAAGLLREAGSGGRERADWRRRQLRKVRSVELDQLPEQPLFLAASPPASSTSPSPEPADAAGSGTGFQPVAVPPPHGAASRGGAHLTESVAAPDSGASSPAAAEPGEKRAPAAEPSPAAAPAGREMENKETLKGLHKMDDRPEERMIREKLKATCMPAWKHEWLERRNRRGPVVVKPIPVKGDGSEMNHLAAESPGEVQASAASPASKGRRSPSPGNSPSGRTVKSESPGVRRKRVSPVPFQSGRITPPRRAPSPDGFSPYSPEETNRRVNKVMRARLYLLQQIGPNSFLIGGDSPDNKYRVFIGPQNCSCARGTFCIHLLFVMLRVFQLEPSDPMLWRKTLKNFEVESLFQKYHSRRSSRIKAPSRNTIQKFVSRMSNSHTLSSSSTSTSSSENSIKDEEEQMCPICLLGMLDEESLTVCEDGCRNKLHHHCMSIWAEECRRNREPLICPLCRSKWRSHDFYSHELSSPVDSPSSLRAAQQQTVQQQPLAGSRRNQESNFNLTHYGTQQIPPAYKDLAEPWIQVFGMELVGCLFSRNWNVREMALRRLSHDVSGALLLANGESTGNSGGSSGSSPSGGATSGSSQTSISGDVVEACCSVLSMVCADPVYKVYVAALKTLRAMLVYTPCHSLAERIKLQRLLQPVVDTILVKCADANSRTSQLSISTLLELCKGQAGELAVGREILKAGSIGIGGVDYVLNCILGNQTESNNWQELLGRLCLIDRLLLEFPAEFYPHIVSTDVSQAEPVEIRYKKLLSLLTFALQSIDNSHSMVGKLSRRIYLSSARMVTTVPHVFSKLLEMLSVSSSTHFTRMRRRLMAIADEVEIAEAIQLGVEDTLDGQQDSFLQASVPNNYLETTENSSPECTVHLEKTGKGLCATKLSASSEDISERLASISVGPSSSTTTTTTTTEQPKPMVQTKGRPHSQCLNSSPLSHHSQLMFPALSTPSSSTPSVPAGTATDVSKHRLQGFIPCRIPSASPQTQRKFSLQFHRNCPENKDSDKLSPVFTQSRPLPSSNIHRPKPSRPTPGNTSKQGDPSKNSMTLDLNSSSKCDDSFGCSSNSSNAVIPSDETVFTPVEEKCRLDVNTELNSSIEDLLEASMPSSDTTVTFKSEVAVLSPEKAENDDTYKDDVNHNQKCKEKMEAEEEEALAIAMAMSASQDALPIVPQLQVENGEDIIIIQQDTPETLPGHTKAKQPYREDTEWLKGQQIGLGAFSSCYQAQDVGTGTLMAVKQVTYVRNTSSEQEEVVEALREEIRMMSHLNHPNIIRMLGATCEKSNYNLFIEWMAGGSVAHLLSKYGAFKESVVINYTEQLLRGLSYLHENQIIHRDVKGANLLIDSTGQRLRIADFGAAARLASKGTGAGEFQGQLLGTIAFMAPEVLRGQQYGRSCDVWSVGCAIIEMACAKPPWNAEKHSNHLALIFKIASATTAPSIPSHLSPGLRDVALRCLELQPQDRPPSRELLKHPVFRTTW	chr5:56815549-56896152[+]	"Component of a protein kinase signal transduction cascade. Activates the ERK and JNK kinase pathways by phosphorylation of MAP2K1 and MAP2K4. May phosphorylate the MAPK8/JNK1 kinase. Activates CHUK and IKBKB, the central protein kinases of the NF-kappa-B pathway."	PDB: 6WHB	HGNC:6848	M3K1_HUMAN	Reviewed	ENSG00000095015	.	.	.	.	.
Mol00485	Protein	Mitogen-activated protein kinase kinase kinase 5 (MAP3K5)	Apoptosis signal-regulating kinase 1; ASK-1; MAPK/ERK kinase kinase 5; MEK kinase 5; MEKK 5; ASK1; MAPKKK5; MEKK5	MAP3K5	4217	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359015.5, MAP3K5-201, 5157; ENST00000463140.1, MAP3K5-202, 365"	MSTEADEGITFSVPPFAPSGFCTIPEGGICRRGGAAAVGEGEEHQLPPPPPGSFWNVESAAAPGIGCPAATSSSSATRGRGSSVGGGSRRTTVAYVINEASQGQLVVAESEALQSLREACETVGATLETLHFGKLDFGETTVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTMCTGNYTFVPYMITPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFIQLLKVAQASSSQYFRESILNDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEGQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHMRVIQASEKLFKLKTPAWYLKSIVETILIYKHFVKLTTEQPVAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFSASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKKFFEMVNTITEEKGRSTEEGDCESDLLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLVDEFLKVSSKKKKTQPKLSALSAGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKVDPFSFKTRAKSCGERDVKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKIVRNLMESLAQGAEEPKLKWEHITTLIASLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADQEDLDVEDDHEEQPSNQTVRRPQAVIEDAVATSGVSTLSSTVSHDSQSAHRSLNVQLGRMKIETNRLLEELVRKEKELQALLHRAIEEKDQEIKHLKLKSQPIEIPELPVFHLNSSGTNTEDSELTDWLRVNGADEDTISRFLAEDYTLLDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKQT	chr6:136557046-136792477[-]	"Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1)."	PDB: 2CLQ; PDB: 3VW6; PDB: 4BF2; PDB: 4BHN; PDB: 4BIB; PDB: 4BIC; PDB: 4BID; PDB: 4BIE; PDB: 5ULM; PDB: 5UOR; PDB: 5UOX; PDB: 5UP3; PDB: 5V19; PDB: 5V24; PDB: 5VIL; PDB: 5VIO; PDB: 6E2M; PDB: 6E2N; PDB: 6E2O; PDB: 6EJL; PDB: 6OYT; PDB: 6OYW; PDB: 6VRE; PDB: 6XIH	HGNC:6857	M3K5_HUMAN	Reviewed	ENSG00000197442	.	.	.	.	.
Mol00486	Protein	Mitogen-activated protein kinase kinase kinase 8 (MAP3K8)	Cancer Osaka thyroid oncogene; Proto-oncogene c-Cot; Serine/threonine-protein kinase cot; Tumor progression locus 2; TPL-2; COT; ESTF	MAP3K8	1326	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263056.6, MAP3K8-201, 2850; ENST00000542547.5, MAP3K8-207, 2782; ENST00000375321.1, MAP3K8-202, 2518; ENST00000415139.5, MAP3K8-205, 1026; ENST00000375322.2, MAP3K8-203, 932; ENST00000413724.5, MAP3K8-204, 776; ENST00000430603.1, MAP3K8-206, 647"	MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKKVIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVYFPKDLRGTEIYMSPEVILCRGHSTKADIYSLGATLIHMQTGTPPWVKRYPRSAYPSYLYIIHKQAPPLEDIADDCSPGMRELIEASLERNPNHRPRAADLLKHEALNPPREDQPRCQSLDSALLERKRLLSRKELELPENIADSSCTGSTEESEMLKRQRSLYIDLGALAGYFNLVRGPPTLEYG	chr10:30434021-30461833[+]	"Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the proinflammatory cytokine TNF-alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. In vitro, activates MAPK/ERK pathway in response to IL1 in an IRAK1-independent manner, leading to up-regulation of IL8 and CCL4. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. Isoform 1 shows some transforming activity, although it is much weaker than that of the activated oncogenic variant."	PDB: 4Y83; PDB: 4Y85; PDB: 5IU2	HGNC:6860	M3K8_HUMAN	Reviewed	ENSG00000107968	.	.	.	.	.
Mol00487	Protein	Mitogen-activated protein kinase kinase kinase kinase 3 (MAP4K3)	Germinal center kinase-related protein kinase; GLK; MAPK/ERK kinase kinase kinase 3; MEK kinase kinase 3; MEKKK 3; RAB8IPL1	MAP4K3	8491	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263881.8, MAP4K3-201, 4335; ENST00000341681.9, MAP4K3-202, 4271; ENST00000437545.5, MAP4K3-205, 3924; ENST00000484274.1, MAP4K3-211, 407; ENST00000429397.5, MAP4K3-204, 689; ENST00000414968.1, MAP4K3-203, 558; ENST00000437968.1, MAP4K3-206, 500; ENST00000474502.5, MAP4K3-208, 556; ENST00000479708.1, MAP4K3-210, 577; ENST00000495648.3, MAP4K3-212, 564; ENST00000497566.5, MAP4K3-213, 528; ENST00000475457.1, MAP4K3-209, 428; ENST00000465701.1, MAP4K3-207, 201"	MNPGFDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQHLTRSLAIELLDKVNNPDHSTYHDFDDDDPEPLVAVPHRIHSTSRNVREEKTRSEITFGQVKFDPPLRKETEPHHELPDSDGFLDSSEEIYYTARSNLDLQLEYGQGHQGGYFLGANKSLLKSVEEELHQRGHVAHLEDDEGDDDESKHSTLKAKIPPPLPPKPKSIFIPQEMHSTEDENQGTIKRCPMSGSPAKPSQVPPRPPPPRLPPHKPVALGNGMSSFQLNGERDGSLCQQQNEHRGTNLSRKEKKDVPKPISNGLPPTPKVHMGACFSKVFNGCPLKIHCASSWINPDTRDQYLIFGAEEGIYTLNLNELHETSMEQLFPRRCTWLYVMNNCLLSISGKASQLYSHNLPGLFDYARQMQKLPVAIPAHKLPDRILPRKFSVSAKIPETKWCQKCCVVRNPYTGHKYLCGALQTSIVLLEWVEPMQKFMLIKHIDFPIPCPLRMFEMLVVPEQEYPLVCVGVSRGRDFNQVVRFETVNPNSTSSWFTESDTPQTNVTHVTQLERDTILVCLDCCIKIVNLQGRLKSSRKLSSELTFDFQIESIVCLQDSVLAFWKHGMQGRSFRSNEVTQEISDSTRIFRLLGSDRVVVLESRPTDNPTANSNLYILAGHENSY	chr2:39249266-39437301[-]	May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway.	PDB: 5J5T	HGNC:6865	M4K3_HUMAN	Reviewed	ENSG00000011566	.	.	.	.	.
Mol00488	Protein	Max dimerization protein 4 (MXD4)	Max dimerizer 4; Class C basic helix-loop-helix protein 12; bHLHc12; Max-associated protein 4; Max-interacting transcriptional repressor MAD4; BHLHC12; MAD4	MXD4	10608	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000337190.7, MXD4-201, 3871; ENST00000513380.1, MXD4-204, 624; ENST00000510822.1, MXD4-202, 561; ENST00000515378.5, MXD4-205, 522; ENST00000513372.5, MXD4-203, 4228"	MELNSLLILLEAAEYLERRDREAEHGYASVLPFDGDFAREKTKAAGLVRKAPNNRSSHNELEKHRRAKLRLYLEQLKQLVPLGPDSTRHTTLSLLKRAKVHIKKLEEQDRRALSIKEQLQQEHRFLKRRLEQLSVQSVERVRTDSTGSAVSTDDSEQEVDIEGMEFGPGELDSVGSSSDADDHYSLQSGTGGDSGFGPHCRRLGRPALS	chr4:2247432-2262109[-]	Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation (By similarity).	.	HGNC:13906	MAD4_HUMAN	Reviewed	ENSG00000123933	.	.	.	.	.
Mol00489	Protein	Melanoma-associated antigen 2 (MAGEA2)	Cancer/testis antigen 1.2; CT1.2; MAGE-2 antigen; MAGE2; MAGEA2A; MAGE2; MAGEA2	MAGEA2	266740	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000682532.1, MAGEA2B-212, 1886; ENST00000331220.6, MAGEA2B-201, 1946; ENST00000370293.6, MAGEA2B-202, 1714; ENST00000423993.5, MAGEA2B-205, 879; ENST00000453150.5, MAGEA2B-207, 753; ENST00000447530.5, MAGEA2B-206, 750; ENST00000422085.5, MAGEA2B-204, 652; ENST00000458057.5, MAGEA2B-208, 576; ENST00000409560.1, MAGEA2B-203, 445; ENST00000467743.1, MAGEA2B-209, 704; ENST00000497578.5, MAGEA2B-211, 526; ENST00000492402.5, MAGEA2B-210, 309"	MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQQTASSSSTLVEVTLGEVPAADSPSPPHSPQGASSFSTTINYTLWRQSDEGSSNQEEEGPRMFPDLESEFQAAISRKMVELVHFLLLKYRAREPVTKAEMLESVLRNCQDFFPVIFSKASEYLQLVFGIEVVEVVPISHLYILVTCLGLSYDGLLGDNQVMPKTGLLIIVLAIIAIEGDCAPEEKIWEELSMLEVFEGREDSVFAHPRKLLMQDLVQENYLEYRQVPGSDPACYEFLWGPRALIETSYVKVLHHTLKIGGEPHISYPPLHERALREGEE	chrX:152714586-152718607[+]	Reduces p53/TP53 transactivation function through recruitment of HDAC3 to p53/TP53 transcription sites. Also represses p73/TP73 activity. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination by TRIM28 potentially in presence of Ubl-conjugating enzyme UBE2H. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. Negatively regulates acetylation and sumoylation of PML and represses PML-induced p53/TP53 acetylation and activation.	.	HGNC:19340	MAGA2_HUMAN	Reviewed	ENSG00000183305	.	.	.	.	.
Mol00490	Protein	Melanoma-associated antigen 3 (MAGEA3)	Antigen MZ2-D; Cancer/testis antigen 1.3; CT1.3; MAGE-3 antigen; MAGE3	MAGEA3	4102	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000370278.4, MAGEA3-201, 1682; ENST00000598245.2, MAGEA3-203, 1762; ENST00000417212.5, MAGEA3-202, 853"	MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQEAASSSSTLVEVTLGEVPAAESPDPPQSPQGASSLPTTMNYPLWSQSYEDSSNQEEEGPSTFPDLESEFQAALSRKVAELVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASSSLQLVFGIELMEVDPIGHLYIFATCLGLSYDGLLGDNQIMPKAGLLIIVLAIIAREGDCAPEEKIWEELSVLEVFEGREDSILGDPKKLLTQHFVQENYLEYRQVPGSDPACYEFLWGPRALVETSYVKVLHHMVKISGGPHISYPPLHEWVLREGEE	chrX:152698767-152702347[+]	Activator of ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases that acts as a as repressor of autophagy. May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes.	PDB: 1QEW; PDB: 4V0P; PDB: 5BRZ	HGNC:6801	MAGA3_HUMAN	Reviewed	ENSG00000221867	.	.	.	.	.
Mol00491	Protein	Membrane-associated guanylate kinase inverted 2 (MAGI2)	Atrophin-1-interacting protein 1; AIP-1; Atrophin-1-interacting protein A; Membrane-associated guanylate kinase inverted 2; MAGI-2; ACVRINP1; AIP1; KIAA0705	MAGI2	9863	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354212.9, MAGI2-201, 6975; ENST00000419488.5, MAGI2-202, 6800; ENST00000629359.2, MAGI2-216, 6704; ENST00000628980.2, MAGI2-214, 6212; ENST00000535697.5, MAGI2-210, 6146; ENST00000637441.1, MAGI2-235, 5822; ENST00000636039.1, MAGI2-221, 5671; ENST00000522391.3, MAGI2-207, 4878; ENST00000626691.2, MAGI2-211, 4599; ENST00000519748.5, MAGI2-204, 3316; ENST00000637282.1, MAGI2-234, 3174; ENST00000630991.2, MAGI2-217, 2349; ENST00000636178.1, MAGI2-223, 2316; ENST00000628781.1, MAGI2-213, 2013; ENST00000636717.1, MAGI2-227, 1661; ENST00000628361.1, MAGI2-212, 715; ENST00000522342.3, MAGI2-206, 643; ENST00000524268.1, MAGI2-208, 533; ENST00000634996.1, MAGI2-218, 492; ENST00000637585.1, MAGI2-238, 190; ENST00000637486.1, MAGI2-236, 4355; ENST00000636234.1, MAGI2-224, 5702; ENST00000636993.1, MAGI2-230, 4948; ENST00000637249.1, MAGI2-233, 3426; ENST00000635863.1, MAGI2-219, 1605; ENST00000637728.1, MAGI2-239, 934; ENST00000636989.1, MAGI2-229, 666; ENST00000440555.2, MAGI2-203, 574; ENST00000524316.5, MAGI2-209, 549; ENST00000636424.1, MAGI2-225, 102; ENST00000636040.1, MAGI2-222, 100; ENST00000635961.1, MAGI2-220, 100; ENST00000637976.1, MAGI2-242, 100; ENST00000636593.1, MAGI2-226, 100; ENST00000636936.1, MAGI2-228, 100; ENST00000637136.1, MAGI2-232, 100; ENST00000637515.1, MAGI2-237, 100; ENST00000637824.1, MAGI2-240, 100; ENST00000637879.1, MAGI2-241, 100; ENST00000637074.1, MAGI2-231, 89; ENST00000676103.1, MAGI2-243, 2802; ENST00000520379.2, MAGI2-205, 1510; ENST00000628997.1, MAGI2-215, 641"	MSKSLKKKSHWTSKVHESVIGRNPEGQLGFELKGGAENGQFPYLGEVKPGKVAYESGSKLVSEELLLEVNETPVAGLTIRDVLAVIKHCKDPLRLKCVKQGGIVDKDLRHYLNLRFQKGSVDHELQQIIRDNLYLRTVPCTTRPHKEGEVPGVDYIFITVEDFMELEKSGALLESGTYEDNYYGTPKPPAEPAPLLLNVTDQILPGATPSAEGKRKRNKSVSNMEKASIEPPEEEEEERPVVNGNGVVVTPESSEHEDKSAGASGEMPSQPYPAPVYSQPEELKEQMDDTKPTKPEDNEEPDPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRLAKKAKPPEECKENELPYGWEKIDDPIYGTYYVDHINRRTQFENPVLEAKRKLQQHNMPHTELGTKPLQAPGFREKPLFTRDASQLKGTFLSTTLKKSNMGFGFTIIGGDEPDEFLQVKSVIPDGPAAQDGKMETGDVIVYINEVCVLGHTHADVVKLFQSVPIGQSVNLVLCRGYPLPFDPEDPANSMVPPLAIMERPPPVMVNGRHNYETYLEYISRTSQSVPDITDRPPHSLHSMPTDGQLDGTYPPPVHDDNVSMASSGATQAELMTLTIVKGAQGFGFTIADSPTGQRVKQILDIQGCPGLCEGDLIVEINQQNVQNLSHTEVVDILKDCPIGSETSLIIHRGGFFSPWKTPKPIMDRWENQGSPQTSLSAPAIPQNLPFPPALHRSSFPDSTEAFDPRKPDPYELYEKSRAIYESRQQVPPRTSFRMDSSGPDYKELDVHLRRMESGFGFRILGGDEPGQPILIGAVIAMGSADRDGRLHPGDELVYVDGIPVAGKTHRYVIDLMHHAARNGQVNLTVRRKVLCGGEPCPENGRSPGSVSTHHSSPRSDYATYTNSNHAAPSSNASPPEGFASHSLQTSDVVIHRKENEGFGFVIISSLNRPESGSTITVPHKIGRIIDGSPADRCAKLKVGDRILAVNGQSIINMPHADIVKLIKDAGLSVTLRIIPQEELNSPTSAPSSEKQSPMAQQSPLAQQSPLAQPSPATPNSPIAQPAPPQPLQLQGHENSYRSEVKARQDVKPDIRQPPFTDYRQPPLDYRQPPGGDYQQPPPLDYRQPPLLDYRQHSPDTRQYPLSDYRQPQDFDYFTVDMEKGAKGFGFSIRGGREYKMDLYVLRLAEDGPAIRNGRMRVGDQIIEINGESTRDMTHARAIELIKSGGRRVRLLLKRGTGQVPEYDEPAPWSSPAAAAPGLPEVGVSLDDGLAPFSPSHPAPPSDPSHQISPGPTWDIKREHDVRKPKELSACGQKKQRLGEQRERSASPQRAARPRLEEAPGGQGRPEAGRPASEARAPGLAAADAADAARAGGKEAPRAAAGSELCRREGPGAAPAFAGPGGGGSGALEAEGRAGARAGPRPGPRPPGGAPARKAAVAPGPWKVPGSDKLPSVLKPGASAASR	chr7:78017055-79453667[-]	Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. May play a role in regulating activin-mediated signaling in neuronal cells. Enhances the ability of PTEN to suppress AKT1 activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth.	.	HGNC:18957	MAGI2_HUMAN	Reviewed	ENSG00000187391	.	.	.	.	.
Mol00492	Protein	E3 ubiquitin-protein ligase Mdm2 (MDM2)	Double minute 2 protein; Hdm2; Oncoprotein Mdm2; RING-type E3 ubiquitin transferase Mdm2; p53-binding protein Mdm2	MDM2	4193	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000258149.11, MDM2-202, 7490; ENST00000299252.8, MDM2-203, 966; ENST00000539479.6, MDM2-224, 2523; ENST00000393416.7, MDM2-212, 1748; ENST00000544561.6, MDM2-231, 1480; ENST00000393412.7, MDM2-209, 1404; ENST00000350057.9, MDM2-206, 1401; ENST00000258148.11, MDM2-201, 1361; ENST00000360430.6, MDM2-207, 891; ENST00000545204.2, MDM2-232, 866; ENST00000393415.7, MDM2-211, 842; ENST00000348801.7, MDM2-205, 799; ENST00000393410.5, MDM2-208, 732; ENST00000478070.2, MDM2-216, 693; ENST00000393413.7, MDM2-210, 657; ENST00000523991.5, MDM2-221, 505; ENST00000543323.5, MDM2-229, 427; ENST00000517852.5, MDM2-220, 393; ENST00000393417.8, MDM2-213, 1683; ENST00000311420.13, MDM2-204, 1583; ENST00000671567.1, MDM2-236, 1527; ENST00000666617.1, MDM2-235, 1499; ENST00000665020.1, MDM2-234, 1472; ENST00000540352.5, MDM2-225, 1315; ENST00000536089.5, MDM2-222, 1181; ENST00000542502.5, MDM2-227, 1127; ENST00000481186.6, MDM2-217, 1057; ENST00000537182.5, MDM2-223, 1011; ENST00000496959.5, MDM2-219, 897; ENST00000546048.5, MDM2-233, 363; ENST00000544125.1, MDM2-230, 649; ENST00000540709.1, MDM2-226, 502; ENST00000400501.2, MDM2-214, 406; ENST00000493419.1, MDM2-218, 577; ENST00000543046.1, MDM2-228, 432; ENST00000471946.1, MDM2-215, 251"	MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP	chr12:68808177-68845544[+]	"E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation. Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells. Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis. Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis. Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis."	PDB: 1RV1; PDB: 1T4E; PDB: 1T4F; PDB: 1YCR; PDB: 1Z1M; PDB: 2AXI; PDB: 2C6A; PDB: 2C6B; PDB: 2F1Y; PDB: 2FOP; PDB: 2GV2; PDB: 2HDP; PDB: 2LZG; PDB: 2M86; PDB: 2MPS; PDB: 2RUH; PDB: 2VJE; PDB: 2VJF; PDB: 3EQS; PDB: 3G03; PDB: 3IUX; PDB: 3IWY; PDB: 3JZK; PDB: 3JZR; PDB: 3JZS; PDB: 3LBK; PDB: 3LBL; PDB: 3LNJ; PDB: 3LNZ; PDB: 3MQS; PDB: 3TJ2; PDB: 3TPX; PDB: 3TU1; PDB: 3V3B; PDB: 3VBG; PDB: 3VZV; PDB: 3W69; PDB: 4DIJ; PDB: 4ERE; PDB: 4ERF; PDB: 4HBM; PDB: 4HFZ; PDB: 4HG7; PDB: 4JV7; PDB: 4JV9; PDB: 4JVE; PDB: 4JVR; PDB: 4JWR; PDB: 4MDN; PDB: 4MDQ; PDB: 4OAS; PDB: 4OBA; PDB: 4OCC; PDB: 4ODE; PDB: 4ODF; PDB: 4OGN; PDB: 4OGT; PDB: 4OGV; PDB: 4OQ3; PDB: 4QO4; PDB: 4QOC; PDB: 4UD7; PDB: 4UE1; PDB: 4UMN; PDB: 4WT2; PDB: 4XXB; PDB: 4ZFI; PDB: 4ZGK; PDB: 4ZYC; PDB: 4ZYF; PDB: 4ZYI; PDB: 5AFG; PDB: 5C5A; PDB: 5HMH; PDB: 5HMI; PDB: 5HMK; PDB: 5J7F; PDB: 5J7G; PDB: 5LAV; PDB: 5LAW; PDB: 5LAY; PDB: 5LAZ; PDB: 5LN2; PDB: 5MNJ; PDB: 5OAI; PDB: 5OC8; PDB: 5SWK; PDB: 5TRF; PDB: 5UMM; PDB: 5VK0; PDB: 5WTS; PDB: 5XXK; PDB: 5Z02; PDB: 5ZXF; PDB: 6AAW; PDB: 6GGN; PDB: 6H22; PDB: 6HFA; PDB: 6I29; PDB: 6I3S; PDB: 6IM9; PDB: 6KZU; PDB: 6Q96; PDB: 6Q9H; PDB: 6Q9L; PDB: 6Q9O; PDB: 6SQO; PDB: 6T2D; PDB: 6T2E; PDB: 6T2F; PDB: 6Y4Q; PDB: 7AD0; PDB: 7AI0; PDB: 7AI1; PDB: 7AYE; PDB: 7BIR; PDB: 7BIT; PDB: 7BIV; PDB: 7BJ0; PDB: 7BJ6; PDB: 7BMG; PDB: 7NUS	HGNC:6973	MDM2_HUMAN	Reviewed	ENSG00000135679	.	.	.	.	.
Mol00493	Protein	Protein Mdm4 (MDM4)	Double minute 4 protein; Mdm2-like p53-binding protein; Protein Mdmx; p53-binding protein Mdm4; MDMX	MDM4	4194	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367182.8, MDM4-203, 10050; ENST00000391947.6, MDM4-205, 10008; ENST00000454264.6, MDM4-207, 9926; ENST00000614459.4, MDM4-215, 9782; ENST00000616250.4, MDM4-216, 9597; ENST00000612738.4, MDM4-214, 9407; ENST00000367183.7, MDM4-204, 9098; ENST00000507825.3, MDM4-213, 481; ENST00000367179.7, MDM4-201, 697; ENST00000367180.5, MDM4-202, 547; ENST00000444261.1, MDM4-206, 513; ENST00000463049.5, MDM4-209, 6102; ENST00000470797.5, MDM4-210, 909; ENST00000470908.5, MDM4-211, 884; ENST00000462012.1, MDM4-208, 582; ENST00000471783.1, MDM4-212, 552"	MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA	chr1:204516379-204558120[+]	"Along with MDM2, contributes to TP53 regulation. Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions."	PDB: 2CR8; PDB: 2MWY; PDB: 2N06; PDB: 2N0U; PDB: 2N0W; PDB: 2N14; PDB: 2VJE; PDB: 2VJF; PDB: 2VYR; PDB: 3DAB; PDB: 3EQY; PDB: 3FDO; PDB: 3FE7; PDB: 3FEA; PDB: 3JZO; PDB: 3JZP; PDB: 3JZQ; PDB: 3LBJ; PDB: 3MQR; PDB: 3U15; PDB: 4RXZ; PDB: 5MNJ; PDB: 5UML; PDB: 5VK1; PDB: 6Q9Q; PDB: 6Q9S; PDB: 6Q9U; PDB: 6Q9W; PDB: 6Q9Y; PDB: 7C3Q; PDB: 7C3Y; PDB: 7C44; PDB: 7EL4	HGNC:6974	MDM4_HUMAN	Reviewed	ENSG00000198625	.	.	.	.	.
Mol00494	Protein	Multidrug resistance protein 3 (ABCB4)	ATP-binding cassette sub-family B member 4; Multidrug resistance protein 3; P-glycoprotein 3; MDR3; PGY3	ABCB4	5244	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649586.2, ABCB4-212, 4293; ENST00000265723.8, ABCB4-201, 4020; ENST00000359206.8, ABCB4-202, 3961; ENST00000453593.5, ABCB4-205, 3699; ENST00000417608.1, ABCB4-203, 2007; ENST00000440025.1, ABCB4-204, 523; ENST00000643670.1, ABCB4-210, 2284; ENST00000644106.1, ABCB4-211, 2112; ENST00000473795.1, ABCB4-209, 1115; ENST00000467079.1, ABCB4-206, 794; ENST00000469770.1, ABCB4-208, 746; ENST00000467983.1, ABCB4-207, 414"	MDLEAAKNGTAWRPTSAEGDFELGISSKQKRKKTKTVKMIGVLTLFRYSDWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFSLSLLNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQTSGSQIQSEEFELNDEKAATRMAPNGWKSRLFRHSTQKNLKNSQMCQKSLDVETDGLEANVPPVSFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTQNL	chr7:87401696-87480435[-]	"[Isoform 1]: Energy-dependent phospholipid efflux translocator that acts as a positive regulator of biliary lipid secretion. Functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi of hepatocytes. Translocation of PC makes the biliary phospholipids available for extraction into the canaliculi lumen by bile salt mixed micelles and therefore protects the biliary tree from the detergent activity of bile salts. Plays a role in the recruitment of phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to nonraft membranes and to further enrichment of SM and cholesterol in raft membranes in hepatocytes. Required for proper phospholipid bile formation. Indirectly involved in cholesterol efflux activity from hepatocytes into the canalicular lumen in the presence of bile salts in an ATP-dependent manner. Promotes biliary phospholipid secretion as canaliculi-containing vesicles from the canalicular plasma membrane. In cooperation with ATP8B1, functions to protect hepatocytes from the deleterious detergent activity of bile salts. Does not confer multidrug resistance."	PDB: 6S7P; PDB: 7NIU; PDB: 7NIV; PDB: 7NIW	HGNC:45	MDR3_HUMAN	Reviewed	ENSG00000005471	.	.	.	.	.
Mol00495	Protein	Mediator of RNA polymerase II transcription subunit 1 (MED1)	Activator-recruited cofactor 205 kDa component; ARC205; Mediator complex subunit 1; Peroxisome proliferator-activated receptor-binding protein; PBP; PPAR-binding protein; Thyroid hormone receptor-associated protein complex 220 kDa component; Trap220; Thyroid receptor-interacting protein 2; TR-interacting protein 2; TRIP-2; Vitamin D receptor-interacting protein complex component DRIP205; p53 regulatory protein RB18A; ARC205; CRSP1; CRSP200; DRIP205; DRIP230; PBP; PPARBP; PPARGBP; RB18A; TRAP220; TRIP2	MED1	5469	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000300651.11, MED1-201, 8137; ENST00000394287.7, MED1-202, 2870; ENST00000577831.5, MED1-203, 4584; ENST00000581334.1, MED1-204, 580; ENST00000584308.1, MED1-205, 467"	MKAQGETEESEKLSKMSSLLERLHAKFNQNRPWSETIKLVRQVMEKRVVMSSGGHQHLVSCLETLQKALKVTSLPAMTDRLESIARQNGLGSHLSASGTECYITSDMFYVEVQLDPAGQLCDVKVAHHGENPVSCPELVQQLREKNFDEFSKHLKGLVNLYNLPGDNKLKTKMYLALQSLEQDLSKMAIMYWKATNAGPLDKILHGSVGYLTPRSGGHLMNLKYYVSPSDLLDDKTASPIILHENNVSRSLGMNASVTIEGTSAVYKLPIAPLIMGSHPVDNKWTPSFSSITSANSVDLPACFFLKFPQPIPVSRAFVQKLQNCTGIPLFETQPTYAPLYELITQFELSKDPDPIPLNHNMRFYAALPGQQHCYFLNKDAPLPDGRSLQGTLVSKITFQHPGRVPLILNLIRHQVAYNTLIGSCVKRTILKEDSPGLLQFEVCPLSESRFSVSFQHPVNDSLVCVVMDVQDSTHVSCKLYKGLSDALICTDDFIAKVVQRCMSIPVTMRAIRRKAETIQADTPALSLIAETVEDMVKKNLPPASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTLYGSSPLERQNSSSGSPRMEICSGSNKTKKKKSSRLPPEKPKHQTEDDFQRELFSMDVDSQNPIFDVNMTADTLDTPHITPAPSQCSTPPTTYPQPVPHPQPSIQRMVRLSSSDSIGPDVTDILSDIAEEASKLPSTSDDCPAIGTPLRDSSSSGHSQSTLFDSDVFQTNNNENPYTDPADLIADAAGSPSSDSPTNHFFHDGVDFNPDLLNSQSQSGFGEEYFDESSQSGDNDDFKGFASQALNTLGVPMLGGDNGETKFKGNNQADTVDFSIISVAGKALAPADLMEHHSGSQGPLLTTGDLGKEKTQKRVKEGNGTSNSTLSGPGLDSKPGKRSRTPSNDGKSKDKPPKRKKADTEGKSPSHSSSNRPFTPPTSTGGSKSPGSAGRSQTPPGVATPPIPKITIQIPKGTVMVGKPSSHSQYTSSGSVSSSGSKSHHSHSSSSSSSASTSGKMKSSKSEGSSSSKLSSSMYSSQGSSGSSQSKNSSQSGGKPGSSPITKHGLSSGSSSTKMKPQGKPSSLMNPSLSKPNISPSHSRPPGGSDKLASPMKPVPGTPPSSKAKSPISSGSGGSHMSGTSSSSGMKSSSGLGSSGSLSQKTPPSSNSCTASSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKPSLTAVIDKLKHGVVTSGPGGEDPLDGQMGVSTNSSSHPMSSKHNMSGGEFQGKREKSDKDKSKVSTSGSSVDSSKKTSESKNVGSTGVAKIIISKHDGGSPSIKAKVTLQKPGESSGEGLRPQMASSKNYGSPLISGSTPKHERGSPSHSKSPAYTPQNLDSESESGSSIAEKSYQNSPSSDDGIRPLPEYSTEKHKKHKKEKKKVKDKDRDRDRDKDRDKKKSHSIKPESWSKSPISSDQSLSMTSNTILSADRPSRLSPDFMIGEEDDDLMDVALIGN	chr17:39404285-39451272[-]	"Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells."	PDB: 1RJK; PDB: 1RK3; PDB: 1RKG; PDB: 1RKH; PDB: 2O4J; PDB: 2O4R; PDB: 2ZFX; PDB: 3A2H; PDB: 3AUN; PDB: 3VJS; PDB: 3VJT; PDB: 3VRT; PDB: 3VRU; PDB: 3VRV; PDB: 3VRW; PDB: 3W0G; PDB: 3W0H; PDB: 3W0I; PDB: 3W0J; PDB: 3W5P; PDB: 3W5Q; PDB: 3W5R; PDB: 3W5T; PDB: 3WT5; PDB: 3WT6; PDB: 3WT7; PDB: 3WTQ; PDB: 4YNK; PDB: 5AWJ; PDB: 5AWK; PDB: 5B41; PDB: 5B5B; PDB: 5GIC; PDB: 5GID; PDB: 5GIE; PDB: 5XPM; PDB: 5XPN; PDB: 5XPO; PDB: 5XPP; PDB: 5XUQ; PDB: 5XZF; PDB: 5XZH; PDB: 5ZWE; PDB: 5ZWF; PDB: 5ZWH; PDB: 5ZWI; PDB: 6D94; PDB: 6JEZ; PDB: 6K5O; PDB: 6ONJ; PDB: 7C7V; PDB: 7C7W; PDB: 7EMF; PDB: 7ENA; PDB: 7ENC; PDB: 7ENJ	HGNC:9234	MED1_HUMAN	Reviewed	ENSG00000125686	.	.	.	.	.
Mol00496	Protein	Mediator of RNA polymerase II transcription subunit 12 (MED12)	Activator-recruited cofactor 240 kDa component; ARC240; CAG repeat protein 45; Mediator complex subunit 12; OPA-containing protein; Thyroid hormone receptor-associated protein complex 230 kDa component; Trap230; Trinucleotide repeat-containing gene 11 protein; ARC240; CAGH45; HOPA; KIAA0192; TNRC11; TRAP230	MED12	9968	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374080.8, MED12-202, 6925; ENST00000692304.1, MED12-247, 8628; ENST00000690242.1, MED12-234, 6912; ENST00000374102.6, MED12-203, 6901; ENST00000333646.11, MED12-201, 6797; ENST00000687382.1, MED12-217, 6764; ENST00000690145.1, MED12-233, 6739; ENST00000693324.1, MED12-253, 5764; ENST00000691468.1, MED12-245, 5726; ENST00000693391.1, MED12-254, 4699; ENST00000444034.2, MED12-205, 1675; ENST00000690690.1, MED12-237, 1070; ENST00000688231.1, MED12-222, 854; ENST00000686548.1, MED12-215, 6852; ENST00000688663.1, MED12-225, 6470; ENST00000691113.1, MED12-241, 5245; ENST00000689008.1, MED12-230, 3867; ENST00000692864.1, MED12-248, 3277; ENST00000489199.2, MED12-209, 1201; ENST00000688774.1, MED12-227, 1186; ENST00000690807.1, MED12-238, 1184; ENST00000429213.3, MED12-204, 707; ENST00000691283.1, MED12-242, 667; ENST00000685655.1, MED12-212, 568; ENST00000690878.1, MED12-240, 439; ENST00000685789.1, MED12-213, 388; ENST00000688622.1, MED12-224, 579; ENST00000685082.1, MED12-210, 301; ENST00000690828.1, MED12-239, 6245; ENST00000691426.1, MED12-244, 6035; ENST00000689768.1, MED12-232, 5891; ENST00000688079.1, MED12-221, 4676; ENST00000690250.1, MED12-235, 4336; ENST00000692893.1, MED12-249, 4057; ENST00000687701.1, MED12-219, 3499; ENST00000687161.1, MED12-216, 3481; ENST00000691909.1, MED12-246, 3460; ENST00000685182.1, MED12-211, 3446; ENST00000686169.1, MED12-214, 3148; ENST00000692964.1, MED12-250, 3020; ENST00000688881.1, MED12-228, 2911; ENST00000690523.1, MED12-236, 2850; ENST00000691385.1, MED12-243, 2621; ENST00000688993.1, MED12-229, 2590; ENST00000688718.1, MED12-226, 2346; ENST00000688508.1, MED12-223, 2263; ENST00000462984.2, MED12-207, 1541; ENST00000687973.1, MED12-220, 1423; ENST00000693050.1, MED12-251, 1381; ENST00000693182.1, MED12-252, 1172; ENST00000689489.1, MED12-231, 1094; ENST00000687542.1, MED12-218, 672; ENST00000471663.5, MED12-208, 439; ENST00000460771.1, MED12-206, 330"	MAAFGILSYEHRPLKRPRLGPPDVYPQDPKQKEDELTALNVKQGFNNQPAVSGDEHGSAKNVSFNPAKISSNFSSIIAEKLRCNTLPDTGRRKPQVNQKDNFWLVTARSQSAINTWFTDLAGTKPLTQLAKKVPIFSKKEEVFGYLAKYTVPVMRAAWLIKMTCAYYAAISETKVKKRHVDPFMEWTQIITKYLWEQLQKMAEYYRPGPAGSGGCGSTIGPLPHDVEVAIRQWDYTEKLAMFMFQDGMLDRHEFLTWVLECFEKIRPGEDELLKLLLPLLLRYSGEFVQSAYLSRRLAYFCTRRLALQLDGVSSHSSHVISAQSTSTLPTTPAPQPPTSSTPSTPFSDLLMCPQHRPLVFGLSCILQTILLCCPSALVWHYSLTDSRIKTGSPLDHLPIAPSNLPMPEGNSAFTQQVRAKLREIEQQIKERGQAVEVRWSFDKCQEATAGFTIGRVLHTLEVLDSHSFERSDFSNSLDSLCNRIFGLGPSKDGHEISSDDDAVVSLLCEWAVSCKRSGRHRAMVVAKLLEKRQAEIEAERCGESEAADEKGSIASGSLSAPSAPIFQDVLLQFLDTQAPMLTDPRSESERVEFFNLVLLFCELIRHDVFSHNMYTCTLISRGDLAFGAPGPRPPSPFDDPADDPEHKEAEGSSSSKLEDPGLSESMDIDPSSSVLFEDMEKPDFSLFSPTMPCEGKGSPSPEKPDVEKEVKPPPKEKIEGTLGVLYDQPRHVQYATHFPIPQEESCSHECNQRLVVLFGVGKQRDDARHAIKKITKDILKVLNRKGTAETDQLAPIVPLNPGDLTFLGGEDGQKRRRNRPEAFPTAEDIFAKFQHLSHYDQHQVTAQVSRNVLEQITSFALGMSYHLPLVQHVQFIFDLMEYSLSISGLIDFAIQLLNELSVVEAELLLKSSDLVGSYTTSLCLCIVAVLRHYHACLILNQDQMAQVFEGLCGVVKHGMNRSDGSSAERCILAYLYDLYTSCSHLKNKFGELFSDFCSKVKNTIYCNVEPSESNMRWAPEFMIDTLENPAAHTFTYTGLGKSLSENPANRYSFVCNALMHVCVGHHDPDRVNDIAILCAELTGYCKSLSAEWLGVLKALCCSSNNGTCGFNDLLCNVDVSDLSFHDSLATFVAILIARQCLLLEDLIRCAAIPSLLNAACSEQDSEPGARLTCRILLHLFKTPQLNPCQSDGNKPTVGIRSSCDRHLLAASQNRIVDGAVFAVLKAVFVLGDAELKGSGFTVTGGTEELPEEEGGGGSGGRRQGGRNISVETASLDVYAKYVLRSICQQEWVGERCLKSLCEDSNDLQDPVLSSAQAQRLMQLICYPHRLLDNEDGENPQRQRIKRILQNLDQWTMRQSSLELQLMIKQTPNNEMNSLLENIAKATIEVFQQSAETGSSSGSTASNMPSSSKTKPVLSSLERSGVWLVAPLIAKLPTSVQGHVLKAAGEELEKGQHLGSSSRKERDRQKQKSMSLLSQQPFLSLVLTCLKGQDEQREGLLTSLYSQVHQIVNNWRDDQYLDDCKPKQLMHEALKLRLNLVGGMFDTVQRSTQQTTEWAMLLLEIIISGTVDMQSNNELFTTVLDMLSVLINGTLAADMSSISQGSMEENKRAYMNLAKKLQKELGERQSDSLEKVRQLLPLPKQTRDVITCEPQGSLIDTKGNKIAGFDSIFKKEGLQVSTKQKISPWDLFEGLKPSAPLSWGWFGTVRVDRRVARGEEQQRLLLYHTHLRPRPRAYYLEPLPLPPEDEEPPAPTLLEPEKKAPEPPKTDKPGAAPPSTEERKKKSTKGKKRSQPATKTEDYGMGPGRSGPYGVTVPPDLLHHPNPGSITHLNYRQGSIGLYTQNQPLPAGGPRVDPYRPVRLPMQKLPTRPTYPGVLPTTMTGVMGLEPSSYKTSVYRQQQPAVPQGQRLRQQLQQSQGMLGQSSVHQMTPSSSYGLQTSQGYTPYVSHVGLQQHTGPAGTMVPPSYSSQPYQSTHPSTNPTLVDPTRHLQQRPSGYVHQQAPTYGHGLTSTQRFSHQTLQQTPMISTMTPMSAQGVQAGVRSTAILPEQQQQQQQQQQQQQQQQQQQQQQQQQQYHIRQQQQQQILRQQQQQQQQQQQQQQQQQQQQQQQQQQHQQQQQQQAAPPQPQPQSQPQFQRQGLQQTQQQQQTAALVRQLQQQLSNTQPQPSTNIFGRY	chrX:71118543-71144103[+]	"Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway."	.	HGNC:11957	MED12_HUMAN	Reviewed	ENSG00000184634	.	.	.	.	.
Mol00497	Protein	Merlin (NF2)	Moesin-ezrin-radixin-like protein; Neurofibromin-2; Schwannomerlin; Schwannomin; SCH	NF2	4771	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000338641.10, NF2-202, 5950; ENST00000672896.1, NF2-214, 5995; ENST00000361452.8, NF2-205, 5884; ENST00000413209.6, NF2-210, 4733; ENST00000403999.7, NF2-209, 2999; ENST00000334961.11, NF2-201, 2020; ENST00000397789.3, NF2-207, 1857; ENST00000353887.8, NF2-203, 1845; ENST00000361676.8, NF2-206, 1716; ENST00000403435.5, NF2-208, 2568; ENST00000361166.9, NF2-204, 1463; ENST00000672461.1, NF2-212, 2935; ENST00000672805.1, NF2-213, 2478; ENST00000673312.1, NF2-215, 2063; ENST00000432151.5, NF2-211, 1000"	MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL	chr22:29603556-29698598[+]	"Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex."	PDB: 1H4R; PDB: 3U8Z; PDB: 4ZRI; PDB: 4ZRJ; PDB: 6CDS; PDB: 7LWH	HGNC:7773	MERL_HUMAN	Reviewed	ENSG00000186575	.	.	.	.	.
Mol00498	Protein	Methylated-DNA--protein-cysteine methyltransferase (MGMT)	6-O-methylguanine-DNA methyltransferase; MGMT; O-6-methylguanine-DNA-alkyltransferase	MGMT	4255	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000651593.1, MGMT-205, 4678; ENST00000306010.8, MGMT-201, 1265; ENST00000462672.1, MGMT-202, 776; ENST00000482653.1, MGMT-204, 589; ENST00000482547.1, MGMT-203, 959"	MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPAAVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLWKLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVCSSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSGSPPAGRN	chr10:129467190-129770983[+]	Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.	PDB: 1EH6; PDB: 1EH7; PDB: 1EH8; PDB: 1QNT; PDB: 1T38; PDB: 1T39; PDB: 1YFH	HGNC:7059	MGMT_HUMAN	Reviewed	ENSG00000170430	.	.	.	.	.
Mol00499	Protein	Microphthalmia-associated transcription factor (MITF)	Class E basic helix-loop-helix protein 32; bHLHe32; BHLHE32	MITF	4286	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000352241.9, MITF-203, 4799; ENST00000642352.1, MITF-216, 4767; ENST00000314589.10, MITF-202, 4670; ENST00000394351.9, MITF-205, 4475; ENST00000472437.5, MITF-212, 1995; ENST00000314557.10, MITF-201, 1798; ENST00000531774.1, MITF-215, 1074; ENST00000394348.2, MITF-204, 1069; ENST00000448226.9, MITF-208, 4675; ENST00000687384.1, MITF-217, 2214; ENST00000693031.1, MITF-219, 2011; ENST00000693549.1, MITF-220, 1893; ENST00000451708.5, MITF-209, 1116; ENST00000433517.5, MITF-207, 589; ENST00000429090.5, MITF-206, 542; ENST00000478490.5, MITF-213, 1642; ENST00000689390.1, MITF-218, 2108; ENST00000461014.1, MITF-210, 752; ENST00000461511.1, MITF-211, 574; ENST00000495741.1, MITF-214, 473"	MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHPGASKPPISSSSMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVPVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRQQVKQYLSTTLANKHANQVLSLPCPNQPGDHVMPPVPGSSAPNSPMAMLTLNSNCEKEGFYKFEEQNRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYGNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQQRAKELENRQKKLEHANRHLLLRIQELEMQARAHGLSLIPSTGLCSPDLVNRIIKQEPVLENCSQDLLQHHADLTCTTTLDLTDGTITFNNNLGTGTEANQAYSVPTKMGSKLEDILMDDTLSPVGVTDPLLSSVSPGASKTSSRRSSMSMEETEHTC	chr3:69739456-69968336[+]	"Transcription factor that regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium."	PDB: 4C7N; PDB: 7D8R; PDB: 7D8S; PDB: 7D8T	HGNC:7105	MITF_HUMAN	Reviewed	ENSG00000187098	.	.	.	.	.
Mol00501	Protein	Mitogen-activated protein kinase 3 (MAPK3)	MAP kinase 3; MAPK 3; ERT2; Extracellular signal-regulated kinase 1; ERK-1; Insulin-stimulated MAP2 kinase; MAP kinase isoform p44; p44-MAPK; Microtubule-associated protein 2 kinase; p44-ERK1; ERK1; PRKM3	MAPK3	5595	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263025.9, MAPK3-201, 1787; ENST00000322266.9, MAPK3-202, 1743; ENST00000395199.7, MAPK3-203, 1074; ENST00000395202.5, MAPK3-205, 1008; ENST00000484663.5, MAPK3-212, 2567; ENST00000395200.5, MAPK3-204, 997; ENST00000478356.5, MAPK3-209, 961; ENST00000481230.1, MAPK3-210, 465; ENST00000466521.5, MAPK3-207, 1878; ENST00000490298.5, MAPK3-214, 1718; ENST00000461737.5, MAPK3-206, 612; ENST00000494643.1, MAPK3-215, 498; ENST00000485579.1, MAPK3-213, 739; ENST00000483869.1, MAPK3-211, 738; ENST00000473431.1, MAPK3-208, 368"	MAAAAAQGGGGGEPRRTEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP	chr16:30114105-30123506[-]	"Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade plays also a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade."	PDB: 2ZOQ; PDB: 4QTB; PDB: 6GES	HGNC:6877	MK03_HUMAN	Reviewed	ENSG00000102882	.	.	.	.	.
Mol00502	Protein	Mitogen-activated protein kinase 7 (MAPK7)	MAP kinase 7; MAPK 7; Big MAP kinase 1; BMK-1; Extracellular signal-regulated kinase 5; ERK-5; BMK1; ERK5; PRKM7	MAPK7	5598	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000395604.8, MAPK7-204, 2902; ENST00000308406.9, MAPK7-202, 3149; ENST00000395602.8, MAPK7-203, 3059; ENST00000299612.11, MAPK7-201, 2715; ENST00000443215.5, MAPK7-205, 850; ENST00000482850.1, MAPK7-206, 640; ENST00000579284.5, MAPK7-216, 615; ENST00000603493.1, MAPK7-218, 582; ENST00000581260.5, MAPK7-217, 773; ENST00000571657.5, MAPK7-210, 699; ENST00000572968.5, MAPK7-213, 556; ENST00000573417.1, MAPK7-214, 418; ENST00000570306.5, MAPK7-209, 4533; ENST00000490660.2, MAPK7-208, 2867; ENST00000572716.1, MAPK7-211, 776; ENST00000573466.5, MAPK7-215, 661; ENST00000486905.1, MAPK7-207, 615; ENST00000572853.1, MAPK7-212, 564"	MAEPLKEEDGEDGSAEPPGPVKAEPAHTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVEMPSPWAPSGDCAMESPPPAPPPCPGPAPDTIDLTLQPPPPVSEPAPPKKDGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGASGGPSTDPLAGLVLSDNDRSLLERWTRMARPAAPALTSVPAPAPAPTPTPTPVQPTSPPPGPVAQPTGPQPQSAGSTSGPVPQPACPPPGPAPHPTGPPGPIPVPAPPQIATSTSLLAAQSLVPPPGLPGSSTPGVLPYFPPGLPPPDAGGAPQSSMSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQDP	chr17:19377721-19383544[+]	"Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression. Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction."	PDB: 2Q8Y; PDB: 4B99; PDB: 4IC7; PDB: 4IC8; PDB: 4ZSG; PDB: 4ZSJ; PDB: 4ZSL; PDB: 5BYY; PDB: 5BYZ; PDB: 5O7I; PDB: 6HKM; PDB: 6HKN	HGNC:6880	MK07_HUMAN	Reviewed	ENSG00000166484	.	.	.	.	.
Mol00503	Protein	DNA mismatch repair protein Mlh1 (MLH1)	MutL protein homolog 1; COCA2	MLH1	4292	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000231790.8, MLH1-201, 2494; ENST00000458205.6, MLH1-216, 2608; ENST00000674019.1, MLH1-235, 2576; ENST00000536378.5, MLH1-221, 2567; ENST00000435176.5, MLH1-206, 2428; ENST00000455445.6, MLH1-212, 2296; ENST00000539477.6, MLH1-222, 2280; ENST00000456676.6, MLH1-213, 2230; ENST00000673673.1, MLH1-224, 2205; ENST00000441265.6, MLH1-207, 1982; ENST00000673715.1, MLH1-227, 1978; ENST00000673899.1, MLH1-231, 1712; ENST00000616768.5, MLH1-223, 1408; ENST00000429117.5, MLH1-204, 562; ENST00000413740.1, MLH1-203, 342; ENST00000450420.5, MLH1-210, 233; ENST00000673947.1, MLH1-232, 2698; ENST00000673972.1, MLH1-233, 2473; ENST00000432299.6, MLH1-205, 2444; ENST00000674111.1, MLH1-237, 2403; ENST00000673897.1, MLH1-230, 2338; ENST00000447829.6, MLH1-209, 2247; ENST00000413212.2, MLH1-202, 2183; ENST00000457004.5, MLH1-214, 668; ENST00000458009.5, MLH1-215, 660; ENST00000454028.5, MLH1-211, 570; ENST00000673990.1, MLH1-234, 1711; ENST00000492474.5, MLH1-220, 589; ENST00000485889.1, MLH1-219, 566; ENST00000466900.5, MLH1-217, 555; ENST00000674107.1, MLH1-236, 2827; ENST00000673889.1, MLH1-229, 1799; ENST00000673713.1, MLH1-226, 1586; ENST00000673741.1, MLH1-228, 1495; ENST00000442249.6, MLH1-208, 1303; ENST00000476172.6, MLH1-218, 1246; ENST00000674125.1, MLH1-238, 1167; ENST00000673686.1, MLH1-225, 1127"	MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC	chr3:36993350-37050846[+]	"Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis."	PDB: 3RBN; PDB: 4P7A; PDB: 5U5P; PDB: 6WBA; PDB: 6WBB; PDB: 6WBC; PDB: 7M60	HGNC:7127	MLH1_HUMAN	Reviewed	ENSG00000076242	.	.	.	.	.
Mol00504	Protein	Microtubule-associated proteins 1A/1B light chain 3A (MAP1LC3A)	Autophagy-related protein LC3 A; Autophagy-related ubiquitin-like modifier LC3 A; MAP1 light chain 3-like protein 1; MAP1A/MAP1B light chain 3 A; MAP1A/MAP1B LC3 A; Microtubule-associated protein 1 light chain 3 alpha	MAP1LC3A	84557	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000360668.8, MAP1LC3A-201, 964; ENST00000374837.7, MAP1LC3A-202, 961; ENST00000397709.1, MAP1LC3A-203, 698; ENST00000476428.1, MAP1LC3A-204, 851"	MPSDRPFKQRRSFADRCKEVQQIRDQHPSKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELVKIIRRRLQLNPTQAFFLLVNQHSMVSVSTPIADIYEQEKDEDGFLYMVYASQETFGF	chr20:34546854-34560345[+]	"Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover."	PDB: 3ECI; PDB: 3WAL; PDB: 3WAN; PDB: 4ZDV; PDB: 5CX3; PDB: 5DPR; PDB: 6TBE	HGNC:6838	MLP3A_HUMAN	Reviewed	ENSG00000101460	.	.	.	.	.
Mol00506	Protein	Matrix metalloproteinase-16 (MMP16)	MMP-16; MMP-X2; Membrane-type matrix metalloproteinase 3; MT-MMP 3; MTMMP3; Membrane-type-3 matrix metalloproteinase; MT3-MMP; MT3MMP; C8orf57; MMPX2	MMP16	4325	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000286614.11, MMP16-201, 11551; ENST00000522726.1, MMP16-203, 551; ENST00000544227.5, MMP16-204, 1512; ENST00000520568.1, MMP16-202, 605"	MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV	chr8:88032011-88328025[-]	"Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells."	PDB: 1RM8	HGNC:7162	MMP16_HUMAN	Reviewed	ENSG00000156103	.	.	.	.	.
Mol00507	Protein	MOB kinase activator 1A (MOB1A)	Mob1 alpha; Mob1A; Mob1 homolog 1B; Mps one binder kinase activator-like 1B; C2orf6; MOB4B; MOBK1B; MOBKL1B	MOB1A	55233	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000396049.5, MOB1A-201, 4896; ENST00000497054.5, MOB1A-206, 784; ENST00000495286.5, MOB1A-205, 741; ENST00000494600.1, MOB1A-204, 493; ENST00000488006.1, MOB1A-203, 482; ENST00000463975.1, MOB1A-202, 1799"	MSFLFSSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRQAVMLPEGEDLNEWIAVNTVDFFNQINMLYGTITEFCTEASCPVMSAGPRYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDSVMQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLGSKDR	chr2:74152528-74178898[-]	"Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38 and STK38L. Acts cooperatively with STK3/MST2 to activate STK38."	PDB: 1PI1; PDB: 4J1V; PDB: 4JIZ; PDB: 5BRK; PDB: 5BRM; PDB: 5TWF; PDB: 5TWG; PDB: 5TWH; PDB: 5XQZ; PDB: 6MCP; PDB: 6MCQ	HGNC:16015	MOB1A_HUMAN	Reviewed	ENSG00000114978	.	.	.	.	.
Mol00509	Protein	MAPK/ERK kinase 1 (MEK1)	MAP kinase kinase 1; MAPKK 1; MKK1; ERK activator kinase 1; MAPK/ERK kinase 1; MEK 1; MEK1; PRKMK1	MAP2K1	5604	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000307102.10, MAP2K1-201, 2547; ENST00000689951.1, MAP2K1-211, 2710; ENST00000685763.1, MAP2K1-206, 2512; ENST00000691937.1, MAP2K1-214, 2445; ENST00000691576.1, MAP2K1-213, 2407; ENST00000685172.1, MAP2K1-205, 2389; ENST00000692683.1, MAP2K1-216, 2350; ENST00000686347.1, MAP2K1-207, 2209; ENST00000693150.1, MAP2K1-217, 2133; ENST00000566326.1, MAP2K1-203, 1432; ENST00000692487.1, MAP2K1-215, 4868; ENST00000691077.1, MAP2K1-212, 4428; ENST00000684779.1, MAP2K1-204, 1887; ENST00000687191.1, MAP2K1-208, 4354; ENST00000688689.1, MAP2K1-210, 1855; ENST00000687481.1, MAP2K1-209, 1526; ENST00000425818.2, MAP2K1-202, 1338"	MPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMAIFELLDYIVNEPPPKLPSGVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV	chr15:66386837-66491656[+]	"Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation, predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements. One target of the MAPK/ERK cascade is peroxisome proliferator-activated receptor gamma (PPARG), a nuclear receptor that promotes differentiation and apoptosis. MAP2K1/MEK1 has been shown to export PPARG from the nucleus. The MAPK/ERK cascade is also involved in the regulation of endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC), as well as in the fragmentation of the Golgi apparatus during mitosis."	PDB: 1S9J; PDB: 2P55; PDB: 3DV3; PDB: 3DY7; PDB: 3E8N; PDB: 3EQB; PDB: 3EQC; PDB: 3EQD; PDB: 3EQF; PDB: 3EQG; PDB: 3EQH; PDB: 3EQI; PDB: 3MBL; PDB: 3ORN; PDB: 3OS3; PDB: 3PP1; PDB: 3SLS; PDB: 3V01; PDB: 3V04; PDB: 3VVH; PDB: 3W8Q; PDB: 3WIG; PDB: 3ZLS; PDB: 3ZLW; PDB: 3ZLX; PDB: 3ZLY; PDB: 3ZM4; PDB: 4AN2; PDB: 4AN3; PDB: 4AN9; PDB: 4ANB; PDB: 4ARK; PDB: 4LMN; PDB: 4MNE; PDB: 4U7Z; PDB: 4U80; PDB: 4U81; PDB: 5BX0; PDB: 5EYM; PDB: 5HZE; PDB: 5YT3; PDB: 6NYB; PDB: 6PP9; PDB: 6Q0J; PDB: 6Q0T; PDB: 6U2G; PDB: 6V2W; PDB: 6X2P; PDB: 6X2S; PDB: 6X2X; PDB: 7B3M; PDB: 7B7R; PDB: 7B94; PDB: 7B9L; PDB: 7M0T; PDB: 7M0U; PDB: 7M0V; PDB: 7M0W; PDB: 7M0X; PDB: 7M0Y; PDB: 7M0Z	HGNC:6840	MP2K1_HUMAN	Reviewed	ENSG00000169032	.	.	.	.	.
Mol00510	Protein	MAPK/ERK kinase 2 (MEK2)	MAP kinase kinase 2; MAPKK 2; ERK activator kinase 2; MAPK/ERK kinase 2; MEK 2; MEK2; MKK2; PRKMK2	MAP2K2	5605	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262948.10, MAP2K2-201, 1727; ENST00000599021.1, MAP2K2-207, 314; ENST00000689792.1, MAP2K2-215, 1384; ENST00000599345.1, MAP2K2-208, 923; ENST00000593364.5, MAP2K2-203, 872; ENST00000595715.1, MAP2K2-204, 861; ENST00000688751.1, MAP2K2-214, 598; ENST00000597263.5, MAP2K2-206, 552; ENST00000602167.5, MAP2K2-211, 431; ENST00000688002.1, MAP2K2-213, 3491; ENST00000600584.5, MAP2K2-209, 2926; ENST00000687128.1, MAP2K2-212, 2270; ENST00000394867.9, MAP2K2-202, 1899; ENST00000601786.5, MAP2K2-210, 1778; ENST00000597008.5, MAP2K2-205, 866"	MLARRKPVLPALTINPTIAEGPSPTSEGASEANLVDLQKKLEELELDEQQKKRLEAFLTQKAKVGELKDDDFERISELGAGNGGVVTKVQHRPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMAPERLQGTHYSVQSDIWSMGLSLVELAVGRYPIPPPDAKELEAIFGRPVVDGEEGEPHSISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEPPPKLPNGVFTPDFQEFVNKCLIKNPAERADLKMLTNHTFIKRSEVEEVDFAGWLCKTLRLNQPGTPTRTAV	chr19:4090321-4124122[-]	Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP kinases. Activates the ERK1 and ERK2 MAP kinases. Activates BRAF in a KSR1 or KSR2-dependent manner; by binding to KSR1 or KSR2 releases the inhibitory intramolecular interaction between KSR1 or KSR2 protein kinase and N-terminal domains which promotes KSR1 or KSR2-BRAF dimerization and BRAF activation.	PDB: 1S9I; PDB: 4H3Q	HGNC:6842	MP2K2_HUMAN	Reviewed	ENSG00000126934	.	.	.	.	.
Mol00511	Protein	MAPK/ERK kinase 6 (MEK6)	MAP kinase kinase 6; MAPKK 6; MAPK/ERK kinase 6; MEK 6; Stress-activated protein kinase kinase 3; SAPK kinase 3; SAPKK-3; SAPKK3; MEK6; MKK6; PRKMK6; SKK3	MAP2K6	5608	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000590474.7, MAP2K6-206, 13405; ENST00000589647.5, MAP2K6-205, 1512; ENST00000613873.4, MAP2K6-209, 1509; ENST00000589295.5, MAP2K6-204, 669; ENST00000588110.5, MAP2K6-203, 632; ENST00000359094.7, MAP2K6-201, 1851; ENST00000591445.1, MAP2K6-207, 3076; ENST00000586641.5, MAP2K6-202, 1542; ENST00000592348.1, MAP2K6-208, 431"	MSQSKGKKRNPGLKIPKEAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIMELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDISMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINALGQVKMCDFGISGYLVDSVAKTIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSAEFVDFTSQCLKKNSKERPTYPELMQHPFFTLHESKGTDVASFVKLILGD	chr17:69414697-69553865[+]	"Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. With MAP3K3/MKK3, catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinases p38 MAPK11, MAPK12, MAPK13 and MAPK14 and plays an important role in the regulation of cellular responses to cytokines and all kinds of stresses. Especially, MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 and MAPK13 induced by environmental stress, whereas MAP2K6/MKK6 is the major MAPK11 activator in response to TNF. MAP2K6/MKK6 also phosphorylates and activates PAK6. The p38 MAP kinase signal transduction pathway leads to direct activation of transcription factors. Nuclear targets of p38 MAP kinase include the transcription factors ATF2 and ELK1. Within the p38 MAPK signal transduction pathway, MAP3K6/MKK6 mediates phosphorylation of STAT4 through MAPK14 activation, and is therefore required for STAT4 activation and STAT4-regulated gene expression in response to IL-12 stimulation. The pathway is also crucial for IL-6-induced SOCS3 expression and down-regulation of IL-6-mediated gene induction; and for IFNG-dependent gene transcription. Has a role in osteoclast differentiation through NF-kappa-B transactivation by TNFSF11, and in endochondral ossification and since SOX9 is another likely downstream target of the p38 MAPK pathway. MAP2K6/MKK6 mediates apoptotic cell death in thymocytes. Acts also as a regulator for melanocytes dendricity, through the modulation of Rho family GTPases."	PDB: 2Y8O; PDB: 3ENM; PDB: 3FME; PDB: 3VN9; PDB: 5ETF	HGNC:6846	MP2K6_HUMAN	Reviewed	ENSG00000108984	.	.	.	.	.
Mol00512	Protein	Microtubule-associated proteins 1A/1B light chain 3 beta 2 (MAP1LC3B2)	Microtubule-associated proteins 1A/1B light chain 3B-like	MAP1LC3B2	643246	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000556529.4, MAP1LC3B2-202, 818; ENST00000547114.3, MAP1LC3B2-201, 732; ENST00000630062.1, MAP1LC3B2-204, 251; ENST00000625301.1, MAP1LC3B2-203, 605"	MPSEKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYESEKDEDGFLYMVCASQETFGMKLSV	chr12:116548105-116576606[+]	"Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria. While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation."	.	HGNC:34390	MP3B2_HUMAN	Reviewed	ENSG00000258102	.	.	.	.	.
Mol00513	Protein	Cation-independent mannose-6-phosphate receptor (IGF2R)	.	IGF2R	3482	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356956.6, IGF2R-201, 14061; ENST00000678224.1, IGF2R-211, 7977; ENST00000475834.2, IGF2R-203, 762; ENST00000677704.1, IGF2R-210, 14231; ENST00000676781.1, IGF2R-208, 14227; ENST00000475584.1, IGF2R-202, 597; ENST00000650503.1, IGF2R-207, 6468; ENST00000569097.2, IGF2R-205, 5609; ENST00000677628.1, IGF2R-209, 2814; ENST00000649737.1, IGF2R-206, 2755; ENST00000487607.2, IGF2R-204, 355"	MGAAAGRSPHLGPAPARRPQRSLLLLQLLLLVAAPGSTQAQAAPFPELCSYTWEAVDTKNNVLYKINICGSVDIVQCGPSSAVCMHDLKTRTYHSVGDSVLRSATRSLLEFNTTVSCDQQGTNHRVQSSIAFLCGKTLGTPEFVTATECVHYFEWRTTAACKKDIFKANKEVPCYVFDEELRKHDLNPLIKLSGAYLVDDSDPDTSLFINVCRDIDTLRDPGSQLRACPPGTAACLVRGHQAFDVGQPRDGLKLVRKDRLVLSYVREEAGKLDFCDGHSPAVTITFVCPSERREGTIPKLTAKSNCRYEIEWITEYACHRDYLESKTCSLSGEQQDVSIDLTPLAQSGGSSYISDGKEYLFYLNVCGETEIQFCNKKQAAVCQVKKSDTSQVKAAGRYHNQTLRYSDGDLTLIYFGGDECSSGFQRMSVINFECNKTAGNDGKGTPVFTGEVDCTYFFTWDTEYACVKEKEDLLCGATDGKKRYDLSALVRHAEPEQNWEAVDGSQTETEKKHFFINICHRVLQEGKARGCPEDAAVCAVDKNGSKNLGKFISSPMKEKGNIQLSYSDGDDCGHGKKIKTNITLVCKPGDLESAPVLRTSGEGGCFYEFEWHTAAACVLSKTEGENCTVFDSQAGFSFDLSPLTKKNGAYKVETKKYDFYINVCGPVSVSPCQPDSGACQVAKSDEKTWNLGLSNAKLSYYDGMIQLNYRGGTPYNNERHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECVVTDPSTLEQYDLSSLAKSEGGLGGNWYAMDNSGEHVTWRKYYINVCRPLNPVPGCNRYASACQMKYEKDQGSFTEVVSISNLGMAKTGPVVEDSGSLLLEYVNGSACTTSDGRQTTYTTRIHLVCSRGRLNSHPIFSLNWECVVSFLWNTEAACPIQTTTDTDQACSIRDPNSGFVFNLNPLNSSQGYNVSGIGKIFMFNVCGTMPVCGTILGKPASGCEAETQTEELKNWKPARPVGIEKSLQLSTEGFITLTYKGPLSAKGTADAFIVRFVCNDDVYSGPLKFLHQDIDSGQGIRNTYFEFETALACVPSPVDCQVTDLAGNEYDLTGLSTVRKPWTAVDTSVDGRKRTFYLSVCNPLPYIPGCQGSAVGSCLVSEGNSWNLGVVQMSPQAAANGSLSIMYVNGDKCGNQRFSTRITFECAQISGSPAFQLQDGCEYVFIWRTVEACPVVRVEGDNCEVKDPRHGNLYDLKPLGLNDTIVSAGEYTYYFRVCGKLSSDVCPTSDKSKVVSSCQEKREPQGFHKVAGLLTQKLTYENGLLKMNFTGGDTCHKVYQRSTAIFFYCDRGTQRPVFLKETSDCSYLFEWRTQYACPPFDLTECSFKDGAGNSFDLSSLSRYSDNWEAITGTGDPEHYLINVCKSLAPQAGTEPCPPEAAACLLGGSKPVNLGRVRDGPQWRDGIIVLKYVDGDLCPDGIRKKSTTIRFTCSESQVNSRPMFISAVEDCEYTFAWPTATACPMKSNEHDDCQVTNPSTGHLFDLSSLSGRAGFTAAYSEKGLVYMSICGENENCPPGVGACFGQTRISVGKANKRLRYVDQVLQLVYKDGSPCPSKSGLSYKSVISFVCRPEARPTNRPMLISLDKQTCTLFFSWHTPLACEQATECSVRNGSSIVDLSPLIHRTGGYEAYDESEDDASDTNPDFYINICQPLNPMHGVPCPAGAAVCKVPIDGPPIDIGRVAGPPILNPIANEIYLNFESSTPCLADKHFNYTSLIAFHCKRGVSMGTPKLLRTSECDFVFEWETPVVCPDEVRMDGCTLTDEQLLYSFNLSSLSTSTFKVTRDSRTYSVGVCTFAVGPEQGGCKDGGVCLLSGTKGASFGRLQSMKLDYRHQDEAVVLSYVNGDRCPPETDDGVPCVFPFIFNGKSYEECIIESRAKLWCSTTADYDRDHEWGFCRHSNSYRTSSIIFKCDEDEDIGRPQVFSEVRGCDVTFEWKTKVVCPPKKLECKFVQKHKTYDLRLLSSLTGSWSLVHNGVSYYINLCQKIYKGPLGCSERASICRRTTTGDVQVLGLVHTQKLGVIGDKVVVTYSKGYPCGGNKTASSVIELTCTKTVGRPAFKRFDIDSCTYYFSWDSRAACAVKPQEVQMVNGTITNPINGKSFSLGDIYFKLFRASGDMRTNGDNYLYEIQLSSITSSRNPACSGANICQVKPNDQHFSRKVGTSDKTKYYLQDGDLDVVFASSSKCGKDKTKSVSSTIFFHCDPLVEDGIPEFSHETADCQYLFSWYTSAVCPLGVGFDSENPGDDGQMHKGLSERSQAVGAVLSLLLVALTCCLLALLLYKKERRETVISKLTTCCRRSSNVSYKYSKVNKEEETDENETEWLMEEIQLPPPRQGKEGQENGHITTKSVKALSSLHGDDQDSEDEVLTIPEVKVHSGRGAGAESSHPVRNAQSNALQEREDDRVGLVRGEKARKGKSSSAQQKTVSSTKLVSFHDDSDEDLLHI	chr6:159969082-160113507[+]	Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation by binding DPP4.	PDB: 1E6F; PDB: 1GP0; PDB: 1GP3; PDB: 1GQB; PDB: 1JPL; PDB: 1JWG; PDB: 1LF8; PDB: 2CNJ; PDB: 2L29; PDB: 2L2A; PDB: 2M68; PDB: 2M6T; PDB: 2V5N; PDB: 2V5O; PDB: 2V5P; PDB: 5IEI; PDB: 6N5X; PDB: 6N5Y; PDB: 6P8I; PDB: 6V02; PDB: 6Z30; PDB: 6Z31; PDB: 6Z32	HGNC:5467	MPRI_HUMAN	Reviewed	ENSG00000197081	.	.	.	.	.
Mol00514	Protein	ATP-binding cassette sub-family C4 (ABCC4)	MRP/cMOAT-related ABC transporter; Multi-specific organic anion transporter B; MOAT-B; Multidrug resistance-associated protein 4; MOATB; MRP4	ABCC4	10257	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000645237.2, ABCC4-214, 5855; ENST00000646439.1, ABCC4-216, 3863; ENST00000629385.1, ABCC4-206, 2903; ENST00000536256.3, ABCC4-205, 2840; ENST00000645532.1, ABCC4-215, 2103; ENST00000643051.1, ABCC4-208, 6171; ENST00000643842.1, ABCC4-211, 5999; ENST00000643556.1, ABCC4-209, 3059; ENST00000642524.1, ABCC4-207, 2256; ENST00000471041.2, ABCC4-202, 747; ENST00000644880.1, ABCC4-213, 562; ENST00000643816.1, ABCC4-210, 3480; ENST00000644471.1, ABCC4-212, 2225; ENST00000484109.1, ABCC4-204, 532; ENST00000474158.2, ABCC4-203, 448; ENST00000467685.2, ABCC4-201, 357"	MLPVYQEVKPNPLQDANLCSRVFFWWLNPLFKIGHKRRLEEDDMYSVLPEDRSQHLGEELQGFWDKEVLRAENDAQKPSLTRAIIKCYWKSYLVLGIFTLIEESAKVIQPIFLGKIINYFENYDPMDSVALNTAYAYATVLTFCTLILAILHHLYFYHVQCAGMRLRVAMCHMIYRKALRLSNMAMGKTTTGQIVNLLSNDVNKFDQVTVFLHFLWAGPLQAIAVTALLWMEIGISCLAGMAVLIILLPLQSCFGKLFSSLRSKTATFTDARIRTMNEVITGIRIIKMYAWEKSFSNLITNLRKKEISKILRSSCLRGMNLASFFSASKIIVFVTFTTYVLLGSVITASRVFVAVTLYGAVRLTVTLFFPSAIERVSEAIVSIRRIQTFLLLDEISQRNRQLPSDGKKMVHVQDFTAFWDKASETPTLQGLSFTVRPGELLAVVGPVGAGKSSLLSAVLGELAPSHGLVSVHGRIAYVSQQPWVFSGTLRSNILFGKKYEKERYEKVIKACALKKDLQLLEDGDLTVIGDRGTTLSGGQKARVNLARAVYQDADIYLLDDPLSAVDAEVSRHLFELCICQILHEKITILVTHQLQYLKAASQILILKDGKMVQKGTYTEFLKSGIDFGSLLKKDNEESEQPPVPGTPTLRNRTFSESSVWSQQSSRPSLKDGALESQDTENVPVTLSEENRSEGKVGFQAYKNYFRAGAHWIVFIFLILLNTAAQVAYVLQDWWLSYWANKQSMLNVTVNGGGNVTEKLDLNWYLGIYSGLTVATVLFGIARSLLVFYVLVNSSQTLHNKMFESILKAPVLFFDRNPIGRILNRFSKDIGHLDDLLPLTFLDFIQTLLQVVGVVSVAVAVIPWIAIPLVPLGIIFIFLRRYFLETSRDVKRLESTTRSPVFSHLSSSLQGLWTIRAYKAEERCQELFDAHQDLHSEAWFLFLTTSRWFAVRLDAICAMFVIIVAFGSLILAKTLDAGQVGLALSYALTLMGMFQWCVRQSAEVENMMISVERVIEYTDLEKEAPWEYQKRPPPAWPHEGVIIFDNVNFMYSPGGPLVLKHLTALIKSQEKVGIVGRTGAGKSSLISALFRLSEPEGKIWIDKILTTEIGLHDLRKKMSIIPQEPVLFTGTMRKNLDPFNEHTDEELWNALQEVQLKETIEDLPGKMDTELAESGSNFSVGQRQLVCLARAILRKNQILIIDEATANVDPRTDELIQKKIREKFAHCTVLTIAHRLNTIIDSDKIMVLDSGRLKEYDEPYVLLQNKESLFYKMVQQLGKAEAAALTETAKQVYFKRNYPHIGHTDHMVTNTSNGQPSTLTIFETAL	chr13:95019835-95301475[-]	"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules. Confers resistance to anticancer agents such as methotrexate."	.	HGNC:55	MRP4_HUMAN	Reviewed	ENSG00000125257	.	.	.	.	.
Mol00515	Protein	ATP-binding cassette sub-family C5 (ABCC5)	Multi-specific organic anion transporter C; MOAT-C; Multidrug resistance-associated protein 5; SMRP; pABC11; MRP5	ABCC5	10057	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000334444.11, ABCC5-202, 5790; ENST00000382494.6, ABCC5-203, 1923; ENST00000265586.10, ABCC5-201, 5712; ENST00000427120.6, ABCC5-205, 4697; ENST00000392579.6, ABCC5-204, 1848; ENST00000446941.2, ABCC5-211, 883; ENST00000437341.5, ABCC5-207, 591; ENST00000437205.5, ABCC5-206, 5852; ENST00000443376.5, ABCC5-209, 2000; ENST00000438979.6, ABCC5-208, 821; ENST00000443497.1, ABCC5-210, 550; ENST00000492216.1, ABCC5-213, 954; ENST00000476402.1, ABCC5-212, 732"	MKDIDIGKEYIIPSPGYRSVRERTSTSGTHRDREDSKFRRTRPLECQDALETAARAEGLSLDASMHSQLRILDEEHPKGKYHHGLSALKPIRTTSKHQHPVDNAGLFSCMTFSWLSSLARVAHKKGELSMEDVWSLSKHESSDVNCRRLERLWQEELNEVGPDAASLRRVVWIFCRTRLILSIVCLMITQLAGFSGPAFMVKHLLEYTQATESNLQYSLLLVLGLLLTEIVRSWSLALTWALNYRTGVRLRGAILTMAFKKILKLKNIKEKSLGELINICSNDGQRMFEAAAVGSLLAGGPVVAILGMIYNVIILGPTGFLGSAVFILFYPAMMFASRLTAYFRRKCVAATDERVQKMNEVLTYIKFIKMYAWVKAFSQSVQKIREEERRILEKAGYFQSITVGVAPIVVVIASVVTFSVHMTLGFDLTAAQAFTVVTVFNSMTFALKVTPFSVKSLSEASVAVDRFKSLFLMEEVHMIKNKPASPHIKIEMKNATLAWDSSHSSIQNSPKLTPKMKKDKRASRGKKEKVRQLQRTEHQAVLAEQKGHLLLDSDERPSPEEEEGKHIHLGHLRLQRTLHSIDLEIQEGKLVGICGSVGSGKTSLISAILGQMTLLEGSIAISGTFAYVAQQAWILNATLRDNILFGKEYDEERYNSVLNSCCLRPDLAILPSSDLTEIGERGANLSGGQRQRISLARALYSDRSIYILDDPLSALDAHVGNHIFNSAIRKHLKSKTVLFVTHQLQYLVDCDEVIFMKEGCITERGTHEELMNLNGDYATIFNNLLLGETPPVEINSKKETSGSQKKSQDKGPKTGSVKKEKAVKPEEGQLVQLEEKGQGSVPWSVYGVYIQAAGGPLAFLVIMALFMLNVGSTAFSTWWLSYWIKQGSGNTTVTRGNETSVSDSMKDNPHMQYYASIYALSMAVMLILKAIRGVVFVKGTLRASSRLHDELFRRILRSPMKFFDTTPTGRILNRFSKDMDEVDVRLPFQAEMFIQNVILVFFCVGMIAGVFPWFLVAVGPLVILFSVLHIVSRVLIRELKRLDNITQSPFLSHITSSIQGLATIHAYNKGQEFLHRYQELLDDNQAPFFLFTCAMRWLAVRLDLISIALITTTGLMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERINHYIKTLSLEAPARIKNKAPSPDWPQEGEVTFENAEMRYRENLPLVLKKVSFTIKPKEKIGIVGRTGSGKSSLGMALFRLVELSGGCIKIDGVRISDIGLADLRSKLSIIPQEPVLFSGTVRSNLDPFNQYTEDQIWDALERTHMKECIAQLPLKLESEVMENGDNFSVGERQLLCIARALLRHCKILILDEATAAMDTETDLLIQETIREAFADCTMLTIAHRLHTVLGSDRIMVLAQGQVVEFDTPSVLLSNDSSRFYAMFAAAENKVAVKG	chr3:183919934-184017939[-]	"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of endogenous metabolites such as cAMP and cGMP, folic acid and N-lactoyl-amino acids (in vitro). Acts also as a general glutamate conjugate and analog transporter that can limit the brain levels of endogenous metabolites, drugs, and toxins. Confers resistance to the antiviral agent PMEA. Able to transport several anticancer drugs including methotrexate, and nucleotide analogs in vitro, however it does with low affinity, thus the exact role of ABCC5 in mediating resistance still needs to be elucidated. Acts as a heme transporter required for the translocation of cytosolic heme to the secretory pathway. May play a role in energy metabolism by regulating the glucagon-like peptide 1 (GLP-1) secretion from enteroendocrine cells."	.	HGNC:56	MRP5_HUMAN	Reviewed	ENSG00000114770	.	.	.	.	.
Mol00516	Protein	ATP-binding cassette sub-family C10 (ABCC10)	Multidrug resistance-associated protein 7; MRP7; SIMRP7	ABCC10	89845	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000372530.9, ABCC10-204, 5043; ENST00000244533.7, ABCC10-201, 5088; ENST00000372515.8, ABCC10-203, 933; ENST00000505344.1, ABCC10-210, 721; ENST00000443426.2, ABCC10-206, 774; ENST00000502549.1, ABCC10-209, 478; ENST00000463024.1, ABCC10-207, 4542; ENST00000437104.3, ABCC10-205, 733; ENST00000372512.2, ABCC10-202, 405; ENST00000469856.1, ABCC10-208, 285"	MERLLAQLCGSSAAWPLPLWEGDTTGHCFTQLVLSALPHALLAVLSACYLGTPRSPDYILPCSPGWRLRLAASFLLSVFPLLDLLPVALPPGAGPGPIGLEVLAGCVAAVAWISHSLALWVLAHSPHGHSRGPLALALVALLPAPALVLTVLWHCQRGTLLPPLLPGPMARLCLLILQLAALLAYALGWAAPGGPREPWAQEPLLPEDQEPEVAEDGESWLSRFSYAWLAPLLARGACGELRQPQDICRLPHRLQPTYLARVFQAHWQEGARLWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTVLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGRLLQEESKKEGAVALHVYQAYWKAVGQGLALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQEAQPSTSPASMGLFSPQLLLFSPGNLYIPVFPLPKAAPNGSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQEPQGQPLQLGTGWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQPHSLFQQLLQSSQQGVPASLGGP	chr6:43427366-43450427[+]	"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Lipophilic anion transporter that mediates ATP-dependent transport of glucuronide conjugates such as estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4). Mediates multidrug resistance (MDR) in cancer cells by preventing the intracellular accumulation of certain antitumor drugs, such as, docetaxel and paclitaxel. Does not transport glycocholic acid, taurocholic acid, MTX, folic acid, cAMP, or cGMP."	.	HGNC:52	MRP7_HUMAN	Reviewed	ENSG00000124574	.	.	.	.	.
Mol00517	Protein	DNA mismatch repair protein Msh2 (MSH2)	hMSH2; MutS protein homolog 2	MSH2	4436	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000233146.7, MSH2-201, 3115; ENST00000543555.6, MSH2-204, 3018; ENST00000645506.1, MSH2-208, 7893; ENST00000406134.5, MSH2-202, 3628; ENST00000644092.1, MSH2-205, 5343; ENST00000646415.1, MSH2-209, 4523; ENST00000645339.1, MSH2-207, 3113; ENST00000644900.1, MSH2-206, 1663; ENST00000467323.1, MSH2-203, 313"	MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLEREQGEKIIQEFLSKVKQMPFTEMSEENITIKLKQLKAEVIAKNNSFVNEIISRIKVTT	chr2:47403067-47663146[+]	"Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containing DNA strand. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis."	PDB: 2O8B; PDB: 2O8C; PDB: 2O8D; PDB: 2O8E; PDB: 2O8F; PDB: 3THW; PDB: 3THX; PDB: 3THY; PDB: 3THZ	HGNC:7325	MSH2_HUMAN	Reviewed	ENSG00000095002	.	.	.	.	.
Mol00518	Protein	DNA mismatch repair protein Msh6 (MSH6)	hMSH6; G/T mismatch-binding protein; GTBP; GTMBP; MutS protein homolog 6; MutS-alpha 160 kDa subunit; p160; GTBP	MSH6	2956	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000234420.11, MSH6-201, 4265; ENST00000614496.4, MSH6-212, 4150; ENST00000538136.1, MSH6-209, 4055; ENST00000540021.6, MSH6-210, 3829; ENST00000652107.1, MSH6-213, 7669; ENST00000673637.1, MSH6-214, 3959; ENST00000455383.5, MSH6-206, 578; ENST00000411819.1, MSH6-202, 548; ENST00000420813.5, MSH6-203, 491; ENST00000445503.5, MSH6-204, 4158; ENST00000456246.1, MSH6-207, 846; ENST00000607272.2, MSH6-211, 2219; ENST00000493177.1, MSH6-208, 813; ENST00000454137.5, MSH6-205, 725; ENST00000673922.1, MSH6-215, 573"	MSRQSTLYSFFPKSPALSDANKASARASREGGRAAAAPGASPSPGGDAAWSEAGPGPRPLARSASPPKAKNLNGGLRRSVAPAAPTSCDFSPGDLVWAKMEGYPWWPCLVYNHPFDGTFIREKGKSVRVHVQFFDDSPTRGWVSKRLLKPYTGSKSKEAQKGGHFYSAKPEILRAMQRADEALNKDKIKRLELAVCDEPSEPEEEEEMEVGTTYVTDKSEEDNEIESEEEVQPKTQGSRRSSRQIKKRRVISDSESDIGGSDVEFKPDTKEEGSSDEISSGVGDSESEGLNSPVKVARKRKRMVTGNGSLKRKSSRKETPSATKQATSISSETKNTLRAFSAPQNSESQAHVSGGGDDSSRPTVWYHETLEWLKEEKRRDEHRRRPDHPDFDASTLYVPEDFLNSCTPGMRKWWQIKSQNFDLVICYKVGKFYELYHMDALIGVSELGLVFMKGNWAHSGFPEIAFGRYSDSLVQKGYKVARVEQTETPEMMEARCRKMAHISKYDRVVRREICRIITKGTQTYSVLEGDPSENYSKYLLSLKEKEEDSSGHTRAYGVCFVDTSLGKFFIGQFSDDRHCSRFRTLVAHYPPVQVLFEKGNLSKETKTILKSSLSCSLQEGLIPGSQFWDASKTLRTLLEEEYFREKLSDGIGVMLPQVLKGMTSESDSIGLTPGEKSELALSALGGCVFYLKKCLIDQELLSMANFEEYIPLDSDTVSTTRSGAIFTKAYQRMVLDAVTLNNLEIFLNGTNGSTEGTLLERVDTCHTPFGKRLLKQWLCAPLCNHYAINDRLDAIEDLMVVPDKISEVVELLKKLPDLERLLSKIHNVGSPLKSQNHPDSRAIMYEETTYSKKKIIDFLSALEGFKVMCKIIGIMEEVADGFKSKILKQVISLQTKNPEGRFPDLTVELNRWDTAFDHEKARKTGLITPKAGFDSDYDQALADIRENEQSLLEYLEKQRNRIGCRTIVYWGIGRNRYQLEIPENFTTRNLPEEYELKSTKKGCKRYWTKTIEKKLANLINAEERRDVSLKDCMRRLFYNFDKNYKDWQSAVECIAVLDVLLCLANYSRGGDGPMCRPVILLPEDTPPFLELKGSRHPCITKTFFGDDFIPNDILIGCEEEEQENGKAYCVLVTGPNMGGKSTLMRQAGLLAVMAQMGCYVPAEVCRLTPIDRVFTRLGASDRIMSGESTFFVELSETASILMHATAHSLVLVDELGRGTATFDGTAIANAVVKELAETIKCRTLFSTHYHSLVEDYSQNVAVRLGHMACMVENECEDPSQETITFLYKFIKGACPKSYGFNAARLANLPEEVIQKGHRKAREFEKMNQSLRLFREVCLASERSTVDAEAVHKLLTLIKEL	chr2:47695530-47810063[+]	"Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction."	PDB: 2GFU; PDB: 2O8B; PDB: 2O8C; PDB: 2O8D; PDB: 2O8E; PDB: 2O8F; PDB: 6OQM	HGNC:7329	MSH6_HUMAN	Reviewed	ENSG00000116062	.	.	.	.	.
Mol00519	Protein	Myb-related protein B (MYBL2)	B-Myb; Myb-like protein 2; BMYB	MYBL2	4605	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000217026.5, MYBL2-201, 2668; ENST00000396863.8, MYBL2-202, 2704"	MSRRTRCEDLDELHYQDTDSDVPEQRDSKCKVKWTHEEDEQLRALVRQFGQQDWKFLASHFPNRTDQQCQYRWLRVLNPDLVKGPWTKEEDQKVIELVKKYGTKQWTLIAKHLKGRLGKQCRERWHNHLNPEVKKSCWTEEEDRIICEAHKVLGNRWAEIAKMLPGRTDNAVKNHWNSTIKRKVDTGGFLSESKDCKPPVYLLLELEDKDGLQSAQPTEGQGSLLTNWPSVPPTIKEEENSEEELAAATTSKEQEPIGTDLDAVRTPEPLEEFPKREDQEGSPPETSLPYKWVVEAANLLIPAVGSSLSEALDLIESDPDAWCDLSKFDLPEEPSAEDSINNSLVQLQASHQQQVLPPRQPSALVPSVTEYRLDGHTISDLSRSSRGELIPISPSTEVGGSGIGTPPSVLKRQRKRRVALSPVTENSTSLSFLDSCNSLTPKSTPVKTLPFSPSQFLNFWNKQDTLELESPSLTSTPVCSQKVVVTTPLHRDKTPLHQKHAAFVTPDQKYSMDNTPHTPTPFKNALEKYGPLKPLPQTPHLEEDLKEVLRSEAGIELIIEDDIRPEKQKRKPGLRRSPIKKVRKSLALDIVDEDVKLMMSTLPKSLSLPTTAPSNSSSLTLSGIKEDNSLLNQGFLQAKPEKAAVAQKPRSHFTTPAPMSSAWKTVACGGTRDQLFMQEKARQLLGRLKPSHTSRTLILS	chr20:43667019-43716495[+]	"Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene."	PDB: 6C48	HGNC:7548	MYBB_HUMAN	Reviewed	ENSG00000101057	.	.	.	.	.
Mol00520	Protein	N-myc proto-oncogene protein (MYCN)	Class E basic helix-loop-helix protein 37; bHLHe37; BHLHE37; NMYC	MYCN	4613	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000281043.4, MYCN-201, 2613; ENST00000638417.1, MYCN-202, 1693"	MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC	chr2:15940550-15947007[+]	Positively regulates the transcription of MYCNOS in neuroblastoma cells.	PDB: 5G1X	HGNC:7559	MYCN_HUMAN	Reviewed	ENSG00000134323	.	.	.	.	.
Mol00521	Protein	Myeloid differentiation primary response protein MyD88 (MYD88)	.	MYD88	4615	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650905.2, MYD88-210, 2667; ENST00000396334.8, MYD88-201, 2850; ENST00000421516.3, MYD88-204, 2691; ENST00000652213.1, MYD88-212, 2655; ENST00000417037.8, MYD88-203, 2638; ENST00000651800.2, MYD88-211, 2483; ENST00000650112.2, MYD88-209, 2352; ENST00000481122.5, MYD88-207, 712; ENST00000463956.1, MYD88-206, 583; ENST00000484513.1, MYD88-208, 3314; ENST00000652590.1, MYD88-213, 2839; ENST00000416282.3, MYD88-202, 2725; ENST00000460295.1, MYD88-205, 1088"	MAAGGPGAGSAAPVSSTSSLPLAALNMRVRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDVLLELGPSIEEDCQKYILKQQQEEAEKPLQVAAVDSSVPRTAELAGITTLDDPLGHMPERFDAFICYCPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDDYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKAMKKEFPSILRFITVCDYTNPCTKSWFWTRLAKALSLP	chr3:38138478-38143022[+]	"Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses such as SARS-CoV-2, SARS-CoV and HIV-1, induces IL1B release through NLRP3 inflammasome activation. MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine."	PDB: 2JS7; PDB: 2Z5V; PDB: 3MOP; PDB: 4DOM; PDB: 4EO7; PDB: 6I3N; PDB: 7BEQ; PDB: 7BER; PDB: 7L6W	HGNC:7562	MYD88_HUMAN	Reviewed	ENSG00000172936	.	.	.	.	.
Mol00522	Protein	Unconventional myosin-X (MYO10)	Unconventional myosin-10; KIAA0799	MYO10	4651	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000513610.6, MYO10-210, 11442; ENST00000274203.13, MYO10-201, 11456; ENST00000515803.5, MYO10-212, 4839; ENST00000505695.5, MYO10-203, 4803; ENST00000513882.5, MYO10-211, 2910; ENST00000507288.1, MYO10-205, 1677; ENST00000502436.5, MYO10-202, 766; ENST00000512061.5, MYO10-209, 807; ENST00000506343.5, MYO10-204, 575; ENST00000510401.6, MYO10-207, 537; ENST00000511972.1, MYO10-208, 583; ENST00000508318.5, MYO10-206, 582"	MDNFFTEGTRVWLRENGQHFPSTVNSCAEGIVVFRTDYGQVFTYKQSTITHQKVTAMHPTNEEGVDDMASLTELHGGSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVERAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMDVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYACCFEWVIKKINSRIKGNEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLRESLEQKLEKRREEEVSHAAMVIRAHVLGFLARKQYRKVLYCVVIIQKNYRAFLLRRRFLHLKKAAIVFQKQLRGQIARRVYRQLLAEKREQEEKKKQEEEEKKKREEEERERERERREAELRAQQEEETRKQQELEALQKSQKEAELTRELEKQKENKQVEEILRLEKEIEDLQRMKEQQELSLTEASLQKLQERRDQELRRLEEEACRAAQEFLESLNFDEIDECVRNIERSLSVGSEFSSELAESACEEKPNFNFSQPYPEEEVDEGFEADDDAFKDSPNPSEHGHSDQRTSGIRTSDDSSEEDPYMNDTVVPTSPSADSTVLLAPSVQDSGSLHNSSSGESTYCMPQNAGDLPSPDGDYDYDQDDYEDGAITSGSSVTFSNSYGSQWSPDYRCSVGTYNSSGAYRFSSEGAQSSFEDSEEDFDSRFDTDDELSYRRDSVYSCVTLPYFHSFLYMKGGLMNSWKRRWCVLKDETFLWFRSKQEALKQGWLHKKGGGSSTLSRRNWKKRWFVLRQSKLMYFENDSEEKLKGTVEVRTAKEIIDNTTKENGIDIIMADRTFHLIAESPEDASQWFSVLSQVHASTDQEIQEMHDEQANPQNAVGTLDVGLIDSVCASDSPDRPNSFVIITANRVLHCNADTPEEMHHWITLLQRSKGDTRVEGQEFIVRGWLHKEVKNSPKMSSLKLKKRWFVLTHNSLDYYKSSEKNALKLGTLVLNSLCSVVPPDEKIFKETGYWNVTVYGRKHCYRLYTKLLNEATRWSSAIQNVTDTKAPIDTPTQQLIQDIKENCLNSDVVEQIYKRNPILRYTHHPLHSPLLPLPYGDINLNLLKDKGYTTLQDEAIKIFNSLQQLESMSDPIPIIQGILQTGHDLRPLRDELYCQLIKQTNKVPHPGSVGNLYSWQILTCLSCTFLPSRGILKYLKFHLKRIREQFPGSEMEKYALFTYESLKKTKCREFVPSRDEIEALIHRQEMTSTVYCHGGGSCKITINSHTTAGEVVEKLIRGLAMEDSRNMFALFEYNGHVDKAIESRTVVADVLAKFEKLAATSEVGDLPWKFYFKLYCFLDTDNVPKDSVEFAFMFEQAHEAVIHGHHPAPEENLQVLAALRLQYLQGDYTLHAAIPPLEEVYSLQRLKARISQSTKTFTPCERLEKRRTSFLEGTLRRSFRTGSVVRQKVEEEQMLDMWIKEEVSSARASIIDKWRKFQGMNQEQAMAKYMALIKEWPGYGSTLFDVECKEGGFPQELWLGVSADAVSVYKRGEGRPLEVFQYEHILSFGAPLANTYKIVVDERELLFETSEVVDVAKLMKAYISMIVKKRYSTTRSASSQGSSR	chr5:16661907-16936288[-]	"Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts."	PDB: 2LW9; PDB: 3AU4; PDB: 3AU5; PDB: 3PZD; PDB: 5I0H; PDB: 5I0I; PDB: 5KG8	HGNC:7593	MYO10_HUMAN	Reviewed	ENSG00000145555	.	.	.	.	.
Mol00523	Protein	Neuron navigator 3 (NAV3)	Pore membrane and/or filament-interacting-like protein 1; Steerin-3; Unc-53 homolog 3; unc53H3; KIAA0938; POMFIL1; STEERIN3	NAV3	89795	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000397909.7, NAV3-201, 10219; ENST00000536525.6, NAV3-202, 7386; ENST00000644176.1, NAV3-216, 7084; ENST00000552895.5, NAV3-215, 6266; ENST00000549464.5, NAV3-207, 2595; ENST00000550788.1, NAV3-211, 2398; ENST00000550042.2, NAV3-208, 2232; ENST00000550503.1, NAV3-209, 698; ENST00000551162.1, NAV3-212, 1226; ENST00000552300.1, NAV3-214, 570; ENST00000549369.5, NAV3-206, 567; ENST00000547725.1, NAV3-203, 468; ENST00000550673.1, NAV3-210, 325; ENST00000551277.1, NAV3-213, 297; ENST00000548948.5, NAV3-205, 593; ENST00000547884.1, NAV3-204, 463"	MPVLGVASKLRQPAVGSKPVHTALPIPNLGTTGSQHCSSRPLELTETESSMLSCQLALKSTCEFGEKKPLQGKAKEKEDSKIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYKQQQHHQQQYYQSLVELQQRVTHASPPSEASQAKTQQDMQSSLAARYATQSNHSGIATSQKKPTRLPGPSRVPAAGSSSKVQGASNLNRRSQSFNSIDKNKPPNYANGNEKDSSKGPQSSSGVNGNVQPPSTAGQPPASAIPSPSASKPWRSKSMNVKHSATSTMLTVKQSSTATSPTPSSDRLKPPVSEGVKTAPSGQKSMLEKFKLVNARTALRPPQPPSSGPSDGGKDDDAFSESGEMEGFNSGLNSGGSTNSSPKVSPKLAPPKAGSKNLSNKKSLLQPKEKEEKNRDKNKVCTEKPVKEEKDQVTEMAPKKTSKIASLIPKGSKTTAAKKESLIPSSSGIPKPGSKVPTVKQTISPGSTASKESEKFRTTKGSPSQSLSKPITMEKASASSCPAPLEGREAGQASPSGSCTMTVAQSSGQSTGNGAVQLPQQQQHSHPNTATVAPFIYRAHSENEGTALPSADSCTSPTKMDLSYSKTAKQCLEEISGEDPETRRMRTVKNIADLRQNLEETMSSLRGTQISHSTLETTFDSTVTTEVNGRTIPNLTSRPTPMTWRLGQACPRLQAGDAPSLGAGYPRSGTSRFIHTDPSRFMYTTPLRRAAVSRLGNMSQIDMSEKASSDLDMSSEVDVGGYMSDGDILGKSLRTDDINSGYMTDGGLNLYTRSLNRIPDTATSRDIIQRGVHDVTVDADSWDDSSSVSSGLSDTLDNISTDDLNTTSSVSSYSNITVPSRKNTQLRTDSEKRSTTDETWDSPEELKKPEEDFDSHGDAGGKWKTVSSGLPEDPEKAGQKASLSVSQTGSWRRGMSAQGGAPSRQKAGTSALKTPGKTDDAKASEKGKAPLKGSSLQRSPSDAGKSSGDEGKKPPSGIGRSTATSSFGFKKPSGVGSSAMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTTLQYRSLPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDSESVSLSGSPKSSPTSASACGAQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGVKSSSVMPSPSTTLARQGSLESPSSGTGSMGSAGGLSGSSSPLFNKPSDLTTDVISLSHSLASSPASVHSFTSGGLVWAANMSSSSAGSKDTPSYQSMTSLHTSSESIDLPLSHHGSLSGLTTGTHEVQSLLMRTGSVRSTLSESMQLDRNTLPKKGLRYTPSSRQANQEEGKEWLRSHSTGGLQDTGNQSPLVSPSAMSSSAAGKYHFSNLVSPTNLSQFNLPGPSMMRSNSIPAQDSSFDLYDDSQLCGSATSLEERPRAISHSGSFRDSMEEVHGSSLSLVSSTSSLYSTAEEKAHSEQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAIQGALNGPDHPPKDLRIRRQHSSESVSSINSATSHSSIGSGNDADSKKKKKKNWVNSRGSELRSSFKQAFGKKKSTKPPSSHSDIEELTDSSLPASPKLPHNAGDCGSASMKPSQSASASPLVWPPKKRQNGPVIYKHRSRICECTEAEAEIILQLKSELREKELKLTDIRLEALSSAHHLDQIREAMNRMQNEIEILKAENDRLKAETGNTAKPTRPPSESSSSTSSSSSRQSLGLSLNNLNITEAVSSDILLDDAGDATGHKDGRSVKIIVSISKGYGRAKDQKSQAYLIGSIGVSGKTKWDVLDGVIRRLFKEYVFRIDTSTSLGLSSDCIASYCIGDLIRSHNLEVPELLPCGYLVGDNNIITVNLKGVEENSLDSFVFDTLIPKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGVELPVVIILDNLHHVGSLSDIFNGFLNCKYNKCPYIIGTMNQGVSSSPNLELHHNFRWVLCANHTEPVKGFLGRYLRRKLIEIEIERNIRNNDLVKIIDWIPKTWHHLNSFLETHSSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYILEAVREGLQMYGKRTPWEDPSKWVLDTYPWSSATLPQESPALLQLRPEDVGYESCTSTKEATTSKHIPQTDTEGDPLMNMLMKLQEAANYSSTQSCDSESTSHHEDILDSSLESTL	chr12:77324641-78213010[+]	May regulate IL2 production by T-cells. May be involved in neuron regeneration.	.	HGNC:15998	NAV3_HUMAN	Reviewed	ENSG00000067798	.	.	.	.	.
Mol00524	Protein	Nuclear receptor coactivator 3 (NCOA3)	NCoA-3; ACTR; Amplified in breast cancer 1 protein; AIB-1; CBP-interacting protein; pCIP; Class E basic helix-loop-helix protein 42; bHLHe42; Receptor-associated coactivator 3; RAC-3; Steroid receptor coactivator protein 3; SRC-3; Thyroid hormone receptor activator molecule 1; TRAM-1; AIB1; BHLHE42; RAC3; TRAM1	NCOA3	8202	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371998.8, NCOA3-202, 7961; ENST00000372004.7, NCOA3-203, 7939; ENST00000371997.3, NCOA3-201, 6750; ENST00000497292.1, NCOA3-205, 824; ENST00000490248.1, NCOA3-204, 226"	MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC	chr20:47501887-47656877[+]	"Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit."	PDB: 1KBH; PDB: 3L3X; PDB: 3L3Z; PDB: 6ES7; PDB: 6SQC	HGNC:7670	NCOA3_HUMAN	Reviewed	ENSG00000124151	.	.	.	.	.
Mol00525	Protein	Bifunctional heparan sulfate N-deacetylase/sulfotransferase 1 (NDST1)	Glucosaminyl N-deacetylase/N-sulfotransferase 1; NDST-1; N-heparan sulfate sulfotransferase 1; N-HSST 1; [Heparan sulfate]-glucosamine N-sulfotransferase 1; HSNST 1; HSST; HSST1	NDST1	3340	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261797.7, NDST1-201, 8011; ENST00000523767.5, NDST1-207, 3449; ENST00000522491.1, NDST1-206, 777; ENST00000518299.1, NDST1-202, 769; ENST00000519157.1, NDST1-204, 576; ENST00000521752.1, NDST1-205, 569; ENST00000518346.1, NDST1-203, 496; ENST00000524161.1, NDST1-208, 437; ENST00000624156.1, NDST1-209, 486"	MPALACLRRLCRHVSPQAVLFLLFIFCLFSVFISAYYLYGWKRGLEPSADAPEPDCGDPPPVAPSRLLPLKPVQAATPSRTDPLVLVFVESLYSQLGQEVVAILESSRFKYRTEIAPGKGDMPTLTDKGRGRFALIIYENILKYVNLDAWNRELLDKYCVAYGVGIIGFFKANENSLLSAQLKGFPLFLHSNLGLKDCSINPKSPLLYVTRPSEVEKGVLPGEDWTVFQSNHSTYEPVLLAKTRSSESIPHLGADAGLHAALHATVVQDLGLHDGIQRVLFGNNLNFWLHKLVFVDAVAFLTGKRLSLPLDRYILVDIDDIFVGKEGTRMKVEDVKALFDTQNELRAHIPNFTFNLGYSGKFFHTGTNAEDAGDDLLLSYVKEFWWFPHMWSHMQPHLFHNQSVLAEQMALNKKFAVEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKQVWSIRVTSTEEYPHLKPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSSELDKIINGGELFLTVLLNPISIFMTHLSNYGNDRLGLYTFKHLVRFLHSWTNLRLQTLPPVQLAQKYFQIFSEEKDPLWQDPCEDKRHKDIWSKEKTCDRFPKLLIIGPQKTGTTALYLFLGMHPDLSSNYPSSETFEEIQFFNGHNYHKGIDWYMEFFPIPSNTTSDFYFEKSANYFDSEVAPRRAAALLPKAKVLTILINPADRAYSWYQHQRAHDDPVALKYTFHEVITAGSDASSKLRALQNRCLVPGWYATHIERWLSAYHANQILVLDGKLLRTEPAKVMDMVQKFLGVTNTIDYHKTLAFDPKKGFWCQLLEGGKTKCLGKSKGRKYPEMDLDSRAFLKDYYRDHNIELSKLLYKMGQTLPTWLREDLQNTR	chr5:150485818-150558211[+]	"Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Compared to other NDST enzymes, its presence is absolutely required. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response. Required for the exosomal release of SDCBP, CD63 and syndecan."	PDB: 1NST	HGNC:7680	NDST1_HUMAN	Reviewed	ENSG00000070614	.	.	.	.	.
Mol00526	Protein	NF-kappa-B essential modulator (IKBKG)	NEMO; FIP-3; IkB kinase-associated protein 1; IKKAP1; Inhibitor of nuclear factor kappa-B kinase subunit gamma; I-kappa-B kinase subunit gamma; IKK-gamma; IKKG; IkB kinase subunit gamma; NF-kappa-B essential modifier; FIP3; NEMO	IKBKG	8517	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000594239.6, IKBKG-206, 1973; ENST00000611071.4, IKBKG-207, 2103; ENST00000618670.4, IKBKG-214, 2069; ENST00000617207.4, IKBKG-212, 1949; ENST00000611176.4, IKBKG-208, 1654; ENST00000422680.6, IKBKG-202, 1583; ENST00000445622.6, IKBKG-204, 1539; ENST00000440286.6, IKBKG-203, 1468; ENST00000692948.1, IKBKG-221, 2030; ENST00000413620.6, IKBKG-201, 1529; ENST00000689906.1, IKBKG-219, 1482; ENST00000619941.4, IKBKG-215, 1463; ENST00000615874.4, IKBKG-211, 1460; ENST00000686378.1, IKBKG-216, 1068; ENST00000615186.5, IKBKG-210, 1001; ENST00000492469.3, IKBKG-205, 720; ENST00000612051.1, IKBKG-209, 1972; ENST00000686774.1, IKBKG-217, 1316; ENST00000617838.1, IKBKG-213, 285; ENST00000693029.1, IKBKG-222, 2975; ENST00000687445.1, IKBKG-218, 2514; ENST00000692816.1, IKBKG-220, 1223"	MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE	chrX:154541199-154565046[+]	"Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much higher affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination."	PDB: 2JVX; PDB: 2JVY; PDB: 3BRT; PDB: 3BRV; PDB: 3CL3; PDB: 3FX0; PDB: 4BWN; PDB: 5AAY; PDB: 5LDE; PDB: 6MI3; PDB: 6MI4; PDB: 6YEK	HGNC:5961	NEMO_HUMAN	Reviewed	ENSG00000269335	.	.	.	.	.
Mol00527	Protein	Neurofibromin (NF1)	Neurofibromatosis-related protein NF-1	NF1	4763	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000358273.9, NF1-202, 12373; ENST00000356175.7, NF1-201, 12362; ENST00000431387.8, NF1-204, 2889; ENST00000696138.1, NF1-236, 12484; ENST00000691014.1, NF1-231, 12415; ENST00000456735.6, NF1-205, 7787; ENST00000693617.1, NF1-235, 7501; ENST00000684826.1, NF1-224, 7344; ENST00000687027.1, NF1-227, 6985; ENST00000689464.1, NF1-230, 5082; ENST00000487476.5, NF1-211, 2265; ENST00000686189.1, NF1-226, 1453; ENST00000490416.2, NF1-214, 1329; ENST00000468273.1, NF1-207, 592; ENST00000579081.5, NF1-219, 8788; ENST00000495910.6, NF1-216, 8223; ENST00000581113.7, NF1-220, 2335; ENST00000471572.6, NF1-208, 2028; ENST00000696139.1, NF1-237, 1639; ENST00000581790.5, NF1-221, 1256; ENST00000466819.5, NF1-206, 1177; ENST00000479614.1, NF1-210, 1114; ENST00000696141.1, NF1-239, 827; ENST00000479536.2, NF1-209, 811; ENST00000422121.2, NF1-203, 619; ENST00000696140.1, NF1-238, 1318; ENST00000498569.5, NF1-217, 620; ENST00000489712.6, NF1-213, 543; ENST00000488981.1, NF1-212, 331; ENST00000577967.1, NF1-218, 5799; ENST00000493220.5, NF1-215, 5691; ENST00000688507.1, NF1-229, 5344; ENST00000687863.1, NF1-228, 5018; ENST00000684998.1, NF1-225, 4634; ENST00000692326.1, NF1-233, 2696; ENST00000691649.1, NF1-232, 2459; ENST00000693210.1, NF1-234, 1873; ENST00000584328.1, NF1-223, 566; ENST00000582892.1, NF1-222, 462"	MAAHRPVEWVQAVVSRFDEQLPIKTGQQNTHTKVSTEHNKECLINISKYKFSLVISGLTTILKNVNNMRIFGEAAEKNLYLSQLIILDTLEKCLAGQPKDTMRLDETMLVKQLLPEICHFLHTCREGNQHAAELRNSASGVLFSLSCNNFNAVFSRISTRLQELTVCSEDNVDVHDIELLQYINVDCAKLKRLLKETAFKFKALKKVAQLAVINSLEKAFWNWVENYPDEFTKLYQIPQTDMAECAEKLFDLVDGFAESTKRKAAVWPLQIILLILCPEIIQDISKDVVDENNMNKKLFLDSLRKALAGHGGSRQLTESAAIACVKLCKASTYINWEDNSVIFLLVQSMVVDLKNLLFNPSKPFSRGSQPADVDLMIDCLVSCFRISPHNNQHFKICLAQNSPSTFHYVLVNSLHRIITNSALDWWPKIDAVYCHSVELRNMFGETLHKAVQGCGAHPAIRMAPSLTFKEKVTSLKFKEKPTDLETRSYKYLLLSMVKLIHADPKLLLCNPRKQGPETQGSTAELITGLVQLVPQSHMPEIAQEAMEALLVLHQLDSIDLWNPDAPVETFWEISSQMLFYICKKLTSHQMLSSTEILKWLREILICRNKFLLKNKQADRSSCHFLLFYGVGCDIPSSGNTSQMSMDHEELLRTPGASLRKGKGNSSMDSAAGCSGTPPICRQAQTKLEVALYMFLWNPDTEAVLVAMSCFRHLCEEADIRCGVDEVSVHNLLPNYNTFMEFASVSNMMSTGRAALQKRVMALLRRIEHPTAGNTEAWEDTHAKWEQATKLILNYPKAKMEDGQAAESLHKTIVKRRMSHVSGGGSIDLSDTDSLQEWINMTGFLCALGGVCLQQRSNSGLATYSPPMGPVSERKGSMISVMSSEGNADTPVSKFMDRLLSLMVCNHEKVGLQIRTNVKDLVGLELSPALYPMLFNKLKNTISKFFDSQGQVLLTDTNTQFVEQTIAIMKNLLDNHTEGSSEHLGQASIETMMLNLVRYVRVLGNMVHAIQIKTKLCQLVEVMMARRDDLSFCQEMKFRNKMVEYLTDWVMGTSNQAADDDVKCLTRDLDQASMEAVVSLLAGLPLQPEEGDGVELMEAKSQLFLKYFTLFMNLLNDCSEVEDESAQTGGRKRGMSRRLASLRHCTVLAMSNLLNANVDSGLMHSIGLGYHKDLQTRATFMEVLTKILQQGTEFDTLAETVLADRFERLVELVTMMGDQGELPIAMALANVVPCSQWDELARVLVTLFDSRHLLYQLLWNMFSKEVELADSMQTLFRGNSLASKIMTFCFKVYGATYLQKLLDPLLRIVITSSDWQHVSFEVDPTRLEPSESLEENQRNLLQMTEKFFHAIISSSSEFPPQLRSVCHCLYQATCHSLLNKATVKEKKENKKSVVSQRFPQNSIGAVGSAMFLRFINPAIVSPYEAGILDKKPPPRIERGLKLMSKILQSIANHVLFTKEEHMRPFNDFVKSNFDAARRFFLDIASDCPTSDAVNHSLSFISDGNVLALHRLLWNNQEKIGQYLSSNRDHKAVGRRPFDKMATLLAYLGPPEHKPVADTHWSSLNLTSSKFEEFMTRHQVHEKEEFKALKTLSIFYQAGTSKAGNPIFYYVARRFKTGQINGDLLIYHVLLTLKPYYAKPYEIVVDLTHTGPSNRFKTDFLSKWFVVFPGFAYDNVSAVYIYNCNSWVREYTKYHERLLTGLKGSKRLVFIDCPGKLAEHIEHEQQKLPAATLALEEDLKVFHNALKLAHKDTKVSIKVGSTAVQVTSAERTKVLGQSVFLNDIYYASEIEEICLVDENQFTLTIANQGTPLTFMHQECEAIVQSIIHIRTRWELSQPDSIPQHTKIRPKDVPGTLLNIALLNLGSSDPSLRSAAYNLLCALTCTFNLKIEGQLLETSGLCIPANNTLFIVSISKTLAANEPHLTLEFLEECISGFSKSSIELKHLCLEYMTPWLSNLVRFCKHNDDAKRQRVTAILDKLITMTINEKQMYPSIQAKIWGSLGQITDLLDVVLDSFIKTSATGGLGSIKAEVMADTAVALASGNVKLVSSKVIGRMCKIIDKTCLSPTPTLEQHLMWDDIAILARYMLMLSFNNSLDVAAHLPYLFHVVTFLVATGPLSLRASTHGLVINIIHSLCTCSQLHFSEETKQVLRLSLTEFSLPKFYLLFGISKVKSAAVIAFRSSYRDRSFSPGSYERETFALTSLETVTEALLEIMEACMRDIPTCKWLDQWTELAQRFAFQYNPSLQPRALVVFGCISKRVSHGQIKQIIRILSKALESCLKGPDTYNSQVLIEATVIALTKLQPLLNKDSPLHKALFWVAVAVLQLDEVNLYSAGTALLEQNLHTLDSLRIFNDKSPEEVFMAIRNPLEWHCKQMDHFVGLNFNSNFNFALVGHLLKGYRHPSPAIVARTVRILHTLLTLVNKHRNCDKFEVNTQSVAYLAALLTVSEEVRSRCSLKHRKSLLLTDISMENVPMDTYPIHHGDPSYRTLKETQPWSSPKGSEGYLAATYPTVGQTSPRARKSMSLDMGQPSQANTKKLLGTRKSFDHLISDTKAPKRQEMESGITTPPKMRRVAETDYEMETQRISSSQQHPHLRKVSVSESNVLLDEEVLTDPKIQALLLTVLATLVKYTTDEFDQRILYEYLAEASVVFPKVFPVVHNLLDSKINTLLSLCQDPNLLNPIHGIVQSVVYHEESPPQYQTSYLQSFGFNGLWRFAGPFSKQTQIPDYAELIVKFLDALIDTYLPGIDEETSEESLLTPTSPYPPALQSQLSITANLNLSNSMTSLATSQHSPGIDKENVELSPTTGHCNSGRTRHGSASQVQKQRSAGSFKRNSIKKIV	chr17:31094927-31382116[+]	"Stimulates the GTPase activity of Ras. NF1 shows greater affinity for Ras GAP, but lower specific activity. May be a regulator of Ras activity."	PDB: 1NF1; PDB: 2D4Q; PDB: 2E2X; PDB: 3P7Z; PDB: 3PEG; PDB: 3PG7; PDB: 6OB2; PDB: 6OB3; PDB: 6V65; PDB: 6V6F	HGNC:7765	NF1_HUMAN	Reviewed	ENSG00000196712	.	.	.	.	.
Mol00528	Protein	Nuclear factor of activated T-cells 3 (NFATC3)	NF-ATc3; NFATc3; NFATx; T-cell transcription factor NFAT4; NF-AT4; NF-AT4c; NFAT4	NFATC3	4775	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000346183.8, NFATC3-202, 6328; ENST00000349223.9, NFATC3-203, 6328; ENST00000329524.8, NFATC3-201, 6144; ENST00000575270.5, NFATC3-222, 3824; ENST00000562926.5, NFATC3-211, 3748; ENST00000570212.5, NFATC3-221, 3181; ENST00000565750.2, NFATC3-215, 529; ENST00000539828.6, NFATC3-206, 2484; ENST00000561714.5, NFATC3-209, 792; ENST00000568466.6, NFATC3-219, 737; ENST00000562171.1, NFATC3-210, 707; ENST00000535127.2, NFATC3-205, 4194; ENST00000563319.5, NFATC3-213, 4122; ENST00000566301.5, NFATC3-216, 3840; ENST00000563288.5, NFATC3-212, 3790; ENST00000563796.5, NFATC3-214, 3753; ENST00000569766.5, NFATC3-220, 3555; ENST00000567152.5, NFATC3-218, 3186; ENST00000566893.5, NFATC3-217, 715; ENST00000553077.5, NFATC3-208, 3870; ENST00000549350.5, NFATC3-207, 3588; ENST00000379165.8, NFATC3-204, 3583"	MTTANCGAHDELDFKLVFGEDGAPAPPPPGSRPADLEPDDCASIYIFNVDPPPSTLTTPLCLPHHGLPSHSSVLSPSFQLQSHKNYEGTCEIPESKYSPLGGPKPFECPSIQITSISPNCHQELDAHEDDLQINDPEREFLERPSRDHLYLPLEPSYRESSLSPSPASSISSRSWFSDASSCESLSHIYDDVDSELNEAAARFTLGSPLTSPGGSPGGCPGEETWHQQYGLGHSLSPRQSPCHSPRSSVTDENWLSPRPASGPSSRPTSPCGKRRHSSAEVCYAGSLSPHHSPVPSPGHSPRGSVTEDTWLNASVHGGSGLGPAVFPFQYCVETDIPLKTRKTSEDQAAILPGKLELCSDDQGSLSPARETSIDDGLGSQYPLKKDSCGDQFLSVPSPFTWSKPKPGHTPIFRTSSLPPLDWPLPAHFGQCELKIEVQPKTHHRAHYETEGSRGAVKASTGGHPVVKLLGYNEKPINLQMFIGTADDRYLRPHAFYQVHRITGKTVATASQEIIIASTKVLEIPLLPENNMSASIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHIPQPSGKVLSLQIASIPVECSQRSAQELPHIEKYSINSCSVNGGHEMVVTGSNFLPESKIIFLEKGQDGRPQWEVEGKIIREKCQGAHIVLEVPPYHNPAVTAAVQVHFYLCNGKRKKSQSQRFTYTPVLMKQEHREEIDLSSVPSLPVPHPAQTQRPSSDSGCSHDSVLSGQRSLICSIPQTYASMVTSSHLPQLQCRDESVSKEQHMIPSPIVHQPFQVTPTPPVGSSYQPMQTNVVYNGPTCLPINAASSQEFDSVLFQQDATLSGLVNLGCQPLSSIPFHSSNSGSTGHLLAHTPHSVHTLPHLQSMGYHCSNTGQRSLSSPVADQITGQPSSQLQPITYGPSHSGSATTASPAASHPLASSPLSGPPSPQLQPMPYQSPSSGTASSPSPATRMHSGQHSTQAQSTGQGGLSAPSSLICHSLCDPASFPPDGATVSIKPEPEDREPNFATIGLQDITLDDVNEIIGRDMSQISVSQGAGVSRQAPLPSPESLDLGRSDGL	chr16:68084751-68229259[+]	"Acts as a regulator of transcriptional activation. Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2. Along with NFATC4, involved in embryonic heart development."	PDB: 2XRW; PDB: 2XS0	HGNC:7777	NFAC3_HUMAN	Reviewed	ENSG00000072736	.	.	.	.	.
Mol00529	Protein	Nuclear transcription factor Y subunit beta (NFYB)	CAAT box DNA-binding protein subunit B; Nuclear transcription factor Y subunit B; NF-YB; HAP3	NFYB	4801	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000240055.8, NFYB-201, 3424; ENST00000551727.5, NFYB-205, 1727; ENST00000551446.6, NFYB-204, 3508; ENST00000550881.1, NFYB-203, 893; ENST00000550189.1, NFYB-202, 586"	MTMDGDSSTTDASQLGISADYIGGSHYVIQPHDDTEDSMNDHEDTNGSKESFREQDIYLPIANVARIMKNAIPQTGKIAKDAKECVQECVSEFISFITSEASERCHQEKRKTINGEDILFAMSTLGFDSYVEPLKLYLQKFREAMKGEKGIGGAVTATDGLSEELTEEAFTNQLPAGLITTDGQQQNVMVYTTSYQQISGVQQIQFS	chr12:104117086-104138241[-]	"Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors."	PDB: 1N1J; PDB: 4AWL; PDB: 4CSR; PDB: 6QMP; PDB: 6QMQ; PDB: 6QMS; PDB: 7AH8	HGNC:7805	NFYB_HUMAN	Reviewed	ENSG00000120837	.	.	.	.	.
Mol00530	Protein	Protein naked cuticle homolog 2 (NKD2)	Naked-2; hNkd2	NKD2	85409	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000296849.10, NKD2-202, 2182; ENST00000274150.4, NKD2-201, 1940; ENST00000513296.2, NKD2-203, 1060; ENST00000523688.1, NKD2-205, 872; ENST00000519933.5, NKD2-204, 491"	MGKLQSKHAAAARKRRESPEGDSFVASAYASGRKGAEEAERRARDKQELPNGDPKEGPFREDQCPLQVALPAEKAEGREHPGQLLSADDGERAANREGPRGPGGQRLNIDALQCDVSVEEDDRQEWTFTLYDFDNCGKVTREDMSSLMHTIYEVVDASVNHSSGSSKTLRVKLTVSPEPSSKRKEGPPAGQDREPTRCRMEGELAEEPRVADRRLSAHVRRPSTDPQPCSERGPYCVDENTERRNHYLDLAGIENYTSRFGPGSPPVQAKQEPQGRASHLQARSRSQEPDTHAVHHRRSQVLVEHVVPASEPAARALDTQPRPKGPEKQFLKSPKGSGKPPGVPASSKSGKAFSYYLPAVLPPQAPQDGHHLPQPPPPPYGHKRYRQKGREGHSPLKAPHAQPATVEHEVVRDLPPTPAGEGYAVPVIQRHEHHHHHEHHHHHHHHHFHPS	chr5:1008802-1038943[+]	Cell autonomous antagonist of the canonical Wnt signaling pathway. May activate a second Wnt signaling pathway that controls planar cell polarity (By similarity). Required for processing of TGFA and for targeting of TGFA to the basolateral membrane of polarized epithelial cells.	.	HGNC:17046	NKD2_HUMAN	Reviewed	ENSG00000145506	.	.	.	.	.
Mol00531	Protein	Serine/threonine-protein kinase NLK (NLK)	Nemo-like kinase; Protein LAK1; LAK1	NLK	51701	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000407008.8, NLK-201, 3526; ENST00000582037.2, NLK-203, 1503; ENST00000496808.1, NLK-202, 1702; ENST00000583517.1, NLK-204, 695; ENST00000584188.1, NLK-205, 451; ENST00000584878.1, NLK-206, 777"	MSLCGARANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSNAIDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPSLEAMRTACEGAKAHILRGPHKQPSLPVLYTLSSQATHEAVHLLCRMLVFDPSKRISAKDALAHPYLDEGRLRYHTCMCKCCFSTSTGRVYTSDFEPVTNPKFDDTFEKNLSSVRQVKEIIHQFILEQQKGNRVPLCINPQSAAFKSFISSTVAQPSEMPPSPLVWE	chr17:28041737-28196381[+]	"Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination. Positive effector of the non-canonical Wnt signaling pathway, acting downstream of WNT5A, MAP3K7/TAK1 and HIPK2. Negative regulator of the canonical Wnt/beta-catenin signaling pathway. Binds to and phosphorylates TCF7L2/TCF4 and LEF1, promoting the dissociation of the TCF7L2/LEF1/beta-catenin complex from DNA, as well as the ubiquitination and subsequent proteolysis of LEF1. Together these effects inhibit the transcriptional activation of canonical Wnt/beta-catenin target genes. Negative regulator of the Notch signaling pathway. Binds to and phosphorylates NOTCH1, thereby preventing the formation of a transcriptionally active ternary complex of NOTCH1, RBPJ/RBPSUH and MAML1. Negative regulator of the MYB family of transcription factors. Phosphorylation of MYB leads to its subsequent proteolysis while phosphorylation of MYBL1 and MYBL2 inhibits their interaction with the coactivator CREBBP. Other transcription factors may also be inhibited by direct phosphorylation of CREBBP itself. Acts downstream of IL6 and MAP3K7/TAK1 to phosphorylate STAT3, which is in turn required for activation of NLK by MAP3K7/TAK1. Upon IL1B stimulus, cooperates with ATF5 to activate the transactivation activity of C/EBP subfamily members. Phosphorylates ATF5 but also stabilizes ATF5 protein levels in a kinase-independent manner."	.	HGNC:29858	NLK_HUMAN	Reviewed	ENSG00000087095	.	.	.	.	.
Mol00532	Protein	Noggin (NOG)	.	NOG	9241	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000332822.6, NOG-201, 1913"	MERCPSLGVTLYALVVVLGLRATPAGGQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPPEDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGGQRCGWIPIQYPIISECKCSC	chr17:56593699-56595611[+]	"Inhibitor of bone morphogenetic proteins (BMP) signaling which is required for growth and patterning of the neural tube and somite. Essential for cartilage morphogenesis and joint formation. Inhibits chondrocyte differentiation through its interaction with GDF5 and, probably, GDF6."	PDB: 1M4U	HGNC:7866	NOGG_HUMAN	Reviewed	ENSG00000183691	.	.	.	.	.
Mol00533	Protein	Neurogenic locus notch homolog protein 2 (NOTCH2)	Notch 2; hN2; N2ECD; N2ICD	NOTCH2	4853	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256646.7, NOTCH2-201, 11425; ENST00000652302.1, NOTCH2-210, 1847; ENST00000652264.1, NOTCH2-209, 593; ENST00000652737.1, NOTCH2-211, 367; ENST00000640021.1, NOTCH2-206, 2058; ENST00000651371.1, NOTCH2-208, 492; ENST00000650638.1, NOTCH2-207, 2917; ENST00000493703.1, NOTCH2-205, 553; ENST00000478864.1, NOTCH2-202, 520; ENST00000489731.1, NOTCH2-204, 414; ENST00000479412.2, NOTCH2-203, 3221"	MPALRPALLWALLALWLCCAAPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCPQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPGFEGSTCERNIDDCPNHRCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCANRNGGYGCVCVNGWSGDDCSENIDDCAFASCTPGSTCIDRVASFSCMCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEINECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGVLCEENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGVNCEINFDDCASNPCIHGICMDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINGVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGINCEVDKNECLSNPCQNGGTCDNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDISGYTCHCVLPYTGKNCQTVLAPCSPNPCENAAVCKESPNFESYTCLCAPGWQGQRCTIDIDECISKPCMNHGLCHNTQGSYMCECPPGFSGMDCEEDIDDCLANPCQNGGSCMDGVNTFSCLCLPGFTGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCKCQAGFDGVHCENNINECTESSCFNGGTCVDGINSFSCLCPVGFTGSFCLHEINECSSHPCLNEGTCVDGLGTYRCSCPLGYTGKNCQTLVNLCSRSPCKNKGTCVQKKAESQCLCPSGWAGAYCDVPNVSCDIAASRRGVLVEHLCQHSGVCINAGNTHYCQCPLGYTGSYCEEQLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDDCARGPHCLNGGQCMDRIGGYSCRCLPGFAGERCEGDINECLSNPCSSEGSLDCIQLTNDYLCVCRSAFTGRHCETFVDVCPQMPCLNGGTCAVASNMPDGFICRCPPGFSGARCQSSCGQVKCRKGEQCVHTASGPRCFCPSPRDCESGCASSPCQHGGSCHPQRQPPYYSCQCAPPFSGSRCELYTAPPSTPPATCLSQYCADKARDGVCDEACNSHACQWDGGDCSLTMENPWANCSSPLPCWDYINNQCDELCNTVECLFDNFECQGNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCAADQPENLAEGTLVIVVLMPPEQLLQDARSFLRALGTLLHTNLRIKRDSQGELMVYPYYGEKSAAMKKQRMTRRSLPGEQEQEVAGSKVFLEIDNRQCVQDSDHCFKNTDAAAALLASHAIQGTLSYPLVSVVSESLTPERTQLLYLLAVAVVIILFIILLGVIMAKRKRKHGSLWLPEGFTLRRDASNHKRREPVGQDAVGLKNLSVQVSEANLIGTGTSEHWVDDEGPQPKKVKAEDEALLSEEDDPIDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVICGPNRSFLSLKHTPMGKKSRRPSAKSTMPTSLPNLAKEAKDAKGSRRKKSLSEKVQLSESSVTLSPVDSLESPHTYVSDTTSSPMITSPGILQASPNPMLATAAPPAPVHAQHALSFSNLHEMQPLAHGASTVLPSVSQLLSHHHIVSPGSGSAGSLSRLHPVPVPADWMNRMEVNETQYNEMFGMVLAPAEGTHPGIAPQSRPPEGKHITTPREPLPPIVTFQLIPKGSIAQPAGAPQPQSTCPPAVAGPLPTMYQIPEMARLPSVAFPTAMMPQQDGQVAQTILPAYHPFPASVGKYPTPPSQHSYASSNAAERTPSHSGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGAGGGQRGPGTHMSEPPHNNMQVYA	chr1:119911553-120100779[-]	"Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Positively regulates self-renewal of liver cancer cells."	PDB: 2OO4; PDB: 5MWB	HGNC:7882	NOTC2_HUMAN	Reviewed	ENSG00000134250	.	.	.	.	.
Mol00534	Protein	Neurogenic locus notch homolog protein 3 (NOTCH3)	Notch 3	NOTCH3	4854	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263388.7, NOTCH3-201, 8680; ENST00000601011.1, NOTCH3-206, 3858; ENST00000597756.1, NOTCH3-204, 559; ENST00000595514.1, NOTCH3-203, 564; ENST00000600841.1, NOTCH3-205, 748; ENST00000595045.1, NOTCH3-202, 558"	MGPGARGRRRRRRPMSPPPPPPPVRALPLLLLLAGPGAAAPPCLDGSPCANGGRCTQLPSREAACLCPPGWVGERCQLEDPCHSGPCAGRGVCQSSVVAGTARFSCRCPRGFRGPDCSLPDPCLSSPCAHGARCSVGPDGRFLCSCPPGYQGRSCRSDVDECRVGEPCRHGGTCLNTPGSFRCQCPAGYTGPLCENPAVPCAPSPCRNGGTCRQSGDLTYDCACLPGFEGQNCEVNVDDCPGHRCLNGGTCVDGVNTYNCQCPPEWTGQFCTEDVDECQLQPNACHNGGTCFNTLGGHSCVCVNGWTGESCSQNIDDCATAVCFHGATCHDRVASFYCACPMGKTGLLCHLDDACVSNPCHEDAICDTNPVNGRAICTCPPGFTGGACDQDVDECSIGANPCEHLGRCVNTQGSFLCQCGRGYTGPRCETDVNECLSGPCRNQATCLDRIGQFTCICMAGFTGTYCEVDIDECQSSPCVNGGVCKDRVNGFSCTCPSGFSGSTCQLDVDECASTPCRNGAKCVDQPDGYECRCAEGFEGTLCDRNVDDCSPDPCHHGRCVDGIASFSCACAPGYTGTRCESQVDECRSQPCRHGGKCLDLVDKYLCRCPSGTTGVNCEVNIDDCASNPCTFGVCRDGINRYDCVCQPGFTGPLCNVEINECASSPCGEGGSCVDGENGFRCLCPPGSLPPLCLPPSHPCAHEPCSHGICYDAPGGFRCVCEPGWSGPRCSQSLARDACESQPCRAGGTCSSDGMGFHCTCPPGVQGRQCELLSPCTPNPCEHGGRCESAPGQLPVCSCPQGWQGPRCQQDVDECAGPAPCGPHGICTNLAGSFSCTCHGGYTGPSCDQDINDCDPNPCLNGGSCQDGVGSFSCSCLPGFAGPRCARDVDECLSNPCGPGTCTDHVASFTCTCPPGYGGFHCEQDLPDCSPSSCFNGGTCVDGVNSFSCLCRPGYTGAHCQHEADPCLSRPCLHGGVCSAAHPGFRCTCLESFTGPQCQTLVDWCSRQPCQNGGRCVQTGAYCLCPPGWSGRLCDIRSLPCREAAAQIGVRLEQLCQAGGQCVDEDSSHYCVCPEGRTGSHCEQEVDPCLAQPCQHGGTCRGYMGGYMCECLPGYNGDNCEDDVDECASQPCQHGGSCIDLVARYLCSCPPGTLGVLCEINEDDCGPGPPLDSGPRCLHNGTCVDLVGGFRCTCPPGYTGLRCEADINECRSGACHAAHTRDCLQDPGGGFRCLCHAGFSGPRCQTVLSPCESQPCQHGGQCRPSPGPGGGLTFTCHCAQPFWGPRCERVARSCRELQCPVGVPCQQTPRGPRCACPPGLSGPSCRSFPGSPPGASNASCAAAPCLHGGSCRPAPLAPFFRCACAQGWTGPRCEAPAAAPEVSEEPRCPRAACQAKRGDQRCDRECNSPGCGWDGGDCSLSVGDPWRQCEALQCWRLFNNSRCDPACSSPACLYDNFDCHAGGRERTCNPVYEKYCADHFADGRCDQGCNTEECGWDGLDCASEVPALLARGVLVLTVLLPPEELLRSSADFLQRLSAILRTSLRFRLDAHGQAMVFPYHRPSPGSEPRARRELAPEVIGSVVMLEIDNRLCLQSPENDHCFPDAQSAADYLGALSAVERLDFPYPLRDVRGEPLEPPEPSVPLLPLLVAGAVLLLVILVLGVMVARRKREHSTLWFPEGFSLHKDVASGHKGRREPVGQDALGMKNMAKGESLMGEVATDWMDTECPEAKRLKVEEPGMGAEEAVDCRQWTQHHLVAADIRVAPAMALTPPQGDADADGMDVNVRGPDGFTPLMLASFCGGALEPMPTEEDEADDTSASIISDLICQGAQLGARTDRTGETALHLAARYARADAAKRLLDAGADTNAQDHSGRTPLHTAVTADAQGVFQILIRNRSTDLDARMADGSTALILAARLAVEGMVEELIASHADVNAVDELGKSALHWAAAVNNVEATLALLKNGANKDMQDSKEETPLFLAAREGSYEAAKLLLDHFANREITDHLDRLPRDVAQERLHQDIVRLLDQPSGPRSPPGPHGLGPLLCPPGAFLPGLKAAQSGSKKSRRPPGKAGLGPQGPRGRGKKLTLACPGPLADSSVTLSPVDSLDSPRPFGGPPASPGGFPLEGPYAAATATAVSLAQLGGPGRAGLGRQPPGGCVLSLGLLNPVAVPLDWARLPPPAPPGPSFLLPLAPGPQLLNPGTPVSPQERPPPYLAVPGHGEEYPAAGAHSSPPKARFLRVPSEHPYLTPSPESPEHWASPSPPSLSDWSESTPSPATATGAMATTTGALPAQPLPLSVPSSLAQAQTQLGPQPEVTPKRQVLA	chr19:15159038-15200995[-]	"Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs."	PDB: 4ZLP; PDB: 5CZV; PDB: 5CZX; PDB: 6WQU; PDB: 6XSW	HGNC:7883	NOTC3_HUMAN	Reviewed	ENSG00000074181	.	.	.	.	.
Mol00535	Protein	Solute carrier family 34 member 2 (SLC34A2)	Sodium-phosphate transport protein 2B; Na(+)-dependent phosphate cotransporter 2B; NaPi3b; Sodium/phosphate cotransporter 2B; Na(+)/Pi cotransporter 2B; NaPi-2b; Solute carrier family 34 member 2	SLC34A2	10568	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000382051.8, SLC34A2-201, 4115; ENST00000645788.1, SLC34A2-207, 2439; ENST00000503434.5, SLC34A2-202, 2174; ENST00000504570.5, SLC34A2-203, 2162; ENST00000507530.1, SLC34A2-204, 582; ENST00000513204.5, SLC34A2-206, 549; ENST00000510033.2, SLC34A2-205, 700"	MAPWPELGDAQPNPDKYLEGAAGQQPTAPDKSKETNKTDNTEAPVTKIELLPSYSTATLIDEPTEVDDPWNLPTLQDSGIKWSERDTKGKILCFFQGIGRLILLLGFLYFFVCSLDILSSAFQLVGGKMAGQFFSNSSIMSNPLLGLVIGVLVTVLVQSSSTSTSIVVSMVSSSLLTVRAAIPIIMGANIGTSITNTIVALMQVGDRSEFRRAFAGATVHDFFNWLSVLVLLPVEVATHYLEIITQLIVESFHFKNGEDAPDLLKVITKPFTKLIVQLDKKVISQIAMNDEKAKNKSLVKIWCKTFTNKTQINVTVPSTANCTSPSLCWTDGIQNWTMKNVTYKENIAKCQHIFVNFHLPDLAVGTILLILSLLVLCGCLIMIVKILGSVLKGQVATVIKKTINTDFPFPFAWLTGYLAILVGAGMTFIVQSSSVFTSALTPLIGIGVITIERAYPLTLGSNIGTTTTAILAALASPGNALRSSLQIALCHFFFNISGILLWYPIPFTRLPIRMAKGLGNISAKYRWFAVFYLIIFFFLIPLTVFGLSLAGWRVLVGVGVPVVFIIILVLCLRLLQSRCPRVLPKKLQNWNFLPLWMRSLKPWDAVVSKFTGCFQMRCCCCCRVCCRACCLLCDCPKCCRCSKCCEDLEEAQEGQDVPVKAPETFDNITISREAQGEVPASDSKTECTAL	chr4:25648011-25678748[+]	May be involved in actively transporting phosphate into cells via Na(+) cotransport. It may be the main phosphate transport protein in the intestinal brush border membrane. May have a role in the synthesis of surfactant in lungs' alveoli.	.	HGNC:11020	NPT2B_HUMAN	Reviewed	ENSG00000157765	.	.	.	.	.
Mol00536	Protein	Quinone reductase 1 (NQO1)	Azoreductase; DT-diaphorase; DTD; Menadione reductase; NAD(P)H:quinone oxidoreductase 1; Phylloquinone reductase; Quinone reductase 1; QR1; DIA4; NMOR1	NQO1	1728	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000320623.10, NQO1-201, 2521; ENST00000379047.7, NQO1-203, 2527; ENST00000379046.6, NQO1-202, 1105; ENST00000439109.6, NQO1-204, 924; ENST00000564043.1, NQO1-206, 892; ENST00000561500.5, NQO1-205, 891; ENST00000569118.1, NQO1-207, 519"	MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK	chr16:69706996-69726668[-]	The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.	PDB: 1D4A; PDB: 1DXO; PDB: 1GG5; PDB: 1H66; PDB: 1H69; PDB: 1KBO; PDB: 1KBQ; PDB: 1QBG; PDB: 2F1O; PDB: 3JSX; PDB: 4CET; PDB: 4CF6; PDB: 5A4K; PDB: 5EA2; PDB: 5EAI; PDB: 5FUQ; PDB: 6FY4; PDB: 6LLC	HGNC:2874	NQO1_HUMAN	Reviewed	ENSG00000181019	.	.	.	.	.
Mol00537	Protein	Long transient receptor potential 2 (TRPM2)	Alpha-1-fetoprotein transcription factor; B1-binding factor; hB1F; CYP7A promoter-binding factor; Hepatocytic transcription factor; Liver receptor homolog 1; LRH-1; B1F; CPF; FTF	NR5A2	2494	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367362.8, NR5A2-203, 4969; ENST00000544748.5, NR5A2-206, 4775; ENST00000236914.7, NR5A2-201, 3115; ENST00000367357.3, NR5A2-202, 1793; ENST00000447034.1, NR5A2-204, 213; ENST00000474307.1, NR5A2-205, 1713"	MSSNSDTGDLQESLKHGLTPIGAGLPDRHGSPIPARGRLVMLPKVETEALGLARSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKRYTCIENQNCQIDKTQRKRCPYCRFQKCLSVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTISSAIQNIHSASKGLPLNHAALPPTDYDRSPFVTSPISMTMPPHGSLQGYQTYGHFPSRAIKSEYPDPYTSSPESIMGYSYMDSYQTSSPASIPHLILELLKCEPDEPQVQAKIMAYLQQEQANRSKHEKLSTFGLMCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLILDHIYRQVVHGKEGSIFLVTGQQVDYSIIASQAGATLNNLMSHAQELVAKLRSLQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQVNAALLDYTMCNYPQQTEKFGQLLLRLPEIRAISMQAEEYLYYKHLNGDVPYNNLLIEMLHAKRA	chr1:200027614-200177420[+]	"Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid metabolism. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex. Binds to the sequence element 5'-AACGACCGACCTTGAG-3' of the enhancer II of hepatitis B virus genes, a critical cis-element of their expression and regulation. May be responsible for the liver-specific activity of enhancer II, probably in combination with other hepatocyte transcription factors. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development. Activates the transcription of CYP2C38."	PDB: 1YOK; PDB: 1YUC; PDB: 1ZDU; PDB: 2A66; PDB: 3PLZ; PDB: 3TX7; PDB: 4DOR; PDB: 4DOS; PDB: 4IS8; PDB: 4ONI; PDB: 4PLD; PDB: 4PLE; PDB: 4RWV; PDB: 5L0M; PDB: 5L11; PDB: 5SYZ; PDB: 5UNJ; PDB: 6OQX; PDB: 6OQY; PDB: 6OR1; PDB: 6VC2; PDB: 6VIF	HGNC:7984	NR5A2_HUMAN	Reviewed	ENSG00000116833	.	.	.	.	.
Mol00538	Protein	Histone-lysine N-methyltransferase NSD2 (NSD2)	Multiple myeloma SET domain-containing protein; MMSET; Nuclear SET domain-containing protein 2; Protein trithorax-5; Wolf-Hirschhorn syndrome candidate 1 protein; KIAA1090; MMSET; TRX5; WHSC1	NSD2	7468	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000508803.6, NSD2-218, 7560; ENST00000503128.5, NSD2-211, 8568; ENST00000398261.6, NSD2-207, 8465; ENST00000382895.7, NSD2-206, 7827; ENST00000382892.6, NSD2-205, 7706; ENST00000382891.9, NSD2-204, 7534; ENST00000420906.6, NSD2-208, 5109; ENST00000514045.5, NSD2-223, 3964; ENST00000677895.1, NSD2-228, 4220; ENST00000382888.3, NSD2-203, 2666; ENST00000512700.2, NSD2-221, 2357; ENST00000509115.5, NSD2-219, 1212; ENST00000514329.5, NSD2-224, 851; ENST00000515806.1, NSD2-226, 816; ENST00000507820.5, NSD2-215, 528; ENST00000312087.10, NSD2-201, 8050; ENST00000353275.9, NSD2-202, 7980; ENST00000678714.1, NSD2-230, 8451; ENST00000677559.1, NSD2-227, 7565; ENST00000511904.1, NSD2-220, 690; ENST00000482415.6, NSD2-209, 3602; ENST00000678128.1, NSD2-229, 1651; ENST00000505643.5, NSD2-213, 990; ENST00000503207.1, NSD2-212, 812; ENST00000513726.5, NSD2-222, 648; ENST00000502425.5, NSD2-210, 421; ENST00000679039.1, NSD2-231, 4552; ENST00000508355.5, NSD2-217, 2092; ENST00000508299.1, NSD2-216, 592; ENST00000515695.1, NSD2-225, 571; ENST00000507094.1, NSD2-214, 563"	MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVAKEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGKSTPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASGEEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKRNRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVCKESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKGKMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKNALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKPTDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAKRDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSGFLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCTKAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGRSYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK	chr4:1871393-1982207[+]	"Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro. Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3). However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells. By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes. In ES cells, associates with developmental transcription factors such as SALL1 and represses inappropriate gene transcription mediated by histone deacetylation. During heart development, associates with transcription factor NKX2-5 to repress transcription of NKX2-5 target genes. Plays an essential role in adipogenesis, by regulating expression of genes involved in pre-adipocyte differentiation. During T-cell receptor (TCR) and CD28-mediated T-cell activation, promotes the transcription of transcription factor BCL6 which is required for follicular helper T (Tfh) cell differentiation. During B-cell development, required for the generation of the B1 lineage. During B2 cell activation, may contribute to the control of isotype class switch recombination (CRS), splenic germinal center formation, and the humoral immune response. Plays a role in class switch recombination of the immunoglobulin heavy chain (IgH) locus during B-cell activation. By regulating the methylation of histone H3 at 'Lys-36' and histone H4 at 'Lys-20' at the IgH locus, involved in TP53BP1 recruitment to the IgH switch region and promotes the transcription of IgA."	PDB: 5LSU; PDB: 5VC8; PDB: 6UE6; PDB: 6XCG; PDB: 7CRO; PDB: 7LMT; PDB: 7MDN	HGNC:12766	NSD2_HUMAN	Reviewed	ENSG00000109685	.	.	.	.	.
Mol00539	Protein	BDNF/NT-3 growth factors receptor (NTRK2)	GP145-TrkB; Trk-B; Neurotrophic tyrosine kinase receptor type 2; TrkB tyrosine kinase; Tropomyosin-related kinase B; TRKB	NTRK2	4915	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000277120.8, NTRK2-201, 8666; ENST00000686496.1, NTRK2-219, 9433; ENST00000692181.1, NTRK2-247, 9200; ENST00000686259.1, NTRK2-214, 8988; ENST00000693539.1, NTRK2-258, 8857; ENST00000686324.1, NTRK2-216, 8795; ENST00000691788.1, NTRK2-246, 8747; ENST00000376213.6, NTRK2-206, 8693; ENST00000376208.6, NTRK2-205, 8633; ENST00000687636.1, NTRK2-226, 8475; ENST00000685720.1, NTRK2-213, 8395; ENST00000686443.1, NTRK2-218, 8349; ENST00000304053.11, NTRK2-202, 8108; ENST00000692389.1, NTRK2-248, 7861; ENST00000693109.1, NTRK2-254, 7605; ENST00000395882.6, NTRK2-207, 7499; ENST00000692506.1, NTRK2-250, 7480; ENST00000692762.1, NTRK2-252, 7406; ENST00000687596.1, NTRK2-225, 7396; ENST00000689815.1, NTRK2-238, 7299; ENST00000689685.1, NTRK2-237, 7293; ENST00000359847.4, NTRK2-204, 7286; ENST00000691415.1, NTRK2-243, 7235; ENST00000690281.1, NTRK2-241, 7148; ENST00000688013.1, NTRK2-228, 6983; ENST00000687148.1, NTRK2-223, 6956; ENST00000323115.11, NTRK2-203, 8723; ENST00000692473.1, NTRK2-249, 7980; ENST00000689301.1, NTRK2-235, 7951; ENST00000686542.1, NTRK2-220, 7585; ENST00000685387.1, NTRK2-210, 6990; ENST00000693127.1, NTRK2-255, 6869; ENST00000686322.1, NTRK2-215, 6379; ENST00000687386.1, NTRK2-224, 3550; ENST00000692804.1, NTRK2-253, 2853; ENST00000693384.1, NTRK2-257, 2433; ENST00000690163.1, NTRK2-240, 2891; ENST00000688978.1, NTRK2-234, 6801; ENST00000687136.1, NTRK2-222, 6590; ENST00000691567.1, NTRK2-244, 6490; ENST00000687690.1, NTRK2-227, 6392; ENST00000686874.1, NTRK2-221, 6216; ENST00000690044.1, NTRK2-239, 6131; ENST00000685209.1, NTRK2-209, 4078; ENST00000688041.1, NTRK2-229, 3534; ENST00000685463.1, NTRK2-212, 3368; ENST00000692654.1, NTRK2-251, 3333; ENST00000688241.1, NTRK2-230, 571; ENST00000688854.1, NTRK2-233, 530; ENST00000686332.1, NTRK2-217, 5876; ENST00000688333.1, NTRK2-231, 5803; ENST00000690882.1, NTRK2-242, 5457; ENST00000689651.1, NTRK2-236, 4681; ENST00000685425.1, NTRK2-211, 3840; ENST00000685095.1, NTRK2-208, 3826; ENST00000693313.1, NTRK2-256, 3092; ENST00000688850.1, NTRK2-232, 1990; ENST00000691710.1, NTRK2-245, 1130"	MSSWIRWHGPAMARLWGFCWLVVGFWRAAFACPTSCKCSASRIWCSDPSPGIVAFPRLEPNSVDPENITEIFIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHINFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIKTLQEAKSSPDTQDLYCLNESSKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDYGTAANDIGDTTNRSNEIPSTDVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG	chr9:84668375-85095751[+]	"Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2. Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia."	PDB: 1HCF; PDB: 1WWB; PDB: 2MFQ; PDB: 4ASZ; PDB: 4AT3; PDB: 4AT4; PDB: 4AT5; PDB: 5MO9	HGNC:8032	NTRK2_HUMAN	Reviewed	ENSG00000148053	.	.	.	.	.
Mol00540	Protein	Nuclear ubiquitous casein CDK substrate 1 (NUCKS1)	P1; NUCKS; JC7	NUCKS1	64710	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367142.5, NUCKS1-201, 6399; ENST00000464938.1, NUCKS1-202, 228"	MSRPVRNRKVVDYSQFQESDDADEDYGRDSGPPTKKIRSSPREAKNKRRSGKNSQEDSEDSEDKDVKTKKDDSHSAEDSEDEKEDHKNVRQQRQAASKAASKQREMLMEDVGSEEEQEEEDEAPFQEKDSGSDEDFLMEDDDDSDYGSSKKKNKKMVKKSKPERKEKKMPKPRLKATVTPSPVKGKGKVGRPTASKASKEKTPSPKEEDEEPESPPEKKTSTSPPPEKSGDEGSEDEAPSGED	chr1:205712822-205750182[-]	"Chromatin-associated protein involved in DNA repair by promoting homologous recombination (HR). Binds double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures, but with less affinity than RAD51AP1."	.	HGNC:29923	NUCKS_HUMAN	Reviewed	ENSG00000069275	.	.	.	.	.
Mol00541	Protein	Ornithine decarboxylase antizyme 2 (OAZ2)	AZ2; ODC-Az 2	OAZ2	4947	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000326005.10, OAZ2-201, 1934; ENST00000560258.6, OAZ2-207, 1744; ENST00000559753.1, OAZ2-205, 785; ENST00000559912.2, OAZ2-206, 576; ENST00000560837.5, OAZ2-209, 707; ENST00000559665.6, OAZ2-204, 541; ENST00000560781.6, OAZ2-208, 540; ENST00000559555.1, OAZ2-203, 264; ENST00000558194.5, OAZ2-202, 7102"	MINTQDSSILPLSNCPQLQCCRHIVPGPLWCSDAPHPLSKIPGGRGGGRDPSLSALIYKDEKLTVTQDLPVNDGKPHIVHFQYEVTEVKVSSWDAVLSSQSLFVEIPDGLLADGSKEGLLALLEFAEEKMKVNYVFICFRKGREDRAPLLKTFSFLGFEIVRPGHPCVPSRPDVMFMVYPLDQNLSDED	chr15:64687573-64703281[-]	"Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol."	.	HGNC:8096	OAZ2_HUMAN	Reviewed	ENSG00000180304	.	.	.	.	.
Mol00542	Protein	Osteopontin (OPN)	Bone sialoprotein 1; Nephropontin; Secreted phosphoprotein 1; SPP-1; Urinary stone protein; Uropontin; BNSP; OPN; PSEC0156	SPP1	6696	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000395080.8, SPP1-203, 1561; ENST00000614857.5, SPP1-211, 1728; ENST00000237623.11, SPP1-201, 1581; ENST00000360804.4, SPP1-202, 1196; ENST00000508233.6, SPP1-207, 923; ENST00000682655.1, SPP1-218, 834; ENST00000681973.1, SPP1-212, 1808; ENST00000509659.5, SPP1-209, 1664; ENST00000683087.1, SPP1-220, 1592; ENST00000682026.1, SPP1-213, 1531; ENST00000509334.5, SPP1-208, 760; ENST00000513981.5, SPP1-210, 719; ENST00000682599.1, SPP1-216, 4066; ENST00000684106.1, SPP1-224, 3828; ENST00000682448.1, SPP1-214, 3064; ENST00000682554.1, SPP1-215, 3026; ENST00000684710.1, SPP1-226, 2869; ENST00000683620.1, SPP1-223, 2760; ENST00000684450.1, SPP1-225, 2637; ENST00000683440.1, SPP1-222, 2506; ENST00000683168.1, SPP1-221, 2332; ENST00000682865.1, SPP1-219, 1862; ENST00000682627.1, SPP1-217, 1498; ENST00000508002.5, SPP1-206, 568; ENST00000504310.5, SPP1-204, 557; ENST00000505146.1, SPP1-205, 252"	MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN	chr4:87975667-87983532[+]	Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.	PDB: 3CXD; PDB: 3DSF	HGNC:11255	OSTP_HUMAN	Reviewed	ENSG00000118785	.	.	.	.	.
Mol00543	Protein	Tumor protein 63 (TP63)	p63; Chronic ulcerative stomatitis protein; CUSP; Keratinocyte transcription factor KET; Transformation-related protein 63; TP63; Tumor protein p73-like; p73L; p40; p51; KET; P63; P73H; P73L; TP73L	TP63	8626	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264731.8, TP63-201, 4944; ENST00000354600.10, TP63-203, 4677; ENST00000418709.6, TP63-207, 2810; ENST00000437221.5, TP63-209, 2500; ENST00000320472.9, TP63-202, 2032; ENST00000440651.6, TP63-210, 2031; ENST00000392460.7, TP63-204, 1668; ENST00000449992.5, TP63-211, 1506; ENST00000392463.6, TP63-206, 1386; ENST00000392461.7, TP63-205, 1251; ENST00000456148.1, TP63-212, 1749; ENST00000434928.5, TP63-208, 676; ENST00000460036.1, TP63-213, 1753; ENST00000486398.1, TP63-214, 546"	MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE	chr3:189631389-189897276[+]	Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter.	PDB: 1RG6; PDB: 2NB1; PDB: 2RMN; PDB: 2Y9T; PDB: 2Y9U; PDB: 3QYM; PDB: 3QYN; PDB: 3US0; PDB: 3US1; PDB: 3US2; PDB: 3ZY0; PDB: 3ZY1; PDB: 4A9Z; PDB: 6FGN; PDB: 6RU6; PDB: 6RU7; PDB: 6RU8	HGNC:15979	P63_HUMAN	Reviewed	ENSG00000073282	.	.	.	.	.
Mol00544	Protein	Tumor protein p73 (TP73)	p53-like transcription factor; p53-related protein; P73	TP73	7161	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000378295.9, TP73-208, 5192; ENST00000378288.8, TP73-206, 5120; ENST00000357733.7, TP73-203, 4899; ENST00000346387.8, TP73-201, 4854; ENST00000604074.5, TP73-211, 4806; ENST00000354437.8, TP73-202, 2140; ENST00000378285.5, TP73-205, 2117; ENST00000378280.5, TP73-204, 2062; ENST00000378290.4, TP73-207, 1831; ENST00000603362.5, TP73-209, 1668; ENST00000604479.5, TP73-213, 1623; ENST00000603364.5, TP73-210, 1551; ENST00000604566.1, TP73-214, 1358; ENST00000604194.1, TP73-212, 1092"	MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH	chr1:3652516-3736201[+]	"Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein."	PDB: 1COK; PDB: 1DXS; PDB: 2KBY; PDB: 2MPS; PDB: 2NB1; PDB: 2WQI; PDB: 2WQJ; PDB: 2WTT; PDB: 2XWC; PDB: 3VD0; PDB: 3VD1; PDB: 3VD2; PDB: 4A63; PDB: 4G82; PDB: 4G83; PDB: 4GUO; PDB: 4GUQ; PDB: 5HOB; PDB: 5HOC; PDB: 5KBD; PDB: 6FGS; PDB: 6IJQ	HGNC:12003	P73_HUMAN	Reviewed	ENSG00000078900	.	.	.	.	.
Mol00545	Protein	PI3-kinase regulatory subunit alpha (PIK3R1)	PI3-kinase regulatory subunit alpha; PI3K regulatory subunit alpha; PtdIns-3-kinase regulatory subunit alpha; Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha; PI3-kinase subunit p85-alpha; PtdIns-3-kinase regulatory subunit p85-alpha; GRB1	PIK3R1	5295	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000521381.6, PIK3R1-211, 6975; ENST00000521657.5, PIK3R1-213, 3891; ENST00000320694.12, PIK3R1-201, 2625; ENST00000523872.1, PIK3R1-216, 2473; ENST00000336483.9, PIK3R1-202, 2439; ENST00000522084.5, PIK3R1-214, 705; ENST00000519025.5, PIK3R1-208, 567; ENST00000523807.5, PIK3R1-215, 552; ENST00000521409.5, PIK3R1-212, 540; ENST00000520675.1, PIK3R1-210, 395; ENST00000517698.5, PIK3R1-205, 945; ENST00000517643.1, PIK3R1-204, 586; ENST00000518813.5, PIK3R1-207, 3722; ENST00000520550.1, PIK3R1-209, 1468; ENST00000517412.1, PIK3R1-203, 865; ENST00000518292.1, PIK3R1-206, 558"	MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGSSKTEADVEQQALTLPDLAEQFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQLLDCDTPSVDLEMIDVHVLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNTENLIKVIEILISTEWNERQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFSSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNYDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR	chr5:68215756-68301821[+]	"Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement."	PDB: 1A0N; PDB: 1AZG; PDB: 1H9O; PDB: 1PBW; PDB: 1PHT; PDB: 1PIC; PDB: 1PKS; PDB: 1PKT; PDB: 2IUG; PDB: 2IUH; PDB: 2IUI; PDB: 2RD0; PDB: 2V1Y; PDB: 3HHM; PDB: 3HIZ; PDB: 3I5R; PDB: 3I5S; PDB: 4A55; PDB: 4JPS; PDB: 4L1B; PDB: 4L23; PDB: 4L2Y; PDB: 4OVU; PDB: 4OVV; PDB: 4WAF; PDB: 4YKN; PDB: 4ZOP; PDB: 5AUL; PDB: 5FI4; PDB: 5GJI; PDB: 5ITD; PDB: 5M6U; PDB: 5SW8; PDB: 5SWG; PDB: 5SWO; PDB: 5SWP; PDB: 5SWR; PDB: 5SWT; PDB: 5SX8; PDB: 5SX9; PDB: 5SXA; PDB: 5SXB; PDB: 5SXC; PDB: 5SXD; PDB: 5SXE; PDB: 5SXF; PDB: 5SXI; PDB: 5SXJ; PDB: 5SXK; PDB: 5UBT; PDB: 5UK8; PDB: 5UKJ; PDB: 5UL1; PDB: 5VLR; PDB: 5XGH; PDB: 5XGI; PDB: 5XGJ; PDB: 6NCT; PDB: 6PYR; PDB: 6PYU; PDB: 7CIO; PDB: 7LM2; PDB: 7RNS	HGNC:8979	P85A_HUMAN	Reviewed	ENSG00000145675	.	.	.	.	.
Mol00546	Protein	PI3-kinase regulatory subunit beta (PIK3R2)	PI3-kinase regulatory subunit beta; PI3K regulatory subunit beta; PtdIns-3-kinase regulatory subunit beta; Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta; PI3-kinase subunit p85-beta; PtdIns-3-kinase regulatory subunit p85-beta	PIK3R2	5296	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000222254.13, PIK3R2-201, 3980; ENST00000617130.5, PIK3R2-207, 3796; ENST00000617642.2, PIK3R2-208, 3639; ENST00000426902.5, PIK3R2-202, 3273; ENST00000672815.1, PIK3R2-209, 741; ENST00000464016.3, PIK3R2-204, 588; ENST00000675271.1, PIK3R2-211, 1231; ENST00000674682.1, PIK3R2-210, 879; ENST00000459743.2, PIK3R2-203, 465; ENST00000474310.1, PIK3R2-205, 425; ENST00000600533.2, PIK3R2-206, 425"	MAGPEGFQYRALYPFRRERPEDLELLPGDVLVVSRAALQALGVAEGGERCPQSVGWMPGLNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAPPLLVKLVEAIERTGLDSESHYRPELPAPRTDWSLSDVDQWDTAALADGIKSFLLALPAPLVTPEASAEARRALREAAGPVGPALEPPTLPLHRALTLRFLLQHLGRVASRAPALGPAVRALGATFGPLLLRAPPPPSSPPPGGAPDGSEPSPDFPALLVEKLLQEHLEEQEVAPPALPPKPPKAKPASTVLANGGSPPSLQDAEWYWGDISREEVNEKLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVDLINHYRHESLAQYNAKLDTRLLYPVSKYQQDQIVKEDSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQQLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLGIKNETEDQYALMEDEDDLPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPPAAR	chr19:18153163-18170532[+]	"Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy. Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement."	PDB: 2KT1; PDB: 2XS6; PDB: 3MTT; PDB: 3O5Z; PDB: 6OX7; PDB: 6U28; PDB: 7RNU	HGNC:8980	P85B_HUMAN	Reviewed	ENSG00000105647	.	.	.	.	.
Mol00547	Protein	Polyadenylate-binding protein 1 (PABPC1)	PABP-1; Poly(A)-binding protein 1; PAB1; PABP; PABP1; PABPC2	PABPC1	26986	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000318607.10, PABPC1-201, 2861; ENST00000523555.6, PABPC1-222, 3116; ENST00000520142.2, PABPC1-214, 2877; ENST00000522720.2, PABPC1-221, 2845; ENST00000520804.2, PABPC1-215, 2839; ENST00000521865.6, PABPC1-218, 2718; ENST00000522658.6, PABPC1-220, 2313; ENST00000676662.1, PABPC1-226, 3322; ENST00000677140.1, PABPC1-228, 3274; ENST00000677787.1, PABPC1-234, 3145; ENST00000677765.1, PABPC1-232, 3085; ENST00000677478.1, PABPC1-231, 2798; ENST00000677380.1, PABPC1-230, 2730; ENST00000519004.5, PABPC1-208, 2401; ENST00000522387.5, PABPC1-219, 2331; ENST00000679197.1, PABPC1-240, 2295; ENST00000519100.6, PABPC1-209, 2207; ENST00000610907.2, PABPC1-224, 1768; ENST00000520868.5, PABPC1-216, 971; ENST00000518196.5, PABPC1-205, 631; ENST00000518293.5, PABPC1-206, 608; ENST00000517403.5, PABPC1-202, 560; ENST00000521067.1, PABPC1-217, 492; ENST00000517990.5, PABPC1-204, 487; ENST00000519363.1, PABPC1-210, 453; ENST00000678954.1, PABPC1-239, 3384; ENST00000523636.5, PABPC1-223, 818; ENST00000519622.5, PABPC1-212, 667; ENST00000676655.1, PABPC1-225, 2382; ENST00000519596.5, PABPC1-211, 771; ENST00000677892.1, PABPC1-235, 3429; ENST00000678709.1, PABPC1-237, 3395; ENST00000677775.1, PABPC1-233, 3278; ENST00000676976.1, PABPC1-227, 2998; ENST00000678290.1, PABPC1-236, 2753; ENST00000517921.2, PABPC1-203, 2485; ENST00000678822.1, PABPC1-238, 2313; ENST00000677285.1, PABPC1-229, 1491; ENST00000518716.1, PABPC1-207, 694; ENST00000519848.1, PABPC1-213, 676"	MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV	chr8:100685816-100722809[-]	"Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability."	PDB: 1CVJ; PDB: 1G9L; PDB: 1JGN; PDB: 1JH4; PDB: 2K8G; PDB: 2RQG; PDB: 2RQH; PDB: 2X04; PDB: 3KTP; PDB: 3KTR; PDB: 3KUI; PDB: 3KUJ; PDB: 3KUR; PDB: 3KUS; PDB: 3KUT; PDB: 3PKN; PDB: 3PTH; PDB: 4F02; PDB: 4F25; PDB: 4F26; PDB: 5DX1; PDB: 5DX8; PDB: 5DXA; PDB: 5LGP; PDB: 5LGQ; PDB: 5LGR; PDB: 5LGS	HGNC:8554	PABP1_HUMAN	Reviewed	ENSG00000070756	.	.	.	.	.
Mol00548	Protein	Protein mono-ADP-ribosyltransferase PARP8 (PARP8)	ADP-ribosyltransferase diphtheria toxin-like 16; ARTD16; Poly [ADP-ribose] polymerase 8; PARP-8	PARP8	79668	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000281631.10, PARP8-201, 7475; ENST00000505554.5, PARP8-211, 3825; ENST00000514067.6, PARP8-219, 2829; ENST00000505697.6, PARP8-212, 2747; ENST00000514342.6, PARP8-220, 2384; ENST00000513738.5, PARP8-218, 596; ENST00000503665.5, PARP8-206, 572; ENST00000515175.6, PARP8-222, 513; ENST00000503046.5, PARP8-203, 464; ENST00000502524.5, PARP8-202, 332; ENST00000515166.5, PARP8-221, 2730; ENST00000510303.6, PARP8-215, 615; ENST00000503888.5, PARP8-209, 577; ENST00000503707.6, PARP8-207, 576; ENST00000503193.5, PARP8-204, 574; ENST00000507812.5, PARP8-213, 554; ENST00000511363.6, PARP8-216, 2860; ENST00000503561.7, PARP8-205, 2818; ENST00000503790.6, PARP8-208, 597; ENST00000505180.5, PARP8-210, 521; ENST00000513414.1, PARP8-217, 484; ENST00000510040.1, PARP8-214, 1728"	MGMCSRQERIQKDIDVVIQKSRAEKDCLFADFRYSDSTFTFTYVGGPRSVSYSVHVSEDYPDNTYVSSSENDEDVLVTTEPIPVIFHRIATELRKTNDINCCLSIKSKLQKENGEESRQNSTVEEDSEGDNDSEEFYYGGQVNYDGELHKHPQLEADLSAVREIYGPHAVSLREYGAIDDVDIDLHIDVSFLDEEIAVAWEVIRTEPIIVRLHCSLTQYLNGPVPTVDVFQISTKERFGLGHQLKKIMQTFVTQQWKQSKEKSNCLHNKKLSEKKVKSPLHLFSTLRRSPSYPPPGCGKSKSKLKSEQDGISKTHKLLRRTCSSTVKTDDVCVTKSHRTFGRSLSSDPRAEQAMTAIKSHKLLNRPCPAAVKSEECLTLKSHRLLTRSCSGDPRCEHNTNLKPHKLLSRSYSSNLRMEELYGLKNHKLLSKSYSSAPKSSKTELFKEPNAEGRRLSLTSGLIGILTPSSSSSSQLAPNGAKCIPVRDRGFLVQTIEFAEQRIPVLNEYCVVCDEPHVFQNGPMLRPTVCERELCVFAFQTLGVMNEAADEIATGAQVVDLLVSMCRSALESPRKVVIFEPYPSVVDPNDPQMLAFNPRKKNYDRVMKALDSITSIREMTQAPYLEIKKQMDKQDPLAHPLLQWVISSNRSHIVKLPVNRQLKFMHTPHQFLLLSSPPAKESNFRAAKKLFGSTFAFHGSHIENWHSILRNGLVVASNTRLQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKVSAKDEPASSSKSSNTSQSQKKGQQSQFLQSRNLKCIALCEVITSSDLHKHGEIWVVPNTDHVCTRFFFVYEDGQVGDANINTQEGGIHKEILRVIGNQTATG	chr5:50665899-50846519[+]	Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins.	.	HGNC:26124	PARP8_HUMAN	Reviewed	ENSG00000151883	.	.	.	.	.
Mol00549	Protein	Paired box protein Pax-6 (PAX6)	Aniridia type II protein; Oculorhombin; AN2	PAX6	5080	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000640368.2, PAX6-268, 2743; ENST00000643871.1, PAX6-281, 6944; ENST00000638914.3, PAX6-243, 6922; ENST00000606377.7, PAX6-230, 6888; ENST00000419022.6, PAX6-209, 6888; ENST00000639386.2, PAX6-253, 6509; ENST00000379109.7, PAX6-203, 3182; ENST00000638629.1, PAX6-234, 2844; ENST00000640610.1, PAX6-271, 2730; ENST00000639916.1, PAX6-257, 2622; ENST00000379129.7, PAX6-207, 2614; ENST00000379107.7, PAX6-202, 2579; ENST00000379132.8, PAX6-208, 2576; ENST00000640975.1, PAX6-280, 2553; ENST00000639409.1, PAX6-255, 2450; ENST00000639034.2, PAX6-247, 1794; ENST00000241001.13, PAX6-201, 1736; ENST00000481563.6, PAX6-217, 1587; ENST00000639548.1, PAX6-256, 1417; ENST00000640125.1, PAX6-262, 1375; ENST00000639109.1, PAX6-251, 2734; ENST00000639079.1, PAX6-250, 2608; ENST00000639943.1, PAX6-259, 2584; ENST00000638762.1, PAX6-238, 2580; ENST00000638685.1, PAX6-235, 2372; ENST00000640872.1, PAX6-278, 2367; ENST00000524853.6, PAX6-219, 2221; ENST00000639950.1, PAX6-260, 2133; ENST00000640431.1, PAX6-269, 2037; ENST00000379123.10, PAX6-206, 1923; ENST00000638346.1, PAX6-233, 1863; ENST00000640766.1, PAX6-276, 1797; ENST00000640460.1, PAX6-270, 1736; ENST00000379111.7, PAX6-204, 1718; ENST00000638963.1, PAX6-244, 1580; ENST00000640684.1, PAX6-274, 1557; ENST00000379115.9, PAX6-205, 1531; ENST00000640613.1, PAX6-272, 1525; ENST00000423822.7, PAX6-210, 1521; ENST00000639006.1, PAX6-246, 1507; ENST00000638802.1, PAX6-239, 1505; ENST00000640287.1, PAX6-266, 1485; ENST00000638250.1, PAX6-231, 1483; ENST00000639061.1, PAX6-249, 1473; ENST00000438681.6, PAX6-211, 1395; ENST00000638878.1, PAX6-241, 1369; ENST00000640242.1, PAX6-264, 1298; ENST00000640963.1, PAX6-279, 1267; ENST00000638853.1, PAX6-240, 1248; ENST00000638696.1, PAX6-236, 1203; ENST00000455099.6, PAX6-212, 1202; ENST00000638755.1, PAX6-237, 1161; ENST00000638965.1, PAX6-245, 979; ENST00000640335.1, PAX6-267, 964; ENST00000639920.1, PAX6-258, 676; ENST00000639394.1, PAX6-254, 1988; ENST00000533156.2, PAX6-226, 848; ENST00000464174.6, PAX6-213, 846; ENST00000530373.6, PAX6-221, 785; ENST00000530714.6, PAX6-222, 650; ENST00000640251.1, PAX6-265, 649; ENST00000534353.5, PAX6-228, 540; ENST00000639203.1, PAX6-252, 532; ENST00000638278.1, PAX6-232, 417; ENST00000640617.1, PAX6-273, 412; ENST00000640819.1, PAX6-277, 368; ENST00000533333.5, PAX6-227, 6173; ENST00000474783.2, PAX6-216, 4392; ENST00000470027.7, PAX6-214, 3587; ENST00000640172.1, PAX6-263, 2525; ENST00000471303.6, PAX6-215, 2423; ENST00000638913.1, PAX6-242, 2390; ENST00000639054.1, PAX6-248, 2254; ENST00000640735.1, PAX6-275, 2060; ENST00000531910.6, PAX6-223, 1958; ENST00000494377.7, PAX6-218, 1911; ENST00000534390.2, PAX6-229, 1084; ENST00000640038.1, PAX6-261, 781; ENST00000532916.5, PAX6-225, 627; ENST00000532175.5, PAX6-224, 524; ENST00000527769.5, PAX6-220, 487"	MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQYWPRLQ	chr11:31784779-31817961[-]	"Transcription factor with important functions in the development of the eye, nose, central nervous system and pancreas. Required for the differentiation of pancreatic islet alpha cells (By similarity). Competes with PAX4 in binding to a common element in the glucagon, insulin and somatostatin promoters. Regulates specification of the ventral neuron subtypes by establishing the correct progenitor domains (By similarity). Acts as a transcriptional repressor of NFATC1-mediated gene expression (By similarity)."	PDB: 2CUE; PDB: 6PAX	HGNC:8620	PAX6_HUMAN	Reviewed	ENSG00000007372	.	.	.	.	.
Mol00550	Protein	Protocadherin-20 (PCDH20)	Protocadherin-13; PCDH13	PCDH20	64881	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000409204.4, PCDH20-201, 4778"	MRGRGNARSSQALGVSWCPATWHPRLDMGRLHRPRSSTSYRNLPHLFLFFLFVGPFSCLGSYSRATELLYSLNEGLPAGVLIGSLAEDLRLLPRSAGRPDPQSQLPERTGAEWNPPLSFSLASRGLSGQYVTLDNRSGELHTSAQEIDREALCVEGGGGTAWSGSVSISSSPSDSCLLLLDVLVLPQEYFRFVKVKIAIRDINDNAPQFPVSQISVWVPENAPVNTRLAIEHPAVDPDVGINGVQTYRLLDYHGMFTLDVEENENGERTPYLIVMGALDRETQDQYVSIIIAEDGGSPPLLGSATLTIGISDINDNCPLFTDSQINVTVYGNATVGTPIAAVQAVDKDLGTNAQITYSYSQKVPQASKDLFHLDENTGVIKLFSKIGGSVLESHKLTILANGPGCIPAVITALVSIIKVIFRPPEIVPRYIANEIDGVVYLKELEPVNTPIAFFTIRDPEGKYKVNCYLDGEGPFRLSPYKPYNNEYLLETTKPMDYELQQFYEVAVVAWNSEGFHVKRVIKVQLLDDNDNAPIFLQPLIELTIEENNSPNAFLTKLYATDADSEERGQVSYFLGPDAPSYFSLDSVTGILTVSTQLDREEKEKYRYTVRAVDCGKPPRESVATVALTVLDKNDNSPRFINKDFSFFVPENFPGYGEIGVISVTDADAGRNGWVALSVVNQSDIFVIDTGKGMLRAKVSLDREQQSSYTLWVEAVDGGEPALSSTAKITILLLDINDNPPLVLFPQSNMSYLLVLPSTLPGSPVTEVYAVDKDTGMNAVIAYSIIGRRGPRPESFRIDPKTGNITLEEALLQTDYGLHRLLVKVSDHGYPEPLHSTVMVNLFVNDTVSNESYIESLLRKEPEINIEEKEPQISIEPTHRKVESVSCMPTLVALSVISLGSITLVTGMGIYICLRKGEKHPREDENLEVQIPLKGKIDLHMRERKPMDISNI	chr13:61409685-61415522[-]	Potential calcium-dependent cell-adhesion protein.	.	HGNC:14257	PCD20_HUMAN	Reviewed	ENSG00000280165	.	.	.	.	.
Mol00551	Protein	Solute carrier family 46 member 1 (SLC46A1)	G21; Heme carrier protein 1; PCFT/HCP1; Solute carrier family 46 member 1; HCP1; PCFT	SLC46A1	113235	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000612814.5, SLC46A1-207, 6492; ENST00000618626.1, SLC46A1-208, 5363; ENST00000584995.5, SLC46A1-206, 1030; ENST00000581516.1, SLC46A1-202, 844; ENST00000582735.1, SLC46A1-204, 574; ENST00000584426.1, SLC46A1-205, 564; ENST00000578217.1, SLC46A1-201, 596; ENST00000582590.1, SLC46A1-203, 1435; ENST00000619923.1, SLC46A1-209, 528"	MEGSASPPEKPRARPAAAVLCRGPVEPLVFLANFALVLQGPLTTQYLWHRFSADLGYNGTRQRGGCSNRSADPTMQEVETLTSHWTLYMNVGGFLVGLFSSTLLGAWSDSVGRRPLLVLASLGLLLQALVSVFVVQLQLHVGYFVLGRILCALLGDFGGLLAASFASVADVSSSRSRTFRMALLEASIGVAGMLASLLGGHWLRAQGYANPFWLALALLIAMTLYAAFCFGETLKEPKSTRLFTFRHHRSIVQLYVAPAPEKSRKHLALYSLAIFVVITVHFGAQDILTLYELSTPLCWDSKLIGYGSAAQHLPYLTSLLALKLLQYCLADAWVAEIGLAFNILGMVVFAFATITPLMFTGYGLLFLSLVITPVIRAKLSKLVRETEQGALFSAVACVNSLAMLTASGIFNSLYPATLNFMKGFPFLLGAGLLLIPAVLIGMLEKADPHLEFQQFPQSP	chr17:28394642-28407197[-]	"Proton-coupled high-affinity folate and heme transporter that plays an essential role in iron metabolism. Acts as the main importer of heme in the intestine. Imports also heme in the retina and retinal pigment epithelium, in neurons of the hippocampus, and in the renal epithelial cells. Participates therefore in the trafficking of heme and increases intracellular iron content. Mediates also intestinal absorption of folates and their transport from blood to cerebrospinal fluid across the choroid plexus."	.	HGNC:30521	PCFT_HUMAN	Reviewed	ENSG00000076351	.	.	.	.	.
Mol00552	Protein	Programmed cell death protein 10 (PDCD10)	Cerebral cavernous malformations 3 protein; TF-1 cell apoptosis-related protein 15; CCM3; TFAR15	PDCD10	11235	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000392750.7, PDCD10-201, 2133; ENST00000473645.6, PDCD10-208, 1360; ENST00000497056.6, PDCD10-218, 1276; ENST00000470131.5, PDCD10-206, 1026; ENST00000461494.5, PDCD10-202, 934; ENST00000475915.6, PDCD10-209, 849; ENST00000492396.5, PDCD10-216, 814; ENST00000471885.5, PDCD10-207, 764; ENST00000487947.6, PDCD10-214, 716; ENST00000462725.6, PDCD10-203, 715; ENST00000492139.5, PDCD10-215, 686; ENST00000464360.5, PDCD10-205, 585; ENST00000479121.5, PDCD10-210, 430; ENST00000494502.6, PDCD10-217, 757; ENST00000487678.1, PDCD10-213, 416; ENST00000462830.1, PDCD10-204, 225; ENST00000483451.5, PDCD10-212, 1119; ENST00000481136.1, PDCD10-211, 674"	MRMTMEEMKNEAETTSMVSMPLYAVMYPVFNELERVNLSAAQTLRAAFIKAEKENPGLTQDIIMKILEKKSVEVNFTESLLRMAADDVEEYMIERPEPEFQDLNEKARALKQILSKIPDEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDGKAINVFVSANRLIHQTNLILQTFKTVA	chr3:167683298-167734939[-]	"Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development."	PDB: 3AJM; PDB: 3L8I; PDB: 3L8J; PDB: 3RQE; PDB: 3RQF; PDB: 3RQG; PDB: 3W8H; PDB: 3W8I; PDB: 4GEH; PDB: 4TVQ	HGNC:8761	PDC10_HUMAN	Reviewed	ENSG00000114209	.	.	.	.	.
Mol00553	Protein	Programmed cell death 6-interacting protein (PDCD6IP)	PDCD6-interacting protein; ALG-2-interacting protein 1; ALG-2-interacting protein X; Hp95; AIP1; ALIX; KIAA1375	PDCD6IP	10015	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000307296.8, PDCD6IP-201, 5884; ENST00000457054.6, PDCD6IP-206, 5962; ENST00000413073.1, PDCD6IP-203, 566; ENST00000648706.1, PDCD6IP-218, 6049; ENST00000412887.5, PDCD6IP-202, 842; ENST00000435909.5, PDCD6IP-205, 587; ENST00000430877.5, PDCD6IP-204, 582; ENST00000498147.5, PDCD6IP-217, 802; ENST00000482561.1, PDCD6IP-211, 626; ENST00000484478.5, PDCD6IP-212, 596; ENST00000477798.5, PDCD6IP-210, 587; ENST00000495235.2, PDCD6IP-216, 428; ENST00000465122.5, PDCD6IP-208, 894; ENST00000489869.1, PDCD6IP-214, 842; ENST00000487821.1, PDCD6IP-213, 750; ENST00000459659.1, PDCD6IP-207, 662; ENST00000494810.1, PDCD6IP-215, 619; ENST00000473593.1, PDCD6IP-209, 540"	MATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYPQQ	chr3:33798571-33869707[+]	"Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. May play a role in the regulation of both apoptosis and cell proliferation. Regulates exosome biogenesis in concert with SDC1/4 and SDCBP. By interacting with F-actin, PARD3 and TJP1 secures the proper assembly and positioning of actomyosin-tight junction complex at the apical sides of adjacent epithelial cells that defines a spatial membrane domain essential for the maintenance of epithelial cell polarity and barrier."	PDB: 2OEV; PDB: 2OEW; PDB: 2OEX; PDB: 2OJQ; PDB: 2R02; PDB: 2R03; PDB: 2R05; PDB: 2XS1; PDB: 2XS8; PDB: 2ZNE; PDB: 3C3O; PDB: 3C3Q; PDB: 3C3R; PDB: 3E1R; PDB: 3WUV; PDB: 4JJY; PDB: 5V3R; PDB: 5WA1; PDB: 6KP3	HGNC:8766	PDC6I_HUMAN	Reviewed	ENSG00000170248	.	.	.	.	.
Mol00554	Protein	Programmed cell death protein 4 (PDCD4)	Neoplastic transformation inhibitor protein; Nuclear antigen H731-like; Protein 197/15a; H731	PDCD4	27250	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000280154.12, PDCD4-201, 3481; ENST00000393104.6, PDCD4-202, 3697; ENST00000444997.1, PDCD4-203, 819; ENST00000481353.5, PDCD4-206, 1120; ENST00000498367.1, PDCD4-211, 975; ENST00000492932.5, PDCD4-210, 813; ENST00000462577.5, PDCD4-204, 789; ENST00000483670.5, PDCD4-208, 774; ENST00000467574.5, PDCD4-205, 735; ENST00000489049.5, PDCD4-209, 547; ENST00000483595.1, PDCD4-207, 531"	MDVENEQILNVNPADPDNLSDSLFSGDEENAGTEEIKNEINGNWISASSINEARINAKAKRRLRKNSSRDSGRGDSVSDSGSDALRSGLTVPTSPKGRLLDRRSRSGKGRGLPKKGGAGGKGVWGTPGQVYDVEEVDVKDPNYDDDQENCVYETVVLPLDERAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVMSTTDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQSVNHLVKEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIIMVLESTGESTFKMILDLLKSLWKSSTITVDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPSRGRKRFVSEGDGGRLKPESY	chr10:110871795-110900006[+]	"Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity)."	PDB: 2GGF; PDB: 2KZT; PDB: 2RG8; PDB: 2ZU6; PDB: 3EIJ	HGNC:8763	PDCD4_HUMAN	Reviewed	ENSG00000150593	.	.	.	.	.
Mol00555	Protein	Phosphodiesterase 4D (PDE4D)	DPDE3; PDE43; DPDE3	PDE4D	5144	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000340635.11, PDE4D-203, 8160; ENST00000636120.1, PDE4D-227, 6659; ENST00000507116.5, PDE4D-216, 3350; ENST00000360047.9, PDE4D-205, 3122; ENST00000358923.10, PDE4D-204, 2969; ENST00000503258.5, PDE4D-210, 2860; ENST00000317118.12, PDE4D-202, 2599; ENST00000502484.6, PDE4D-208, 2478; ENST00000405755.6, PDE4D-207, 2294; ENST00000505453.1, PDE4D-212, 1430; ENST00000502575.1, PDE4D-209, 1040; ENST00000515835.2, PDE4D-225, 590; ENST00000505507.6, PDE4D-213, 577; ENST00000514552.5, PDE4D-222, 494; ENST00000638939.1, PDE4D-228, 375; ENST00000509368.6, PDE4D-218, 2809; ENST00000309641.10, PDE4D-201, 2025; ENST00000621323.4, PDE4D-226, 709; ENST00000512069.6, PDE4D-220, 536; ENST00000405053.7, PDE4D-206, 512; ENST00000515324.1, PDE4D-224, 443; ENST00000504624.1, PDE4D-211, 300; ENST00000515011.5, PDE4D-223, 2175; ENST00000509355.5, PDE4D-217, 847; ENST00000514231.1, PDE4D-221, 733; ENST00000506024.5, PDE4D-214, 599; ENST00000511382.1, PDE4D-219, 581; ENST00000506510.6, PDE4D-215, 558"	MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRPMSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVGEEEESQPEACVIDDRSPDT	chr5:58969038-60522120[-]	"Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes."	PDB: 1E9K; PDB: 1MKD; PDB: 1OYN; PDB: 1PTW; PDB: 1Q9M; PDB: 1TB7; PDB: 1TBB; PDB: 1XOM; PDB: 1XON; PDB: 1XOQ; PDB: 1XOR; PDB: 1Y2B; PDB: 1Y2C; PDB: 1Y2D; PDB: 1Y2E; PDB: 1Y2K; PDB: 1ZKN; PDB: 2FM0; PDB: 2FM5; PDB: 2PW3; PDB: 2QYN; PDB: 3G4G; PDB: 3G4I; PDB: 3G4K; PDB: 3G4L; PDB: 3G58; PDB: 3IAD; PDB: 3IAK; PDB: 3K4S; PDB: 3SL3; PDB: 3SL4; PDB: 3SL5; PDB: 3SL6; PDB: 3SL8; PDB: 3V9B; PDB: 4OGB; PDB: 4W1O; PDB: 4WCU; PDB: 5K1I; PDB: 5K32; PDB: 5LBO; PDB: 5TKB; PDB: 5WH5; PDB: 5WH6; PDB: 5WQA; PDB: 6AKR; PDB: 6BOJ; PDB: 6F6U; PDB: 6F8R; PDB: 6F8T; PDB: 6F8U; PDB: 6F8V; PDB: 6F8W; PDB: 6F8X; PDB: 6FDC; PDB: 6FDI; PDB: 6FE7; PDB: 6FEB; PDB: 6FET; PDB: 6FT0; PDB: 6FTA; PDB: 6FTW; PDB: 6FW3; PDB: 6HWO; PDB: 6IAG; PDB: 6IBF; PDB: 6IM6; PDB: 6IMB; PDB: 6IMD; PDB: 6IMI; PDB: 6IMO; PDB: 6IMR; PDB: 6IMT; PDB: 6IND; PDB: 6INK; PDB: 6INM; PDB: 6KJZ; PDB: 6KK0; PDB: 6LRM; PDB: 6NJH; PDB: 6NJI; PDB: 6NJJ; PDB: 6RCW; PDB: 6ZBA; PDB: 7A8Q; PDB: 7A9V; PDB: 7AAG; PDB: 7AB9; PDB: 7ABD; PDB: 7ABE; PDB: 7ABJ; PDB: 7AY6; PDB: 7B9H; PDB: 7CBJ; PDB: 7CBQ; PDB: 7F2K; PDB: 7F2L; PDB: 7F2M	HGNC:8783	PDE4D_HUMAN	Reviewed	ENSG00000113448	.	.	.	.	.
Mol00556	Protein	Heparan sulfate proteoglycan 2 (HSPG2)	HSPG; Perlecan; PLC	HSPG2	3339	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374695.8, HSPG2-203, 14341; ENST00000635682.1, HSPG2-214, 921; ENST00000374673.4, HSPG2-201, 865; ENST00000644714.1, HSPG2-215, 708; ENST00000374676.4, HSPG2-202, 411; ENST00000427897.1, HSPG2-205, 589; ENST00000412328.5, HSPG2-204, 828; ENST00000486901.1, HSPG2-211, 3586; ENST00000471322.2, HSPG2-208, 1602; ENST00000481644.1, HSPG2-210, 839; ENST00000439717.2, HSPG2-206, 637; ENST00000453796.1, HSPG2-207, 621; ENST00000493940.2, HSPG2-212, 584; ENST00000480900.1, HSPG2-209, 500; ENST00000498495.1, HSPG2-213, 488"	MGWRAAGALLLALLLHGRLLAVTHGLRAYDGLSLPEDIETVTASQMRWTHSYLSDDEDMLADSISGDDLGSGDLGSGDFQMVYFRALVNFTRSIEYSPQLEDAGSREFREVSEAVVDTLESEYLKIPGDQVVSVVFIKELDGWVFVELDVGSEGNADGAQIQEMLLRVISSGSVASYVTSPQGFQFRRLGTVPQFPRACTEAEFACHSYNECVALEYRCDRRPDCRDMSDELNCEEPVLGISPTFSLLVETTSLPPRPETTIMRQPPVTHAPQPLLPGSVRPLPCGPQEAACRNGHCIPRDYLCDGQEDCEDGSDELDCGPPPPCEPNEFPCGNGHCALKLWRCDGDFDCEDRTDEANCPTKRPEEVCGPTQFRCVSTNMCIPASFHCDEESDCPDRSDEFGCMPPQVVTPPRESIQASRGQTVTFTCVAIGVPTPIINWRLNWGHIPSHPRVTVTSEGGRGTLIIRDVKESDQGAYTCEAMNARGMVFGIPDGVLELVPQRGPCPDGHFYLEHSAACLPCFCFGITSVCQSTRRFRDQIRLRFDQPDDFKGVNVTMPAQPGTPPLSSTQLQIDPSLHEFQLVDLSRRFLVHDSFWALPEQFLGNKVDSYGGSLRYNVRYELARGMLEPVQRPDVVLMGAGYRLLSRGHTPTQPGALNQRQVQFSEEHWVHESGRPVQRAELLQVLQSLEAVLIQTVYNTKMASVGLSDIAMDTTVTHATSHGRAHSVEECRCPIGYSGLSCESCDAHFTRVPGGPYLGTCSGCNCNGHASSCDPVYGHCLNCQHNTEGPQCNKCKAGFFGDAMKATATSCRPCPCPYIDASRRFSDTCFLDTDGQATCDACAPGYTGRRCESCAPGYEGNPIQPGGKCRPVNQEIVRCDERGSMGTSGEACRCKNNVVGRLCNECADGSFHLSTRNPDGCLKCFCMGVSRHCTSSSWSRAQLHGASEEPGHFSLTNAASTHTTNEGIFSPTPGELGFSSFHRLLSGPYFWSLPSRFLGDKVTSYGGELRFTVTQRSQPGSTPLHGQPLVVLQGNNIILEHHVAQEPSPGQPSTFIVPFREQAWQRPDGQPATREHLLMALAGIDTLLIRASYAQQPAESRVSGISMDVAVPEETGQDPALEVEQCSCPPGYRGPSCQDCDTGYTRTPSGLYLGTCERCSCHGHSEACEPETGACQGCQHHTEGPRCEQCQPGYYGDAQRGTPQDCQLCPCYGDPAAGQAAHTCFLDTDGHPTCDACSPGHSGRHCERCAPGYYGNPSQGQPCQRDSQVPGPIGCNCDPQGSVSSQCDAAGQCQCKAQVEGLTCSHCRPHHFHLSASNPDGCLPCFCMGITQQCASSAYTRHLISTHFAPGDFQGFALVNPQRNSRLTGEFTVEPVPEGAQLSFGNFAQLGHESFYWQLPETYQGDKVAAYGGKLRYTLSYTAGPQGSPLSDPDVQITGNNIMLVASQPALQGPERRSYEIMFREEFWRRPDGQPATREHLLMALADLDELLIRATFSSVPLAASISAVSLEVAQPGPSNRPRALEVEECRCPPGYIGLSCQDCAPGYTRTGSGLYLGHCELCECNGHSDLCHPETGACSQCQHNAAGEFCELCAPGYYGDATAGTPEDCQPCACPLTNPENMFSRTCESLGAGGYRCTACEPGYTGQYCEQCGPGYVGNPSVQGGQCLPETNQAPLVVEVHPARSIVPQGGSHSLRCQVSGSPPHYFYWSREDGRPVPSGTQQRHQGSELHFPSVQPSDAGVYICTCRNLHQSNTSRAELLVTEAPSKPITVTVEEQRSQSVRPGADVTFICTAKSKSPAYTLVWTRLHNGKLPTRAMDFNGILTIRNVQLSDAGTYVCTGSNMFAMDQGTATLHVQASGTLSAPVVSIHPPQLTVQPGQLAEFRCSATGSPTPTLEWTGGPGGQLPAKAQIHGGILRLPAVEPTDQAQYLCRAHSSAGQQVARAVLHVHGGGGPRVQVSPERTQVHAGRTVRLYCRAAGVPSATITWRKEGGSLPPQARSERTDIATLLIPAITTADAGFYLCVATSPAGTAQARIQVVVLSASDASPPPVKIESSSPSVTEGQTLDLNCVVAGSAHAQVTWYRRGGSLPPHTQVHGSRLRLPQVSPADSGEYVCRVENGSGPKEASITVSVLHGTHSGPSYTPVPGSTRPIRIEPSSSHVAEGQTLDLNCVVPGQAHAQVTWHKRGGSLPARHQTHGSLLRLHQVTPADSGEYVCHVVGTSGPLEASVLVTIEASVIPGPIPPVRIESSSSTVAEGQTLDLSCVVAGQAHAQVTWYKRGGSLPARHQVRGSRLYIFQASPADAGQYVCRASNGMEASITVTVTGTQGANLAYPAGSTQPIRIEPSSSQVAEGQTLDLNCVVPGQSHAQVTWHKRGGSLPVRHQTHGSLLRLYQASPADSGEYVCRVLGSSVPLEASVLVTIEPAGSVPALGVTPTVRIESSSSQVAEGQTLDLNCLVAGQAHAQVTWHKRGGSLPARHQVHGSRLRLLQVTPADSGEYVCRVVGSSGTQEASVLVTIQQRLSGSHSQGVAYPVRIESSSASLANGHTLDLNCLVASQAPHTITWYKRGGSLPSRHQIVGSRLRIPQVTPADSGEYVCHVSNGAGSRETSLIVTIQGSGSSHVPSVSPPIRIESSSPTVVEGQTLDLNCVVARQPQAIITWYKRGGSLPSRHQTHGSHLRLHQMSVADSGEYVCRANNNIDALEASIVISVSPSAGSPSAPGSSMPIRIESSSSHVAEGETLDLNCVVPGQAHAQVTWHKRGGSLPSHHQTRGSRLRLHHVSPADSGEYVCRVMGSSGPLEASVLVTIEASGSSAVHVPAPGGAPPIRIEPSSSRVAEGQTLDLKCVVPGQAHAQVTWHKRGGNLPARHQVHGPLLRLNQVSPADSGEYSCQVTGSSGTLEASVLVTIEPSSPGPIPAPGLAQPIYIEASSSHVTEGQTLDLNCVVPGQAHAQVTWYKRGGSLPARHQTHGSQLRLHLVSPADSGEYVCRAASGPGPEQEASFTVTVPPSEGSSYRLRSPVISIDPPSSTVQQGQDASFKCLIHDGAAPISLEWKTRNQELEDNVHISPNGSIITIVGTRPSNHGTYRCVASNAYGVAQSVVNLSVHGPPTVSVLPEGPVWVKVGKAVTLECVSAGEPRSSARWTRISSTPAKLEQRTYGLMDSHAVLQISSAKPSDAGTYVCLAQNALGTAQKQVEVIVDTGAMAPGAPQVQAEEAELTVEAGHTATLRCSATGSPAPTIHWSKLRSPLPWQHRLEGDTLIIPRVAQQDSGQYICNATSPAGHAEATIILHVESPPYATTVPEHASVQAGETVQLQCLAHGTPPLTFQWSRVGSSLPGRATARNELLHFERAAPEDSGRYRCRVTNKVGSAEAFAQLLVQGPPGSLPATSIPAGSTPTVQVTPQLETKSIGASVEFHCAVPSDRGTQLRWFKEGGQLPPGHSVQDGVLRIQNLDQSCQGTYICQAHGPWGKAQASAQLVIQALPSVLINIRTSVQTVVVGHAVEFECLALGDPKPQVTWSKVGGHLRPGIVQSGGVVRIAHVELADAGQYRCTATNAAGTTQSHVLLLVQALPQISMPQEVRVPAGSAAVFPCIASGYPTPDISWSKLDGSLPPDSRLENNMLMLPSVRPQDAGTYVCTATNRQGKVKAFAHLQVPERVVPYFTQTPYSFLPLPTIKDAYRKFEIKITFRPDSADGMLLYNGQKRVPGSPTNLANRQPDFISFGLVGGRPEFRFDAGSGMATIRHPTPLALGHFHTVTLLRSLTQGSLIVGDLAPVNGTSQGKFQGLDLNEELYLGGYPDYGAIPKAGLSSGFIGCVRELRIQGEEIVFHDLNLTAHGISHCPTCRDRPCQNGGQCHDSESSSYVCVCPAGFTGSRCEHSQALHCHPEACGPDATCVNRPDGRGYTCRCHLGRSGLRCEEGVTVTTPSLSGAGSYLALPALTNTHHELRLDVEFKPLAPDGVLLFSGGKSGPVEDFVSLAMVGGHLEFRYELGSGLAVLRSAEPLALGRWHRVSAERLNKDGSLRVNGGRPVLRSSPGKSQGLNLHTLLYLGGVEPSVPLSPATNMSAHFRGCVGEVSVNGKRLDLTYSFLGSQGIGQCYDSSPCERQPCQHGATCMPAGEYEFQCLCRDGFKGDLCEHEENPCQLREPCLHGGTCQGTRCLCLPGFSGPRCQQGSGHGIAESDWHLEGSGGNDAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS	chr1:21822244-21937310[-]	"Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development.; FUNCTION: Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6.; FUNCTION: The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity."	PDB: 3SH4; PDB: 3SH5	HGNC:5273	PGBM_HUMAN	Reviewed	ENSG00000142798	.	.	.	.	.
Mol00557	Protein	Prostaglandin G/H synthase 2 (PTGS2)	Cyclooxygenase-2; COX-2; PHS II; Prostaglandin H2 synthase 2; PGH synthase 2; PGHS-2; Prostaglandin-endoperoxide synthase 2; COX2	PTGS2	5743	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367468.10, PTGS2-201, 4510; ENST00000680451.1, PTGS2-205, 4709; ENST00000681605.1, PTGS2-206, 4506; ENST00000559627.1, PTGS2-204, 1705; ENST00000490885.6, PTGS2-203, 3690; ENST00000466691.1, PTGS2-202, 888"	MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGFQIINTASIQSLICNNVKGCPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKERSTEL	chr1:186671791-186680922[-]	"Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia."	PDB: 5F19; PDB: 5F1A; PDB: 5IKQ; PDB: 5IKR; PDB: 5IKT; PDB: 5IKV; PDB: 5KIR	HGNC:9605	PGH2_HUMAN	Reviewed	ENSG00000073756	.	.	.	.	.
Mol00558	Protein	Phosphoglycerate kinase 1 (PGK1)	Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2; PGKA; MIG10; OK/SW-cl.110	PGK1	5230	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373316.5, PGK1-201, 4812; ENST00000644362.1, PGK1-206, 2405; ENST00000476531.1, PGK1-203, 960; ENST00000491291.1, PGK1-205, 702; ENST00000477335.5, PGK1-204, 353; ENST00000474281.1, PGK1-202, 307"	MSLSNKLTLDKLDVKGKRVVMRVDFNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI	chrX:77910739-78129295[+]	"Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility."	PDB: 2WZB; PDB: 2WZC; PDB: 2WZD; PDB: 2X13; PDB: 2X14; PDB: 2X15; PDB: 2XE6; PDB: 2XE7; PDB: 2XE8; PDB: 2Y3I; PDB: 2YBE; PDB: 2ZGV; PDB: 3C39; PDB: 3C3A; PDB: 3C3B; PDB: 3C3C; PDB: 3ZOZ; PDB: 4AXX; PDB: 4O33; PDB: 5M1R; PDB: 5M3U; PDB: 5M6Z; PDB: 5MXM; PDB: 5NP8; PDB: 5O7D	HGNC:8896	PGK1_HUMAN	Reviewed	ENSG00000102144	.	.	.	.	.
Mol00559	Protein	PH domain leucine-rich repeat-containing protein phosphatase 2 (PHLPP2)	PH domain leucine-rich repeat-containing protein phosphatase-like; PHLPP-like; KIAA0931; PHLPPL	PHLPP2	23035	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000568954.5, PHLPP2-206, 8317; ENST00000393524.6, PHLPP2-201, 8467; ENST00000567016.1, PHLPP2-204, 4812; ENST00000568004.5, PHLPP2-205, 3099; ENST00000564884.5, PHLPP2-203, 2077; ENST00000538126.5, PHLPP2-202, 3485; ENST00000574977.1, PHLPP2-207, 547"	MKRNGSRNCLNRRSRFGSRERDWLREDVKRGCVYLYGADTTTATTTTTTSSSSSSSSSSSDLHLVLCTVETPASEICAGEGRESLYLQLHGDLVRRLEPTERPLQIVYDYLSRLGFDDPVRIQEEATNPDLGCMIRFYGEKPCHMDRLDRILLSGIYNVRKGKTQLHKWAERLVVLCGTCLIVSSVKDCQTGKMHILPLVGGKIEEVKRRQYSLAFSSAGAQAQTYHVSFETLAEYQRWQRQASKVVSQRISTVDLSCYSLEEVPEHLFYSQDITYLNLRHNFMQLERPGGLDTLYKFSQLKGLNLSHNKLGLFPILLCEISTLTELNLSCNGFHDLPSQIGNLLNLQTLCLDGNFLTTLPEELGNLQQLSSLGISFNNFSQIPEVYEKLTMLDRVVMAGNCLEVLNLGVLNRMNHIKHVDLRMNHLKTMVIENLEGNKHITHVDLRDNRLTDLDLSSLCSLEQLHCGRNQLRELTLSGFSLRTLYASSNRLTAVNVYPVPSLLTFLDLSRNLLECVPDWACEAKKIEVLDVSYNLLTEVPVRILSSLSLRKLMLGHNHVQNLPTLVEHIPLEVLDLQHNALTRLPDTLFSKALNLRYLNASANSLESLPSACTGEESLSMLQLLYLTNNLLTDQCIPVLVGHLHLRILHLANNQLQTFPASKLNKLEQLEELNLSGNKLKTIPTTIANCKRLHTLVAHSNNISIFPEILQLPQIQFVDLSCNDLTEILIPEALPATLQDLDLTGNTNLVLEHKTLDIFSHITTLKIDQKPLPTTDSTVTSTFWSHGLAEMAGQRNKLCVSALAMDSFAEGVGAVYGMFDGDRNEELPRLLQCTMADVLLEEVQQSTNDTVFMANTFLVSHRKLGMAGQKLGSSALLCYIRPDTADPASSFSLTVANVGTCQAVLCRGGKPVPLSKVFSLEQDPEEAQRVKDQKAIITEDNKVNGVTCCTRMLGCTYLYPWILPKPHISSTPLTIQDELLILGNKALWEHLSYTEAVNAVRHVQDPLAAAKKLCTLAQSYGCQDNVGAMVVYLNIGEEGCTCEMNGLTLPGPVGFASTTTIKDAPKPATPSSSSGIASEFSSEMSTSEVSSEVGSTASDEHNAGGLDTALLPRPERRCSLHPTPTSGLFQRQPSSATFSSNQSDNGLDSDDDQPVEGVITNGSKVEVEVDIHCCRGRDLENSPPLIESSPTLCSEEHARGSCFGIRRQNSVNSGMLLPMSKDRMELQKSPSTSCLYGKKLSNGSIVPLEDSLNLIEVATEVPKRKTGYFAAPTQMEPEDQFVVPHDLEEEVKEQMKQHQDSRLEPEPHEEDRTEPPEEFDTAL	chr16:71637835-71724701[-]	"Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser-657' of PRKCA. Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis. Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation. Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates RAF1 inhibiting its kinase activity."	.	HGNC:29149	PHLP2_HUMAN	Reviewed	ENSG00000040199	.	.	.	.	.
Mol00560	Protein	E3 SUMO-protein ligase PIAS3 (PIAS3)	E3 SUMO-protein transferase PIAS3; Protein inhibitor of activated STAT protein 3	PIAS3	10401	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393045.7, PIAS3-203, 2902; ENST00000369298.5, PIAS3-201, 2761; ENST00000393046.3, PIAS3-204, 952; ENST00000463514.2, PIAS3-205, 429; ENST00000475261.1, PIAS3-207, 2679; ENST00000472114.5, PIAS3-206, 2386; ENST00000369299.7, PIAS3-202, 1235; ENST00000498436.2, PIAS3-209, 1142; ENST00000484423.5, PIAS3-208, 1042"	MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPGPLAPIPPTLLAPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQVQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTSLRVSLMCPLGKMRLTVPCRALTCAHLQSFDAALYLQMNEKKPTWTCPVCDKKAPYESLIIDGLFMEILSSCSDCDEIQFMEDGSWCPMKPKKEASEVCPPPGYGLDGLQYSPVQGGDPSENKKKVEVIDLTIESSSDEEDLPPTKKHCSVTSAAIPALPGSKGVLTSGHQPSSVLRSPAMGTLGGDFLSSLPLHEYPPAFPLGADIQGLDLFSFLQTESQHYGPSVITSLDEQDALGHFFQYRGTPSHFLGPLAPTLGSSHCSATPAPPPGRVSSIVAPGGALREGHGGPLPSGPSLTGCRSDIISLD	chr1:145848522-145859836[-]	"Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pathway. Involved in regulating STAT3 signaling via inhibiting STAT3 DNA-binding and suppressing cell growth. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Sumoylates CCAR2 which promotes its interaction with SIRT1. Diminishes the sumoylation of ZFHX3 by preventing the colocalization of ZFHX3 with SUMO1 in the nucleus."	PDB: 4MVT	HGNC:16861	PIAS3_HUMAN	Reviewed	ENSG00000131788	.	.	.	.	.
Mol00561	Protein	Piwi-like protein 2 (PIWIL2)	Cancer/testis antigen 80; CT80; HILI	PIWIL2	55124	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356766.11, PIWIL2-201, 5114; ENST00000521356.5, PIWIL2-204, 3488; ENST00000454009.6, PIWIL2-202, 3442; ENST00000611073.1, PIWIL2-205, 2864; ENST00000519884.1, PIWIL2-203, 1262"	MDPFRPSFRGQSPIHPSQCQAVRMPGCWPQASKPLDPALGRGAPAGRGHVFGKPEEPSTQRGPAQRESVGLVSMFRGLGIETVSKTPLKREMLPSGRGILGRGLSANLVRKDREELSPTFWDPKVLAAGDSKMAETSVGWSRTLGRGSSDASLLPLGRAAGGISREVDKPPCTFSTPSRGPPQLSSPPALPQSPLHSPDRPLVLTVEHKEKELIVKQGSKGTPQSLGLNLVKIQCHNEAVYQYHVTFSPNVECKSMRFGMLKDHQAVTGNVTAFDGSILYLPVKLQQVLELKSQRKTDSAEISIKIQMTKILEPCSDLCIPFYNVVFRRVMKLLDMKLVGRNFYDPTSAMVLQQHRLQIWPGYAASIRRTDGGLFLLADVSHKVIRNDCVLDVMHAIYQQNKEHFQDECTKLLVGNIVITRYNNRTYRIDDVDWNKTPKDSFTMSDGKEITFLEYYSKNYGITVKEEDQPLLIHRPSERQDNHGMLLKGEILLLPELSFMTGIPEKMKKDFRAMKDLAQQINLSPKQHHSALECLLQRIAKNEAATNELMRWGLRLQKDVHKIEGRVLPMERINLKNTSFITSQELNWVKEVTRDPSILTIPMHFWALFYPKRAMDQARELVNMLEKIAGPIGMRMSPPAWVELKDDRIETYVRTIQSTLGAEGKIQMVVCIIMGPRDDLYGAIKKLCCVQSPVPSQVVNVRTIGQPTRLRSVAQKILLQINCKLGGELWGVDIPLKQLMVIGMDVYHDPSRGMRSVVGFVASINLTLTKWYSRVVFQMPHQEIVDSLKLCLVGSLKKFYEVNHCLPEKIVVYRDGVSDGQLKTVANYEIPQLQKCFEAFENYQPKMVVFVVQKKISTNLYLAAPQNFVTPTPGTVVDHTITSCEWVDFYLLAHHVRQGCGIPTHYVCVLNTANLSPDHMQRLTFKLCHMYWNWPGTIRVPAPCKYAHKLAFLSGHILHHEPAIQLCENLFFL	chr8:22275316-22357568[+]	"Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermatogonial stem cells. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' PIWIL4. PIWIL2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded. Required for PIWIL4/MIWI2 nuclear localization and association with secondary piRNAs antisense. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Indirectly modulates expression of genes such as PDGFRB, SLC2A1, ITGA6, GJA7, THY1, CD9 and STRA8. When overexpressed, acts as an oncogene by inhibition of apoptosis and promotion of proliferation in tumors. Represses circadian rhythms by promoting the stability and activity of core clock components ARNTL/BMAL1 and CLOCK by inhibiting GSK3B-mediated phosphorylation and ubiquitination-dependent degradation of these proteins."	PDB: 3O7X; PDB: 3QIR	HGNC:17644	PIWL2_HUMAN	Reviewed	ENSG00000197181	.	.	.	.	.
Mol00562	Protein	PI3-kinase alpha (PIK3CA)	PI3-kinase subunit alpha; PI3K-alpha; PI3Kalpha; PtdIns-3-kinase subunit alpha; Phosphatidylinositol 4;5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha; PtdIns-3-kinase subunit p110-alpha; p110alpha; Phosphoinositide 3-kinase alpha; Phosphoinositide-3-kinase catalytic alpha polypeptide; Serine/threonine protein kinase PIK3CA	PIK3CA	5290	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263967.4, PIK3CA-201, 9259; ENST00000643187.1, PIK3CA-205, 4130; ENST00000468036.1, PIK3CA-203, 620; ENST00000477735.1, PIK3CA-204, 245; ENST00000675786.1, PIK3CA-209, 4148; ENST00000674622.1, PIK3CA-207, 2348; ENST00000675467.1, PIK3CA-208, 7021; ENST00000674534.1, PIK3CA-206, 4835; ENST00000675796.1, PIK3CA-210, 3845; ENST00000462255.2, PIK3CA-202, 2882"	MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLITIKHELFKEARKYPLHQLLQDESSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFAIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPMDCFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHAGLSNRLARDNELRENDKEQLKAISTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRGFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRRPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQECTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFMKQMNDAHHGGWTTKMDWIFHTIKQHALN	chr3:179148114-179240093[+]	"Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. In addition to its lipid kinase activity, it displays a serine-protein kinase activity that results in the autophosphorylation of the p85alpha regulatory subunit as well as phosphorylation of other proteins such as 4EBP1, H-Ras, the IL-3 beta c receptor and possibly others. Plays a role in the positive regulation of phagocytosis and pinocytosis."	.	HGNC:8975	PK3CA_HUMAN	Reviewed	ENSG00000121879	.	.	.	.	.
Mol00563	Protein	PI3-kinase delta (PIK3CD)	PI3-kinase subunit delta; PI3K-delta; PI3Kdelta; PtdIns-3-kinase subunit delta; Phosphatidylinositol 4;5-bisphosphate 3-kinase 110 kDa catalytic subunit delta; PtdIns-3-kinase subunit p110-delta; p110delta	PIK3CD	5293	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377346.9, PIK3CD-202, 5412; ENST00000628140.2, PIK3CD-206, 5483; ENST00000361110.6, PIK3CD-201, 3508; ENST00000484851.1, PIK3CD-205, 515; ENST00000479223.1, PIK3CD-203, 539; ENST00000481137.1, PIK3CD-204, 386"	MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ	chr1:9651731-9729114[+]	"Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Plays a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Plays important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity."	PDB: 5DXU; PDB: 5M6U; PDB: 5T8F; PDB: 5UBT; PDB: 5VLR; PDB: 6G6W; PDB: 6OCO; PDB: 6OCU; PDB: 6PYR; PDB: 6PYU; PDB: 7JIS; PDB: 7LM2	HGNC:8977	PK3CD_HUMAN	Reviewed	ENSG00000171608	.	.	.	.	.
Mol00564	Protein	Polycystin-2 (PKD2)	PC2; Autosomal dominant polycystic kidney disease type II protein; Polycystic kidney disease 2 protein; Polycystwin; R48321; Transient receptor potential cation channel subfamily P member 2; TRPP2	PKD2	5311	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000237596.7, PKD2-201, 5089; ENST00000508588.5, PKD2-205, 1720; ENST00000502363.1, PKD2-202, 1222; ENST00000511337.5, PKD2-206, 1362; ENST00000512858.1, PKD2-207, 1554; ENST00000506367.1, PKD2-203, 693; ENST00000506727.1, PKD2-204, 550"	MVNSSRVQPQQPGDAKRPPAPRAPDPGRLMAGCAAVGASLAAPGGLCEQRGLEIEMQRIRQAAARDPPAGAAASPSPPLSSCSRQAWSRDNPGFEAEEEEEEVEGEEGGMVVEMDVEWRPGSRRSAASSAVSSVGARSRGLGGYHGAGHPSGRRRRREDQGPPCPSPVGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESSTNREKYLKSVLRELVTYLLFLIVLCILTYGMMSSNVYYYTRMMSQLFLDTPVSKTEKTNFKTLSSMEDFWKFTEGSLLDGLYWKMQPSNQTEADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGTRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQNTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKNTVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRDDLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEIHREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGGNGSSNVHV	chr4:88007635-88077777[+]	"Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel. Functions as a cation channel involved in fluid-flow mechanosensation by the primary cilium in renal epithelium. Functions as outward-rectifying K(+) channel, but is also permeable to Ca(2+), and to a much lesser degree also to Na(+). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum. Together with TRPV4, forms mechano- and thermosensitive channels in cilium. PKD1 and PKD2 may function through a common signaling pathway that is necessary to maintain the normal, differentiated state of renal tubule cells. Acts as a regulator of cilium length, together with PKD1. The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling. The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling. Also involved in left-right axis specification via its role in sensing nodal flow; forms a complex with PKD1L1 in cilia to facilitate flow detection in left-right patterning. Detection of asymmetric nodal flow gives rise to a Ca(2+) signal that is required for normal, asymmetric expression of genes involved in the specification of body left-right laterality."	PDB: 2KLD; PDB: 2KLE; PDB: 2KQ6; PDB: 2Y4Q; PDB: 3HRN; PDB: 3HRO; PDB: 5K47; PDB: 5MKE; PDB: 5MKF; PDB: 5T4D; PDB: 6A70; PDB: 6D1W; PDB: 6T9N; PDB: 6T9O; PDB: 6WB8	HGNC:9009	PKD2_HUMAN	Reviewed	ENSG00000118762	.	.	.	.	.
Mol00565	Protein	Zinc finger protein PLAG1 (PLAG1)	Pleiomorphic adenoma gene 1 protein	PLAG1	5324	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000316981.8, PLAG1-201, 7311; ENST00000429357.2, PLAG1-203, 1899; ENST00000423799.6, PLAG1-202, 1684; ENST00000519027.1, PLAG1-204, 435; ENST00000522009.1, PLAG1-205, 2163"	MATVIPGDLSEVRDTQKVPSGKRKRGETKPRKNFPCQLCDKAFNSVEKLKVHSYSHTGERPYKCIQQDCTKAFVSKYKLQRHMATHSPEKTHKCNYCEKMFHRKDHLKNHLHTHDPNKETFKCEECGKNYNTKLGFKRHLALHAATSGDLTCKVCLQTFESTGVLLEHLKSHAGKSSGGVKEKKHQCEHCDRRFYTRKDVRRHMVVHTGRKDFLCQYCAQRFGRKDHLTRHMKKSHNQELLKVKTEPVDFLDPFTCNVSVPIKDELLPVMSLPSSELLSKPFTNTLQLNLYNTPFQSMQSSGSAHQMITTLPLGMTCPIDMDTVHPSHHLSFKYPFSSTSYAISIPEKEQPLKGEIESYLMELQGGVPSSSQDSQASSSSKLGLDPQIGSLDDGAGDLSLSKSSISISDPLNTPALDFSQLFNFIPLNGPPYNPLSVGSLGMSYSQEEAHSSVSQLPPQTQDLQDPANTIGLGSLHSLSAAFTSSLSTSTTLPRFHQAFQ	chr8:56160909-56211324[-]	"Transcription factor whose activation results in up-regulation of target genes, such as IGFII, leading to uncontrolled cell proliferation: when overexpressed in cultured cells, higher proliferation rate and transformation are observed. Other target genes such as CRLF1, CRABP2, CRIP2, PIGF are strongly induced in cells with PLAG1 induction. Proto-oncogene whose ectopic expression can trigger the development of pleomorphic adenomas of the salivary gland and lipoblastomas. Overexpression is associated with up-regulation of IGFII, is frequently observed in hepatoblastoma, common primary liver tumor in childhood. Cooperates with CBFB-MYH11, a fusion gene important for myeloid leukemia."	.	HGNC:9045	PLAG1_HUMAN	Reviewed	ENSG00000181690	.	.	.	.	.
Mol00566	Protein	Lysophosphatidic acid acyltransferase beta (AGPAT2)	1-acylglycerol-3-phosphate O-acyltransferase 2; 1-AGP acyltransferase 2; 1-AGPAT 2; Lysophosphatidic acid acyltransferase beta; LPAAT-beta	AGPAT2	10555	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371696.7, AGPAT2-202, 1546; ENST00000371694.7, AGPAT2-201, 1391; ENST00000538402.1, AGPAT2-205, 1357; ENST00000472820.1, AGPAT2-204, 808; ENST00000470861.1, AGPAT2-203, 720"	MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENMSIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAKRELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGDLLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAADVPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ	chr9:136673143-136687457[-]	"Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone."	.	HGNC:325	PLCB_HUMAN	Reviewed	ENSG00000169692	.	.	.	.	.
Mol00567	Protein	Phosphoinositide phospholipase C-gamma-2 (PLCG2)	Phosphoinositide phospholipase C-gamma-2; Phospholipase C-IV; PLC-IV; Phospholipase C-gamma-2; PLC-gamma-2	PLCG2	5336	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000564138.6, PLCG2-206, 8666; ENST00000563193.1, PLCG2-202, 1282; ENST00000565054.5, PLCG2-208, 912; ENST00000563375.1, PLCG2-204, 454; ENST00000565400.5, PLCG2-209, 823; ENST00000569523.1, PLCG2-213, 575; ENST00000562605.5, PLCG2-201, 556; ENST00000563834.1, PLCG2-205, 260; ENST00000567980.5, PLCG2-212, 2892; ENST00000569929.5, PLCG2-214, 1051; ENST00000567373.5, PLCG2-211, 840; ENST00000567356.1, PLCG2-210, 581; ENST00000565020.1, PLCG2-207, 566; ENST00000570198.1, PLCG2-216, 563; ENST00000570196.1, PLCG2-215, 551; ENST00000563269.1, PLCG2-203, 539"	MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADKIEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAVNWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSAKFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASAVYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENSIWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDCWDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKAFKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGELYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKRTSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYYLTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDMLMRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYYEKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDYKAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQIIEDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGDPPVEFATDRVEELFEWFQSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVETKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKYMQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSIACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEEDMFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSCRQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSNSKFYS	chr16:81739097-81962685[+]	"The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling."	PDB: 2K2J; PDB: 2W2W; PDB: 2W2X	HGNC:9066	PLCG2_HUMAN	Reviewed	ENSG00000197943	.	.	.	.	.
Mol00568	Protein	Serine/threonine-protein kinase PLK1 (PLK1)	Polo-like kinase 1; PLK-1; Serine/threonine-protein kinase 13; STPK13; PLK	PLK1	5347	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000300093.9, PLK1-201, 2160; ENST00000567897.6, PLK1-207, 711; ENST00000568568.1, PLK1-208, 582; ENST00000570220.5, PLK1-209, 910; ENST00000564202.1, PLK1-204, 584; ENST00000562272.5, PLK1-202, 4135; ENST00000564794.1, PLK1-205, 683; ENST00000564947.1, PLK1-206, 553; ENST00000562407.1, PLK1-203, 540"	MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS	chr16:23677656-23690367[+]	"Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis. Polo-like kinase proteins acts by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins. Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains. Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation. Promotes the central spindle recruitment of ECT2. Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase. Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity. Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation. Required for kinetochore localization of BUB1B. Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function. Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome. Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53. Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA. Contributes to the regulation of AURKA function. Also required for recovery after DNA damage checkpoint and entry into mitosis. Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning. Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage. Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope. Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock. Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression. Regulates mitotic progression by phosphorylating RIOK2. Through the phosphorylation of DZIP1 regulates the localization during mitosis of the BBSome, a ciliary protein complex involved in cilium biogenesis."	PDB: 1Q4K; PDB: 1Q4O; PDB: 1UMW; PDB: 2OGQ; PDB: 2OJX; PDB: 2OU7; PDB: 2OWB; PDB: 2RKU; PDB: 2V5Q; PDB: 2YAC; PDB: 3BZI; PDB: 3C5L; PDB: 3FC2; PDB: 3FVH; PDB: 3HIH; PDB: 3HIK; PDB: 3KB7; PDB: 3P2W; PDB: 3P2Z; PDB: 3P34; PDB: 3P35; PDB: 3P36; PDB: 3P37; PDB: 3Q1I; PDB: 3RQ7; PDB: 3THB; PDB: 4A4L; PDB: 4A4O; PDB: 4DFW; PDB: 4E67; PDB: 4E9C; PDB: 4E9D; PDB: 4H5X; PDB: 4H71; PDB: 4HAB; PDB: 4HCO; PDB: 4HY2; PDB: 4J52; PDB: 4J53; PDB: 4LKL; PDB: 4LKM; PDB: 4O56; PDB: 4O6W; PDB: 4O9W; PDB: 4RCP; PDB: 4WHH; PDB: 4WHK; PDB: 4WHL; PDB: 4X9R; PDB: 4X9V; PDB: 4X9W; PDB: 5J19; PDB: 5NEI; PDB: 5NFU; PDB: 5NJE; PDB: 5NMM; PDB: 5NN1; PDB: 5NN2; PDB: 5TA6; PDB: 5TA8; PDB: 6AX4; PDB: 6GY2	HGNC:9077	PLK1_HUMAN	Reviewed	ENSG00000166851	.	.	.	.	.
Mol00569	Protein	Proteasome maturation protein (POMP)	Proteassemblin; Protein UMP1 homolog; hUMP1; Voltage-gated K channel beta subunit 4.1; C13orf12; UMP1; HSPC014; HSPC036; PNAS-110	POMP	51371	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000380842.5, POMP-201, 1338; ENST00000460403.1, POMP-202, 1428"	MNARGLGSELKDSIPVTELSASGPFESHDLLRKGFSCVKNELLPSHPLELSEKNFQLNQDKMNFSTLRNIQGLFAPLKLQMEFKAVQQVQRLPFLSSSNLSLDVLRGNDETIGFEDILNDPSQSEVMGEPHLMVEYKLGLL	chr13:28659104-28678959[+]	Molecular chaperone essential for the assembly of standard proteasomes and immunoproteasomes. Degraded after completion of proteasome maturation. Mediates the association of 20S preproteasome with the endoplasmic reticulum.	.	HGNC:20330	POMP_HUMAN	Reviewed	ENSG00000132963	.	.	.	.	.
Mol00570	Protein	Peroxisome proliferator-activated receptor alpha (PPARA)	PPAR-alpha; Nuclear receptor subfamily 1 group C member 1; NR1C1; PPAR	PPARA	5465	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000407236.6, PPARA-202, 10118; ENST00000402126.1, PPARA-201, 1558; ENST00000420804.5, PPARA-204, 572; ENST00000415785.5, PPARA-203, 531; ENST00000440343.5, PPARA-205, 368; ENST00000481567.5, PPARA-207, 567; ENST00000496865.1, PPARA-210, 449; ENST00000460086.1, PPARA-206, 433; ENST00000484619.1, PPARA-208, 278; ENST00000493286.1, PPARA-209, 1564; ENST00000624793.1, PPARA-211, 1556"	MVDTESPLCPLSPLEAGDLESPLSEEFLQEMGNIQEISQSIGEDSSGSFGFTEYQYLGSCPGSDGSVITDTLSPASSPSSVTYPVVPGSVDESPSGALNIECRICGDKASGYHYGVHACEGCKGFFRRTIRLKLVYDKCDRSCKIQKKNRNKCQYCRFHKCLSVGMSHNAIRFGRMPRSEKAKLKAEILTCEHDIEDSETADLKSLAKRIYEAYLKNFNMNKVKARVILSGKASNNPPFVIHDMETLCMAEKTLVAKLVANGIQNKEAEVRIFHCCQCTSVETVTELTEFAKAIPGFANLDLNDQVTLLKYGVYEAIFAMLSSVMNKDGMLVAYGNGFITREFLKSLRKPFCDIMEPKFDFAMKFNALELDDSDISLFVAAIICCGDRPGLLNVGHIEKMQEGIVHVLRLHLQSNHPDDIFLFPKLLQKMADLRQLVTEHAQLVQIIKKTESDAALHPLLQEIYRDMY	chr22:46150521-46243755[+]	"Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2."	PDB: 1I7G; PDB: 1K7L; PDB: 1KKQ; PDB: 2NPA; PDB: 2P54; PDB: 2REW; PDB: 2ZNN; PDB: 3ET1; PDB: 3FEI; PDB: 3G8I; PDB: 3KDT; PDB: 3KDU; PDB: 3SP6; PDB: 3VI8; PDB: 4BCR; PDB: 4CI4; PDB: 5AZT; PDB: 5HYK; PDB: 6KAX; PDB: 6KAY; PDB: 6KAZ; PDB: 6KB0; PDB: 6KB1; PDB: 6KB2; PDB: 6KB3; PDB: 6KB4; PDB: 6KB5; PDB: 6KB6; PDB: 6KB7; PDB: 6KB8; PDB: 6KB9; PDB: 6KBA; PDB: 6KXX; PDB: 6KXY; PDB: 6KYP; PDB: 6L36; PDB: 6L37; PDB: 6L38; PDB: 6L96; PDB: 6LX4; PDB: 6LX5; PDB: 6LX6; PDB: 6LX7; PDB: 6LX8; PDB: 6LX9; PDB: 6LXA; PDB: 6LXB; PDB: 6LXC; PDB: 7BPY; PDB: 7BPZ; PDB: 7BQ0; PDB: 7BQ1; PDB: 7BQ2; PDB: 7BQ3; PDB: 7BQ4; PDB: 7C6Q; PDB: 7E5F; PDB: 7E5G; PDB: 7E5H; PDB: 7E5I	HGNC:9232	PPARA_HUMAN	Reviewed	ENSG00000186951	.	.	.	.	.
Mol00571	Protein	DNA-dependent catalytic protein kinase (PRKDC)	DNA-PK catalytic subunit; DNA-PKcs; DNPK1; p460; HYRC; HYRC1	PRKDC	5591	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000314191.7, PRKDC-201, 13459; ENST00000338368.7, PRKDC-202, 12784; ENST00000536429.1, PRKDC-206, 659; ENST00000540819.1, PRKDC-209, 537; ENST00000521331.5, PRKDC-204, 1087; ENST00000536483.1, PRKDC-207, 834; ENST00000541488.1, PRKDC-210, 719; ENST00000546304.1, PRKDC-211, 589; ENST00000432581.2, PRKDC-203, 583; ENST00000536710.1, PRKDC-208, 554; ENST00000535375.1, PRKDC-205, 464"	MAGSGAGVRCSLLRLQETLSAADRCGAALAGHQLIRGLGQECVLSSSPAVLALQTSLVFSRDFGLLVFVRKSLNSIEFRECREEILKFLCIFLEKMGQKIAPYSVEIKNTCTSVYTKDRAAKCKIPALDLLIKLLQTFRSSRLMDEFKIGELFSKFYGELALKKKIPDTVLEKVYELLGLLGEVHPSEMINNAENLFRAFLGELKTQMTSAVREPKLPVLAGCLKGLSSLLCNFTKSMEEDPQTSREIFNFVLKAIRPQIDLKRYAVPSAGLRLFALHASQFSTCLLDNYVSLFEVLLKWCAHTNVELKKAALSALESFLKQVSNMVAKNAEMHKNKLQYFMEQFYGIIRNVDSNNKELSIAIRGYGLFAGPCKVINAKDVDFMYVELIQRCKQMFLTQTDTGDDRVYQMPSFLQSVASVLLYLDTVPEVYTPVLEHLVVMQIDSFPQYSPKMQLVCCRAIVKVFLALAAKGPVLRNCISTVVHQGLIRICSKPVVLPKGPESESEDHRASGEVRTGKWKVPTYKDYVDLFRHLLSSDQMMDSILADEAFFSVNSSSESLNHLLYDEFVKSVLKIVEKLDLTLEIQTVGEQENGDEAPGVWMIPTSDPAANLHPAKPKDFSAFINLVEFCREILPEKQAEFFEPWVYSFSYELILQSTRLPLISGFYKLLSITVRNAKKIKYFEGVSPKSLKHSPEDPEKYSCFALFVKFGKEVAVKMKQYKDELLASCLTFLLSLPHNIIELDVRAYVPALQMAFKLGLSYTPLAEVGLNALEEWSIYIDRHVMQPYYKDILPCLDGYLKTSALSDETKNNWEVSALSRAAQKGFNKVVLKHLKKTKNLSSNEAISLEEIRIRVVQMLGSLGGQINKNLLTVTSSDEMMKSYVAWDREKRLSFAVPFREMKPVIFLDVFLPRVTELALTASDRQTKVAACELLHSMVMFMLGKATQMPEGGQGAPPMYQLYKRTFPVLLRLACDVDQVTRQLYEPLVMQLIHWFTNNKKFESQDTVALLEAILDGIVDPVDSTLRDFCGRCIREFLKWSIKQITPQQQEKSPVNTKSLFKRLYSLALHPNAFKRLGASLAFNNIYREFREEESLVEQFVFEALVIYMESLALAHADEKSLGTIQQCCDAIDHLCRIIEKKHVSLNKAKKRRLPRGFPPSASLCLLDLVKWLLAHCGRPQTECRHKSIELFYKFVPLLPGNRSPNLWLKDVLKEEGVSFLINTFEGGGCGQPSGILAQPTLLYLRGPFSLQATLCWLDLLLAALECYNTFIGERTVGALQVLGTEAQSSLLKAVAFFLESIAMHDIIAAEKCFGTGAAGNRTSPQEGERYNYSKCTVVVRIMEFTTTLLNTSPEGWKLLKKDLCNTHLMRVLVQTLCEPASIGFNIGDVQVMAHLPDVCVNLMKALKMSPYKDILETHLREKITAQSIEELCAVNLYGPDAQVDRSRLAAVVSACKQLHRAGLLHNILPSQSTDLHHSVGTELLSLVYKGIAPGDERQCLPSLDLSCKQLASGLLELAFAFGGLCERLVSLLLNPAVLSTASLGSSQGSVIHFSHGEYFYSLFSETINTELLKNLDLAVLELMQSSVDNTKMVSAVLNGMLDQSFRERANQKHQGLKLATTILQHWKKCDSWWAKDSPLETKMAVLALLAKILQIDSSVSFNTSHGSFPEVFTTYISLLADTKLDLHLKGQAVTLLPFFTSLTGGSLEELRRVLEQLIVAHFPMQSREFPPGTPRFNNYVDCMKKFLDALELSQSPMLLELMTEVLCREQQHVMEELFQSSFRRIARRGSCVTQVGLLESVYEMFRKDDPRLSFTRQSFVDRSLLTLLWHCSLDALREFFSTIVVDAIDVLKSRFTKLNESTFDTQITKKMGYYKILDVMYSRLPKDDVHAKESKINQVFHGSCITEGNELTKTLIKLCYDAFTENMAGENQLLERRRLYHCAAYNCAISVICCVFNELKFYQGFLFSEKPEKNLLIFENLIDLKRRYNFPVEVEVPMERKKKYIEIRKEAREAANGDSDGPSYMSSLSYLADSTLSEEMSQFDFSTGVQSYSYSSQDPRPATGRFRRREQRDPTVHDDVLELEMDELNRHECMAPLTALVKHMHRSLGPPQGEEDSVPRDLPSWMKFLHGKLGNPIVPLNIRLFLAKLVINTEEVFRPYAKHWLSPLLQLAASENNGGEGIHYMVVEIVATILSWTGLATPTGVPKDEVLANRLLNFLMKHVFHPKRAVFRHNLEIIKTLVECWKDCLSIPYRLIFEKFSGKDPNSKDNSVGIQLLGIVMANDLPPYDPQCGIQSSEYFQALVNNMSFVRYKEVYAAAAEVLGLILRYVMERKNILEESLCELVAKQLKQHQNTMEDKFIVCLNKVTKSFPPLADRFMNAVFFLLPKFHGVLKTLCLEVVLCRVEGMTELYFQLKSKDFVQVMRHRDDERQKVCLDIIYKMMPKLKPVELRELLNPVVEFVSHPSTTCREQMYNILMWIHDNYRDPESETDNDSQEIFKLAKDVLIQGLIDENPGLQLIIRNFWSHETRLPSNTLDRLLALNSLYSPKIEVHFLSLATNFLLEMTSMSPDYPNPMFEHPLSECEFQEYTIDSDWRFRSTVLTPMFVETQASQGTLQTRTQEGSLSARWPVAGQIRATQQQHDFTLTQTADGRSSFDWLTGSSTDPLVDHTSPSSDSLLFAHKRSERLQRAPLKSVGPDFGKKRLGLPGDEVDNKVKGAAGRTDLLRLRRRFMRDQEKLSLMYARKGVAEQKREKEIKSELKMKQDAQVVLYRSYRHGDLPDIQIKHSSLITPLQAVAQRDPIIAKQLFSSLFSGILKEMDKFKTLSEKNNITQKLLQDFNRFLNTTFSFFPPFVSCIQDISCQHAALLSLDPAAVSAGCLASLQQPVGIRLLEEALLRLLPAELPAKRVRGKARLPPDVLRWVELAKLYRSIGEYDVLRGIFTSEIGTKQITQSALLAEARSDYSEAAKQYDEALNKQDWVDGEPTEAEKDFWELASLDCYNHLAEWKSLEYCSTASIDSENPPDLNKIWSEPFYQETYLPYMIRSKLKLLLQGEADQSLLTFIDKAMHGELQKAILELHYSQELSLLYLLQDDVDRAKYYIQNGIQSFMQNYSSIDVLLHQSRLTKLQSVQALTEIQEFISFISKQGNLSSQVPLKRLLNTWTNRYPDAKMDPMNIWDDIITNRCFFLSKIEEKLTPLPEDNSMNVDQDGDPSDRMEVQEQEEDISSLIRSCKFSMKMKMIDSARKQNNFSLAMKLLKELHKESKTRDDWLVSWVQSYCRLSHCRSRSQGCSEQVLTVLKTVSLLDENNVSSYLSKNILAFRDQNILLGTTYRIIANALSSEPACLAEIEEDKARRILELSGSSSEDSEKVIAGLYQRAFQHLSEAVQAAEEEAQPPSWSCGPAAGVIDAYMTLADFCDQQLRKEEENASVIDSAELQAYPALVVEKMLKALKLNSNEARLKFPRLLQIIERYPEETLSLMTKEISSVPCWQFISWISHMVALLDKDQAVAVQHSVEEITDNYPQAIVYPFIISSESYSFKDTSTGHKNKEFVARIKSKLDQGGVIQDFINALDQLSNPELLFKDWSNDVRAELAKTPVNKKNIEKMYERMYAALGDPKAPGLGAFRRKFIQTFGKEFDKHFGKGGSKLLRMKLSDFNDITNMLLLKMNKDSKPPGNLKECSPWMSDFKVEFLRNELEIPGQYDGRGKPLPEYHVRIAGFDERVTVMASLRRPKRIIIRGHDEREHPFLVKGGEDLRQDQRVEQLFQVMNGILAQDSACSQRALQLRTYSVVPMTSRLGLIEWLENTVTLKDLLLNTMSQEEKAAYLSDPRAPPCEYKDWLTKMSGKHDVGAYMLMYKGANRTETVTSFRKRESKVPADLLKRAFVRMSTSPEAFLALRSHFASSHALICISHWILGIGDRHLNNFMVAMETGGVIGIDFGHAFGSATQFLPVPELMPFRLTRQFINLMLPMKETGLMYSIMVHALRAFRSDPGLLTNTMDVFVKEPSFDWKNFEQKMLKKGGSWIQEINVAEKNWYPRQKICYAKRKLAGANPAVITCDELLLGHEKAPAFRDYVAVARGSKDHNIRAQEPESGLSEETQVKCLMDQATDPNILGRTWEGWEPWM	chr8:47773111-47960178[-]	"Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). Recruited by XRCC5 and XRCC6 to DNA ends and is required to protect and align broken ends of DNA, thereby preventing their degradation, and sequester the DSB for repair by NHEJ. Act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. As part of the DNA-PK complex, involved in the early steps of ribosome assembly by promoting the processing of precursor rRNA into mature 18S rRNA in the small-subunit processome. Binding to U3 small nucleolar RNA, recruits PRKDC and XRCC5/Ku86 to the small-subunit processome. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, FH, SRF, NHEJ1/XLF, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate p53/TP53 in the presence of supercoiled DNA is dependent on C1D. Contributes to the determination of the circadian period length by antagonizing phosphorylation of CRY1 'Ser-588' and increasing CRY1 protein stability, most likely through an indirect mechanism. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway. Also regulates the cGAS-STING pathway by catalyzing phosphorylation of CGAS, thereby impairing CGAS oligomerization and activation."	PDB: 5LUQ; PDB: 5W1R; PDB: 5Y3R; PDB: 6ZFP; PDB: 6ZH2; PDB: 6ZH4; PDB: 6ZH6; PDB: 6ZH8; PDB: 6ZHA; PDB: 6ZHE; PDB: 7K0Y; PDB: 7K10; PDB: 7K11; PDB: 7K19; PDB: 7K1B; PDB: 7K1J; PDB: 7K1K; PDB: 7K1N; PDB: 7LT3; PDB: 7NFC; PDB: 7NFE	HGNC:9413	PRKDC_HUMAN	Reviewed	ENSG00000253729	.	.	.	.	.
Mol00572	Protein	Proteasome subunit beta type-5 (PSMB5)	Macropain epsilon chain; Multicatalytic endopeptidase complex epsilon chain; Proteasome chain 6; Proteasome epsilon chain; Proteasome subunit MB1; Proteasome subunit X; LMPX; MB1; X	PSMB5	5693	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361611.11, PSMB5-202, 1044; ENST00000493471.2, PSMB5-205, 1117; ENST00000425762.2, PSMB5-203, 900; ENST00000460922.2, PSMB5-204, 729; ENST00000555895.5, PSMB5-206, 444; ENST00000334454.10, PSMB5-201, 796"	MALASVLERPLPVNQRGFFGLGGRADLLDLGPGSLSDGLSLAAPGWGVPEEPGIEMLHGTTTLAFKFRHGVIVAADSRATAGAYIASQTVKKVIEINPYLLGTMAGGAADCSFWERLLARQCRIYELRNKERISVAAASKLLANMVYQYKGMGLSMGTMICGWDKRGPGLYYVDSEGNRISGATFSVGSGSVYAYGVMDRGYSYDLEVEQAYDLARRAIYQATYRDAYSGGAVNLYHVREDGWIRVSSDNVADLHEKYSGSTP	chr14:23016543-23035230[-]	"Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity."	PDB: 4R3O; PDB: 4R67; PDB: 5A0Q; PDB: 5GJQ; PDB: 5GJR; PDB: 5L4G; PDB: 5L5W; PDB: 5L5X; PDB: 5L5Y; PDB: 5L5Z; PDB: 5L60; PDB: 5L61; PDB: 5L62; PDB: 5L63; PDB: 5L64; PDB: 5LE5; PDB: 5LEX; PDB: 5LEY; PDB: 5LEZ; PDB: 5LF0; PDB: 5LF1; PDB: 5LF3; PDB: 5LF4; PDB: 5LF6; PDB: 5LF7; PDB: 5LN3; PDB: 5M32; PDB: 5T0C; PDB: 5T0G; PDB: 5T0H; PDB: 5T0I; PDB: 5T0J; PDB: 5VFO; PDB: 5VFP; PDB: 5VFQ; PDB: 5VFR; PDB: 5VFS; PDB: 5VFT; PDB: 5VFU; PDB: 6KWY; PDB: 6MSB; PDB: 6MSD; PDB: 6MSE; PDB: 6MSG; PDB: 6MSH; PDB: 6MSJ; PDB: 6MSK; PDB: 6R70; PDB: 6REY; PDB: 6RGQ; PDB: 6WJD; PDB: 6WJN; PDB: 6XMJ; PDB: 7LXV; PDB: 7NHT; PDB: 7PG9; PDB: 7V5G; PDB: 7V5M	HGNC:9542	PSB5_HUMAN	Reviewed	ENSG00000100804	.	.	.	.	.
Mol00573	Protein	Proteasome assembly chaperone 2 (PSMG2)	PAC-2; Hepatocellular carcinoma-susceptibility protein 3; Tumor necrosis factor superfamily member 5-induced protein 1; HCCA3; PAC2; TNFSF5IP1	PSMG2	56984	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000317615.11, PSMG2-201, 1070; ENST00000585331.6, PSMG2-204, 983; ENST00000590217.5, PSMG2-210, 1036; ENST00000586445.5, PSMG2-206, 646; ENST00000586587.1, PSMG2-207, 711; ENST00000400514.2, PSMG2-203, 471; ENST00000585853.2, PSMG2-205, 377; ENST00000589405.5, PSMG2-209, 328; ENST00000400512.1, PSMG2-202, 261; ENST00000588824.1, PSMG2-208, 794"	MFVPCGESAPDLAGFTLLMPAVSVGNVGQLAMDLIISTLNMSKIGYFYTDCLVPMVGNNPYATTEGNSTELSINAEVYSLPSRKLVALQLRSIFIKYKSKPFCEKLLSWVKSSGCARVIVLSSSHSYQRNDLQLRSTPFRYLLTPSMQKSVQNKIKSLNWEEMEKSRCIPEIDDSEFCIRIPGGGITKTLYDESCSKEIQMAVLLKFVSEGDNIPDALGLVEYLNEWLQILKPLSDDPTVSASRWKIPSSWRLLFGSGLPPALF	chr18:12658043-12725740[+]	"Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization."	.	HGNC:24929	PSMG2_HUMAN	Reviewed	ENSG00000128789	.	.	.	.	.
Mol00574	Protein	Presenilin-1 (PSEN1)	PS-1; Protein S182; PS1-CTF12; AD3; PS1; PSNL1	PSEN1	5663	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000324501.10, PSEN1-201, 6018; ENST00000394164.5, PSEN1-204, 3046; ENST00000357710.8, PSEN1-202, 2776; ENST00000406768.1, PSEN1-205, 4062; ENST00000394157.7, PSEN1-203, 1249; ENST00000557511.5, PSEN1-223, 1230; ENST00000555254.5, PSEN1-212, 754; ENST00000553719.5, PSEN1-208, 712; ENST00000560005.6, PSEN1-225, 699; ENST00000556066.1, PSEN1-216, 612; ENST00000553599.5, PSEN1-207, 591; ENST00000554131.5, PSEN1-210, 591; ENST00000557293.5, PSEN1-221, 576; ENST00000556864.5, PSEN1-218, 574; ENST00000557356.5, PSEN1-222, 571; ENST00000557037.5, PSEN1-220, 555; ENST00000556951.5, PSEN1-219, 552; ENST00000556533.5, PSEN1-217, 550; ENST00000556011.5, PSEN1-215, 442; ENST00000555386.5, PSEN1-213, 1484; ENST00000553855.5, PSEN1-209, 1254; ENST00000559361.5, PSEN1-224, 795; ENST00000553447.6, PSEN1-206, 572; ENST00000555867.1, PSEN1-214, 876; ENST00000554995.1, PSEN1-211, 592"	MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI	chr14:73136418-73223691[+]	"Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin). Under conditions of apoptosis or calcium influx, cleaves CDH1. This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling. Required for normal embryonic brain and skeleton development, and for normal angiogenesis. Mediates the proteolytic cleavage of EphB2/CTF1 into EphB2/CTF2. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is therefore involved in calcium homeostasis. Involved in the regulation of neurite outgrowth. Is a regulator of presynaptic facilitation, spike transmission and synaptic vesicles replenishment in a process that depends on gamma-secretase activity. It acts through the control of SYT7 presynaptic expression."	PDB: 2KR6; PDB: 4UIS; PDB: 5A63; PDB: 5FN2; PDB: 5FN3; PDB: 5FN4; PDB: 5FN5; PDB: 6IDF; PDB: 6IYC; PDB: 6LQG; PDB: 6LR4; PDB: 7C9I; PDB: 7D8X	HGNC:9508	PSN1_HUMAN	Reviewed	ENSG00000080815	.	.	.	.	.
Mol00575	Protein	Protein-tyrosine phosphatase 1B (PTPN1)	Protein-tyrosine phosphatase 1B; PTP-1B; PTP1B	PTPN1	5770	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371621.5, PTPN1-201, 3979; ENST00000541713.5, PTPN1-202, 3469"	MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNGKCREFFPNHQWVKEETQEDKDCPIKEEKGSPLNAAPYGIESMSQDTEVRSRVVGGSLRGAQAASPAKGEPSLPEKDEDHALSYWKPFLVNMCVATVLTAGAYLCYRFLFNSNT	chr20:50510321-50585241[+]	Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.	PDB: 1A5Y; PDB: 1AAX; PDB: 1BZC; PDB: 1BZH; PDB: 1BZJ; PDB: 1C83; PDB: 1C84; PDB: 1C85; PDB: 1C86; PDB: 1C87; PDB: 1C88; PDB: 1ECV; PDB: 1EEN; PDB: 1EEO; PDB: 1G1F; PDB: 1G1G; PDB: 1G1H; PDB: 1G7F; PDB: 1G7G; PDB: 1GFY; PDB: 1I57; PDB: 1JF7; PDB: 1KAK; PDB: 1KAV; PDB: 1L8G; PDB: 1LQF; PDB: 1NL9; PDB: 1NNY; PDB: 1NO6; PDB: 1NWE; PDB: 1NWL; PDB: 1NZ7; PDB: 1OEM; PDB: 1OEO; PDB: 1OES; PDB: 1OET; PDB: 1OEU; PDB: 1OEV; PDB: 1ONY; PDB: 1ONZ; PDB: 1PA1; PDB: 1PH0; PDB: 1PTT; PDB: 1PTU; PDB: 1PTV; PDB: 1PTY; PDB: 1PXH; PDB: 1PYN; PDB: 1Q1M; PDB: 1Q6J; PDB: 1Q6M; PDB: 1Q6N; PDB: 1Q6P; PDB: 1Q6S; PDB: 1Q6T; PDB: 1QXK; PDB: 1SUG; PDB: 1T48; PDB: 1T49; PDB: 1T4J; PDB: 1WAX; PDB: 1XBO; PDB: 2AZR; PDB: 2B07; PDB: 2B4S; PDB: 2BGD; PDB: 2BGE; PDB: 2CM2; PDB: 2CM3; PDB: 2CM7; PDB: 2CM8; PDB: 2CMA; PDB: 2CMB; PDB: 2CMC; PDB: 2CNE; PDB: 2CNF; PDB: 2CNG; PDB: 2CNH; PDB: 2CNI; PDB: 2F6F; PDB: 2F6T; PDB: 2F6V; PDB: 2F6W; PDB: 2F6Y; PDB: 2F6Z; PDB: 2F70; PDB: 2F71; PDB: 2FJM; PDB: 2FJN; PDB: 2H4G; PDB: 2H4K; PDB: 2HB1; PDB: 2HNP; PDB: 2HNQ; PDB: 2NT7; PDB: 2NTA; PDB: 2QBP; PDB: 2QBQ; PDB: 2QBR; PDB: 2QBS; PDB: 2VEU; PDB: 2VEV; PDB: 2VEW; PDB: 2VEX; PDB: 2VEY; PDB: 2ZMM; PDB: 2ZN7; PDB: 3A5J; PDB: 3A5K; PDB: 3CWE; PDB: 3D9C; PDB: 3EAX; PDB: 3EB1; PDB: 3EU0; PDB: 3I7Z; PDB: 3I80; PDB: 3QKP; PDB: 3QKQ; PDB: 3SME; PDB: 3ZMP; PDB: 3ZMQ; PDB: 3ZV2; PDB: 4BJO; PDB: 4I8N; PDB: 4QAH; PDB: 4QAP; PDB: 4QBE; PDB: 4QBW; PDB: 4Y14; PDB: 4ZRT; PDB: 5K9V; PDB: 5K9W; PDB: 5KA0; PDB: 5KA1; PDB: 5KA2; PDB: 5KA3; PDB: 5KA4; PDB: 5KA7; PDB: 5KA8; PDB: 5KA9; PDB: 5KAA; PDB: 5KAB; PDB: 5KAC; PDB: 5KAD; PDB: 5QDE; PDB: 5QDF; PDB: 5QDG; PDB: 5QDH; PDB: 5QDI; PDB: 5QDJ; PDB: 5QDK; PDB: 5QDL; PDB: 5QDM; PDB: 5QDN; PDB: 5QDO; PDB: 5QDP; PDB: 5QDQ; PDB: 5QDR; PDB: 5QDS; PDB: 5QDT; PDB: 5QDU; PDB: 5QDV; PDB: 5QDW; PDB: 5QDX; PDB: 5QDY; PDB: 5QDZ; PDB: 5QE0; PDB: 5QE1; PDB: 5QE2; PDB: 5QE3; PDB: 5QE4; PDB: 5QE5; PDB: 5QE6; PDB: 5QE7; PDB: 5QE8; PDB: 5QE9; PDB: 5QEA; PDB: 5QEB; PDB: 5QEC; PDB: 5QED; PDB: 5QEE; PDB: 5QEF; PDB: 5QEG; PDB: 5QEH; PDB: 5QEI; PDB: 5QEJ; PDB: 5QEK; PDB: 5QEL; PDB: 5QEM; PDB: 5QEN; PDB: 5QEO; PDB: 5QEP; PDB: 5QEQ; PDB: 5QER; PDB: 5QES; PDB: 5QET; PDB: 5QEU; PDB: 5QEV; PDB: 5QEW; PDB: 5QEX; PDB: 5QEY; PDB: 5QEZ; PDB: 5QF0; PDB: 5QF1; PDB: 5QF2; PDB: 5QF3; PDB: 5QF4; PDB: 5QF5; PDB: 5QF6; PDB: 5QF7; PDB: 5QF8; PDB: 5QF9; PDB: 5QFA; PDB: 5QFB; PDB: 5QFC; PDB: 5QFD; PDB: 5QFE; PDB: 5QFF; PDB: 5QFG; PDB: 5QFH; PDB: 5QFI; PDB: 5QFJ; PDB: 5QFK; PDB: 5QFL; PDB: 5QFM; PDB: 5QFN; PDB: 5QFO; PDB: 5QFP; PDB: 5QFQ; PDB: 5QFR; PDB: 5QFS; PDB: 5QFT; PDB: 5QFU; PDB: 5QFV; PDB: 5QFW; PDB: 5QFX; PDB: 5QFY; PDB: 5QFZ; PDB: 5QG0; PDB: 5QG1; PDB: 5QG2; PDB: 5QG3; PDB: 5QG4; PDB: 5QG5; PDB: 5QG6; PDB: 5QG7; PDB: 5QG8; PDB: 5QG9; PDB: 5QGA; PDB: 5QGB; PDB: 5QGC; PDB: 5QGD; PDB: 5QGE; PDB: 5QGF; PDB: 5T19; PDB: 6B8E; PDB: 6B8T; PDB: 6B8X; PDB: 6B8Z; PDB: 6B90; PDB: 6B95; PDB: 6BAI; PDB: 6CWU; PDB: 6CWV; PDB: 6NTP; PDB: 6OL4; PDB: 6OLQ; PDB: 6OLV; PDB: 6OMY; PDB: 6PFW; PDB: 6PG0; PDB: 6PGT; PDB: 6PHA; PDB: 6PHS; PDB: 6PM8; PDB: 6W30; PDB: 7KEN; PDB: 7L0C; PDB: 7L0H; PDB: 7LFO; PDB: 7MM1; PDB: 7RIN	HGNC:9642	PTN1_HUMAN	Reviewed	ENSG00000196396	.	.	.	.	.
Mol00576	Protein	Tyrosine-protein phosphatase non-receptor type 12 (PTPN12)	PTP-PEST; Protein-tyrosine phosphatase G1; PTPG1	PTPN12	5782	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000248594.11, PTPN12-201, 3384; ENST00000435495.6, PTPN12-206, 2526; ENST00000415482.6, PTPN12-203, 2316; ENST00000407343.3, PTPN12-202, 704; ENST00000522115.6, PTPN12-215, 642; ENST00000418110.5, PTPN12-204, 564; ENST00000433369.6, PTPN12-205, 552; ENST00000440186.5, PTPN12-207, 159; ENST00000447995.2, PTPN12-208, 572; ENST00000523952.5, PTPN12-216, 500; ENST00000520947.1, PTPN12-214, 664; ENST00000481154.1, PTPN12-211, 630; ENST00000460731.5, PTPN12-209, 582; ENST00000464313.1, PTPN12-210, 551; ENST00000494248.1, PTPN12-212, 470; ENST00000519553.1, PTPN12-213, 395"	MEQVEILRKFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCEDEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKIADGVNEINTENMVSSIEPEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDNDRYHPKPVLHMVSSEQHSADLNRNYSKSTELPGKNESTIEQIDKKLERNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASPCIADKISKPQELSSDLNVGDTSQNSCVDCSVTQSNKVSVTPPEESQNSDTPPRPDRLPLDEKGHVTWSFHGPENAIPIPDLSEGNSSDINYQTRKTVSLTPSPTTQVETPDLVDHDNTSPLFRTPLSFTNPLHSDDSDSDERNSDGAVTQNKTNISTASATVSAATSTESISTRKVLPMSIARHNIAGTTHSGAEKDVDVSEDSPPPLPERTPESFVLASEHNTPVRSEWSELQSQERSEQKKSEGLITSENEKCDHPAGGIHYEMCIECPPTFSDKREQISENPTEATDIGFGNRCGKPKGPRDPPSEWT	chr7:77537295-77640069[+]	"Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades. Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2. Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248'."	PDB: 5HDE; PDB: 5J8R; PDB: 5O2P	HGNC:9645	PTN12_HUMAN	Reviewed	ENSG00000127947	.	.	.	.	.
Mol00577	Protein	Tyrosine-protein phosphatase non-receptor type 13 (PTPN13)	Fas-associated protein-tyrosine phosphatase 1; FAP-1; PTP-BAS; Protein-tyrosine phosphatase 1E; PTP-E1; hPTPE1; Protein-tyrosine phosphatase PTPL1; PNP1; PTP1E; PTPL1	PTPN13	5783	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000411767.7, PTPN13-202, 8548; ENST00000436978.5, PTPN13-204, 8573; ENST00000427191.6, PTPN13-203, 8487; ENST00000511467.1, PTPN13-209, 8076; ENST00000316707.10, PTPN13-201, 7546; ENST00000502971.5, PTPN13-205, 1708; ENST00000507902.5, PTPN13-206, 516; ENST00000511105.1, PTPN13-208, 645; ENST00000508063.1, PTPN13-207, 457"	MHVSLAEALEVRGGPLQEEEIWAVLNQSAESLQELFRKVSLADPAALGFIISPWSLLLLPSGSVSFTDENISNQDLRAFTAPEVLQNQSLTSLSDVEKIHIYSLGMTLYWGADYEVPQSQPIKLGDHLNSILLGMCEDVIYARVSVRTVLDACSAHIRNSNCAPSFSYVKHLVKLVLGNLSGTDQLSCNSEQKPDRSQAIRDRLRGKGLPTGRSSTSDVLDIQKPPLSHQTFLNKGLSKSMGFLSIKDTQDENYFKDILSDNSGREDSENTFSPYQFKTSGPEKKPIPGIDVLSKKKIWASSMDLLCTADRDFSSGETATYRRCHPEAVTVRTSTTPRKKEARYSDGSIALDIFGPQKMDPIYHTRELPTSSAISSALDRIRERQKKLQVLREAMNVEEPVRRYKTYHGDVFSTSSESPSIISSESDFRQVRRSEASKRFESSSGLPGVDETLSQGQSQRPSRQYETPFEGNLINQEIMLKRQEEELMQLQAKMALRQSRLSLYPGDTIKASMLDITRDPLREIALETAMTQRKLRNFFGPEFVKMTIEPFISLDLPRSILTKKGKNEDNRRKVNIMLLNGQRLELTCDTKTICKDVFDMVVAHIGLVEHHLFALATLKDNEYFFVDPDLKLTKVAPEGWKEEPKKKTKATVNFTLFFRIKFFMDDVSLIQHTLTCHQYYLQLRKDILEERMHCDDETSLLLASLALQAEYGDYQPEVHGVSYFRMEHYLPARVMEKLDLSYIKEELPKLHNTYVGASEKETELEFLKVCQRLTEYGVHFHRVHPEKKSQTGILLGVCSKGVLVFEVHNGVRTLVLRFPWRETKKISFSKKKITLQNTSDGIKHGFQTDNSKICQYLLHLCSYQHKFQLQMRARQSNQDAQDIERASFRSLNLQAESVRGFNMGRAISTGSLASSTLNKLAVRPLSVQAEILKRLSCSELSLYQPLQNSSKEKNDKASWEEKPREMSKSYHDLSQASLYPHRKNVIVNMEPPPQTVAELVGKPSHQMSRSDAESLAGVTKLNNSKSVASLNRSPERRKHESDSSSIEDPGQAYVLGMTMHSSGNSSSQVPLKENDVLHKRWSIVSSPEREITLVNLKKDAKYGLGFQIIGGEKMGRLDLGIFISSVAPGGPADLDGCLKPGDRLISVNSVSLEGVSHHAAIEILQNAPEDVTLVISQPKEKISKVPSTPVHLTNEMKNYMKKSSYMQDSAIDSSSKDHHWSRGTLRHISENSFGPSGGLREGSLSSQDSRTESASLSQSQVNGFFASHLGDQTWQESQHGSPSPSVISKATEKETFTDSNQSKTKKPGISDVTDYSDRGDSDMDEATYSSSQDHQTPKQESSSSVNTSNKMNFKTFSSSPPKPGDIFEVELAKNDNSLGISVTGGVNTSVRHGGIYVKAVIPQGAAESDGRIHKGDRVLAVNGVSLEGATHKQAVETLRNTGQVVHLLLEKGQSPTSKEHVPVTPQCTLSDQNAQGQGPEKVKKTTQVKDYSFVTEENTFEVKLFKNSSGLGFSFSREDNLIPEQINASIVRVKKLFPGQPAAESGKIDVGDVILKVNGASLKGLSQQEVISALRGTAPEVFLLLCRPPPGVLPEIDTALLTPLQSPAQVLPNSSKDSSQPSCVEQSTSSDENEMSDKSKKQCKSPSRRDSYSDSSGSGEDDLVTAPANISNSTWSSALHQTLSNMVSQAQSHHEAPKSQEDTICTMFYYPQKIPNKPEFEDSNPSPLPPDMAPGQSYQPQSESASSSSMDKYHIHHISEPTRQENWTPLKNDLENHLEDFELEVELLITLIKSEKGSLGFTVTKGNQRIGCYVHDVIQDPAKSDGRLKPGDRLIKVNDTDVTNMTHTDAVNLLRAASKTVRLVIGRVLELPRIPMLPHLLPDITLTCNKEELGFSLCGGHDSLYQVVYISDINPRSVAAIEGNLQLLDVIHYVNGVSTQGMTLEEVNRALDMSLPSLVLKATRNDLPVVPSSKRSAVSAPKSTKGNGSYSVGSCSQPALTPNDSFSTVAGEEINEISYPKGKCSTYQIKGSPNLTLPKESYIQEDDIYDDSQEAEVIQSLLDVVDEEAQNLLNENNAAGYSCGPGTLKMNGKLSEERTEDTDCDGSPLPEYFTEATKMNGCEEYCEEKVKSESLIQKPQEKKTDDDEITWGNDELPIERTNHEDSDKDHSFLTNDELAVLPVVKVLPSGKYTGANLKSVIRVLRGLLDQGIPSKELENLQELKPLDQCLIGQTKENRRKNRYKNILPYDATRVPLGDEGGYINASFIKIPVGKEEFVYIACQGPLPTTVGDFWQMIWEQKSTVIAMMTQEVEGEKIKCQRYWPNILGKTTMVSNRLRLALVRMQQLKGFVVRAMTLEDIQTREVRHISHLNFTAWPDHDTPSQPDDLLTFISYMRHIHRSGPIITHCSAGIGRSGTLICIDVVLGLISQDLDFDISDLVRCMRLQRHGMVQTEDQYIFCYQVILYVLTRLQAEEEQKQQPQLLK	chr4:86594315-86815171[+]	Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling. May regulate phosphoinositide 3-kinase (PI3K) signaling through dephosphorylation of PIK3R2.	PDB: 1D5G; PDB: 1Q7X; PDB: 1WCH; PDB: 2M0Z; PDB: 2M10; PDB: 3LNX; PDB: 3LNY; PDB: 3PDZ; PDB: 5GLJ	HGNC:9646	PTN13_HUMAN	Reviewed	ENSG00000163629	.	.	.	.	.
Mol00578	Protein	Tyrosine-protein phosphatase non-receptor type 18 (PTPN18)	Brain-derived phosphatase; BDP1	PTPN18	26469	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000175756.10, PTPN18-201, 3616; ENST00000347849.7, PTPN18-202, 2472; ENST00000409022.2, PTPN18-203, 993; ENST00000428843.5, PTPN18-205, 785; ENST00000420717.5, PTPN18-204, 599; ENST00000462321.1, PTPN18-207, 1717; ENST00000481492.1, PTPN18-211, 1394; ENST00000490812.5, PTPN18-215, 833; ENST00000462996.1, PTPN18-208, 759; ENST00000483617.5, PTPN18-212, 595; ENST00000495400.1, PTPN18-216, 552; ENST00000479295.1, PTPN18-210, 513; ENST00000489215.5, PTPN18-213, 460; ENST00000490137.1, PTPN18-214, 411; ENST00000460992.1, PTPN18-206, 398; ENST00000464576.1, PTPN18-209, 393"	MSRSLDSARSFLERLEARGGREGAVLAGEFSDIQACSAAWKADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMFCSTLQNASPHYQNIKENCAPLYDDALFLRTPQALLAIPRPPGGVLRSISVPGSPGHAMADTYAVVQKRGAPAGAGSGTQTGTGTGTGARSAEEAPLYSKVTPRAQRPGAHAEDARGTLPGRVPADQSPAGSGAYEDVAGGAQTGGLGFNLRIGRPKGPRDPPAEWTRV	chr2:130356045-130375405[+]	Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues.	PDB: 2OC3; PDB: 4GFU; PDB: 4GFV; PDB: 4NND	HGNC:9649	PTN18_HUMAN	Reviewed	ENSG00000072135	.	.	.	.	.
Mol00579	Protein	Transcriptional activator protein Pur-alpha (PURA)	Purine-rich single-stranded DNA-binding protein alpha; PUR1	PURA	5813	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331327.5, PURA-201, 11511; ENST00000651386.1, PURA-204, 1919; ENST00000505703.2, PURA-203, 784; ENST00000502351.1, PURA-202, 502; ENST00000676000.1, PURA-205, 415"	MADRDSGSEQGGAALGSGGSLGHPGSGSGSGGGGGGGGGGGGSGGGGGGAPGGLQHETQELASKRVDIQNKRFYLDVKQNAKGRFLKIAEVGAGGNKSRLTLSMSVAVEFRDYLGDFIEHYAQLGPSQPPDLAQAQDEPRRALKSEFLVRENRKYYMDLKENQRGRFLRIRQTVNRGPGLGSTQGQTIALPAQGLIEFRDALAKLIDDYGVEEEPAELPEGTSLTVDNKRFFFDVGSNKYGVFMRVSEVKPTYRNSITVPYKVWAKFGHTFCKYSEEMKKIQEKQREKRAACEQLHQQQQQQQEETAAATLLLQGEEEGEED	chr5:140107777-140125619[+]	This is a probable transcription activator that specifically binds the purine-rich single strand of the PUR element located upstream of the MYC gene. May play a role in the initiation of DNA replication and in recombination.	.	HGNC:9701	PURA_HUMAN	Reviewed	ENSG00000185129	.	.	.	.	.
Mol00581	Protein	Protein quaking (QKI)	Hqk; HqkI; HKQ	QKI	9444	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361752.8, QKI-203, 9384; ENST00000392127.6, QKI-205, 7911; ENST00000275262.11, QKI-201, 6964; ENST00000453779.6, QKI-207, 5685; ENST00000361195.6, QKI-202, 1063; ENST00000537883.5, QKI-210, 1106; ENST00000424802.7, QKI-206, 954; ENST00000544361.1, QKI-213, 613; ENST00000544823.5, QKI-215, 597; ENST00000537041.5, QKI-208, 583; ENST00000537124.5, QKI-209, 551; ENST00000544436.5, QKI-214, 495; ENST00000361758.8, QKI-204, 6085; ENST00000545607.5, QKI-217, 846; ENST00000545346.1, QKI-216, 457; ENST00000541696.1, QKI-212, 1097; ENST00000540719.1, QKI-211, 588"	MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN	chr6:163414000-163578592[+]	"RNA-binding protein that plays a central role in myelinization. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Regulates target mRNA stability. In addition, acts by regulating pre-mRNA splicing, mRNA export and protein translation. Required to protect and promote stability of mRNAs such as MBP and CDKN1B. Regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia. Participates in mRNA transport by regulating the nuclear export of MBP mRNA. Also involved in regulation of mRNA splicing of MAG pre-mRNA. Acts as a translational repressor."	PDB: 4JVH	HGNC:21100	QKI_HUMAN	Reviewed	ENSG00000112531	.	.	.	.	.
Mol00582	Protein	DNA repair protein RAD51 homolog 4 (RAD51D)	R51H3; RAD51 homolog D; RAD51-like protein 3; TRAD; RAD51L3	RAD51D	5892	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000345365.11, RAD51D-202, 9966; ENST00000394589.8, RAD51D-203, 2287; ENST00000590016.5, RAD51D-218, 1528; ENST00000335858.11, RAD51D-201, 1353; ENST00000460118.6, RAD51D-205, 1064; ENST00000592577.5, RAD51D-221, 762; ENST00000587405.5, RAD51D-212, 676; ENST00000590631.1, RAD51D-219, 561; ENST00000586186.2, RAD51D-210, 289; ENST00000588372.5, RAD51D-215, 2214; ENST00000587977.5, RAD51D-213, 1732; ENST00000586044.5, RAD51D-209, 1571; ENST00000588594.5, RAD51D-216, 1409; ENST00000586210.5, RAD51D-211, 1194; ENST00000585343.5, RAD51D-206, 603; ENST00000592850.5, RAD51D-222, 386; ENST00000415064.6, RAD51D-204, 986; ENST00000592430.5, RAD51D-220, 698; ENST00000587982.5, RAD51D-214, 682; ENST00000585982.5, RAD51D-208, 596; ENST00000592928.2, RAD51D-223, 207; ENST00000585947.5, RAD51D-207, 672; ENST00000589506.1, RAD51D-217, 564"	MGVLRVGLCPGLTEEMIQLLRSHRIKTVVDLVSADLEEVAQKCGLSYKALVALRRVLLAQFSAFPVNGADLYEELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCMAANVAHGLQQNVLYVDSNGGLTASRLLQLLQAKTQDEEEQAEALRRIQVVHAFDIFQMLDVLQELRGTVAQQVTGSSGTVKVVVVDSVTAVVSPLLGGQQREGLALMMQLARELKTLARDLGMAVVVTNHITRDRDSGRLKPALGRSWSFVPSTRILLDTIEGAGASGGRRMACLAKSSRQPTGFQEMVDIGTWGTSEQSATLQGDQT	chr17:35092221-35121522[-]	"Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the Rad21 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM."	PDB: 2KZ3	HGNC:9823	RA51D_HUMAN	Reviewed	ENSG00000185379	.	.	.	.	.
Mol00583	Protein	Ras-related protein Rab-14 (RAB14)	.	RAB14	51552	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373840.9, RAB14-201, 4149; ENST00000451303.1, RAB14-202, 711"	MATAPYNYSYIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVSGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDARNLTNPNTVIILIGNKADLEAQRDVTYEEAKQFAEENGLLFLEASAKTGENVEDAFLEAAKKIYQNIQDGSLDLNAAESGVQHKPSAPQGGRLTSEPQPQREGCGC	chr9:121178133-121223014[-]	"Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity). Regulates, together with its guanine nucleotide exchange factor DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion."	PDB: 1Z0F; PDB: 4D0G; PDB: 4DRZ	HGNC:16524	RAB14_HUMAN	Reviewed	ENSG00000119396	.	.	.	.	.
Mol00584	Protein	Ras-related C3 botulinum toxin substrate 1 (RAC1)	Cell migration-inducing gene 5 protein; Ras-like protein TC25; p21-Rac1; TC25; MIG5	RAC1	5879	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000348035.9, RAC1-201, 2309; ENST00000356142.4, RAC1-202, 907; ENST00000488373.5, RAC1-204, 845; ENST00000497741.5, RAC1-206, 651; ENST00000696666.1, RAC1-207, 5408; ENST00000495499.1, RAC1-205, 615; ENST00000473564.1, RAC1-203, 576"	MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL	chr7:6374527-6403967[+]	"Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In neurons, is involved in dendritic spine formation and synaptic plasticity. In hippocampal neurons, involved in spine morphogenesis and synapse formation, through local activation at synapses by guanine nucleotide exchange factors (GEFs), such as ARHGEF6/ARHGEF7/PIX. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3. In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in PAK1 activation and eventually F-actin stabilization."	PDB: 1E96; PDB: 1FOE; PDB: 1G4U; PDB: 1HE1; PDB: 1HH4; PDB: 1I4D; PDB: 1I4L; PDB: 1I4T; PDB: 1MH1; PDB: 1RYF; PDB: 1RYH; PDB: 2FJU; PDB: 2H7V; PDB: 2NZ8; PDB: 2P2L; PDB: 2RMK; PDB: 2VRW; PDB: 2WKP; PDB: 2WKQ; PDB: 2WKR; PDB: 2YIN; PDB: 3B13; PDB: 3BJI; PDB: 3RYT; PDB: 3SBD; PDB: 3SBE; PDB: 3SU8; PDB: 3SUA; PDB: 3TH5; PDB: 4GZL; PDB: 4GZM; PDB: 4YON; PDB: 5FI0; PDB: 5HZH; PDB: 5N6O; PDB: 5O33; PDB: 5QQD; PDB: 5QQE; PDB: 5QQF; PDB: 5QQG; PDB: 5QQH; PDB: 5QQI; PDB: 5QQJ; PDB: 5QQK; PDB: 5QQL; PDB: 5QQM; PDB: 5QQN; PDB: 5QU9; PDB: 6AGP; PDB: 6BC1; PDB: 6TGC; PDB: 6X1G; PDB: 7AJK; PDB: 7DPA	HGNC:9801	RAC1_HUMAN	Reviewed	ENSG00000136238	.	.	.	.	.
Mol00585	Protein	DNA repair protein RAD51 homolog 1 (RAD51)	HsRAD51; hRAD51; RAD51 homolog A; RAD51A; RECA	RAD51	5888	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000267868.8, RAD51-201, 2436; ENST00000645673.2, RAD51-211, 2439; ENST00000423169.6, RAD51-203, 1611; ENST00000382643.7, RAD51-202, 1588; ENST00000532743.6, RAD51-208, 1539; ENST00000557850.5, RAD51-210, 1397; ENST00000526763.6, RAD51-205, 665; ENST00000527860.5, RAD51-206, 566; ENST00000525066.5, RAD51-204, 1545; ENST00000531277.2, RAD51-207, 658; ENST00000533741.1, RAD51-209, 425"	MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD	chr15:40694774-40732340[+]	"Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair."	PDB: 1B22; PDB: 1N0W; PDB: 5H1B; PDB: 5H1C; PDB: 5JZC; PDB: 5NP7; PDB: 5NWL; PDB: 7C9A	HGNC:9817	RAD51_HUMAN	Reviewed	ENSG00000051180	.	.	.	.	.
Mol00586	Protein	RAF proto-oncogene serine/threonine-protein kinase (RAF1)	Proto-oncogene c-RAF; cRaf; Raf-1; RAF	RAF1	5894	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000442415.7, RAF1-205, 3251; ENST00000685653.1, RAF1-217, 4402; ENST00000251849.9, RAF1-201, 3191; ENST00000691899.1, RAF1-262, 2983; ENST00000688543.1, RAF1-236, 4662; ENST00000692093.1, RAF1-264, 3187; ENST00000690460.1, RAF1-252, 3141; ENST00000690397.1, RAF1-251, 3037; ENST00000687923.1, RAF1-231, 3031; ENST00000693312.1, RAF1-272, 2899; ENST00000689389.1, RAF1-245, 2899; ENST00000685437.1, RAF1-215, 2866; ENST00000432427.3, RAF1-204, 2077; ENST00000691888.1, RAF1-261, 1734; ENST00000692959.1, RAF1-270, 1429; ENST00000691718.1, RAF1-258, 1248; ENST00000689226.1, RAF1-244, 1215; ENST00000685740.1, RAF1-220, 1098; ENST00000689033.1, RAF1-242, 1048; ENST00000685959.1, RAF1-221, 963; ENST00000688753.1, RAF1-238, 659; ENST00000687326.1, RAF1-227, 5593; ENST00000689418.1, RAF1-246, 4974; ENST00000688625.1, RAF1-237, 4704; ENST00000685348.1, RAF1-214, 4615; ENST00000685738.1, RAF1-219, 3261; ENST00000689914.1, RAF1-250, 3215; ENST00000689876.1, RAF1-249, 3198; ENST00000691724.1, RAF1-259, 3171; ENST00000686762.1, RAF1-225, 3140; ENST00000684903.1, RAF1-213, 3129; ENST00000691396.1, RAF1-256, 3104; ENST00000693664.1, RAF1-273, 3079; ENST00000692773.1, RAF1-267, 3073; ENST00000423275.6, RAF1-203, 3034; ENST00000691779.1, RAF1-260, 2944; ENST00000689097.1, RAF1-243, 2877; ENST00000692830.1, RAF1-269, 2808; ENST00000693705.1, RAF1-274, 2506; ENST00000689481.1, RAF1-247, 2102; ENST00000688326.1, RAF1-234, 1594; ENST00000690585.1, RAF1-253, 1586; ENST00000693069.1, RAF1-271, 1356; ENST00000416093.2, RAF1-202, 801; ENST00000687348.1, RAF1-228, 774; ENST00000691268.1, RAF1-255, 535; ENST00000687486.1, RAF1-229, 385; ENST00000460610.2, RAF1-206, 7152; ENST00000686409.1, RAF1-222, 6107; ENST00000692069.1, RAF1-263, 5746; ENST00000686455.1, RAF1-223, 5552; ENST00000692558.1, RAF1-266, 5400; ENST00000687257.1, RAF1-226, 5175; ENST00000689540.1, RAF1-248, 5062; ENST00000475353.2, RAF1-209, 5001; ENST00000688444.1, RAF1-235, 4972; ENST00000688803.1, RAF1-240, 4273; ENST00000494557.2, RAF1-212, 4000; ENST00000691643.1, RAF1-257, 3906; ENST00000690625.1, RAF1-254, 3798; ENST00000692311.1, RAF1-265, 3641; ENST00000685697.1, RAF1-218, 3588; ENST00000688269.1, RAF1-233, 3413; ENST00000687505.1, RAF1-230, 2752; ENST00000687940.1, RAF1-232, 2650; ENST00000686479.1, RAF1-224, 2234; ENST00000491290.2, RAF1-210, 2084; ENST00000465826.6, RAF1-207, 1958; ENST00000692777.1, RAF1-268, 1946; ENST00000471449.2, RAF1-208, 1614; ENST00000688914.1, RAF1-241, 1174; ENST00000685438.1, RAF1-216, 701; ENST00000492690.1, RAF1-211, 633; ENST00000688779.1, RAF1-239, 568"	MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF	chr3:12582101-12664201[-]	"Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation."	PDB: 1C1Y; PDB: 1FAQ; PDB: 1FAR; PDB: 1GUA; PDB: 1RFA; PDB: 3CU8; PDB: 3IQJ; PDB: 3IQU; PDB: 3IQV; PDB: 3KUC; PDB: 3KUD; PDB: 3NKX; PDB: 3O8I; PDB: 3OMV; PDB: 4FJ3; PDB: 4G0N; PDB: 4G3X; PDB: 4IEA; PDB: 4IHL; PDB: 6NTC; PDB: 6NTD; PDB: 6PTS; PDB: 6PTW; PDB: 6VJJ; PDB: 6XGU; PDB: 6XGV; PDB: 6XHA; PDB: 6XHB; PDB: 6XI7; PDB: 7JHP	HGNC:9829	RAF1_HUMAN	Reviewed	ENSG00000132155	.	.	.	.	.
Mol00587	Protein	Ran GTPase-activating protein 1 (RANGAP1)	RanGAP1; KIAA1835; SD	RANGAP1	5905	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356244.8, RANGAP1-201, 3828; ENST00000455915.6, RANGAP1-207, 4222; ENST00000405486.5, RANGAP1-202, 3469; ENST00000422838.1, RANGAP1-204, 946; ENST00000446258.5, RANGAP1-205, 759; ENST00000418067.1, RANGAP1-203, 650; ENST00000452543.5, RANGAP1-206, 603"	MASEDIAKLAETLAKTQVAGGQLSFKGKSLKLNTAEDAKDVIKEIEDFDSLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRTEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVQGFEALLKSSACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFRVIGTLEEVHMPQNGINHPGITALAQAFAVNPLLRVINLNDNTFTEKGAVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAIRGGLPKLKELNLSFCEIKRDAALAVAEAMADKAELEKLDLNGNTLGEEGCEQLQEVLEGFNMAKVLASLSDDEDEEEEEEGEEEEEEAEEEEEEDEEEEEEEEEEEEEEPQQRGQGEKSATPSRKILDPNTGEPAPVLSSPPPADVSTFLAFPSPEKLLRLGPKSSVLIAQQTDTSDPEKVVSAFLKVSSVFKDEATVRMAVQDAVDALMQKAFNSSSFNSNTFLTRLLVHMGLLKSEDKVKAIANLYGPLMALNHMVQQDYFPKALAPLLLAFVTKPNSALESCSFARHSLLQTLYKV	chr22:41244779-41286187[-]	"GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export. Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export."	.	HGNC:9854	RAGP1_HUMAN	Reviewed	ENSG00000100401	.	.	.	.	.
Mol00588	Protein	Ras-related protein Rap-1A (RAP1A)	C21KG; G-22K; GTP-binding protein smg p21A; Ras-related protein Krev-1; KREV1	RAP1A	5906	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369709.4, RAP1A-202, 5018; ENST00000687939.1, RAP1A-204, 5101; ENST00000356415.5, RAP1A-201, 1586; ENST00000494982.1, RAP1A-203, 1083"	MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL	chr1:111542218-111716691[+]	"Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in nerve growth factor (NGF)-induced neurite outgrowth. Plays a role in the regulation of embryonic blood vessel formation. Involved in the establishment of basal endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR expression at endothelial cell-cell junctions."	PDB: 1C1Y; PDB: 1GUA; PDB: 3KUC; PDB: 4KVG	HGNC:9855	RAP1A_HUMAN	Reviewed	ENSG00000116473	.	.	.	.	.
Mol00589	Protein	Ras-related protein Rap-1b (RAP1B)	GTP-binding protein smg p21B; OK/SW-cl.11	RAP1B	5908	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000250559.14, RAP1B-201, 13378; ENST00000393436.9, RAP1B-204, 2049; ENST00000450214.6, RAP1B-207, 1466; ENST00000540209.5, RAP1B-221, 1264; ENST00000537460.5, RAP1B-216, 1072; ENST00000542145.5, RAP1B-228, 1060; ENST00000539091.5, RAP1B-220, 977; ENST00000341355.9, RAP1B-202, 714; ENST00000378985.7, RAP1B-203, 1017; ENST00000543393.5, RAP1B-229, 874; ENST00000425247.6, RAP1B-206, 855; ENST00000543697.5, RAP1B-230, 734; ENST00000541216.1, RAP1B-224, 701; ENST00000545270.5, RAP1B-232, 640; ENST00000542018.5, RAP1B-227, 633; ENST00000534899.5, RAP1B-214, 606; ENST00000538283.5, RAP1B-217, 591; ENST00000538980.5, RAP1B-219, 587; ENST00000540781.5, RAP1B-222, 571; ENST00000489473.6, RAP1B-212, 561; ENST00000541167.5, RAP1B-223, 561; ENST00000545720.6, RAP1B-233, 552; ENST00000538877.5, RAP1B-218, 550; ENST00000453560.6, RAP1B-208, 530; ENST00000535492.5, RAP1B-215, 509; ENST00000541386.5, RAP1B-225, 480; ENST00000422358.6, RAP1B-205, 468; ENST00000485252.6, RAP1B-211, 312; ENST00000463493.5, RAP1B-210, 781; ENST00000460800.5, RAP1B-209, 755; ENST00000501412.2, RAP1B-213, 1488; ENST00000544639.1, RAP1B-231, 531; ENST00000541968.1, RAP1B-226, 478"	MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL	chr12:68610855-68671901[+]	"GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function."	.	HGNC:9857	RAP1B_HUMAN	Reviewed	ENSG00000127314	.	.	.	.	.
Mol00590	Protein	Ras association domain-containing protein 1 (RASSF1)	RDA32	RASSF1	11186	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359365.9, RASSF1-203, 1847; ENST00000357043.6, RASSF1-202, 1864; ENST00000616212.4, RASSF1-210, 1842; ENST00000327761.7, RASSF1-201, 1757; ENST00000395126.7, RASSF1-205, 1657; ENST00000395117.6, RASSF1-204, 1745; ENST00000482447.1, RASSF1-207, 1711; ENST00000488024.1, RASSF1-208, 1385; ENST00000478619.1, RASSF1-206, 2060; ENST00000494145.1, RASSF1-209, 1358"	MSGEPELIELRELAPAGRAGKGRTRLERANALRIARGTACNPTRQLVPGRGHRFQPAGPATHTWCDLCGDFIWGVVRKGLQCARLSADCKFTCHYRCRALVCLDCCGPRDLGWEPAVERDTNVDEPVEWETPDLSQAEIEQKIKEYNAQINSNLFMSLNKDGSYTGFIKVQLKLVRPVSVPSSKKPPSLQDARRGPGRGTSVRRRTSFYLPKDAVKHLHVLSRTRAREVIEALLRKFLVVDDPRKFALFERAERHGQVYLRKLLDDEQPLRLRLLAGPSDKALSFVLKENDSGEVNWDAFSMPELHNFLRILQREEEEHLRQILQKYSYCRQKIQEALHACPLG	chr3:50329782-50340980[-]	"Potential tumor suppressor. Required for death receptor-dependent apoptosis. Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Isoform A interacts with CDC20, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage."	PDB: 2KZU	HGNC:9882	RASF1_HUMAN	Reviewed	ENSG00000068028	.	.	.	.	.
Mol00591	Protein	GTPase Hras (HRAS)	H-Ras-1; Ha-Ras; Transforming protein p21; c-H-ras; p21ras; HRAS1	HRAS	3265	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000311189.8, HRAS-201, 1070; ENST00000417302.6, HRAS-204, 1244; ENST00000451590.5, HRAS-205, 1151; ENST00000397596.6, HRAS-203, 1100; ENST00000468682.2, HRAS-207, 749; ENST00000397594.6, HRAS-202, 639; ENST00000493230.5, HRAS-210, 1114; ENST00000462734.2, HRAS-206, 1939; ENST00000482021.1, HRAS-209, 167; ENST00000479482.1, HRAS-208, 485"	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS	chr11:532242-537321[-]	Involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.	PDB: 121P; PDB: 1AA9; PDB: 1AGP; PDB: 1BKD; PDB: 1CLU; PDB: 1CRP; PDB: 1CRQ; PDB: 1CRR; PDB: 1CTQ; PDB: 1GNP; PDB: 1GNQ; PDB: 1GNR; PDB: 1HE8; PDB: 1IAQ; PDB: 1IOZ; PDB: 1JAH; PDB: 1JAI; PDB: 1K8R; PDB: 1LF0; PDB: 1LF5; PDB: 1LFD; PDB: 1NVU; PDB: 1NVV; PDB: 1NVW; PDB: 1NVX; PDB: 1P2S; PDB: 1P2T; PDB: 1P2U; PDB: 1P2V; PDB: 1PLJ; PDB: 1PLK; PDB: 1PLL; PDB: 1Q21; PDB: 1QRA; PDB: 1RVD; PDB: 1WQ1; PDB: 1XCM; PDB: 1XD2; PDB: 1XJ0; PDB: 1ZVQ; PDB: 1ZW6; PDB: 221P; PDB: 2C5L; PDB: 2CE2; PDB: 2CL0; PDB: 2CL6; PDB: 2CL7; PDB: 2CLC; PDB: 2CLD; PDB: 2EVW; PDB: 2LCF; PDB: 2LWI; PDB: 2N42; PDB: 2N46; PDB: 2Q21; PDB: 2QUZ; PDB: 2RGA; PDB: 2RGB; PDB: 2RGC; PDB: 2RGD; PDB: 2RGE; PDB: 2RGG; PDB: 2UZI; PDB: 2VH5; PDB: 2X1V; PDB: 3DDC; PDB: 3I3S; PDB: 3K8Y; PDB: 3K9L; PDB: 3K9N; PDB: 3KKM; PDB: 3KKN; PDB: 3KUD; PDB: 3L8Y; PDB: 3L8Z; PDB: 3LBH; PDB: 3LBI; PDB: 3LBN; PDB: 3LO5; PDB: 3OIU; PDB: 3OIV; PDB: 3OIW; PDB: 3RRY; PDB: 3RRZ; PDB: 3RS0; PDB: 3RS2; PDB: 3RS3; PDB: 3RS4; PDB: 3RS5; PDB: 3RS7; PDB: 3RSL; PDB: 3RSO; PDB: 3TGP; PDB: 421P; PDB: 4DLR; PDB: 4DLS; PDB: 4DLT; PDB: 4DLU; PDB: 4DLV; PDB: 4DLW; PDB: 4DLX; PDB: 4DLY; PDB: 4DLZ; PDB: 4DST; PDB: 4DSU; PDB: 4EFL; PDB: 4EFM; PDB: 4EFN; PDB: 4G0N; PDB: 4G3X; PDB: 4K81; PDB: 4L9S; PDB: 4L9W; PDB: 4NYI; PDB: 4NYJ; PDB: 4NYM; PDB: 4Q21; PDB: 4RSG; PDB: 4URU; PDB: 4URV; PDB: 4URW; PDB: 4URX; PDB: 4URY; PDB: 4URZ; PDB: 4US0; PDB: 4US1; PDB: 4US2; PDB: 4XVQ; PDB: 4XVR; PDB: 521P; PDB: 5B2Z; PDB: 5B30; PDB: 5E95; PDB: 5P21; PDB: 5VBE; PDB: 5VBZ; PDB: 5WDO; PDB: 5WDP; PDB: 5WDQ; PDB: 5WFO; PDB: 5WFP; PDB: 5WFQ; PDB: 5WFR; PDB: 5WPL; PDB: 5X9S; PDB: 5ZC6; PDB: 621P; PDB: 6AMB; PDB: 6AXG; PDB: 6BVI; PDB: 6BVJ; PDB: 6BVK; PDB: 6BVL; PDB: 6BVM; PDB: 6CUO; PDB: 6CUP; PDB: 6CUR; PDB: 6D55; PDB: 6D56; PDB: 6D59; PDB: 6D5E; PDB: 6D5G; PDB: 6D5H; PDB: 6D5J; PDB: 6D5L; PDB: 6D5M; PDB: 6D5V; PDB: 6D5W; PDB: 6DZH; PDB: 6E6C; PDB: 6E6P; PDB: 6MQT; PDB: 6NTC; PDB: 6NTD; PDB: 6Q21; PDB: 6V94; PDB: 6V9F; PDB: 6V9J; PDB: 6V9L; PDB: 6V9M; PDB: 6V9N; PDB: 6V9O; PDB: 6ZJ0; PDB: 6ZL3; PDB: 721P; PDB: 7DPH; PDB: 7DPJ; PDB: 7JHP; PDB: 7L0F; PDB: 7L0G; PDB: 821P	HGNC:5173	RASH_HUMAN	Reviewed	ENSG00000174775	.	.	.	.	.
Mol00592	Protein	RasGAP-activating-like protein 1 (RASAL1)	RAS protein activator like 1; Ras GTPase-activating-like protein; RASAL	RASAL1	8437	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000548055.2, RASAL1-207, 3368; ENST00000546530.5, RASAL1-204, 3817; ENST00000261729.9, RASAL1-201, 3382; ENST00000446861.7, RASAL1-203, 3040; ENST00000418411.6, RASAL1-202, 2472; ENST00000548972.5, RASAL1-208, 2180; ENST00000549444.5, RASAL1-209, 895; ENST00000547810.1, RASAL1-206, 582; ENST00000551051.5, RASAL1-210, 2733; ENST00000546727.5, RASAL1-205, 2561"	MAKSSSLNVRVVEGRALPAKDVSGSSDPYCLVKVDDEVVARTATVWRSLGPFWGEEYTVHLPLDFHQLAFYVLDEDTVGHDDIIGKISLSREAITADPRGIDSWINLSRVDPDAEVQGEICLSVQMLEDGQGRCLRCHVLQARDLAPRDISGTSDPFARVFWGSQSLETSTIKKTRFPHWDEVLELREMPGAPSPLRVELWDWDMVGKNDFLGMVEFSPKTLQQKPPKGWFRLLPFPRAEEDSGGNLGALRVKVRLIEDRVLPSQCYQPLMELLMESVQGPAEEDTASPLALLEELTLGDCRQDLATKLVKLFLGRGLAGRFLDYLTRREVARTMDPNTLFRSNSLASKSMEQFMKLVGMPYLHEVLKPVISRVFEEKKYMELDPCKMDLGRTRRISFKGALSEEQMRETSLGLLTGYLGPIVDAIVGSVGRCPPAMRLAFKQLHRRVEERFPQAEHQDVKYLAISGFLFLRFFAPAILTPKLFDLRDQHADPQTSRSLLLLAKAVQSIGNLGQQLGQGKELWMAPLHPFLLQCVSRVRDFLDRLVDVDGDEAGVPARALFPPSAIVREGYLLKRKEEPAGLATRFAFKKRYVWLSGETLSFSKSPEWQMCHSIPVSHIRAVERVDEGAFQLPHVMQVVTQDGTGALHTTYLQCKNVNELNQWLSALRKASAPNPNKLAACHPGAFRSARWTCCLQAERSAAGCSRTHSAVTLGDWSDPLDPDAEAQTVYRQLLLGRDQLRLKLLEDSNMDTTLEADTGACPEVLARQRAATARLLEVLADLDRAHEEFQQQERGKAALGPLGP	chr12:113098819-113136239[-]	Probable inhibitory regulator of the Ras-cyclic AMP pathway. Plays a role in dendrite formation by melanocytes.	.	HGNC:9873	RASL1_HUMAN	Reviewed	ENSG00000111344	.	.	.	.	.
Mol00593	Protein	GTPase Nras (NRAS)	Transforming protein N-Ras; HRAS1	NRAS	4893	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369535.5, NRAS-201, 4326"	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM	chr1:114704469-114716771[-]	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.	PDB: 2N9C; PDB: 3CON; PDB: 5UHV; PDB: 6E6H; PDB: 6MPP; PDB: 6ULI; PDB: 6ULK; PDB: 6ULN; PDB: 6ULR; PDB: 6UON; PDB: 6WGH; PDB: 6ZIO; PDB: 6ZIR; PDB: 6ZIZ	HGNC:7989	RASN_HUMAN	Reviewed	ENSG00000213281	.	.	.	.	.
Mol00594	Protein	Retinoblastoma-associated protein (RB1)	p105-Rb; p110-RB1; pRb; Rb; pp110	RB1	5925	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000267163.6, RB1-201, 4768; ENST00000650461.1, RB1-209, 4629; ENST00000646097.1, RB1-208, 633; ENST00000643064.1, RB1-207, 329; ENST00000467505.5, RB1-202, 480; ENST00000531171.5, RB1-206, 658; ENST00000480491.1, RB1-203, 617; ENST00000525036.1, RB1-205, 1490; ENST00000484879.1, RB1-204, 1097"	MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK	chr13:48303744-48599436[+]	"Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle. The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes. Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase. RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex."	PDB: 1AD6; PDB: 1GH6; PDB: 1GUX; PDB: 1H25; PDB: 1N4M; PDB: 1O9K; PDB: 1PJM; PDB: 2AZE; PDB: 2QDJ; PDB: 2R7G; PDB: 3N5U; PDB: 3POM; PDB: 4CRI; PDB: 4ELJ; PDB: 4ELL	HGNC:9884	RB_HUMAN	Reviewed	ENSG00000139687	.	.	.	.	.
Mol00595	Protein	Ras-related protein Rab-22A (RAP22A)	Rab-22; RAB22	RAB22A	57403	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000244040.4, RAB22A-201, 8651; ENST00000488949.1, RAB22A-202, 1032"	MALRELKVCLLGDTGVGKSSIVWRFVEDSFDPNINPTIGASFMTKTVQYQNELHKFLIWDTAGQERFRALAPMYYRGSAAAIIVYDITKEETFSTLKNWVKELRQHGPPNIVVAIAGNKCDLIDVREVMERDAKDYADSIHAIFVETSAKNAININELFIEISRRIPSTDANLPSGGKGFKLRRQPSEPKRSCC	chr20:58309715-58367507[+]	"Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth. Binds GTP and GDP and has low GTPase activity. Alternates between a GTP-bound active form and a GDP-bound inactive form."	.	HGNC:9764	RB22A_HUMAN	Reviewed	ENSG00000124209	.	.	.	.	.
Mol00596	Protein	Ras-related protein Rab-27A (RAP27A)	Rab-27; GTP-binding protein Ram; RAB27	RAB27A	5873	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000336787.6, RAB27A-201, 3447; ENST00000396307.6, RAB27A-202, 3459; ENST00000564609.5, RAB27A-205, 1057; ENST00000569493.5, RAB27A-212, 1013; ENST00000565972.5, RAB27A-207, 809; ENST00000563262.5, RAB27A-204, 702; ENST00000567380.5, RAB27A-209, 701; ENST00000566877.5, RAB27A-208, 663; ENST00000568803.1, RAB27A-211, 432; ENST00000561545.1, RAB27A-203, 830; ENST00000567639.1, RAB27A-210, 592; ENST00000565776.1, RAB27A-206, 567"	MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRASGPDGATGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRVVKEEEAIALAEKYGIPYFETSAANGTNISQAIEMLLDLIMKRMERCVDKSWIPEGVVRSNGHASTDQLSEEKEKGACGC	chr15:55202966-55319113[-]	"Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion. Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse."	PDB: 6HUF	HGNC:9766	RB27A_HUMAN	Reviewed	ENSG00000069974	.	.	.	.	.
Mol00597	Protein	Receptor tyrosine-protein kinase erbB-3 (ERBB3)	Proto-oncogene-like protein c-ErbB-3; Tyrosine kinase-type cell surface receptor HER3; HER3	ERBB3	2065	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000267101.8, ERBB3-201, 5615; ENST00000411731.6, ERBB3-202, 1027; ENST00000683164.1, ERBB3-230, 5614; ENST00000683059.1, ERBB3-228, 5439; ENST00000683018.1, ERBB3-227, 5417; ENST00000415288.6, ERBB3-203, 4353; ENST00000549832.1, ERBB3-213, 3289; ENST00000550070.6, ERBB3-214, 2729; ENST00000549282.5, ERBB3-209, 561; ENST00000549061.5, ERBB3-207, 560; ENST00000550828.1, ERBB3-215, 266; ENST00000643266.1, ERBB3-222, 237; ENST00000551085.5, ERBB3-217, 4382; ENST00000551242.5, ERBB3-219, 2755; ENST00000550869.5, ERBB3-216, 572; ENST00000683142.1, ERBB3-229, 2382; ENST00000643518.1, ERBB3-223, 296; ENST00000682431.1, ERBB3-224, 6264; ENST00000684500.1, ERBB3-232, 5819; ENST00000683653.1, ERBB3-231, 5511; ENST00000684766.1, ERBB3-233, 3382; ENST00000553131.5, ERBB3-221, 3237; ENST00000682512.1, ERBB3-225, 3119; ENST00000682873.1, ERBB3-226, 2446; ENST00000549672.6, ERBB3-212, 1207; ENST00000549205.1, ERBB3-208, 971; ENST00000546884.1, ERBB3-205, 660; ENST00000546748.1, ERBB3-204, 574; ENST00000548709.1, ERBB3-206, 551; ENST00000549472.1, ERBB3-210, 519; ENST00000549644.1, ERBB3-211, 306; ENST00000552691.1, ERBB3-220, 291; ENST00000551176.1, ERBB3-218, 277"	MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT	chr12:56076799-56103505[+]	Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase. May also be activated by CSPG5. Involved in the regulation of myeloid cell differentiation.	PDB: 1M6B; PDB: 2L9U; PDB: 3KEX; PDB: 3LMG; PDB: 3P11; PDB: 4LEO; PDB: 4P59; PDB: 4RIW; PDB: 4RIX; PDB: 4RIY; PDB: 5CUS; PDB: 5O4O; PDB: 5O7P; PDB: 6KBI; PDB: 6OP9; PDB: 7D85; PDB: 7MN5; PDB: 7MN6	HGNC:3431	ERBB3_HUMAN	Reviewed	ENSG00000065361	.	.	.	.	.
Mol00598	Protein	Reversion-inducing cysteine-rich protein with Kazal motifs (RECK)	hRECK; Suppressor of tumorigenicity 15 protein; ST15	RECK	8434	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377966.4, RECK-201, 4412; ENST00000479053.1, RECK-203, 1717; ENST00000475774.5, RECK-202, 1128"	MATVRASLRGALLLLLAVAGVAEVAGGLAPGSAGALCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWNCMNSSLPGVFKKSDGWVGLGCCELAIALECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRFCEYNPVEVSMLTCLADVREPCQLGCRNLTYCTNFNNRPTELFRSCNAQSDQGAMNDMKLWEKGSIKMPFINIPVLDIKKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEDHTAESICELLSPTDDLKNCIPLDTYLRPSTLGNIVEEVTHPCNPNPCPANELCEVNRKGCPSGDPCLPYFCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFSIDCNVCSCFAGNLVCSTRLCLSEHSSEDDRRTFTGLPCNCADQFVPVCGQNGRTYPSACIARCVGLQDHQFEFGSCMSKDPCNPNPCQKNQRCIPKPQVCLTTFDKFGCSQYECVPRQLACDQVQDPVCDTDHMEHNNLCTLYQRGKSLSYKGPCQPFCRATEPVCGHNGETYSSVCAAYSDRVAVDYYGDCQAVGVLSEHSSVAECASVKCPSLLAAGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTNKKPITVLEILQKIRMHVSVPQCDVFGYFSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSVPSAGVRARPSCHSLLLPLSLGLALHLLWTYN	chr9:36036913-36124455[+]	"Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation. Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity. Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP)."	.	HGNC:11345	RECK_HUMAN	Reviewed	ENSG00000122707	.	.	.	.	.
Mol00599	Protein	DNA repair protein REV1 (REV1)	Alpha integrin-binding protein 80; AIBP80; Rev1-like terminal deoxycytidyl transferase; REV1L	REV1	51455	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000258428.8, REV1-201, 4731; ENST00000393445.7, REV1-202, 4686; ENST00000450415.1, REV1-205, 577; ENST00000413697.5, REV1-203, 4727; ENST00000438366.1, REV1-204, 545; ENST00000465835.5, REV1-207, 3172; ENST00000486117.1, REV1-215, 582; ENST00000482595.5, REV1-212, 484; ENST00000482887.1, REV1-213, 427; ENST00000473819.1, REV1-209, 1352; ENST00000485487.5, REV1-214, 866; ENST00000465086.1, REV1-206, 813; ENST00000472000.1, REV1-208, 778; ENST00000481719.1, REV1-211, 754; ENST00000477121.1, REV1-210, 564; ENST00000491752.1, REV1-216, 547"	MRRGGWRKRAENDGWETWGGYMAAKVQKLEEQFRSDAAMQKDGTSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSYIPYQLYTKQSSVQKGLSFNPVCRPEDPLPGPSNIAKQLNNRVNHIVKKIETENEVKVNGMNSWNEEDENNDFSFVDLEQTSPGRKQNGIPHPRGSTAIFNGHTPSSNGALKTQDCLVPMVNSVASRLSPAFSQEEDKAEKSSTDFRDCTLQQLQQSTRNTDALRNPHRTNSFSLSPLHSNTKINGAHHSTVQGPSSTKSTSSVSTFSKAAPSVPSKPSDCNFISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKLKKMKTGRSALVVTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRAPLRPGANPQLEWQYYQNKILKGKAADIPDSSLWENPDSAQANGIDSVLSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQLVPTNLNPSTCPSRPSVQSSHFPSGSYSVRDVFQVQKAKKSTEEEHKEVFRAAVDLEISSASRTCTFLPPFPAHLPTSPDTNKAESSGKWNGLHTPVSVQSRLNLSIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQAESHGDKKKEPVNGCNTGILPQPVGTVLLQIPEPQESNSDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQRQGENSTHQQSASASVPKNPLLHLKAAVKEKKRNKKKKTIGSPKRIQSPLNNKLLNSPAKTLPGACGSPQKLIDGFLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT	chr2:99400475-99490035[-]	Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.	PDB: 2EBW; PDB: 2LSI; PDB: 2LSK; PDB: 2LSY; PDB: 2N1G; PDB: 3GQC; PDB: 3VU7; PDB: 4BA9; PDB: 4EXT; PDB: 4GK0; PDB: 4GK5; PDB: 5VZM; PDB: 6ASR; PDB: 6AXD; PDB: 6WS0; PDB: 6WS5	HGNC:14060	REV1_HUMAN	Reviewed	ENSG00000135945	.	.	.	.	.
Mol00600	Protein	DNA polymerase zeta catalytic subunit (REV3L)	Protein reversionless 3-like; REV3-like; hREV3; POLZ; REV3	REV3L	5980	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368802.8, REV3L-202, 10706; ENST00000435970.5, REV3L-206, 10943; ENST00000358835.7, REV3L-201, 10815; ENST00000619481.1, REV3L-213, 969; ENST00000422377.5, REV3L-204, 10964; ENST00000434009.5, REV3L-205, 10644; ENST00000413831.1, REV3L-203, 891; ENST00000462119.5, REV3L-208, 2518; ENST00000467500.1, REV3L-209, 538; ENST00000492520.1, REV3L-211, 442; ENST00000460981.1, REV3L-207, 441; ENST00000470871.1, REV3L-210, 386; ENST00000494858.1, REV3L-212, 281"	MFSVRIVTADYYMASPLQGLDTCQSPLTQAPVKKVPVVRVFGATPAGQKTCLHLHGIFPYLYVPYDGYGQQPESYLSQMAFSIDRALNVALGNPSSTAQHVFKVSLVSGMPFYGYHEKERHFMKIYLYNPTMVKRICELLQSGAIMNKFYQPHEAHIPYLLQLFIDYNLYGMNLINLAAVKFRKARRKSNTLHATGSCKNHLSGNSLADTLFRWEQDEIPSSLILEGVEPQSTCELEVDAVAADILNRLDIEAQIGGNPGLQAIWEDEKQRRRNRNETSQMSQPESQDHRFVPATESEKKFQKRLQEILKQNDFSVTLSGSVDYSDGSQEFSAELTLHSEVLSPEMLQCTPANMVEVHKDKESSKGHTRHKVEEALINEEAILNLMENSQTFQPLTQRLSESPVFMDSSPDEALVHLLAGLESDGYRGERNRMPSPCRSFGNNKYPQNSDDEENEPQIEKEEMELSLVMSQRWDSNIEEHCAKKRSLCRNTHRSSTEDDDSSSGEEMEWSDNSLLLASLSIPQLDGTADENSDNPLNNENSRTHSSVIATSKLSVKPSIFHKDAATLEPSSSAKITFQCKHTSALSSHVLNKEDLIEDLSQTNKNTEKGLDNSVTSFTNESTYSMKYPGSLSSTVHSENSHKENSKKEILPVSSCESSIFDYEEDIPSVTRQVPSRKYTNIRKIEKDSPFIHMHRHPNENTLGKNSFNFSDLNHSKNKVSSEGNEKGNSTALSSLFPSSFTENCELLSCSGENRTMVHSLNSTADESGLNKLKIRYEEFQEHKTEKPSLSQQAAHYMFFPSVVLSNCLTRPQKLSPVTYKLQPGNKPSRLKLNKRKLAGHQETSTKSSETGSTKDNFIQNNPCNSNPEKDNALASDLTKTTRGAFENKTPTDGFIDCHFGDGTLETEQSFGLYGNKYTLRAKRKVNYETEDSESSFVTHNSKISLPHPMEIGESLDGTLKSRKRRKMSKKLPPVIIKYIIINRFRGRKNMLVKLGKIDSKEKQVILTEEKMELYKKLAPLKDFWPKVPDSPATKYPIYPLTPKKSHRRKSKHKSAKKKTGKQQRTNNENIKRTLSFRKKRSHAILSPPSPSYNAETEDCDLNYSDVMSKLGFLSERSTSPINSSPPRCWSPTDPRAEEIMAAAEKEAMLFKGPNVYKKTVNSRIGKTSRARAQIKKSKAKLANPSIVTKKRNKRNQTNKLVDDGKKKPRAKQKTNEKGTSRKHTTLKDEKIKSQSGAEVKFVLKHQNVSEFASSSGGSQLLFKQKDMPLMGSAVDHPLSASLPTGINAQQKLSGCFSSFLESKKSVDLQTFPSSRDDLHPSVVCNSIGPGVSKINVQRPHNQSAMFTLKESTLIQKNIFDLSNHLSQVAQNTQISSGMSSKIEDNANNIQRNYLSSIGKLSEYRNSLESKLDQAYTPNFLHCKDSQQQIVCIAEQSKHSETCSPGNTASEESQMPNNCFVTSLRSPIKQIAWEQKQRGFILDMSNFKPERVKPRSLSEAISQTKALSQCKNRNVSTPSAFGEGQSGLAVLKELLQKRQQKAQNANTTQDPLSNKHQPNKNISGSLEHNKANKRTRSVTSPRKPRTPRSTKQKEKIPKLLKVDSLNLQNSSQLDNSVSDDSPIFFSDPGFESCYSLEDSLSPEHNYNFDINTIGQTGFCSFYSGSQFVPADQNLPQKFLSDAVQDLFPGQAIEKNEFLSHDNQKCDEDKHHTTDSASWIRSGTLSPEIFEKSTIDSNENRRHNQWKNSFHPLTTRSNSIMDSFCVQQAEDCLSEKSRLNRSSVSKEVFLSLPQPNNSDWIQGHTRKEMGQSLDSANTSFTAILSSPDGELVDVACEDLELYVSRNNDMLTPTPDSSPRSTSSPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHDLSETIYQEPFCSNPSDVPEKPREIGGRLLMVETRLANDLAEFEGDFSLEGLRLWKTAFSAMTQNPRPGSPLRSGQGVVNKGSSNSPKMVEDKKIVIMPCKCAPSRQLVQVWLQAKEEYERSKKLPKTKPTGVVKSAENFSSSVNPDDKPVVPPKMDVSPCILPTTAHTKEDVDNSQIALQAPTTGCSQTASESQMLPPVASASDPEKDEDDDDNYYISYSSPDSPVIPPWQQPISPDSKALNGDDRPSSPVEELPSLAFENFLKPIKDGIQKSPCSEPQEPLVISPINTRARTGKCESLCFHSTPIIQRKLLERLPEAPGLSPLSTEPKTQKLSNKKGSNTDTLRRVLLTQAKNQFAAVNTPQKETSQIDGPSLNNTYGFKVSIQNLQEAKALHEIQNLTLISVELHARTRRDLEPDPEFDPICALFYCISSDTPLPDTEKTELTGVIVIDKDKTVFSQDIRYQTPLLIRSGITGLEVTYAADEKALFHEIANIIKRYDPDILLGYEIQMHSWGYLLQRAAALSIDLCRMISRVPDDKIENRFAAERDEYGSYTMSEINIVGRITLNLWRIMRNEVALTNYTFENVSFHVLHQRFPLFTFRVLSDWFDNKTDLYRWKMVDHYVSRVRGNLQMLEQLDLIGKTSEMARLFGIQFLHVLTRGSQYRVESMMLRIAKPMNYIPVTPSVQQRSQMRAPQCVPLIMEPESRFYSNSVLVLDFQSLYPSIVIAYNYCFSTCLGHVENLGKYDEFKFGCTSLRVPPDLLYQVRHDITVSPNGVAFVKPSVRKGVLPRMLEEILKTRFMVKQSMKAYKQDRALSRMLDARQLGLKLIANVTFGYTSANFSGRMPCIEVGDSIVHKARETLERAIKLVNDTKKWGARVVYGDTDSMFVLLKGATKEQSFKIGQEIAEAVTATNPKPVKLKFEKVYLPCVLQTKKRYVGYMYETLDQKDPVFDAKGIETVRRDSCPAVSKILERSLKLLFETRDISLIKQYVQRQCMKLLEGKASIQDFIFAKEYRGSFSYKPGACVPALELTRKMLTYDRRSEPQVGERVPYVIIYGTPGVPLIQLVRRPVEVLQDPTLRLNATYYITKQILPPLARIFSLIGIDVFSWYHELPRIHKATSSSRSEPEGRKGTISQYFTTLHCPVCDDLTQHGICSKCRSQPQHVAVILNQEIRELERQQEQLVKICKNCTGCFDRHIPCVSLNCPVLFKLSRVNRELSKAPYLRQLLDQF	chr6:111299028-111483715[-]	"Catalytic subunit of the DNA polymerase zeta complex, an error-prone polymerase specialized in translesion DNA synthesis (TLS). Lacks an intrinsic 3'-5' exonuclease activity and thus has no proofreading function."	PDB: 3ABD; PDB: 3ABE; PDB: 3VU7; PDB: 4EXT; PDB: 4GK0; PDB: 4GK5; PDB: 5O8K; PDB: 6BC8; PDB: 6BCD; PDB: 6BI7; PDB: 6EKM; PDB: 6KEA; PDB: 6WS0; PDB: 6WS5	HGNC:9968	REV3L_HUMAN	Reviewed	ENSG00000009413	.	.	.	.	.
Mol00601	Protein	Rho-related GTP-binding protein RhoB (RHOB)	Rho cDNA clone 6; h6; ARH6; ARHB	RHOB	388	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000272233.6, RHOB-201, 2367"	MAAIRKKLVVVGDGACGKTCLLIVFSKDEFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSVDSPDSLENIPEKWVPEVKHFCPNVPIILVANKKDLRSDEHVRTELARMKQEPVRTDDGRAMAVRIQAYDYLECSAKTKEGVREVFETATRAALQKRYGSQNGCINCCKVL	chr2:20447074-20449440[+]	Mediates apoptosis in neoplastically transformed cells after DNA damage. Not essential for development but affects cell adhesion and growth factor signaling in transformed cells. Plays a negative role in tumorigenesis as deletion causes tumor formation. Involved in intracellular protein trafficking of a number of proteins. Targets PKN1 to endosomes and is involved in trafficking of the EGF receptor from late endosomes to lysosomes. Also required for stability and nuclear trafficking of AKT1/AKT which promotes endothelial cell survival during vascular development. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Required for genotoxic stress-induced cell death in breast cancer cells.	PDB: 2FV8; PDB: 6HXU; PDB: 6SGE	HGNC:668	RHOB_HUMAN	Reviewed	ENSG00000143878	.	.	.	.	.
Mol00602	Protein	Rapamycin-insensitive companion of mTOR (RICTOR)	AVO3 homolog; hAVO3; KIAA1999	RICTOR	253260	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357387.8, RICTOR-202, 9533; ENST00000296782.9, RICTOR-201, 7505; ENST00000514735.1, RICTOR-209, 686; ENST00000511516.5, RICTOR-207, 7312; ENST00000503698.1, RICTOR-203, 780; ENST00000509567.5, RICTOR-205, 638; ENST00000510711.5, RICTOR-206, 3126; ENST00000513566.1, RICTOR-208, 1762; ENST00000515846.1, RICTOR-210, 677; ENST00000505927.1, RICTOR-204, 570"	MAAIGRGRSLKNLRVRGRNDSGEENVPLDLTREPSDNLREILQNVARLQGVSNMRKLGHLNNFTKLLCDIGHSEEKLGFHYEDIIICLRLALLNEAKEVRAAGLRALRYLIQDSSILQKVLKLKVDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNSLIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFILKDTEEALLINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLYANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKILTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQLEKWHREYNSKYVDLIEEQLNEALTTYRKPVDGDNYVRRSNQRLQRPHVYLPIHLYGQLVHHKTGCHLLEVQNIITELCRNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWDAVRHSRKHLWPVVPDDVEQLCNELSSIPSTLSLNSESTSSRHNSESESVPSSMFILEDDRFGSSSTSTFFLDINEDTEPTFYDRSGPIKDKNSFPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQLETSFMGNKHIEDTGSTPSIGENDLKFTKNFGTENHRENTSRERLVVESSTSSHMKIRSQSFNTDTTTSGISSMSSSPSRETVGVDATTMDTDCGSMSTVVSTKTIKTSHYLTPQSNHLSLSKSNSVSLVPPGSSHTLPRRAQSLKAPSIATIKSLADCNFSYTSSRDAFGYATLKRLQQQRMHPSLSHSEALASPAKDVLFTDTITMKANSFESRLTPSRFMKALSYASLDKEDLLSPINQNTLQRSSSVRSMVSSATYGGSDDYIGLALPVDINDIFQVKDIPYFQTKNIPPHDDRGARAFAHDAGGLPSGTGGLVKNSFHLLRQQMSLTEIMNSIHSDASLFLESTEDTGLQEHTDDNCLYCVCIEILGFQPSNQLSAICSHSDFQDIPYSDWCEQTIHNPLEVVPSKFSGISGCSDGVSQEGSASSTKSTELLLGVKTIPDDTPMCRILLRKEVLRLVINLSSSVSTKCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLPCRRFIQELFQDVQFLQMHEEAEAVLATPPKQPIVDTSAES	chr5:38937920-39074399[-]	"Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in embryonic growth and development."	PDB: 5ZCS; PDB: 6ZWM; PDB: 6ZWO; PDB: 7PE7; PDB: 7PE8; PDB: 7PE9	HGNC:28611	RICTR_HUMAN	Reviewed	ENSG00000164327	.	.	.	.	.
Mol00603	Protein	E3 ubiquitin-protein ligase RING2 (RING2)	Huntingtin-interacting protein 2-interacting protein 3; HIP2-interacting protein 3; Protein DinG; RING finger protein 1B; RING1b; RING finger protein 2; RING finger protein BAP-1; RING-type E3 ubiquitin transferase RING2; BAP1; DING; HIPI3; RING1B	RNF2	6045	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367510.8, RNF2-202, 3407; ENST00000367509.8, RNF2-201, 1677; ENST00000453650.2, RNF2-203, 939; ENST00000498201.1, RNF2-204, 631"	MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAMAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK	chr1:185045526-185102603[+]	"E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity (Probable). Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes. Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation."	PDB: 2H0D; PDB: 3GS2; PDB: 3H8H; PDB: 3IXS; PDB: 3RPG; PDB: 4R8P; PDB: 4S3O; PDB: 7ND1	HGNC:10061	RING2_HUMAN	Reviewed	ENSG00000121481	.	.	.	.	.
Mol00604	Protein	Ribonucleoside-diphosphate reductase large subunit (RRM1)	Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit; RR1	RRM1	6240	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000300738.10, RRM1-201, 3142; ENST00000534285.5, RRM1-214, 2075; ENST00000532170.5, RRM1-210, 3166; ENST00000533349.5, RRM1-212, 2863; ENST00000533495.5, RRM1-213, 2381; ENST00000528442.5, RRM1-205, 783; ENST00000528470.5, RRM1-206, 579; ENST00000526865.5, RRM1-204, 562; ENST00000532710.5, RRM1-211, 549; ENST00000526304.5, RRM1-202, 514; ENST00000531591.5, RRM1-209, 639; ENST00000526350.5, RRM1-203, 583; ENST00000529109.1, RRM1-207, 448; ENST00000530368.1, RRM1-208, 332"	MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS	chr11:4094707-4138932[+]	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.	PDB: 2WGH; PDB: 3HNC; PDB: 3HND; PDB: 3HNE; PDB: 3HNF; PDB: 4X3V; PDB: 5D1Y; PDB: 5TUS; PDB: 6AUI; PDB: 6L3R; PDB: 6L7L; PDB: 6LKM	HGNC:10451	RIR1_HUMAN	Reviewed	ENSG00000167325	.	.	.	.	.
Mol00605	Protein	Ribonucleoside-diphosphate reductase subunit M2 (RRM2)	Ribonucleotide reductase small chain; Ribonucleotide reductase small subunit; RR2	RRM2	6241	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000304567.10, RRM2-201, 3258; ENST00000360566.6, RRM2-202, 3673; ENST00000641198.1, RRM2-213, 3431; ENST00000615152.5, RRM2-212, 3240; ENST00000641498.1, RRM2-214, 1996; ENST00000646978.1, RRM2-216, 911; ENST00000381786.7, RRM2-203, 1897; ENST00000642996.1, RRM2-215, 656; ENST00000607140.1, RRM2-211, 332; ENST00000652660.1, RRM2-217, 3271; ENST00000459969.5, RRM2-204, 787; ENST00000491447.1, RRM2-209, 644; ENST00000487591.5, RRM2-208, 592; ENST00000461327.5, RRM2-205, 580; ENST00000485717.1, RRM2-207, 573; ENST00000498343.5, RRM2-210, 560; ENST00000462343.1, RRM2-206, 454"	MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKTKAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDADF	chr2:10120698-10211725[+]	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.	PDB: 2UW2; PDB: 3OLJ; PDB: 3VPM; PDB: 3VPN; PDB: 3VPO	HGNC:10452	RIR2_HUMAN	Reviewed	ENSG00000171848	.	.	.	.	.
Mol00606	Protein	Rho-related GTP-binding protein RhoE (RND3)	Protein MemB; Rho family GTPase 3; Rho-related GTP-binding protein Rho8; Rnd3; ARHE; RHO8; RHOE	RND3	390	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263895.9, RND3-201, 2684; ENST00000375734.6, RND3-202, 2777; ENST00000409557.5, RND3-203, 2372; ENST00000439275.1, RND3-204, 505; ENST00000454202.5, RND3-205, 481; ENST00000472416.1, RND3-207, 457; ENST00000497865.5, RND3-209, 880; ENST00000473639.1, RND3-208, 432; ENST00000466334.1, RND3-206, 385"	MKERRASQKLSSKSIMDPNQNVKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSALQSENSVRDIFHVATLACVNKTNKNVKRNKSQRATKRISHMPSRPELSAVATDLRKDKAKSCTVM	chr2:150468195-150539011[-]	Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins.	PDB: 1M7B; PDB: 2V55; PDB: 4BG6	HGNC:671	RND3_HUMAN	Reviewed	ENSG00000115963	.	.	.	.	.
Mol00607	Protein	Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1)	hnRNP A1; Helix-destabilizing protein; Single-strand RNA-binding protein; hnRNP core protein A1; HNRPA1	HNRNPA1	3178	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000340913.11, HNRNPA1-202, 3744; ENST00000546500.5, HNRNPA1-203, 4121; ENST00000677210.1, HNRNPA1-231, 2793; ENST00000550482.2, HNRNPA1-209, 2596; ENST00000677385.1, HNRNPA1-238, 3999; ENST00000677249.1, HNRNPA1-234, 2278; ENST00000678077.1, HNRNPA1-250, 2067; ENST00000677375.1, HNRNPA1-237, 1811; ENST00000547276.5, HNRNPA1-204, 1539; ENST00000330752.12, HNRNPA1-201, 1294; ENST00000548688.5, HNRNPA1-208, 711; ENST00000547708.5, HNRNPA1-206, 530; ENST00000551702.5, HNRNPA1-213, 481; ENST00000679101.1, HNRNPA1-279, 394; ENST00000677840.1, HNRNPA1-247, 362; ENST00000676951.1, HNRNPA1-227, 312; ENST00000678611.1, HNRNPA1-266, 297; ENST00000678970.1, HNRNPA1-275, 292; ENST00000676853.1, HNRNPA1-223, 291; ENST00000678581.1, HNRNPA1-264, 291; ENST00000678424.1, HNRNPA1-260, 288; ENST00000677778.1, HNRNPA1-245, 281; ENST00000679079.1, HNRNPA1-278, 277; ENST00000679026.1, HNRNPA1-276, 277; ENST00000676794.1, HNRNPA1-221, 264; ENST00000678919.1, HNRNPA1-272, 254; ENST00000677645.1, HNRNPA1-243, 249; ENST00000677636.1, HNRNPA1-242, 249; ENST00000678347.1, HNRNPA1-256, 249; ENST00000678876.1, HNRNPA1-270, 249; ENST00000677945.1, HNRNPA1-249, 234; ENST00000678873.1, HNRNPA1-269, 231; ENST00000679063.1, HNRNPA1-277, 231; ENST00000678412.1, HNRNPA1-258, 216; ENST00000678934.1, HNRNPA1-273, 210; ENST00000676707.1, HNRNPA1-219, 210; ENST00000677666.1, HNRNPA1-244, 196; ENST00000676472.1, HNRNPA1-215, 195; ENST00000678690.1, HNRNPA1-268, 190; ENST00000678513.1, HNRNPA1-263, 183; ENST00000678597.1, HNRNPA1-265, 180; ENST00000677291.1, HNRNPA1-236, 168; ENST00000677224.1, HNRNPA1-233, 165; ENST00000677279.1, HNRNPA1-235, 162; ENST00000676886.1, HNRNPA1-225, 144; ENST00000678456.1, HNRNPA1-262, 135; ENST00000677518.1, HNRNPA1-240, 126; ENST00000677847.1, HNRNPA1-248, 96; ENST00000678947.1, HNRNPA1-274, 42; ENST00000677488.1, HNRNPA1-239, 36; ENST00000547566.5, HNRNPA1-205, 1234; ENST00000676842.1, HNRNPA1-222, 489; ENST00000677191.1, HNRNPA1-230, 463; ENST00000550994.2, HNRNPA1-210, 455; ENST00000677539.1, HNRNPA1-241, 445; ENST00000676572.1, HNRNPA1-217, 349; ENST00000677220.1, HNRNPA1-232, 338; ENST00000679344.1, HNRNPA1-284, 324; ENST00000678448.1, HNRNPA1-261, 315; ENST00000678212.1, HNRNPA1-254, 311; ENST00000679273.1, HNRNPA1-282, 303; ENST00000678199.1, HNRNPA1-253, 293; ENST00000676661.1, HNRNPA1-218, 271; ENST00000676925.1, HNRNPA1-226, 270; ENST00000677072.1, HNRNPA1-229, 267; ENST00000677832.1, HNRNPA1-246, 259; ENST00000677061.1, HNRNPA1-228, 249; ENST00000679251.1, HNRNPA1-281, 215; ENST00000551803.1, HNRNPA1-214, 372; ENST00000678103.1, HNRNPA1-252, 242; ENST00000678900.1, HNRNPA1-271, 163; ENST00000678279.1, HNRNPA1-255, 142; ENST00000678365.1, HNRNPA1-257, 119; ENST00000676855.1, HNRNPA1-224, 111; ENST00000679319.1, HNRNPA1-283, 105; ENST00000676528.1, HNRNPA1-216, 105; ENST00000678687.1, HNRNPA1-267, 102; ENST00000678093.1, HNRNPA1-251, 89; ENST00000679228.1, HNRNPA1-280, 2515; ENST00000678418.1, HNRNPA1-259, 2008; ENST00000676725.1, HNRNPA1-220, 1987; ENST00000547870.2, HNRNPA1-207, 1610; ENST00000551665.1, HNRNPA1-211, 925; ENST00000551679.1, HNRNPA1-212, 359"	MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF	chr12:54280193-54287088[+]	"Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform. Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1. May bind to specific miRNA hairpins."	PDB: 1HA1; PDB: 1L3K; PDB: 1PGZ; PDB: 1PO6; PDB: 1U1K; PDB: 1U1L; PDB: 1U1M; PDB: 1U1N; PDB: 1U1O; PDB: 1U1P; PDB: 1U1Q; PDB: 1U1R; PDB: 1UP1; PDB: 2H4M; PDB: 2LYV; PDB: 2UP1; PDB: 4YOE; PDB: 5MPG; PDB: 5MPL; PDB: 5ZGD; PDB: 5ZGL; PDB: 6BXX; PDB: 6DCL; PDB: 6J60; PDB: 7BX7	HGNC:5031	ROA1_HUMAN	Reviewed	ENSG00000135486	.	.	.	.	.
Mol00608	Protein	hnRNP A2/B1 (HNRNPA2B1)	hnRNP A2/B1; HNRPA2B1	HNRNPA2B1	3181	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000618183.5, HNRNPA2B1-209, 3628; ENST00000677839.1, HNRNPA2B1-226, 4333; ENST00000356674.8, HNRNPA2B1-202, 4106; ENST00000354667.8, HNRNPA2B1-201, 3664; ENST00000608362.2, HNRNPA2B1-208, 3497; ENST00000676749.1, HNRNPA2B1-213, 2978; ENST00000677574.1, HNRNPA2B1-222, 4092; ENST00000677906.1, HNRNPA2B1-227, 4068; ENST00000679123.1, HNRNPA2B1-246, 4044; ENST00000679021.1, HNRNPA2B1-245, 3850; ENST00000678449.1, HNRNPA2B1-233, 3754; ENST00000677339.1, HNRNPA2B1-219, 3752; ENST00000678962.1, HNRNPA2B1-241, 3730; ENST00000679001.1, HNRNPA2B1-244, 3706; ENST00000678501.1, HNRNPA2B1-234, 3677; ENST00000679243.1, HNRNPA2B1-248, 3622; ENST00000678431.1, HNRNPA2B1-232, 3522; ENST00000677656.1, HNRNPA2B1-224, 3273; ENST00000676903.1, HNRNPA2B1-214, 3258; ENST00000677631.1, HNRNPA2B1-223, 3064; ENST00000676524.1, HNRNPA2B1-211, 2949; ENST00000676497.1, HNRNPA2B1-210, 2870; ENST00000678675.1, HNRNPA2B1-236, 2731; ENST00000678935.1, HNRNPA2B1-240, 2656; ENST00000678998.1, HNRNPA2B1-243, 2612; ENST00000677396.1, HNRNPA2B1-220, 2577; ENST00000678697.1, HNRNPA2B1-237, 2463; ENST00000676746.1, HNRNPA2B1-212, 2438; ENST00000678779.1, HNRNPA2B1-238, 2348; ENST00000679318.1, HNRNPA2B1-249, 2271; ENST00000678884.1, HNRNPA2B1-239, 2224; ENST00000360787.8, HNRNPA2B1-203, 1724; ENST00000678075.1, HNRNPA2B1-229, 4328; ENST00000678035.1, HNRNPA2B1-228, 4172; ENST00000678277.1, HNRNPA2B1-231, 3907; ENST00000679124.1, HNRNPA2B1-247, 3888; ENST00000677571.1, HNRNPA2B1-221, 3829; ENST00000678973.1, HNRNPA2B1-242, 3816; ENST00000677321.1, HNRNPA2B1-218, 3792; ENST00000678183.1, HNRNPA2B1-230, 3589; ENST00000678631.1, HNRNPA2B1-235, 2416; ENST00000677037.1, HNRNPA2B1-216, 2262; ENST00000490912.6, HNRNPA2B1-206, 6718; ENST00000463181.5, HNRNPA2B1-204, 6284; ENST00000476233.2, HNRNPA2B1-205, 4942; ENST00000677075.1, HNRNPA2B1-217, 4469; ENST00000676932.1, HNRNPA2B1-215, 4269; ENST00000677669.1, HNRNPA2B1-225, 4060; ENST00000495810.2, HNRNPA2B1-207, 1580"	MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY	chr7:26171151-26201529[-]	"Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm. Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion. Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform. Also plays a role in the activation of the innate immune response. Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6. In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production."	PDB: 1X4B; PDB: 5EN1; PDB: 5HO4; PDB: 5WWE; PDB: 5WWF; PDB: 5WWG; PDB: 6WPQ; PDB: 6WQK	HGNC:5033	ROA2_HUMAN	Reviewed	ENSG00000122566	.	.	.	.	.
Mol00609	Protein	Rho-associated protein kinase 2 (ROCK2)	Rho kinase 2; Rho-associated; coiled-coil-containing protein kinase 2; Rho-associated; coiled-coil-containing protein kinase II; ROCK-II; p164 ROCK-2; KIAA0619	ROCK2	9475	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000315872.11, ROCK2-202, 8345; ENST00000401753.5, ROCK2-203, 4017; ENST00000431087.1, ROCK2-204, 729; ENST00000261535.7, ROCK2-201, 1795; ENST00000462366.1, ROCK2-206, 563; ENST00000484951.1, ROCK2-207, 895; ENST00000460262.1, ROCK2-205, 597; ENST00000493096.1, ROCK2-208, 461"	MSRPPPTGKMPGAPETAPGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWHWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCRETDSIQSRKNEESQEIQKKLYTLEEHLSNEMQAKEELEQKCKSVNTRLEKTAKELEEEITLRKSVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRICGLEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISTAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS	chr2:11179759-11348330[-]	"Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation."	PDB: 4L6Q; PDB: 4WOT; PDB: 5U7Q; PDB: 5U7R; PDB: 6ED6; PDB: 6P5M; PDB: 6P5P; PDB: 7JNT; PDB: 7JOV	HGNC:10252	ROCK2_HUMAN	Reviewed	ENSG00000134318	.	.	.	.	.
Mol00610	Protein	DNA-directed RNA polymerase I subunit RPA12 (RPA12)	DNA-directed RNA polymerase I subunit H; Zinc ribbon domain-containing protein 1; RPA12; ZNRD1	POLR1H	30834	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000332435.10, POLR1H-201, 851; ENST00000376785.2, POLR1H-204, 754; ENST00000359374.8, POLR1H-202, 743; ENST00000376782.6, POLR1H-203, 736; ENST00000463141.1, POLR1H-205, 571; ENST00000471008.5, POLR1H-206, 3672"	MSVMDLANTCSSFQSDLDFCSDCGSVLPLPGAQDTVTCIRCGFNINVRDFEGKVVKTSVVFHQLGTAMPMSVEEGPECQGPVVDRRCPRCGHEGMAYHTRQMRSADEGQTVFYTCTNCKFQEKEDS	chr6:30058899-30064909[+]	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors.	.	HGNC:13182	RPA12_HUMAN	Reviewed	ENSG00000066379	.	.	.	.	.
Mol00611	Protein	Ribonuclease P protein subunit p21 (RPP21)	RNaseP protein p21; Ribonuclease P/MRP 21 kDa subunit; Ribonucleoprotein V; C6orf135; CAT60	RPP21	79897	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000442966.7, RPP21-224, 528; ENST00000433076.6, RPP21-222, 577; ENST00000436442.2, RPP21-223, 522; ENST00000428040.6, RPP21-221, 594; ENST00000466327.5, RPP21-225, 697; ENST00000491477.5, RPP21-228, 457; ENST00000489124.5, RPP21-227, 450; ENST00000498414.5, RPP21-229, 1492; ENST00000473266.1, RPP21-226, 621"	MAGPVKDREAFQRLNFLYQAAHCVLAQDPENQALARFYCYTERTIAKRLVLRRDPSVKRTLCRGCSSLLVPGLTCTQRQRRCRGQRWTVQTCLTCQRSQRFLNDPGHLLWGDRPEAQLGSQADSKPLQPLPNTAHSISDRLPEEKMQTQGSSNQ	chr6:30345131-30346884[+]	"Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends."	PDB: 6AHR; PDB: 6AHU	HGNC:21300	RPP21_HUMAN	Reviewed	ENSG00000241370	.	.	.	.	.
Mol00612	Protein	Remodeling and spacing factor 1 (RSF1)	Rsf-1; HBV pX-associated protein 8; Hepatitis B virus X-associated protein; p325 subunit of RSF chromatin-remodeling complex; HBXAP; XAP8	RSF1	51773	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308488.11, RSF1-201, 11242; ENST00000480887.5, RSF1-204, 5318; ENST00000526324.5, RSF1-205, 2409; ENST00000528095.5, RSF1-206, 2107; ENST00000531026.5, RSF1-209, 830; ENST00000440064.2, RSF1-202, 604; ENST00000532556.1, RSF1-211, 495; ENST00000530604.1, RSF1-208, 520; ENST00000534794.1, RSF1-212, 487; ENST00000467567.1, RSF1-203, 2982; ENST00000531768.1, RSF1-210, 626; ENST00000529470.1, RSF1-207, 448"	MATAAAAAAVMAPPGCPGSCPNFAVVCSFLERYGPLLDLPELPFPELERVLQAPPPDVGNGEVPKELVELHLKLMRKIGKSVTADRWEKYLIKICQEFNSTWAWEMEKKGYLEMSVECKLALLKYLCECQFDDNLKFKNIINEEDADTMRLQPIGRDKDGLMYWYQLDQDHNVRMYIEEQDDQDGSSWKCIVRNRNELAETLALLKAQIDPVLLKNSSQQDNSSRESPSLEDEETKKEEETPKQEEQKESEKMKSEEQPMDLENRSTANVLEETTVKKEKEDEKELVKLPVIVKLEKPLPENEEKKIIKEESDSFKENVKPIKVEVKECRADPKDTKSSMEKPVAQEPERIEFGGNIKSSHEITEKSTEETEKLKNDQQAKIPLKKREIKLSDDFDSPVKGPLCKSVTPTKEFLKDEIKQEEETCKRISTITALGHEGKQLVNGEVSDERVAPNFKTEPIETKFYETKEESYSPSKDRNIITEGNGTESLNSVITSMKTGELEKETAPLRKDADSSISVLEIHSQKAQIEEPDPPEMETSLDSSEMAKDLSSKTALSSTESCTMKGEEKSPKTKKDKRPPILECLEKLEKSKKTFLDKDAQRLSPIPEEVPKSTLESEKPGSPEAAETSPPSNIIDHCEKLASEKEVVECQSTSTVGGQSVKKVDLETLKEDSEFTKVEMDNLDNAQTSGIEEPSETKGSMQKSKFKYKLVPEEETTASENTEITSERQKEGIKLTIRISSRKKKPDSPPKVLEPENKQEKTEKEEEKTNVGRTLRRSPRISRPTAKVAEIRDQKADKKRGEGEDEVEEESTALQKTDKKEILKKSEKDTNSKVSKVKPKGKVRWTGSRTRGRWKYSSNDESEGSGSEKSSAASEEEEEKESEEAILADDDEPCKKCGLPNHPELILLCDSCDSGYHTACLRPPLMIIPDGEWFCPPCQHKLLCEKLEEQLQDLDVALKKKERAERRKERLVYVGISIENIIPPQEPDFSEDQEEKKKDSKKSKANLLERRSTRTRKCISYRFDEFDEAIDEAIEDDIKEADGGGVGRGKDISTITGHRGKDISTILDEERKENKRPQRAAAARRKKRRRLNDLDSDSNLDEEESEDEFKISDGSQDEFVVSDENPDESEEDPPSNDDSDTDFCSRRLRRHPSRPMRQSRRLRRKTPKKKYSDDDEEEESEENSRDSESDFSDDFSDDFVETRRRRSRRNQKRQINYKEDSESDGSQKSLRRGKEIRRVHKRRLSSSESEESYLSKNSEDDELAKESKRSVRKRGRSTDEYSEADEEEEEEEGKPSRKRLHRIETDEEESCDNAHGDANQPARDSQPRVLPSEQESTKKPYRIESDEEEDFENVGKVGSPLDYSLVDLPSTNGQSPGKAIENLIGKPTEKSQTPKDNSTASASLASNGTSGGQEAGAPEEEEDELLRVTDLVDYVCNSEQL	chr11:77660009-77820869[-]	"Regulatory subunit of the ATP-dependent RSF-1 and RSF-5 ISWI chromatin-remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair. Binds to core histones together with SMARCA5, and is required for the assembly of regular nucleosome arrays by the RSF-5 ISWI chromatin-remodeling complex. Directly stimulates the ATPase activity of SMARCA1 and SMARCA5 in the RSF-1 and RSF-5 ISWI chromatin-remodeling complexes, respectively. The RSF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the RSF-5 ISWI chromatin-remodeling complex. The complexes do not have the ability to slide mononucleosomes to the center of a DNA template. Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF-alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain."	.	HGNC:18118	RSF1_HUMAN	Reviewed	ENSG00000048649	.	.	.	.	.
Mol00613	Protein	Ras suppressor protein 1 (RSU1)	RSP-1; Rsu-1; RSP1	RSU1	6251	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000345264.10, RSU1-201, 3730; ENST00000377921.7, RSU1-203, 3919; ENST00000602389.1, RSU1-205, 3639; ENST00000464074.6, RSU1-204, 1141; ENST00000377911.1, RSU1-202, 955"	MSKSLKKLVEESREKNQPEVDMSDRGISNMLDVNGLFTLSHITQLVLSHNKLTMVPPNIAELKNLEVLNFFNNQIEELPTQISSLQKLKHLNLGMNRLNTLPRGFGSLPALEVLDLTYNNLSENSLPGNFFYLTTLRALYLSDNDFEILPPDIGKLTKLQILSLRDNDLISLPKEIGELTQLKELHIQGNRLTVLPPELGNLDLTGQKQVFKAENNPWVTPIADQFQLGVSHVFEYIRSETYKYLYGRHMQANPEPPKKNNDKSKKISRKPLAAKNR	chr10:16590611-16817463[-]	Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro.	PDB: 7D2S; PDB: 7D2T; PDB: 7D2U; PDB: 7LT8; PDB: 7LT9	HGNC:10464	RSU1_HUMAN	Reviewed	ENSG00000148484	.	.	.	.	.
Mol00614	Protein	Runt-related transcription factor 2 (RUNX2)	Acute myeloid leukemia 3 protein; Core-binding factor subunit alpha-1; CBF-alpha-1; Oncogene AML-3; Osteoblast-specific transcription factor 2; OSF-2; Polyomavirus enhancer-binding protein 2 alpha A subunit; PEA2-alpha A; PEBP2-alpha A; SL3-3 enhancer factor 1 alpha A subunit; SL3/AKV core-binding factor alpha A subunit; AML3; CBFA1; OSF2; PEBP2A	RUNX2	860	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000647337.2, RUNX2-212, 5540; ENST00000371438.5, RUNX2-204, 5698; ENST00000371432.7, RUNX2-202, 5487; ENST00000371436.10, RUNX2-203, 1588; ENST00000625924.1, RUNX2-210, 1458; ENST00000359524.7, RUNX2-201, 5390; ENST00000576263.5, RUNX2-209, 2256; ENST00000646519.1, RUNX2-211, 5877; ENST00000478660.6, RUNX2-206, 2308; ENST00000483377.5, RUNX2-208, 1475; ENST00000483243.5, RUNX2-207, 464; ENST00000473041.1, RUNX2-205, 283"	MASNSLFSTVTPCQQNFFWDPSTSRRFSPPSSSLQPGKMSDVSPVVAAQQQQQQQQQQQQQQQQQQQQQQQEAAAAAAAAAAAAAAAAAVPRLRPPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFSDRLSDLGRIPHPSMRVGVPPQNPRPSLNSAPSPFNPQGQSQITDPRQAQSSPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPAITDVPRRISDDDTATSDFCLWPSTLSKKSQAGASELGPFSDPRQFPSISSLTESRFSNPRMHYPATFTYTPPVTSGMSLGMSATTHYHTYLPPPYPGSSQSQSGPFQTSSTPYLYYGTSSGSYQFPMVPGGDRSPSRMLPPCTTTSNGSTLLNPNLPNQNDGVDADGSHSSSPTVLNSSGRMDESVWRPY	chr6:45328157-45664349[+]	"Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis. Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE). Inhibits KAT6B-dependent transcriptional activation."	PDB: 6VG8; PDB: 6VGD; PDB: 6VGE; PDB: 6VGG	HGNC:10472	RUNX2_HUMAN	Reviewed	ENSG00000124813	.	.	.	.	.
Mol00615	Protein	Runt-related transcription factor 3 (RUNX3)	Acute myeloid leukemia 2 protein; Core-binding factor subunit alpha-3; CBF-alpha-3; Oncogene AML-2; Polyomavirus enhancer-binding protein 2 alpha C subunit; PEA2-alpha C; PEBP2-alpha C; SL3-3 enhancer factor 1 alpha C subunit; SL3/AKV core-binding factor alpha C subunit; AML2; CBFA3; PEBP2A3	RUNX3	864	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308873.11, RUNX3-201, 4267; ENST00000399916.5, RUNX3-203, 4340; ENST00000338888.3, RUNX3-202, 2629; ENST00000496967.1, RUNX3-205, 572; ENST00000479341.1, RUNX3-204, 284"	MRIPVDPSTSRRFTPPSPAFPCGGGGGKMGENSGALSAQAAVGPGGRARPEVRSMVDVLADHAGELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGDVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPTQVATYHRAIKVTVDGPREPRRHRQKLEDQTKPFPDRFGDLERLRMRVTPSTPSPRGSLSTTSHFSSQPQTPIQGTSELNPFSDPRQFDRSFPTLPTLTESRFPDPRMHYPGAMSAAFPYSATPSGTSISSLSVAGMPATSRFHHTYLPPPYPGAPQNQSGPFQANPSPYHLYYGTSSGSYQFSMVAGSSSGGDRSPTRMLASCTSSAASVAAGNLMNPSLGGQSDGVEADGSHSNSPTALSTPGRMDEAVWRPY	chr1:24899511-24965121[-]	"Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters. May be involved in the control of cellular proliferation and/or differentiation. In association with ZFHX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing."	PDB: 5W69	HGNC:10473	RUNX3_HUMAN	Reviewed	ENSG00000020633	.	.	.	.	.
Mol00616	Protein	Protein S100-A8 (S100A8)	Calgranulin-A; Calprotectin L1L subunit; Cystic fibrosis antigen; CFAG; Leukocyte L1 complex light chain; Migration inhibitory factor-related protein 8; MRP-8; p8; S100 calcium-binding protein A8; Urinary stone protein band A; CAGA; CFAG; MRP8	S100A8	6279	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368733.4, S100A8-202, 408; ENST00000368732.5, S100A8-201, 495; ENST00000477801.1, S100A8-203, 717"	MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE	chr1:153390032-153391073[-]	"S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve proinflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its proinflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the proinflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity."	PDB: 1MR8; PDB: 1XK4; PDB: 4GGF; PDB: 4XJK; PDB: 5HLO; PDB: 5HLV; PDB: 5W1F; PDB: 6DS2	HGNC:10498	S10A8_HUMAN	Reviewed	ENSG00000143546	.	.	.	.	.
Mol00617	Protein	Protein S100-A11 (S100A11)	Calgizzarin; Metastatic lymph node gene 70 protein; MLN 70; Protein S100-C; S100 calcium-binding protein A11; MLN70; S100C	S100A11	6282	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000271638.3, S100A11-201, 563; ENST00000478109.1, S100A11-202, 557"	MAKISSPTETERCIESLIAVFQKYAGKDGYNYTLSKTEFLSFMNTELAAFTKNQKDPGVLDRMMKKLDTNSDGQLDFSEFLNLIGGLAMACHDSFLKAVPSQKRT	chr1:152032506-152047907[-]	Facilitates the differentiation and the cornification of keratinocytes.	PDB: 1V4Z; PDB: 1V50; PDB: 2LUC	HGNC:10488	S10AB_HUMAN	Reviewed	ENSG00000163191	.	.	.	.	.
Mol00618	Protein	Solute carrier family 4 member 4 (SLC4A4)	Sodium bicarbonate cotransporter; Na(+)/HCO3(-) cotransporter; Solute carrier family 4 member 4; kNBC1; NBC; NBC1; NBCE1	SLC4A4	8671	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264485.11, SLC4A4-201, 7716; ENST00000340595.4, SLC4A4-202, 7669; ENST00000425175.5, SLC4A4-204, 7596; ENST00000649996.1, SLC4A4-209, 4270; ENST00000351898.10, SLC4A4-203, 3771; ENST00000512686.5, SLC4A4-205, 2316; ENST00000639096.1, SLC4A4-208, 956; ENST00000638464.1, SLC4A4-207, 468; ENST00000514331.1, SLC4A4-206, 2169"	MEDEAVLDRGASFLKHVCDEEEVEGHHTIYIGVHVPKSYRRRRRHKRKTGHKEKKEKERISENYSDKSDIENADESSSSILKPLISPAAERIRFILGEEDDSPAPPQLFTELDELLAVDGQEMEWKETARWIKFEEKVEQGGERWSKPHVATLSLHSLFELRTCMEKGSIMLDREASSLPQLVEMIVDHQIETGLLKPELKDKVTYTLLRKHRHQTKKSNLRSLADIGKTVSSASRMFTNPDNGSPAMTHRNLTSSSLNDISDKPEKDQLKNKFMKKLPRDAEASNVLVGEVDFLDTPFIAFVRLQQAVMLGALTEVPVPTRFLFILLGPKGKAKSYHEIGRAIATLMSDEVFHDIAYKAKDRHDLIAGIDEFLDEVIVLPPGEWDPAIRIEPPKSLPSSDKRKNMYSGGENVQMNGDTPHDGGHGGGGHGDCEELQRTGRFCGGLIKDIKRKAPFFASDFYDALNIQALSAILFIYLATVTNAITFGGLLGDATDNMQGVLESFLGTAVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDNNFDYLEFRLWIGLWSAFLCLILVATDASFLVQYFTRFTEEGFSSLISFIFIYDAFKKMIKLADYYPINSNFKVGYNTLFSCTCVPPDPANISISNDTTLAPEYLPTMSSTDMYHNTTFDWAFLSKKECSKYGGNLVGNNCNFVPDITLMSFILFLGTYTSSMALKKFKTSPYFPTTARKLISDFAIILSILIFCVIDALVGVDTPKLIVPSEFKPTSPNRGWFVPPFGENPWWVCLAAAIPALLVTILIFMDQQITAVIVNRKEHKLKKGAGYHLDLFWVAILMVICSLMALPWYVAATVISIAHIDSLKMETETSAPGEQPKFLGVREQRVTGTLVFILTGLSVFMAPILKFIPMPVLYGVFLYMGVASLNGVQFMDRLKLLLMPLKHQPDFIYLRHVPLRRVHLFTFLQVLCLALLWILKSTVAAIIFPVMILALVAVRKGMDYLFSQHDLSFLDDVIPEKDKKKKEDEKKKKKKKGSLDSDNDDSDCPYSEKVPSIKIPMDIMEQQPFLSDSKPSDRERSPTFLERHTSC	chr4:71062667-71572087[+]	Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH.	PDB: 6CAA	HGNC:11030	S4A4_HUMAN	Reviewed	ENSG00000080493	.	.	.	.	.
Mol00619	Protein	Sal-like protein 4 (SALL4)	Zinc finger protein 797; Zinc finger protein SALL4; ZNF797	SALL4	57167	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000217086.9, SALL4-201, 5209; ENST00000395997.3, SALL4-203, 1918; ENST00000371539.7, SALL4-202, 1151; ENST00000483130.1, SALL4-205, 782; ENST00000481363.1, SALL4-204, 605"	MSRRKQAKPQHINSEEDQGEQQPQQQTPEFADAAPAAPAAGELGAPVNHPGNDEVASEDEATVKRLRREETHVCEKCCAEFFSISEFLEHKKNCTKNPPVLIMNDSEGPVPSEDFSGAVLSHQPTSPGSKDCHRENGGSSEDMKEKPDAESVVYLKTETALPPTPQDISYLAKGKVANTNVTLQALRGTKVAVNQRSADALPAPVPGANSIPWVLEQILCLQQQQLQQIQLTEQIRIQVNMWASHALHSSGAGADTLKTLGSHMSQQVSAAVALLSQKAGSQGLSLDALKQAKLPHANIPSATSSLSPGLAPFTLKPDGTRVLPNVMSRLPSALLPQAPGSVLFQSPFSTVALDTSKKGKGKPPNISAVDVKPKDEAALYKHKCKYCSKVFGTDSSLQIHLRSHTGERPFVCSVCGHRFTTKGNLKVHFHRHPQVKANPQLFAEFQDKVAAGNGIPYALSVPDPIDEPSLSLDSKPVLVTTSVGLPQNLSSGTNPKDLTGGSLPGDLQPGPSPESEGGPTLPGVGPNYNSPRAGGFQGSGTPEPGSETLKLQQLVENIDKATTDPNECLICHRVLSCQSSLKMHYRTHTGERPFQCKICGRAFSTKGNLKTHLGVHRTNTSIKTQHSCPICQKKFTNAVMLQQHIRMHMGGQIPNTPLPENPCDFTGSEPMTVGENGSTGAICHDDVIESIDVEEVSSQEAPSSSSKVPTPLPSIHSASPTLGFAMMASLDAPGKVGPAPFNLQRQGSRENGSVESDGLTNDSSSLMGDQEYQSRSPDILETTSFQALSPANSQAESIKSKSPDAGSKAESSENSRTEMEGRSSLPSTFIRAPPTYVKVEVPGTFVGPSTLSPGMTPLLAAQPRRQAKQHGCTRCGKNFSSASALQIHERTHTGEKPFVCNICGRAFTTKGNLKVHYMTHGANNNSARRGRKLAIENTMALLGTDGKRVSEIFPKEILAPSVNVDPVVWNQYTSMLNGGLAVKTNEISVIQSGGVPTLPVSLGATSVVNNATVSKMDGSQSGISADVEKPSATDGVPKHQFPHFLEENKIAVS	chr20:51782331-51802521[-]	Transcription factor with a key role in the maintenance and self-renewal of embryonic and hematopoietic stem cells.	PDB: 5XWR; PDB: 6UML; PDB: 7BQU; PDB: 7BQV	HGNC:15924	SALL4_HUMAN	Reviewed	ENSG00000101115	.	.	.	.	.
Mol00620	Protein	Protein salvador homolog 1 (SAV1)	45 kDa WW domain protein; hWW45; WW45	SAV1	60485	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000324679.5, SAV1-201, 3094; ENST00000555720.5, SAV1-203, 3034; ENST00000553731.1, SAV1-202, 744; ENST00000556735.1, SAV1-204, 562; ENST00000557458.1, SAV1-205, 338; ENST00000602664.1, SAV1-206, 870"	MLSRKKTKNEVSKPAEVQGKYVKKETSPLLRNLMPSFIRHGPTIPRRTDICLPDSSPNAFSTSGDVVSRNQSFLRTPIQRTPHEIMRRESNRLSAPSYLARSLADVPREYGSSQSFVTEVSFAVENGDSGSRYYYSDNFFDGQRKRPLGDRAHEDYRYYEYNHDLFQRMPQNQGRHASGIGRVAATSLGNLTNHGSEDLPLPPGWSVDWTMRGRKYYIDHNTNTTHWSHPLEREGLPPGWERVESSEFGTYYVDHTNKKAQYRHPCAPSVPRYDQPPPVTYQPQQTERNQSLLVPANPYHTAEIPDWLQVYARAPVKYDHILKWELFQLADLDTYQGMLKLLFMKELEQIVKMYEAYRQALLTELENRKQRQQWYAQQHGKNF	chr14:50632058-50668306[-]	"Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation."	PDB: 6AO5	HGNC:17795	SAV1_HUMAN	Reviewed	ENSG00000151748	.	.	.	.	.
Mol00621	Protein	Protein transport protein Sec23A (SEC23A)	hSec23A; SEC23-related protein A	SEC23A	10484	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000307712.11, SEC23A-201, 3843; ENST00000537403.5, SEC23A-202, 4215; ENST00000545328.6, SEC23A-203, 2734; ENST00000548032.6, SEC23A-204, 907; ENST00000555017.5, SEC23A-208, 588; ENST00000557437.1, SEC23A-214, 575; ENST00000553970.1, SEC23A-206, 574; ENST00000556092.5, SEC23A-212, 571; ENST00000557280.5, SEC23A-213, 561; ENST00000555425.5, SEC23A-210, 547; ENST00000625395.1, SEC23A-215, 261; ENST00000553925.1, SEC23A-205, 484; ENST00000555682.1, SEC23A-211, 398; ENST00000554615.1, SEC23A-207, 3813; ENST00000555363.1, SEC23A-209, 704"	MTTYLEFIQQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCSRTTCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPSYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCMEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPLTQATRGPQVQQPPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIDKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDMHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGGRGAIQFVTQYQHSSGQRRIRVTTIARNWADAQTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDPSSFRFSETFSLYPQFMFHLRRSSFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESGAPILTDDVSLQVFMDHLKKLAVSSAA	chr14:39031919-39109646[-]	"Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. Required for the translocation of insulin-induced glucose transporter SLC2A4/GLUT4 to the cell membrane (By similarity)."	PDB: 2NUP; PDB: 2NUT; PDB: 2YRC; PDB: 2YRD; PDB: 3EFO; PDB: 3EG9; PDB: 3EGD; PDB: 3EGX; PDB: 5KYN; PDB: 5KYU; PDB: 5KYW; PDB: 5KYX; PDB: 5KYY; PDB: 5VNE; PDB: 5VNF; PDB: 5VNG; PDB: 5VNH; PDB: 5VNI; PDB: 5VNJ; PDB: 5VNK; PDB: 5VNL; PDB: 5VNM; PDB: 5VNN; PDB: 5VNO	HGNC:10701	SC23A_HUMAN	Reviewed	ENSG00000100934	.	.	.	.	.
Mol00622	Protein	Syndecan-2 (SDC2)	.	SDC2	6383	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000302190.9, SDC2-201, 3307; ENST00000518385.5, SDC2-202, 1583; ENST00000519914.5, SDC2-204, 1318; ENST00000522911.5, SDC2-207, 677; ENST00000523877.1, SDC2-208, 621; ENST00000521590.5, SDC2-206, 507; ENST00000520233.1, SDC2-205, 563; ENST00000519587.1, SDC2-203, 557"	MRRAWILLTLGLVACVSAESRAELTSDKDMYLDNSSIEEASGVYPIDDDDYASASGSGADEDVESPELTTSRPLPKILLTSAAPKVETTTLNIQNKIPAQTKSPEETDKEKVHLSDSERKMDPAEEDTNVYTEKHSDSLFKRTEVLAAVIAGGVIGFLFAIFLILLLVYRMRKKDEGSYDLGERKPSSAAYQKAPTKEFYA	chr8:96493813-96611790[+]	Cell surface proteoglycan that bears heparan sulfate. Regulates dendritic arbor morphogenesis (By similarity).	PDB: 6ITH	HGNC:10659	SDC2_HUMAN	Reviewed	ENSG00000169439	.	.	.	.	.
Mol00623	Protein	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit (SDHB)	Iron-sulfur subunit of complex II; Ip; SDH; SDH1	SDHB	6390	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375499.8, SDHB-201, 1015; ENST00000463045.2, SDHB-202, 702; ENST00000491274.5, SDHB-208, 649; ENST00000485515.5, SDHB-207, 699; ENST00000475049.5, SDHB-204, 397; ENST00000466613.2, SDHB-203, 828; ENST00000485092.5, SDHB-206, 636; ENST00000475506.1, SDHB-205, 550"	MAAVVALSLRRRLPATTLGGACLQASRGAQTAAATAPRIKKFAIYRWDPDKAGDKPHMQTYEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTNLNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSLYRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEKKASV	chr1:17018722-17054032[-]	"Iron-sulfur protein (IP) subunit of the succinate dehydrogenase complex (mitochondrial respiratory chain complex II), responsible for transferring electrons from succinate to ubiquinone (coenzyme Q)."	PDB: 7KCL; PDB: 7KCM	HGNC:10681	SDHB_HUMAN	Reviewed	ENSG00000117118	.	.	.	.	.
Mol00624	Protein	Secretagogin (SCGN)	SECRET	SCGN	10590	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377961.3, SCGN-202, 1468; ENST00000612225.4, SCGN-203, 1402; ENST00000334979.6, SCGN-201, 704"	MDSSREPTLGRLDAAGFWQVWQRFDADEKGYIEEKELDAFFLHMLMKLGTDDTVMKANLHKVKQQFMTTQDASKDGRIRMKELAGMFLSEDENFLLLFRRENPLDSSVEFMQIWRKYDADSSGFISAAELRNFLRDLFLHHKKAISEAKLEEYTGTMMKIFDRNKDGRLDLNDLARILALQENFLLQFKMDACSTEERKRDFEKIFAYYDVSKTGALEGPEVDGFVKDMMELVQPSISGVDLDKFREILLRHCDVNKDGKIQKSELALCLGLKINP	chr6:25652201-25701783[+]	.	.	HGNC:16941	SEGN_HUMAN	Reviewed	ENSG00000079689	.	.	.	.	.
Mol00625	Protein	Semaphorin-4C (SEMA4C)	KIAA1739; SEMAI; UNQ5855/PRO34487	SEMA4C	54910	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305476.10, SEMA4C-201, 3652; ENST00000449330.1, SEMA4C-203, 839; ENST00000442264.5, SEMA4C-202, 817; ENST00000482925.5, SEMA4C-206, 3776; ENST00000467747.1, SEMA4C-204, 3371; ENST00000474420.1, SEMA4C-205, 2625"	MAPHWAVWLLAARLWGLGIGAEVWWNLVPRKTVSSGELATVVRRFSQTGIQDFLTLTLTEPTGLLYVGAREALFAFSMEALELQGAISWEAPVEKKTECIQKGKNNQTECFNFIRFLQPYNASHLYVCGTYAFQPKCTYVNMLTFTLEHGEFEDGKGKCPYDPAKGHAGLLVDGELYSATLNNFLGTEPIILRNMGPHHSMKTEYLAFWLNEPHFVGSAYVPESVGSFTGDDDKVYFFFRERAVESDCYAEQVVARVARVCKGDMGGARTLQRKWTTFLKARLACSAPNWQLYFNQLQAMHTLQDTSWHNTTFFGVFQAQWGDMYLSAICEYQLEEIQRVFEGPYKEYHEEAQKWDRYTDPVPSPRPGSCINNWHRRHGYTSSLELPDNILNFVKKHPLMEEQVGPRWSRPLLVKKGTNFTHLVADRVTGLDGATYTVLFIGTGDGWLLKAVSLGPWVHLIEELQLFDQEPMRSLVLSQSKKLLFAGSRSQLVQLPVADCMKYRSCADCVLARDPYCAWSVNTSRCVAVGGHSGSLLIQHVMTSDTSGICNLRGSKKVRPTPKNITVVAGTDLVLPCHLSSNLAHARWTFGGRDLPAEQPGSFLYDARLQALVVMAAQPRHAGAYHCFSEEQGARLAAEGYLVAVVAGPSVTLEARAPLENLGLVWLAVVALGAVCLVLLLLVLSLRRRLREELEKGAKATERTLVYPLELPKEPTSPPFRPCPEPDEKLWDPVGYYYSDGSLKIVPGHARCQPGGGPPSPPPGIPGQPLPSPTRLHLGGGRNSNANGYVRLQLGGEDRGGLGHPLPELADELRRKLQQRQPLPDSNPEESSV	chr2:96859718-96870757[-]	"Cell surface receptor for PLXNB2 that plays an important role in cell-cell signaling. PLXNB2 binding promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal brain development, axon guidance and cell migration (By similarity). Probable signaling receptor which may play a role in myogenic differentiation through activation of the stress-activated MAPK cascade."	PDB: 6N5Z	HGNC:10731	SEM4C_HUMAN	Reviewed	ENSG00000168758	.	.	.	.	.
Mol00626	Protein	Splicing factor/proline/glutamine-rich (SFPQ)	100 kDa DNA-pairing protein; hPOMp100; DNA-binding p52/p100 complex; 100 kDa subunit; Polypyrimidine tract-binding protein-associated-splicing factor; PSF; PTB-associated-splicing factor; PSF	SFPQ	6421	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357214.6, SFPQ-201, 3740; ENST00000696553.1, SFPQ-211, 4041; ENST00000470472.5, SFPQ-206, 874; ENST00000460428.5, SFPQ-202, 464; ENST00000468598.5, SFPQ-205, 2835; ENST00000466213.5, SFPQ-203, 1431; ENST00000485365.1, SFPQ-208, 693; ENST00000466745.5, SFPQ-204, 662; ENST00000471991.5, SFPQ-207, 440; ENST00000490668.5, SFPQ-210, 434; ENST00000485454.1, SFPQ-209, 339"	MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF	chr1:35176378-35193446[-]	"DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer binds DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Functions as transcriptional activator. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation. Required for the assembly of nuclear speckles. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway."	PDB: 4WII; PDB: 4WIJ; PDB: 4WIK; PDB: 5WPA; PDB: 6NCQ; PDB: 6OWJ; PDB: 6WMZ; PDB: 7LRQ; PDB: 7LRU	HGNC:10774	SFPQ_HUMAN	Reviewed	ENSG00000116560	.	.	.	.	.
Mol00627	Protein	Sialyltransferase St8Sia IV (SIAT8D)	Alpha-2;8-sialyltransferase 8D; Polysialyltransferase-1; Sialyltransferase 8D; SIAT8-D; Sialyltransferase St8Sia IV; ST8SiaIV; PST; PST1; SIAT8D	ST8SIA4	7903	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000231461.10, ST8SIA4-201, 6321; ENST00000451528.2, ST8SIA4-202, 1794; ENST00000523381.1, ST8SIA4-204, 655; ENST00000507360.2, ST8SIA4-203, 559"	MRSIRKRWTICTISLLLIFYKTKEIARTEEHQETQLIGDGELSLSRSLVNSSDKIIRKAGSSIFQHNVEGWKINSSLVLEIRKNILRFLDAERDVSVVKSSFKPGDVIHYVLDRRRTLNISHDLHSLLPEVSPMKNRRFKTCAVVGNSGILLDSECGKEIDSHNFVIRCNLAPVVEFAADVGTKSDFITMNPSVVQRAFGGFRNESDREKFVHRLSMLNDSVLWIPAFMVKGGEKHVEWVNALILKNKLKVRTAYPSLRLIHAVRGYWLTNKVPIKRPSTGLLMYTLATRFCDEIHLYGFWPFPKDLNGKAVKYHYYDDLKYRYFSNASPHRMPLEFKTLNVLHNRGALKLTTGKCVKQ	chr5:100806933-100903282[-]	"Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells."	PDB: 5Y22; PDB: 5Y3U; PDB: 6AHZ	HGNC:10871	SIA8D_HUMAN	Reviewed	ENSG00000113532	.	.	.	.	.
Mol00628	Protein	E3 ubiquitin-protein ligase SIAH2 (SIAH2)	RING-type E3 ubiquitin transferase SIAH2; Seven in absentia homolog 2; Siah-2; hSiah2	SIAH2	6478	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000312960.4, SIAH2-201, 2311; ENST00000482706.1, SIAH2-203, 427; ENST00000472885.1, SIAH2-202, 452"	MSRPSSTGPSANKPCSKQPPPQPQHTPSPAAPPAAATISAAGPGSSAVPAAAAVISGPGGGGGAGPVSPQHHELTSLFECPVCFDYVLPPILQCQAGHLVCNQCRQKLSCCPTCRGALTPSIRNLAMEKVASAVLFPCKYATTGCSLTLHHTEKPEHEDICEYRPYSCPCPGASCKWQGSLEAVMSHLMHAHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYEGHQQFFAIVLLIGTRKQAENFAYRLELNGNRRRLTWEATPRSIHDGVAAAIMNSDCLVFDTAIAHLFADNGNLGINVTISTCCP	chr3:150741125-150763477[-]	"E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia. It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes. Has some overlapping function with SIAH1. Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not. Promotes monoubiquitination of SNCA. Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation. Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance. Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4."	PDB: 5H9M	HGNC:10858	SIAH2_HUMAN	Reviewed	ENSG00000181788	.	.	.	.	.
Mol00629	Protein	NAD-dependent protein deacetylase sirtuin-1 (SIRT1)	hSIRT1; NAD-dependent protein deacylase sirtuin-1; Regulatory protein SIR2 homolog 1; SIR2-like protein 1; hSIR2; 75SirT1; SIR2L1	SIRT1	23411	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000212015.11, SIRT1-201, 4107; ENST00000432464.5, SIRT1-204, 3587; ENST00000403579.1, SIRT1-202, 3333; ENST00000406900.5, SIRT1-203, 3295; ENST00000497639.5, SIRT1-206, 673; ENST00000473922.1, SIRT1-205, 576"	MADEAALALQPGGSPSAAGADREAASSPAGEPLRKRPRRDGPGLERSPGEPGGAAPEREVPAAARGCPGAAAAALWREAEAEAAAAGGEQEAQATAAAGEGDNGPGLQGPSREPPLADNLYDEDDDDEGEEEEEAAAAAIGYRDNLLFGDEIITNGFHSCESDEEDRASHASSSDWTPRPRIGPYTFVQQHLMIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELAYLSELPPTPLHVSEDSSSPERTSPPDSSVIVTLLDQAAKSNDDLDVSESKGCMEEKPQEVQTSRNVESIAEQMENPDLKNVGSSTGEKNERTSVAGTVRKCWPNRVAKEQISRRLDGNQYLFLPPNRYIFHGAEVYSDSEDDVLSSSSCGSNSDSGTCQSPSLEEPMEDESEIEEFYNGLEDEPDVPERAGGAGFGTDGDDQEAINEAISVKQEVTDMNYPSNKS	chr10:67884656-67918390[+]	"NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of H1-4. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates p300/EP300 and PRMT1. Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation. Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacetylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome. Protects cardiomyocytes against palmitate-induced apoptosis. Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity. Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis. Involved in the CCAR2-mediated regulation of PCK1 and NR1D1. Deacetylates CTNB1 at 'Lys-49'. In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling. In addition to protein deacetylase activity, also acts as protein-lysine deacylase by mediating protein depropionylation and decrotonylation. Mediates depropionylation of Osterix (SP7). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase. Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity. Involved in the regulation of centrosome duplication. Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly. Deacetylates NDC80/HEC1. {ECO:0000250|UniProtKB:Q923E4, ECO:0000269|11672523, ECO:0000269|12006491, ECO:0000269|12535671, ECO:0000269|14976264, ECO:0000269|14980222, ECO:0000269|15126506, ECO:0000269|15152190, ECO:0000269|15205477, ECO:0000269|15469825, ECO:0000269|15692560, ECO:0000269|16079181, ECO:0000269|16166628, ECO:0000269|16892051, ECO:0000269|16998810, ECO:0000269|17283066, ECO:0000269|17290224, ECO:0000269|17334224, ECO:0000269|17505061, ECO:0000269|17612497, ECO:0000269|17620057, ECO:0000269|17936707, ECO:0000269|18203716, ECO:0000269|18296641, ECO:0000269|18485871, ECO:0000269|18662546, ECO:0000269|18687677, ECO:0000269|19188449, ECO:0000269|19220062, ECO:0000269|19364925, ECO:0000269|19690166, ECO:0000269|19934257, ECO:0000269|20097625, ECO:0000269|20100829, ECO:0000269|20203304, ECO:0000269|20375098, ECO:0000269|20620956, ECO:0000269|20670893, ECO:0000269|20817729, ECO:0000269|20955178, ECO:0000269|21149730, ECO:0000269|21245319, ECO:0000269|21471201, ECO:0000269|21504832, ECO:0000269|21555002, ECO:0000269|21698133, ECO:0000269|21701047, ECO:0000269|21775285, ECO:0000269|21807113, ECO:0000269|21841822, ECO:0000269|21890893, ECO:0000269|21947282, ECO:0000269|22274616, ECO:0000269|24415752, ECO:0000269|24824780, ECO:0000269|28497810, ECO:0000269|29765047, ECO:0000269|30193097, ECO:0000269|30409912, ECO:0000269|31722219, ECO:0000269|32034146}.; FUNCTION: [Isoform 2]: Deacetylates 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. {ECO:0000269|20975832}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection. {ECO:0000269|18329615}.; FUNCTION: [SirtT1 75 kDa fragment]: Catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly. {ECO:0000269|21987377}."	PDB: 4I5I; PDB: 4IF6; PDB: 4IG9; PDB: 4KXQ; PDB: 4ZZH; PDB: 4ZZI; PDB: 4ZZJ; PDB: 5BTR	HGNC:14929	SIR1_HUMAN	Reviewed	ENSG00000096717	.	.	.	.	.
Mol00630	Protein	SLAIN motif-containing protein 1 (SLAIN1)	C13orf32	SLAIN1	122060	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000418532.6, SLAIN1-206, 3009; ENST00000351546.7, SLAIN1-203, 2394; ENST00000314070.9, SLAIN1-202, 2118; ENST00000358679.3, SLAIN1-204, 2075; ENST00000488699.5, SLAIN1-216, 1461; ENST00000466548.5, SLAIN1-213, 2637; ENST00000267219.12, SLAIN1-201, 2090; ENST00000441784.5, SLAIN1-208, 1033; ENST00000446759.5, SLAIN1-210, 899; ENST00000442759.5, SLAIN1-209, 829; ENST00000462234.5, SLAIN1-211, 622; ENST00000496045.5, SLAIN1-217, 576; ENST00000377236.2, SLAIN1-205, 572; ENST00000474663.5, SLAIN1-214, 570; ENST00000481614.1, SLAIN1-215, 531; ENST00000422114.5, SLAIN1-207, 472; ENST00000465831.1, SLAIN1-212, 769"	MMAEQVKCASAGVSSGAGSGPVVNAELEVKKLQELVRKLEKQNEQLRSRAASAAAAPHLLLLPPPPPAAPPPAGLQPLGPRSPPAATATAAASGGLGPAFPGTFCLPSPAPSLLCSLAQPPEAPFVYFKPAAGFFGAGGGGPEPGGAGTPPGAAAAPPSPPPTLLDEVELLDLESVAAWRDEDDYTWLYIGSSKTFTSSEKSLTPLQWCRHVLDNPTPEMEAARRSLCFRLEQGYTSRGSPLSPQSSIDSELSTSELEDDSISMGYKLQDLTDVQIMARLQEESLRQDYASTSASVSRHSSSVSLSSGKKGTCSDQEYDQYSLEDEEEFDHLPPPQPRLPRCSPFQRGIPHSQTFSSIRECRRSPSSQYFPSNNYQQQQYYSPQAQTPDQQPNRTNGDKLRRSMPNLARMPSTTAISSNISSPVTVRNSQSFDSSLHGAGNGISRIQSCIPSPGQLQHRVHSVGHFPVSIRQPLKATAYVSPTVQGSSNMPLSNGLQLYSNTGIPTPNKAAASGIMGRSALPRPSLAINGSNLPRSKIAQPVRSFLQPPKPLSSLSTLRDGNWRDGCY	chr13:77697687-77764242[+]	"Microtubule plus-end tracking protein that might be involved in the regulation of cytoplasmic microtubule dynamics, microtubule organization and microtubule elongation."	.	HGNC:26387	SLAI1_HUMAN	Reviewed	ENSG00000139737	.	.	.	.	.
Mol00631	Protein	Schlafen family member 11 (SLFN11)	.	SLFN11	91607	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000685675.1, SLFN11-214, 5139; ENST00000394566.5, SLFN11-202, 5030; ENST00000308377.8, SLFN11-201, 4910; ENST00000592108.1, SLFN11-212, 1124; ENST00000441608.6, SLFN11-205, 791; ENST00000427966.5, SLFN11-203, 714; ENST00000591682.5, SLFN11-211, 634; ENST00000430814.5, SLFN11-204, 606; ENST00000592122.1, SLFN11-213, 588; ENST00000589811.5, SLFN11-210, 584; ENST00000588579.1, SLFN11-208, 575; ENST00000498396.2, SLFN11-206, 582; ENST00000586099.1, SLFN11-207, 579; ENST00000589562.1, SLFN11-209, 553"	MEANQCPLVVEPSYPDLVINVGEVTLGEENRKKLQKIQRDQEKERVMRAACALLNSGGGVIRMAKKVEHPVEMGLDLEQSLRELIQSSDLQAFFETKQQGRCFYIFVKSWSSGPFPEDRSVKPRLCSLSSSLYRRSETSVRSMDSREAFCFLKTKRKPKILEEGPFHKIHKGVYQELPNSDPADPNSDPADLIFQKDYLEYGEILPFPESQLVEFKQFSTKHFQEYVKRTIPEYVPAFANTGGGYLFIGVDDKSREVLGCAKENVDPDSLRRKIEQAIYKLPCVHFCQPQRPITFTLKIVNVLKRGELYGYACMIRVNPFCCAVFSEAPNSWIVEDKYVCSLTTEKWVGMMTDTDPDLLQLSEDFECQLSLSSGPPLSRPVYSKKGLEHKKELQQLLFSVPPGYLRYTPESLWRDLISEHRGLEELINKQMQPFFRGILIFSRSWAVDLNLQEKPGVICDALLIAQNSTPILYTILREQDAEGQDYCTRTAFTLKQKLVNMGGYTGKVCVRAKVLCLSPESSAEALEAAVSPMDYPASYSLAGTQHMEALLQSLVIVLLGFRSLLSDQLGCEVLNLLTAQQYEIFSRSLRKNRELFVHGLPGSGKTIMAMKIMEKIRNVFHCEAHRILYVCENQPLRNFISDRNICRAETRKTFLRENFEHIQHIVIDEAQNFRTEDGDWYGKAKSITRRAKGGPGILWIFLDYFQTSHLDCSGLPPLSDQYPREELTRIVRNADPIAKYLQKEMQVIRSNPSFNIPTGCLEVFPEAEWSQGVQGTLRIKKYLTVEQIMTCVADTCRRFFDRGYSPKDVAVLVSTAKEVEHYKYELLKAMRKKRVVQLSDACDMLGDHIVLDSVRRFSGLERSIVFGIHPRTADPAILPNVLICLASRAKQHLYIFPWGGH	chr17:35350305-35373701[-]	"Inhibitor of DNA replication that promotes cell death in response to DNA damage. Acts as a guardian of the genome by killing cells with defective replication. Persistently blocks stressed replication forks by opening chromatin across replication initiation sites at stressed replication forks, possibly leading to unwind DNA ahead of the MCM helicase and block fork progression, ultimately leading to cell death. Acts independently of ATR. Also acts as an interferon (IFN)-induced antiviral protein which acts as an inhibitor of retrovirus protein synthesis. Specifically abrogates the production of retroviruses such as human immunodeficiency virus 1 (HIV-1) by acting as a specific inhibitor of the synthesis of retroviruses encoded proteins in a codon-usage-dependent manner. Binds to tRNAs and exploits the unique viral codon bias towards A/T nucleotides. The exact inhibition mechanism is unclear: may either sequester tRNAs, prevent their maturation via post-transcriptional processing or may accelerate their deacylation. Does not inhibit reverse transcription, integration or production and nuclear export of viral RNA."	.	HGNC:26633	SLN11_HUMAN	Reviewed	ENSG00000172716	.	.	.	.	.
Mol00632	Protein	Mothers against decapentaplegic homolog 3 (SMAD3)	MAD homolog 3; Mad3; Mothers against DPP homolog 3; hMAD-3; JV15-2; SMAD family member 3; SMAD 3; Smad3; hSMAD3; MADH3	SMAD3	4088	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000327367.9, SMAD3-201, 6464; ENST00000681239.1, SMAD3-218, 5866; ENST00000679624.1, SMAD3-216, 5838; ENST00000540846.6, SMAD3-204, 1567; ENST00000439724.7, SMAD3-202, 1530; ENST00000537194.6, SMAD3-203, 1147; ENST00000558894.5, SMAD3-209, 797; ENST00000560424.1, SMAD3-215, 775; ENST00000558739.1, SMAD3-206, 586; ENST00000559092.1, SMAD3-210, 584; ENST00000559460.5, SMAD3-211, 568; ENST00000558428.5, SMAD3-205, 554; ENST00000558827.1, SMAD3-208, 552; ENST00000560175.5, SMAD3-213, 542; ENST00000558763.1, SMAD3-207, 1957; ENST00000680689.1, SMAD3-217, 1473; ENST00000560402.1, SMAD3-214, 590; ENST00000559937.1, SMAD3-212, 579"	MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS	chr15:67063763-67195173[+]	"Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator."	PDB: 1MHD; PDB: 1MJS; PDB: 1MK2; PDB: 1OZJ; PDB: 1U7F; PDB: 2LAJ; PDB: 2LB2; PDB: 5OD6; PDB: 5ODG; PDB: 5XOC; PDB: 6YIB; PDB: 6ZMN	HGNC:6769	SMAD3_HUMAN	Reviewed	ENSG00000166949	.	.	.	.	.
Mol00633	Protein	Mothers against decapentaplegic homolog 7 (SMAD7)	MAD homolog 7; Mothers against DPP homolog 7; Mothers against decapentaplegic homolog 8; MAD homolog 8; Mothers against DPP homolog 8; SMAD family member 7; SMAD 7; Smad7; hSMAD7; MADH7; MADH8	SMAD7	4092	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262158.8, SMAD7-201, 3341; ENST00000589634.1, SMAD7-207, 1278; ENST00000591805.5, SMAD7-208, 1152; ENST00000586093.1, SMAD7-204, 574; ENST00000585986.1, SMAD7-203, 563; ENST00000587336.1, SMAD7-205, 549; ENST00000588190.1, SMAD7-206, 401; ENST00000545051.2, SMAD7-202, 2211"	MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR	chr18:48919853-48950965[-]	"Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator."	PDB: 2DJY; PDB: 2KXQ; PDB: 2LTV; PDB: 2LTW; PDB: 2LTX; PDB: 2LTY; PDB: 2LTZ	HGNC:6773	SMAD7_HUMAN	Reviewed	ENSG00000101665	.	.	.	.	.
Mol00634	Protein	Structural maintenance of chromosomes protein 4 (SMC4)	SMC protein 4; SMC-4; Chromosome-associated polypeptide C; hCAP-C; XCAP-C homolog; CAPC; SMC4L1	SMC4	10051	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357388.8, SMC4-202, 5116; ENST00000344722.5, SMC4-201, 5356; ENST00000469762.5, SMC4-210, 3998; ENST00000462787.5, SMC4-204, 5033; ENST00000489573.5, SMC4-221, 1553; ENST00000465903.5, SMC4-206, 849; ENST00000490207.5, SMC4-222, 821; ENST00000497311.5, SMC4-226, 708; ENST00000485867.5, SMC4-217, 629; ENST00000485645.5, SMC4-216, 583; ENST00000472991.5, SMC4-214, 582; ENST00000467468.5, SMC4-208, 566; ENST00000469858.5, SMC4-211, 1971; ENST00000470240.5, SMC4-212, 724; ENST00000472282.5, SMC4-213, 667; ENST00000487747.5, SMC4-219, 637; ENST00000494612.1, SMC4-224, 622; ENST00000497984.5, SMC4-227, 563; ENST00000462668.5, SMC4-203, 4235; ENST00000468653.5, SMC4-209, 1756; ENST00000465563.5, SMC4-205, 747; ENST00000486711.1, SMC4-218, 621; ENST00000488017.1, SMC4-220, 592; ENST00000497203.1, SMC4-225, 490; ENST00000484799.1, SMC4-215, 478; ENST00000493695.1, SMC4-223, 457; ENST00000467263.1, SMC4-207, 401"	MPRKGTQPSTARRREEGPPPPSPDGASSDAEPEPPSGRTESPATAAETASEELDNRSLEEILNSIPPPPPPAMTNEAGAPRLMITHIVNQNFKSYAGEKILGPFHKRFSCIIGPNGSGKSNVIDSMLFVFGYRAQKIRSKKLSVLIHNSDEHKDIQSCTVEVHFQKIIDKEGDDYEVIPNSNFYVSRTACRDNTSVYHISGKKKTFKDVGNLLRSHGIDLDHNRFLILQGEVEQIAMMKPKGQTEHDEGMLEYLEDIIGCGRLNEPIKVLCRRVEILNEHRGEKLNRVKMVEKEKDALEGEKNIAIEFLTLENEIFRKKNHVCQYYIYELQKRIAEMETQKEKIHEDTKEINEKSNILSNEMKAKNKDVKDTEKKLNKITKFIEENKEKFTQLDLEDVQVREKLKHATSKAKKLEKQLQKDKEKVEEFKSIPAKSNNIINETTTRNNALEKEKEKEEKKLKEVMDSLKQETQGLQKEKESREKELMGFSKSVNEARSKMDVAQSELDIYLSRHNTAVSQLTKAKEALIAASETLKERKAAIRDIEGKLPQTEQELKEKEKELQKLTQEETNFKSLVHDLFQKVEEAKSSLAMNRSRGKVLDAIIQEKKSGRIPGIYGRLGDLGAIDEKYDVAISSCCHALDYIVVDSIDIAQECVNFLKRQNIGVATFIGLDKMAVWAKKMTEIQTPENTPRLFDLVKVKDEKIRQAFYFALRDTLVADNLDQATRVAYQKDRRWRVVTLQGQIIEQSGTMTGGGSKVMKGRMGSSLVIEISEEEVNKMESQLQNDSKKAMQIQEQKVQLEERVVKLRHSEREMRNTLEKFTASIQRLIEQEEYLNVQVKELEANVLATAPDKKKQKLLEENVSAFKTEYDAVAEKAGKVEAEVKRLHNTIVEINNHKLKAQQDKLDKINKQLDECASAITKAQVAIKTADRNLQKAQDSVLRTEKEIKDTEKEVDDLTAELKSLEDKAAEVVKNTNAAEESLPEIQKEHRNLLQELKVIQENEHALQKDALSIKLKLEQIDGHIAEHNSKIKYWHKEISKISLHPIEDNPIEEISVLSPEDLEAIKNPDSITNQIALLEARCHEMKPNLGAIAEYKKKEELYLQRVAELDKITYERDSFRQAYEDLRKQRLNEFMAGFYIITNKLKENYQMLTLGGDAELELVDSLDPFSEGIMFSVRPPKKSWKKIFNLSGGEKTLSSLALVFALHHYKPTPLYFMDEIDAALDFKNVSIVAFYIYEQTKNAQFIIISLRNNMFEISDRLIGIYKTYNITKSVAVNPKEIASKGLC	chr3:160399274-160434954[+]	"Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases."	PDB: 4U4P	HGNC:14013	SMC4_HUMAN	Reviewed	ENSG00000113810	.	.	.	.	.
Mol00635	Protein	Smoothened homolog (SMO)	SMO; Protein Gx; SMOH	SMO	6608	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000249373.8, SMO-201, 3977; ENST00000655644.1, SMO-205, 3997; ENST00000462420.2, SMO-202, 787; ENST00000475779.1, SMO-203, 582; ENST00000495998.1, SMO-204, 732"	MAAARPARGPELPLLGLLLLLLLGDPGRGAASSGNATGPGPRSAGGSARRSAAVTGPPPPLSHCGRAAPCEPLRYNVCLGSVLPYGATSTLLAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATRGPCAIVERERGWPDFLRCTPDRFPEGCTNEVQNIKFNSSGQCEVPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEPTSNETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSIKSNHPGLLSEKAASKINETMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDCEIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGQSDDEPKRIKKSKMIAKAFSKRHELLQNPGQELSFSMHTVSHDGPVAGLAFDLNEPSADVSSAWAQHVTKMVARRGAILPQDISVTPVATPVPPEEQANLWLVEAEISPELQKRLGRKKKRRKRKKEVCPLAPPPELHPPAPAPSTIPRLPQLPRQKCLVAAGAWGAGDSCRQGAWTLVSNPFCPEPSPPQDPFLPSAPAPVAWAHGRRQGLGPIHSRTNLMDTELMDADSDF	chr7:129188633-129213545[+]	"G protein-coupled receptor that probably associates with the patched protein (PTCH) to transduce the hedgehog's proteins signal. Binding of sonic hedgehog (SHH) to its receptor patched is thought to prevent normal inhibition by patched of smoothened (SMO). Required for the accumulation of KIF7, GLI2 and GLI3 in the cilia. Interacts with DLG5 at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation."	PDB: 4JKV; PDB: 4N4W; PDB: 4O9R; PDB: 4QIM; PDB: 4QIN; PDB: 5L7D; PDB: 5L7I; PDB: 5V56; PDB: 5V57; PDB: 6OT0; PDB: 6XBJ; PDB: 6XBK; PDB: 6XBL; PDB: 6XBM	HGNC:11119	SMO_HUMAN	Reviewed	ENSG00000128602	.	.	.	.	.
Mol00636	Protein	SWI/SNF complex subunit SMARCC1 (SMARCC1)	BRG1-associated factor 155; BAF155; SWI/SNF complex 155 kDa subunit; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1; BAF155	SMARCC1	6599	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000254480.10, SMARCC1-201, 6354; ENST00000454240.1, SMARCC1-203, 636; ENST00000425518.5, SMARCC1-202, 3827; ENST00000462198.5, SMARCC1-204, 785; ENST00000492896.1, SMARCC1-208, 568; ENST00000485833.1, SMARCC1-207, 412; ENST00000483847.1, SMARCC1-205, 804; ENST00000485737.1, SMARCC1-206, 631"	MAAAAGGGGPGTAVGATGSGIAAAAAGLAVYRRKDGGPATKFWESPETVSQLDSVRVWLGKHYKKYVHADAPTNKTLAGLVVQLLQFQEDAFGKHVTNPAFTKLPAKCFMDFKAGGALCHILGAAYKYKNEQGWRRFDLQNPSRMDRNVEMFMNIEKTLVQNNCLTRPNIYLIPDIDLKLANKLKDIIKRHQGTFTDEKSKASHHIYPYSSSQDDEEWLRPVMRKEKQVLVHWGFYPDSYDTWVHSNDVDAEIEDPPIPEKPWKVHVKWILDTDIFNEWMNEEDYEVDENRKPVSFRQRISTKNEEPVRSPERRDRKASANARKRKHSPSPPPPTPTESRKKSGKKGQASLYGKRRSQKEEDEQEDLTKDMEDPTPVPNIEEVVLPKNVNLKKDSENTPVKGGTVADLDEQDEETVTAGGKEDEDPAKGDQSRSVDLGEDNVTEQTNHIIIPSYASWFDYNCIHVIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLTGDVCAVMRVHAFLEQWGLVNYQVDPESRPMAMGPPPTPHFNVLADTPSGLVPLHLRSPQVPAAQQMLNFPEKNKEKPVDLQNFGLRTDIYSKKTLAKSKGASAGREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLENSDASLGPLAYQPVPFSQSGNPVMSTVAFLASVVDPRVASAAAKAALEEFSRVREEVPLELVEAHVKKVQEAARASGKVDPTYGLESSCIAGTGPDEPEKLEGAEEEKMEADPDGQQPEKAENKVENETDEGDKAQDGENEKNSEKEQDSEVSEDTKSEEKETEENKELTDTCKERESDTGKKKVEHEISEGNVATAAAAALASAATKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREKEALEQQRQQLLTERQNFHMEQLKYAELRARQQMEQQQHGQNPQQAHQHSGGPGLAPLGAAGHPGMMPHQQPPPYPLMHHQMPPPHPPQPGQIPGPGSMMPGQHMPGRMIPTVAANIHPSGSGPTPPGMPPMPGNILGPRVPLTAPNGMYPPPPQQQPPPPPPADGVPPPPAPGPPASAAP	chr3:47585269-47782106[-]	"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. May stimulate the ATPase activity of the catalytic subunit of the complex. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth."	PDB: 2YUS; PDB: 5GJK; PDB: 6KZ7; PDB: 6YXO; PDB: 6YXP	HGNC:11104	SMRC1_HUMAN	Reviewed	ENSG00000173473	.	.	.	.	.
Mol00637	Protein	E3 ubiquitin-protein ligase SMURF1 (SMURF1)	hSMURF1; HECT-type E3 ubiquitin transferase SMURF1; SMAD ubiquitination regulatory factor 1; SMAD-specific E3 ubiquitin-protein ligase 1; KIAA1625	SMURF1	57154	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361368.7, SMURF1-202, 5668; ENST00000361125.1, SMURF1-201, 5737; ENST00000480055.5, SMURF1-204, 1012; ENST00000472627.1, SMURF1-203, 825"	MSNPGTRRNGSSIKIRLTVLCAKNLAKKDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGTGGSVVDCRGLLENEGTVYEDSGPGRPLSCFMEEPAPYTDSTGAAAGGGNCRFVESPSQDQRLQAQRLRNPDVRGSLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPSPSGTIPGGDAAFLYEFLLQGHTSEPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLPLPSEGSLEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYMLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE	chr7:99027440-99144108[-]	E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway. Mediates ubiquitination and degradation of SMAD1 and SMAD receptor-regulated SMADs specific for the BMP pathway. Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA. Promotes ubiquitination and subsequent proteasomal degradation of MAVS. Plays a role in dendrite formation by melanocytes.	PDB: 2LAZ; PDB: 2LB0; PDB: 2LB1; PDB: 2LTX; PDB: 3PYC	HGNC:16807	SMUF1_HUMAN	Reviewed	ENSG00000198742	.	.	.	.	.
Mol00638	Protein	Single-strand selective monofunctional uracil DNA glycosylase (SMUG1)	.	SMUG1	23583	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000682136.1, SMUG1-226, 2681; ENST00000513838.5, SMUG1-220, 2119; ENST00000508394.6, SMUG1-215, 1697; ENST00000337581.7, SMUG1-202, 1571; ENST00000401977.6, SMUG1-203, 1082; ENST00000514685.5, SMUG1-222, 926; ENST00000506595.5, SMUG1-213, 712; ENST00000243112.9, SMUG1-201, 627; ENST00000514196.5, SMUG1-221, 553; ENST00000505128.5, SMUG1-209, 2607; ENST00000504338.5, SMUG1-207, 751; ENST00000506169.5, SMUG1-212, 572; ENST00000503306.5, SMUG1-205, 541; ENST00000504797.1, SMUG1-208, 470; ENST00000507904.5, SMUG1-214, 465; ENST00000635546.1, SMUG1-225, 1115; ENST00000509864.5, SMUG1-217, 621; ENST00000505662.1, SMUG1-211, 1422; ENST00000634429.1, SMUG1-223, 1093; ENST00000505597.1, SMUG1-210, 494; ENST00000635234.1, SMUG1-224, 484; ENST00000503231.1, SMUG1-204, 450; ENST00000509078.1, SMUG1-216, 598; ENST00000503447.1, SMUG1-206, 585; ENST00000511522.5, SMUG1-218, 561; ENST00000511854.1, SMUG1-219, 451"	MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEVSGARFWGFFRNLCGQPEVFFHHCFVHNLCPLLFLAPSGRNLTPAELPAKQREQLLGICDAALCRQVQLLGVRLVVGVGRLAEQRARRALAGLMPEVQVEGLLHPSPRNPQANKGWEAVAKERLNELGLLPLLLK	chr12:54121277-54189008[-]	"Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration."	.	HGNC:17148	SMUG1_HUMAN	Reviewed	ENSG00000123415	.	.	.	.	.
Mol00639	Protein	Zinc finger protein SNAI2 (SNAI2)	Neural crest transcription factor Slug; Protein snail homolog 2; SLUG; SLUGH	SNAI2	6591	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000020945.4, SNAI2-201, 2180; ENST00000396822.6, SNAI2-202, 626; ENST00000649776.1, SNAI2-203, 2828"	MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLYESYSMPVIPQPEILSSGAYSPITVWTTAAPFHAQLPNGLSPLSGYSSSLGRVSPPPPSDTSSKDHSGSESPISDEEERLQSKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQSRKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH	chr8:48917598-48921740[-]	"Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis."	.	HGNC:11094	SNAI2_HUMAN	Reviewed	ENSG00000019549	.	.	.	.	.
Mol00640	Protein	Suppressor of cytokine signaling 3 (SOCS3)	SOCS-3; Cytokine-inducible SH2 protein 3; CIS-3; STAT-induced STAT inhibitor 3; SSI-3; CIS3; SSI3	SOCS3	9021	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000330871.3, SOCS3-201, 2734; ENST00000587578.1, SOCS3-202, 361"	MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGAPSFPSPPTEPSSEVPEQPSAQPLPGSPPRRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL	chr17:78356778-78360077[-]	"SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins."	.	HGNC:19391	SOCS3_HUMAN	Reviewed	ENSG00000184557	.	.	.	.	.
Mol00641	Protein	Suppressor of cytokine signaling 6 (SOCS6)	SOCS-6; Cytokine-inducible SH2 protein 4; CIS-4; Suppressor of cytokine signaling 4; SOCS-4; CIS4; SOCS4	SOCS6	9306	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000397942.4, SOCS6-201, 5703; ENST00000582322.1, SOCS6-203, 2625; ENST00000578377.1, SOCS6-202, 894"	MKKISLKTLRKSFNLNKSKEETDFMVVQQPSLASDFGKDDSLFGSCYGKDMASCDINGEDEKGGKNRSKSESLMGTLKRRLSAKQKSKGKAGTPSGSSADEDTFSSSSAPIVFKDVRAQRPIRSTSLRSHHYSPAPWPLRPTNSEETCIKMEVRVKALVHSSSPSPALNGVRKDFHDLQSETTCQEQANSLKSSASHNGDLHLHLDEHVPVVIGLMPQDYIQYTVPLDEGMYPLEGSRSYCLDSSSPMEVSAVPPQVGGRAFPEDESQVDQDLVVAPEIFVDQSVNGLLIGTTGVMLQSPRAGHDDVPPLSPLLPPMQNNQIQRNFSGLTGTEAHVAESMRCHLNFDPNSAPGVARVYDSVQSSGPMVVTSLTEELKKLAKQGWYWGPITRWEAEGKLANVPDGSFLVRDSSDDRYLLSLSFRSHGKTLHTRIEHSNGRFSFYEQPDVEGHTSIVDLIEHSIRDSENGAFCYSRSRLPGSATYPVRLTNPVSRFMQVRSLQYLCRFVIRQYTRIDLIQKLPLPNKMKDYLQEKHY	chr18:70289045-70330199[+]	SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates KIT degradation by ubiquitination of the tyrosine-phosphorylated receptor.	PDB: 2VIF	HGNC:16833	SOCS6_HUMAN	Reviewed	ENSG00000170677	.	.	.	.	.
Mol00642	Protein	Superoxide dismutase Mn (SODM)	.	SOD2	6648	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000538183.7, SOD2-210, 14167; ENST00000546087.5, SOD2-214, 2558; ENST00000452684.2, SOD2-206, 2045; ENST00000337404.8, SOD2-201, 991; ENST00000367055.8, SOD2-203, 990; ENST00000444946.6, SOD2-205, 917; ENST00000367054.6, SOD2-202, 815; ENST00000545162.5, SOD2-213, 571; ENST00000535561.5, SOD2-208, 551; ENST00000401980.3, SOD2-204, 523; ENST00000537657.5, SOD2-209, 507; ENST00000546260.5, SOD2-215, 4302; ENST00000541573.5, SOD2-212, 573; ENST00000540491.1, SOD2-211, 454; ENST00000535459.5, SOD2-207, 581"	MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK	chr6:159669069-159762529[-]	Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.	PDB: 1AP5; PDB: 1AP6; PDB: 1EM1; PDB: 1JA8; PDB: 1LUV; PDB: 1LUW; PDB: 1MSD; PDB: 1N0J; PDB: 1N0N; PDB: 1PL4; PDB: 1PM9; PDB: 1QNM; PDB: 1SZX; PDB: 1VAR; PDB: 1XDC; PDB: 1XIL; PDB: 1ZSP; PDB: 1ZTE; PDB: 1ZUQ; PDB: 2ADP; PDB: 2ADQ; PDB: 2GDS; PDB: 2P4K; PDB: 2QKA; PDB: 2QKC; PDB: 3C3S; PDB: 3C3T; PDB: 5GXO; PDB: 5T30; PDB: 5VF9; PDB: 7KKS; PDB: 7KKU; PDB: 7KKW; PDB: 7KLB	HGNC:11180	SODM_HUMAN	Reviewed	ENSG00000112096	.	.	.	.	.
Mol00643	Protein	Sorcin (SRI)	22 kDa protein; CP-22; CP22; V19	SRI	6717	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265729.7, SRI-201, 1972; ENST00000431660.5, SRI-204, 1418; ENST00000394641.7, SRI-202, 653; ENST00000419179.5, SRI-203, 1307; ENST00000490437.5, SRI-210, 570; ENST00000457606.5, SRI-205, 769; ENST00000486860.5, SRI-207, 1024; ENST00000472930.6, SRI-206, 903; ENST00000488015.5, SRI-208, 588; ENST00000489079.1, SRI-209, 557"	MAYPGHPGAGGGYYPGGYGGAPGGPAFPGQTQDPLYGYFAAVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVLNGWRQHFISFDTDRSGTVDPQELQKALTTMGFRLSPQAVNSIAKRYSTNGKITFDDYIACCVKLRALTDSFRRRDTAQQGVVNFPYDDFIQCVMSV	chr7:88205115-88226993[-]	Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the heart sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels.	PDB: 1JUO; PDB: 2JC2; PDB: 4U8D; PDB: 4UPG; PDB: 4USL; PDB: 5MRA	HGNC:11292	SORCN_HUMAN	Reviewed	ENSG00000075142	.	.	.	.	.
Mol00644	Protein	Transcription factor SOX-10 (SOX10)	.	SOX10	6663	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000396884.8, SOX10-202, 2885; ENST00000360880.6, SOX10-201, 2861; ENST00000446929.5, SOX10-204, 1095; ENST00000427770.1, SOX10-203, 873; ENST00000651746.1, SOX10-206, 484; ENST00000690831.1, SOX10-208, 3054; ENST00000470555.1, SOX10-205, 124; ENST00000652356.1, SOX10-207, 1076"	MAEEQDLSEVELSPVGSEEPRCLSPGSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGEAEQGGTAAIQAHYKSAHLDHRHPGEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSMGEGGKPHIDFGNVDIGEISHEVMSNMETFDVAELDQYLPPNGHPGHVSSYSAAGYGLGSALAVASGHSAWISKPPGVALPTVSPPGVDAKAQVKTETAGPQGPPHYTDQPSTSQIAYTSLSLPHYGSAFPSISRPQFDYSDHQPSGPYYGHSGQASGLYSAFSYMGPSQRPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP	chr22:37970686-37987422[-]	"Transcription factor that plays a central role in developing and mature glia. Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination. Once induced, MYRF cooperates with SOX10 to implement the myelination program. Transcriptional activator of MITF, acting synergistically with PAX3. Transcriptional activator of MBP, via binding to the gene promoter."	.	HGNC:11190	SOX10_HUMAN	Reviewed	ENSG00000100146	.	.	.	.	.
Mol00645	Protein	Transcription factor SOX-7 (SOX7)	.	SOX7	83595	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000304501.2, SOX7-201, 3215"	MASLLGAYPWPEGLECPALDAELSDGQSPPAVPRPPGDKGSESRIRRPMNAFMVWAKDERKRLAVQNPDLHNAELSKMLGKSWKALTLSQKRPYVDEAERLRLQHMQDYPNYKYRPRRKKQAKRLCKRVDPGFLLSSLSRDQNALPEKRSGSRGALGEKEDRGEYSPGTALPSLRGCYHEGPAGGGGGGTPSSVDTYPYGLPTPPEMSPLDVLEPEQTFFSSPCQEEHGHPRRIPHLPGHPYSPEYAPSPLHCSHPLGSLALGQSPGVSMMSPVPGCPPSPAYYSPATYHPLHSNLQAHLGQLSPPPEHPGFDALDQLSQVELLGDMDRNEFDQYLNTPGHPDSATGAMALSGHVPVSQVTPTGPTETSLISVLADATATYYNSYSVS	chr8:10723768-10730511[-]	"Binds to and activates the CDH5 promoter, hence plays a role in the transcriptional regulation of genes expressed in the hemogenic endothelium and blocks further differentiation into blood precursors (By similarity). May be required for the survival of both hematopoietic and endothelial precursors during specification (By similarity). Competes with GATA4 for binding and activation of the FGF3 promoter (By similarity). Represses Wnt/beta-catenin-stimulated transcription, probably by targeting CTNNB1 to proteasomal degradation. Binds the DNA sequence 5'-AACAAT-3'."	.	HGNC:18196	SOX7_HUMAN	Reviewed	ENSG00000171056	.	.	.	.	.
Mol00646	Protein	Transcription factor Sp1 (SP1)	TSFP1	SP1	6667	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000327443.9, SP1-201, 7680; ENST00000426431.2, SP1-202, 7603; ENST00000548560.1, SP1-203, 1061; ENST00000551969.5, SP1-204, 602"	MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVADLQSINISGNGF	chr12:53380176-53416446[+]	"Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component ARNTL/BMAL1. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112."	PDB: 1SP1; PDB: 1SP2; PDB: 1VA1; PDB: 1VA2; PDB: 1VA3; PDB: 6PV0; PDB: 6PV1; PDB: 6PV2; PDB: 6PV3; PDB: 6UCO; PDB: 6UCP	HGNC:11205	SP1_HUMAN	Reviewed	ENSG00000185591	.	.	.	.	.
Mol00647	Protein	Serpin B3 (SERPINB3)	Protein T4-A; Squamous cell carcinoma antigen 1; SCCA-1; SCCA; SCCA1	SERPINB3	6317	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000283752.10, SERPINB3-201, 1707; ENST00000332821.8, SERPINB3-202, 1541"	MNSLSEANTKFMFDLFQQFRKSKENNIFYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDRSGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFYQTSVESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLVNAIYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQAKVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETRVDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLSGVLHKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEEFHCNHPFLFFIRQNKTNSILFYGRFSSP	chr18:63655197-63661893[-]	May act as a papain-like cysteine protease inhibitor to modulate the host immune response against tumor cells. Also functions as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1).	PDB: 2ZV6; PDB: 4ZK0; PDB: 4ZK3	HGNC:10569	SPB3_HUMAN	Reviewed	ENSG00000057149	.	.	.	.	.
Mol00648	Protein	Spindlin-1 (SFPQ)	Ovarian cancer-related protein; Spindlin1; OCR; SPIN	SPIN1	10927	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375859.4, SPIN1-201, 4459; ENST00000469017.6, SPIN1-203, 2082; ENST00000485804.5, SPIN1-206, 814; ENST00000485565.6, SPIN1-205, 706; ENST00000483785.1, SPIN1-204, 659; ENST00000462844.5, SPIN1-202, 599"	MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHKKHRSSVGPSKPVSQPRRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDERVSALEVLPDRVATSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS	chr9:88388430-88478694[+]	"Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway. Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes. May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption."	PDB: 2NS2; PDB: 4H75; PDB: 4MZF; PDB: 4MZG; PDB: 4MZH; PDB: 5JSG; PDB: 5JSJ; PDB: 5Y5W; PDB: 6I8B; PDB: 6I8L; PDB: 6I8Y; PDB: 6QPL; PDB: 7BQZ; PDB: 7BU9; PDB: 7CNA	HGNC:11243	SPIN1_HUMAN	Reviewed	ENSG00000106723	.	.	.	.	.
Mol00649	Protein	SRC kinase signaling inhibitor 1 (SRCIN1)	SNAP-25-interacting protein; SNIP; p130Cas-associated protein; p140Cap; KIAA1684; P140; SNIP	SRCIN1	80725	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000617146.5, SRCIN1-213, 7065; ENST00000622519.4, SRCIN1-218, 5204; ENST00000621492.4, SRCIN1-215, 4644; ENST00000622190.4, SRCIN1-217, 4635; ENST00000612431.1, SRCIN1-211, 1431; ENST00000613927.1, SRCIN1-212, 1150; ENST00000621763.4, SRCIN1-216, 5225; ENST00000621275.1, SRCIN1-214, 453; ENST00000612208.1, SRCIN1-210, 1316"	MGNAPSQDPERSSPPMLSADDAEYPREYRTLGGGGGGGSGGRRFSNVGLVHTSERRHTVIAAQSLEALSGLQKADADRKRDAFMDHLKSKYPQHALALRGQQDRMREQPNYWSFKTRSSRHTQGAQPGLADQAAKLSYASAESLETMSEAELPLGFSRMNRFRQSLPLSRSASQTKLRSPGVLFLQFGEETRRVHITHEVSSLDTLHALIAHMFPQKLTMGMLKSPNTAILIKDEARNVFYELEDVRDIQDRSIIKIYRKEPLYAAFPGSHLTNGDLRREMVYASRESSPTRRLNNLSPAPHLASGSPPPGLPSGLPSGLQSGSPSRSRLSYAGGRPPSYAGSPVHHAAERLGGAPAAQGVSPSPSAILERRDVKPDEDLASKAGGMVLVKGEGLYADPYGLLHEGRLSLAAAAGDPFAYPGAGGLYKRGSVRSLSTYSAAALQSDLEDSLYKAAGGGGPLYGDGYGFRLPPSSPQKLADVAAPPGGPPPPHSPYSGPPSRGSPVRQSFRKDSGSSSVFAESPGGKTRSAGSASTAGAPPSELFPGPGERSLVGFGPPVPAKDTETRERMEAMEKQIASLTGLVQSALLRGSEPETPSEKIEGSNGAATPSAPCGSGGRSSGATPVSGPPPPSASSTPAGQPTAVSRLQMQLHLRGLQNSASDLRGQLQQLRKLQLQNQESVRALLKRTEAELSMRVSEAARRQEDPLQRQRTLVEEERLRYLNDEELITQQLNDLEKSVEKIQRDVSHNHRLVPGPELEEKALVLKQLGETLTELKAHFPGLQSKMRVVLRVEVEAVKFLKEEPQRLDGLLKRCRGVTDTLAQIRRQVDEGVWPPPNNLLSQSPKKVTAETDFNKSVDFEMPPPSPPLNLHELSGPAEGASLTPKGGNPTKGLDTPGKRSVDKAVSVEAAERDWEEKRAALTQYSAKDINRLLEETQAELLKAIPDLDCASKAHPGPAPTPDHKPPKAPHGQKAAPRTEPSGRRGSDELTVPRYRTEKPSKSPPPPPPRRSFPSSHGLTTTRTGEVVVTSKKDSAFIKKAESEELEVQKPQVKLRRAVSEVARPASTPPIMASAIKDEDDEDRIIAELESGGGSVPPMKVVTPGASRLKAAQGQAGSPDKSKHGKQRAEYMRIQAQQQATKPSKEMSGSNETSSPVSEKPSASRTSIPVLTSFGARNSSISF	chr17:38530031-38605952[-]	"Acts as a negative regulator of SRC by activating CSK which inhibits SRC activity and downstream signaling, leading to impaired cell spreading and migration. Regulates dendritic spine morphology. Involved in calcium-dependent exocytosis. May play a role in neurotransmitter release or synapse maintenance."	.	HGNC:29506	SRCN1_HUMAN	Reviewed	ENSG00000277363	.	.	.	.	.
Mol00650	Protein	Serum response factor (SRF)	SRF	SRF	6722	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265354.6, SRF-201, 4231"	MLPTQAGAAAALGRGSALGGSLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGPGRLEREAAAAAATTPAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMEIGMVVGGPEASAAATGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEETDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANGTVLKSTGSGPVSSGGLMQLPTSFTLMPGGAVAQQVPVQAIQVHQAPQQASPSRDSSTDLTQTSSSGTVTLPATIMTSSVPTTVGGHMMYPSPHAVMYAPTSGLGDGSLTVLNAFSQAPSTMQVSHSQVQEPGGVPQVFLTASSGTVQIPVSAVQLHQMAVIGQQAGSSSNLTELQVVNLDTAHSTKSE	chr6:43171269-43181506[+]	"SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration. The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. Required for cardiac differentiation and maturation."	PDB: 1HBX; PDB: 1K6O; PDB: 1SRS	HGNC:11291	SRF_HUMAN	Reviewed	ENSG00000112658	.	.	.	.	.
Mol00651	Protein	Serine/arginine-rich splicing factor 2 (SRSF2)	Protein PR264; Splicing component; 35 kDa; Splicing factor SC35; SC-35; Splicing factor; arginine/serine-rich 2; SFRS2	SRSF2	6427	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359995.10, SRSF2-202, 1888; ENST00000392485.2, SRSF2-203, 2885; ENST00000508921.7, SRSF2-205, 1390; ENST00000358156.6, SRSF2-201, 572; ENST00000583836.1, SRSF2-207, 561; ENST00000585202.5, SRSF2-208, 1359; ENST00000452355.7, SRSF2-204, 1357; ENST00000582449.5, SRSF2-206, 1518; ENST00000586778.1, SRSF2-209, 1001; ENST00000589919.1, SRSF2-210, 595; ENST00000592676.1, SRSF2-211, 559"	MSYGRPPPDVEGMTSLKVDNLTYRTSPDTLRRVFEKYGRVGDVYIPRDRYTKESRGFAFVRFHDKRDAEDAMDAMDGAVLDGRELRVQMARYGRPPDSHHSRRGPPPRRYGGGGYGRRSRSPRRRRRSRSRSRSRSRSRSRSRYSRSKSRSRTRSRSRSTSKSRSARRSKSKSSSVSRSRSRSRSRSRSRSPPPVSKRESKSRSRSKSPPKSPEEEGAVSS	chr17:76734115-76737333[-]	"Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment."	PDB: 2KN4; PDB: 2LEA; PDB: 2LEB; PDB: 2LEC	HGNC:10783	SRSF2_HUMAN	Reviewed	ENSG00000161547	.	.	.	.	.
Mol00652	Protein	START domain-containing protein 10 (STARD10)	StARD10; Antigen NY-CO-28; PCTP-like protein; PCTP-L; Serologically defined colon cancer antigen 28; StAR-related lipid transfer protein 10; SDCCAG28; CGI-52	STARD10	10809	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000334805.11, STARD10-201, 2330; ENST00000543304.5, STARD10-218, 1513; ENST00000538536.5, STARD10-213, 1678; ENST00000537947.5, STARD10-210, 1100; ENST00000545082.5, STARD10-220, 1085; ENST00000542989.5, STARD10-216, 839; ENST00000536377.5, STARD10-207, 798; ENST00000546314.5, STARD10-221, 620; ENST00000540587.1, STARD10-215, 558; ENST00000400925.2, STARD10-202, 541; ENST00000539138.1, STARD10-214, 511; ENST00000544767.5, STARD10-219, 509; ENST00000535054.1, STARD10-203, 460; ENST00000536728.5, STARD10-208, 451; ENST00000536290.5, STARD10-206, 438; ENST00000537351.5, STARD10-209, 426; ENST00000538437.5, STARD10-212, 747; ENST00000538009.5, STARD10-211, 985; ENST00000535267.1, STARD10-205, 579; ENST00000535075.1, STARD10-204, 526; ENST00000543089.1, STARD10-217, 506"	MEKLAASTEPQGPRPVLGRESVQVPDDQDFRSFRSECEAEVGWNLTYSRAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACLKYPEWKQKHLPHFKPWLHPEQSPLPSLALSELSVQHADSLENIDESAVAESREERMGGAGGEGSDDDTSLT	chr11:72754729-72794047[-]	May play metabolic roles in sperm maturation or fertilization (By similarity). Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes.	PDB: 6SER	HGNC:10666	STA10_HUMAN	Reviewed	ENSG00000214530	.	.	.	.	.
Mol00653	Protein	Signal transducer activator transcription 5A (STAT5A)	STAT5	STAT5A	6776	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000590949.6, STAT5A-209, 3770; ENST00000345506.8, STAT5A-201, 4301; ENST00000677301.1, STAT5A-213, 3858; ENST00000676585.1, STAT5A-211, 3799; ENST00000588868.5, STAT5A-207, 3629; ENST00000546010.6, STAT5A-205, 3086; ENST00000677893.1, STAT5A-214, 3801; ENST00000678903.1, STAT5A-215, 3725; ENST00000590726.7, STAT5A-208, 3661; ENST00000676631.1, STAT5A-212, 3627; ENST00000587646.2, STAT5A-206, 3239; ENST00000591556.1, STAT5A-210, 1140; ENST00000468096.5, STAT5A-202, 893; ENST00000469124.1, STAT5A-203, 562; ENST00000479417.1, STAT5A-204, 553"	MAGWIQAQQLQGDALRQMQVLYGQHFPIEVRHYLAQWIESQPWDAIDLDNPQDRAQATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQKTYDRCPLELVRCIRHILYNEQRLVREANNCSSPAGILVDAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFAQLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNECSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRADRRGAESVTEEKFTVLFESQFSVGSNELVFQVKTLSLPVVVIVHGSQDHNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGWNYTFWQWFDGVMEVLKKHHKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSPERNLWNLKPFTTRDFSIRSLADRLGDLSYLIYVFPDRPKDEVFSKYYTPVLAKAVDGYVKPQIKQVVPEFVNASADAGGSSATYMDQAPSPAVCPQAPYNMYPQNPDHVLDQDGEFDLDETMDVARHVEELLRRPMDSLDSRLSPPAGLFTSARGSLS	chr17:42287547-42311943[+]	"Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Mediates cellular responses to ERBB4. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation."	.	HGNC:11366	STA5A_HUMAN	Reviewed	ENSG00000126561	.	.	.	.	.
Mol00654	Protein	Signal transducer activator transcription 5B (STAT5B)	.	STAT5B	6777	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000293328.8, STAT5B-201, 5079; ENST00000415845.1, STAT5B-202, 559; ENST00000468312.1, STAT5B-203, 1799; ENST00000481517.1, STAT5B-206, 999; ENST00000468496.5, STAT5B-204, 897; ENST00000498674.1, STAT5B-207, 542; ENST00000481253.2, STAT5B-205, 491"	MAVWIQAQQLQGEALHQMQALYGQHFPIEVRHYLSQWIESQAWDSVDLDNPQENIKATQLLEGLVQELQKKAEHQVGEDGFLLKIKLGHYATQLQNTYDRCPMELVRCIRHILYNEQRLVREANNGSSPAGSLADAMSQKHLQINQTFEELRLVTQDTENELKKLQQTQEYFIIQYQESLRIQAQFGPLAQLSPQERLSRETALQQKQVSLEAWLQREAQTLQQYRVELAEKHQKTLQLLRKQQTIILDDELIQWKRRQQLAGNGGPPEGSLDVLQSWCEKLAEIIWQNRQQIRRAEHLCQQLPIPGPVEEMLAEVNATITDIISALVTSTFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSLLKNENTRNDYSGEILNNCCVMEYHQATGTLSAHFRNMSLKRIKRSDRRGAESVTEEKFTILFESQFSVGGNELVFQVKTLSLPVVVIVHGSQDNNATATVLWDNAFAEPGRVPFAVPDKVLWPQLCEALNMKFKAEVQSNRGLTKENLVFLAQKLFNNSSSHLEDYSGLSVSWSQFNRENLPGRNYTFWQWFDGVMEVLKKHLKPHWNDGAILGFVNKQQAHDLLINKPDGTFLLRFSDSEIGGITIAWKFDSQERMFWNLMPFTTRDFSIRSLADRLGDLNYLIYVFPDRPKDEVYSKYYTPVPCESATAKAVDGYVKPQIKQVVPEFVNASADAGGGSATYMDQAPSPAVCPQAHYNMYPQNPDSVLDTDGDFDLEDTMDVARRVEELLGRPMDSQWIPHAQS	chr17:42199177-42276707[-]	Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation.	PDB: 6MBW; PDB: 6MBZ	HGNC:11367	STA5B_HUMAN	Reviewed	ENSG00000173757	.	.	.	.	.
Mol00655	Protein	Signal transducer activator transcription 3 (STAT3)	Acute-phase response factor; APRF	STAT3	6774	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264657.10, STAT3-201, 4921; ENST00000678906.1, STAT3-244, 4971; ENST00000678960.1, STAT3-246, 4912; ENST00000678044.1, STAT3-231, 4912; ENST00000679014.1, STAT3-247, 4890; ENST00000677723.1, STAT3-227, 4834; ENST00000677030.1, STAT3-216, 4812; ENST00000678827.1, STAT3-242, 4800; ENST00000585517.5, STAT3-211, 3319; ENST00000588969.5, STAT3-212, 2772; ENST00000404395.3, STAT3-203, 2633; ENST00000677421.1, STAT3-222, 4911; ENST00000678792.1, STAT3-241, 4842; ENST00000678913.1, STAT3-245, 4839; ENST00000678043.1, STAT3-230, 4837; ENST00000677442.1, STAT3-223, 4829; ENST00000679185.1, STAT3-249, 4782; ENST00000678905.1, STAT3-243, 4768; ENST00000679166.1, STAT3-248, 4748; ENST00000678048.1, STAT3-232, 4740; ENST00000678572.1, STAT3-237, 4739; ENST00000677479.1, STAT3-224, 4731; ENST00000678674.1, STAT3-239, 4703; ENST00000677152.1, STAT3-217, 3395; ENST00000677603.1, STAT3-226, 3314; ENST00000678535.1, STAT3-236, 3288; ENST00000677002.1, STAT3-215, 3180; ENST00000389272.7, STAT3-202, 2615; ENST00000678445.1, STAT3-234, 4944; ENST00000677820.1, STAT3-229, 4879; ENST00000676636.1, STAT3-214, 4822; ENST00000677271.1, STAT3-219, 4489; ENST00000677308.1, STAT3-220, 3374; ENST00000677346.1, STAT3-221, 1486; ENST00000590776.1, STAT3-213, 1483; ENST00000491272.2, STAT3-208, 1327; ENST00000677500.1, STAT3-225, 1277; ENST00000462286.3, STAT3-205, 1248; ENST00000678764.1, STAT3-240, 5054; ENST00000679231.1, STAT3-250, 4880; ENST00000677763.1, STAT3-228, 3027; ENST00000678659.1, STAT3-238, 2866; ENST00000677270.1, STAT3-218, 2680; ENST00000678529.1, STAT3-235, 2118; ENST00000678108.1, STAT3-233, 1927; ENST00000471989.5, STAT3-206, 826; ENST00000462269.1, STAT3-204, 698; ENST00000498330.1, STAT3-209, 559; ENST00000585360.1, STAT3-210, 517; ENST00000478276.1, STAT3-207, 186"	MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM	chr17:42313324-42388540[-]	"Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity. Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1. Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation. May play an apoptotic role by transctivating BIRC5 expression under LEP activation. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion."	PDB: 5AX3; PDB: 5U5S; PDB: 6NJS; PDB: 6NUQ; PDB: 6QHD; PDB: 6TLC	HGNC:11364	STAT3_HUMAN	Reviewed	ENSG00000168610	.	.	.	.	.
Mol00656	Protein	Steroidogenic factor 1 (STF1)	SF-1; STF-1; hSF-1; Adrenal 4-binding protein; Fushi tarazu factor homolog 1; Nuclear receptor subfamily 5 group A member 1; Steroid hormone receptor Ad4BP; AD4BP; FTZF1; SF1	NR5A1	2516	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373588.9, NR5A1-202, 3074; ENST00000620110.4, NR5A1-204, 2975; ENST00000455734.1, NR5A1-203, 826; ENST00000373587.3, NR5A1-201, 768"	MDYSYDEDLDELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKHYTCTESQSCKIDKTQRKRCPFCRFQKCLTVGMRLEAVRADRMRGGRNKFGPMYKRDRALKQQKKAQIRANGFKLETGPPMGVPPPPPPAPDYVLPPSLHGPEPKGLAAGPPAGPLGDFGAPALPMAVPGAHGPLAGYLYPAFPGRAIKSEYPEPYASPPQPGLPYGYPEPFSGGPNVPELILQLLQLEPDEDQVRARILGCLQEPTKSRPDQPAAFGLLCRMADQTFISIVDWARRCMVFKELEVADQMTLLQNCWSELLVFDHIYRQVQHGKEGSILLVTGQEVELTTVATQAGSLLHSLVLRAQELVLQLLALQLDRQEFVCLKFIILFSLDLKFLNNHILVKDAQEKANAALLDYTLCHYPHCGDKFQQLLLCLVEVRALSMQAKEYLYHKHLGNEMPRNNLLIEMLQAKQT	chr9:124481236-124507420[-]	"Transcriptional activator. Essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. Binds phosphatidylcholine. Binds phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation."	PDB: 1YOW; PDB: 1ZDT; PDB: 4QJR; PDB: 4QK4; PDB: 7KHT	HGNC:7983	STF1_HUMAN	Reviewed	ENSG00000136931	.	.	.	.	.
Mol00657	Protein	Serine/threonine-protein kinase 4 (MST1)	Mammalian STE20-like protein kinase 1; MST-1; STE20-like kinase MST1; Serine/threonine-protein kinase Krs-2; MST1/N; MST1/C; KRS2; MST1	STK4	6789	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000372806.8, STK4-202, 6366; ENST00000372801.5, STK4-201, 2038; ENST00000499879.6, STK4-207, 6161; ENST00000474717.2, STK4-203, 722; ENST00000487587.2, STK4-205, 1850; ENST00000488618.1, STK4-206, 932; ENST00000480745.5, STK4-204, 549"	METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF	chr20:44966479-45080021[+]	"Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes."	PDB: 2JO8; PDB: 3COM; PDB: 4NR2; PDB: 4OH8; PDB: 5TWG; PDB: 5TWH; PDB: 6YAT	HGNC:11408	STK4_HUMAN	Reviewed	ENSG00000101109	.	.	.	.	.
Mol00658	Protein	Recombining binding protein suppressor of hairless (RBPJ)	CBF-1; J kappa-recombination signal-binding protein; RBP-J kappa; RBP-J; RBP-JK; Renal carcinoma antigen NY-REN-30; IGKJRB; IGKJRB1; RBPJK; RBPSUH	RBPJ	3516	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000355476.8, RBPJ-205, 5395; ENST00000342320.8, RBPJ-202, 5761; ENST00000681484.1, RBPJ-244, 2169; ENST00000505958.6, RBPJ-211, 2136; ENST00000681093.1, RBPJ-240, 2100; ENST00000348160.9, RBPJ-204, 1998; ENST00000342295.6, RBPJ-201, 1992; ENST00000680928.1, RBPJ-238, 1850; ENST00000512671.6, RBPJ-223, 1843; ENST00000361572.10, RBPJ-206, 1697; ENST00000507561.5, RBPJ-214, 1689; ENST00000345843.8, RBPJ-203, 1682; ENST00000681264.1, RBPJ-242, 1675; ENST00000504423.2, RBPJ-207, 1621; ENST00000680511.1, RBPJ-237, 2106; ENST00000681260.1, RBPJ-241, 1737; ENST00000681856.1, RBPJ-248, 1706; ENST00000680140.1, RBPJ-234, 1685; ENST00000504907.5, RBPJ-208, 1682; ENST00000509158.6, RBPJ-216, 1678; ENST00000504938.1, RBPJ-209, 731; ENST00000515573.5, RBPJ-231, 698; ENST00000512351.5, RBPJ-222, 609; ENST00000507574.5, RBPJ-215, 607; ENST00000514675.5, RBPJ-227, 578; ENST00000511546.5, RBPJ-221, 572; ENST00000514730.5, RBPJ-228, 569; ENST00000506956.5, RBPJ-213, 566; ENST00000514807.5, RBPJ-229, 340; ENST00000681506.1, RBPJ-245, 1889; ENST00000679698.1, RBPJ-233, 1878; ENST00000681679.1, RBPJ-246, 1766; ENST00000679469.1, RBPJ-232, 1657; ENST00000681025.1, RBPJ-239, 1637; ENST00000681799.1, RBPJ-247, 1534; ENST00000680204.1, RBPJ-235, 1307; ENST00000510778.7, RBPJ-218, 1198; ENST00000680210.1, RBPJ-236, 1191; ENST00000513182.5, RBPJ-224, 537; ENST00000515023.6, RBPJ-230, 1476; ENST00000511401.5, RBPJ-219, 577; ENST00000514656.3, RBPJ-226, 455; ENST00000689192.1, RBPJ-249, 5297; ENST00000691085.1, RBPJ-250, 5281; ENST00000692303.1, RBPJ-251, 3067; ENST00000681403.1, RBPJ-243, 1671; ENST00000514380.5, RBPJ-225, 1519; ENST00000505727.1, RBPJ-210, 860; ENST00000511451.5, RBPJ-220, 742; ENST00000506903.1, RBPJ-212, 658; ENST00000510725.1, RBPJ-217, 546"	MDHTEGSPAEEPPAHAPSPGKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPPNESNTNSEGSYTNASTNSTSVTSSTATVVS	chr4:26163455-26435131[+]	"Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by repressing transcription of NADPH oxidase subunits."	PDB: 2F8X; PDB: 3NBN; PDB: 3V79; PDB: 6PY8	HGNC:5724	SUH_HUMAN	Reviewed	ENSG00000168214	.	.	.	.	.
Mol00659	Protein	Polycomb protein SUZ12 (SUZ12)	Chromatin precipitated E2F target 9 protein; ChET 9 protein; Joined to JAZF1 protein; Suppressor of zeste 12 protein homolog; CHET9; JJAZ1; KIAA0160	SUZ12	23512	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000322652.10, SUZ12-201, 4495; ENST00000580398.1, SUZ12-204, 3977; ENST00000494429.2, SUZ12-202, 1895; ENST00000578106.1, SUZ12-203, 1367"	MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAVAAATASGGKSGGGSCGGGGSYSASSSSSAAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESASPANEEITEEQNGTANGFSEINSKEKALETDSVSGVSKQSKKQKL	chr17:31937007-32001038[+]	"Polycomb group (PcG) protein. Component of the PRC2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The PRC2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2 complex include HOXC8, HOXA9, MYT1 and CDKN2A."	PDB: 4W2R; PDB: 5HYN; PDB: 5IJ7; PDB: 5IJ8; PDB: 5LS6; PDB: 5WAI; PDB: 5WAK; PDB: 5WG6; PDB: 6B3W; PDB: 6C23; PDB: 6C24; PDB: 6NQ3; PDB: 6WKR; PDB: 7AT8; PDB: 7KSO; PDB: 7KSR; PDB: 7KTP	HGNC:17101	SUZ12_HUMAN	Reviewed	ENSG00000178691	.	.	.	.	.
Mol00660	Protein	TAK1-binding protein 3 (TAB3)	Mitogen-activated protein kinase kinase kinase 7-interacting protein 3; NF-kappa-B-activating protein 1; TAK1-binding protein 3; TAB-3; TGF-beta-activated kinase 1-binding protein 3; MAP3K7IP3	TAB3	257397	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000288422.4, TAB3-201, 6647; ENST00000378933.5, TAB3-205, 6671; ENST00000378930.7, TAB3-203, 6255; ENST00000378932.6, TAB3-204, 3698; ENST00000467136.5, TAB3-206, 7987; ENST00000378928.2, TAB3-202, 405"	MAQSSPQLDIQVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQESSKYLYMEYHSPDDNRMNRNRLLHINLGIHSPSSYHPGDGAQLNGGRTLVHSSSDGHIDPQHAAGKQLICLVQEPHSAPAVVAATPNYNPFFMNEQNRSAATPPSQPPQQPSSMQTGMNPSAMQGPSPPPPPPSYMHIPRYSTNPITVTVSQNLPSGQTVPRALQILPQIPSNLYGSPGSIYIRQTSQSSSGRQTPQSTPWQSSPQGPVPHYSQRPLPVYPHQQNYQPSQYSPKQQQIPQSAYHSPPPSQCPSPFSSPQHQVQPSQLGHIFMPPSPSTTPPHPYQQGPPSYQKQGSHSVAYLPYTASSLSKGSMKKIEITVEPSQRPGTAINRSPSPISNQPSPRNQHSLYTATTPPSSSPSRGISSQPKPPFSVNPVYITYTQPTGPSCTPSPSPRVIPNPTTVFKITVGRATTENLLNLVDQEERSAAPEPIQPISVIPGSGGEKGSHKYQRSSSSGSDDYAYTQALLLHQRARMERLAKQLKLEKEELERLKSEVNGMEHDLMQRRLRRVSCTTAIPTPEEMTRLRSMNRQLQINVDCTLKEVDLLQSRGNFDPKAMNNFYDNIEPGPVVPPKPSKKDSSDPCTIERKARRISVTSKVQADIHDTQAAAADEHRTGSTQSPRTQPRDEDYEGAPWNCDSCTFLNHPALNRCEQCEMPRYT	chrX:30827442-30975084[-]	"Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains. The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1."	.	HGNC:30681	TAB3_HUMAN	Reviewed	ENSG00000157625	.	.	.	.	.
Mol00661	Protein	Antigen peptide transporter 1 (TAP1)	APT1; ATP-binding cassette sub-family B member 2; Peptide supply factor 1; Peptide transporter PSF1; PSF-1; Peptide transporter TAP1; Peptide transporter involved in antigen processing 1; Really interesting new gene 4 protein; RING4; ABCB2; PSF1; RING4; Y3	TAP1	6890	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354258.5, TAP1-201, 2685; ENST00000643049.2, TAP1-204, 1319; ENST00000645078.1, TAP1-206, 2170; ENST00000643923.1, TAP1-205, 1992; ENST00000486332.1, TAP1-202, 2542; ENST00000487296.1, TAP1-203, 1031"	MASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGSKSENAGAQGWLAALKPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGSHPTAFVVSYAAALPAAALWHKLGSLWVPGGQGGSGNPVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQAPADAPE	chr6:32845209-32853816[-]	"ABC transporter associated with antigen processing. In complex with TAP2 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules. Uses the chemical energy of ATP to export peptides against the concentration gradient. During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle. Typically transports intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome. Binds peptides with free N- and C-termini, the first three and the C-terminal residues being critical. Preferentially selects peptides having a highly hydrophobic residue at position 3 and hydrophobic or charged residues at the C-terminal anchor. Proline at position 2 has the most destabilizing effect. As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation."	PDB: 1JJ7; PDB: 5U1D	HGNC:43	TAP1_HUMAN	Reviewed	ENSG00000168394	.	.	.	.	.
Mol00662	Protein	Microtubule-associated protein tau (MAPT)	Neurofibrillary tangle protein; Paired helical filament-tau; PHF-tau; MAPTL; MTBT1; TAU	MAPT	4137	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262410.10, MAPT-201, 6815; ENST00000351559.10, MAPT-204, 5639; ENST00000446361.7, MAPT-208, 5345; ENST00000680542.1, MAPT-217, 2988; ENST00000415613.6, MAPT-205, 2331; ENST00000571987.5, MAPT-212, 2277; ENST00000574436.5, MAPT-214, 1326; ENST00000420682.6, MAPT-206, 1239; ENST00000431008.7, MAPT-207, 1233; ENST00000334239.12, MAPT-202, 1107; ENST00000344290.10, MAPT-203, 2609; ENST00000680674.1, MAPT-218, 1936; ENST00000535772.6, MAPT-209, 1353; ENST00000571311.5, MAPT-211, 544; ENST00000570299.5, MAPT-210, 889; ENST00000577017.1, MAPT-216, 142; ENST00000576518.1, MAPT-215, 6778; ENST00000572440.1, MAPT-213, 5015"	MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQEPESGKVVQEGFLREPGPPGLSHQLMSGMPGAPLLPEGPREATRQPSGTGPEDTEGGRHAPELLKHQLLGDLHQEGPPLKGAGGKERPGSKEEVDEDRDVDESSPQDSPPSKASPAQDGRPPQTAAREATSIPGFPAEGAIPLPVDFLSKVSTEIPASEPDGPSVGRAKGQDAPLEFTFHVEITPNVQKEQAHSEEHLGRAAFPGAPGEGPEARGPSLGEDTKEADLPEPSEKQPAAAPRGKPVSRVPQLKARMVSKSKDGTGSDDKKAKTSTRSSAKTLKNRPCLSPKHPTPGSSDPLIQPSSPAVCPEPPSSPKYVSSVTSRTGSSGAKEMKLKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL	chr17:45894527-46028334[+]	"Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization."	PDB: 1I8H; PDB: 2MZ7; PDB: 2ON9; PDB: 3OVL; PDB: 4E0M; PDB: 4E0N; PDB: 4E0O; PDB: 4FL5; PDB: 4GLR; PDB: 4NP8; PDB: 4TQE; PDB: 4Y32; PDB: 4Y3B; PDB: 4Y5I; PDB: 5DMG; PDB: 5E2V; PDB: 5E2W; PDB: 5HF3; PDB: 5K7N; PDB: 5MO3; PDB: 5MP1; PDB: 5MP3; PDB: 5MP5; PDB: 5N5A; PDB: 5N5B; PDB: 5NVB; PDB: 5O3L; PDB: 5O3O; PDB: 5O3T; PDB: 5V5B; PDB: 5V5C; PDB: 5ZIA; PDB: 5ZV3; PDB: 6BB4; PDB: 6CVJ; PDB: 6CVN; PDB: 6DC8; PDB: 6DC9; PDB: 6DCA; PDB: 6FBW; PDB: 6FI5; PDB: 6GK7; PDB: 6GK8; PDB: 6GX5; PDB: 6H06; PDB: 6HRE; PDB: 6HRF; PDB: 6LRA; PDB: 6N4P; PDB: 6NK4; PDB: 6NWP; PDB: 6NWQ; PDB: 6ODG; PDB: 6PXR; PDB: 6QJH; PDB: 6QJM; PDB: 6QJP; PDB: 6QJQ; PDB: 6TJO; PDB: 6TJX; PDB: 6VH7; PDB: 6VHA; PDB: 6VHL; PDB: 6VI3; PDB: 6XLI; PDB: 7MKF; PDB: 7MKG; PDB: 7MKH; PDB: 7NRQ; PDB: 7NRS; PDB: 7NRT; PDB: 7NRV; PDB: 7NRX; PDB: 7P65; PDB: 7P66; PDB: 7P67; PDB: 7P68; PDB: 7P6A; PDB: 7P6B; PDB: 7P6C; PDB: 7P6D; PDB: 7P6E	HGNC:6893	TAU_HUMAN	Reviewed	ENSG00000186868	.	.	.	.	.
Mol00663	Protein	Tubulin beta-3 chain (TUBB3)	Tubulin beta-4 chain; Tubulin beta-III; TUBB4	TUBB3	10381	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000315491.12, TUBB3-201, 1706; ENST00000554444.5, TUBB3-206, 1978; ENST00000554336.5, TUBB3-205, 903; ENST00000555810.5, TUBB3-210, 767; ENST00000553967.1, TUBB3-203, 736; ENST00000555576.5, TUBB3-208, 572; ENST00000556565.5, TUBB3-212, 566; ENST00000555609.5, TUBB3-209, 1855; ENST00000556536.5, TUBB3-211, 925; ENST00000557262.5, TUBB3-213, 888; ENST00000557490.5, TUBB3-214, 806; ENST00000553656.5, TUBB3-202, 550; ENST00000554116.5, TUBB3-204, 542; ENST00000680788.1, TUBB3-216, 5062; ENST00000680647.1, TUBB3-215, 2921; ENST00000554927.1, TUBB3-207, 561"	MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDEEESEAQGPK	chr16:89921392-89938761[+]	"Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. TUBB3 plays a critical role in proper axon guidance and maintenance. Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion. Plays a role in dorsal root ganglion axon projection towards the spinal cord."	PDB: 5IJ0; PDB: 5IJ9; PDB: 5JCO; PDB: 6E7B; PDB: 6S8L; PDB: 6WSL; PDB: 7LXB; PDB: 7M18; PDB: 7M20; PDB: 7PJF	HGNC:20772	TBB3_HUMAN	Reviewed	ENSG00000258947	.	.	.	.	.
Mol00664	Protein	Transcription factor 7 (TCF7)	TCF-7; T-cell-specific transcription factor 1; T-cell factor 1; TCF-1; TCF1	TCF7	6932	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000342854.10, TCF7-201, 3288; ENST00000378560.8, TCF7-202, 2929; ENST00000395023.5, TCF7-203, 2815; ENST00000520958.5, TCF7-218, 1408; ENST00000518915.5, TCF7-211, 1254; ENST00000395029.5, TCF7-204, 3330; ENST00000517855.5, TCF7-209, 799; ENST00000517851.5, TCF7-208, 600; ENST00000518887.5, TCF7-210, 584; ENST00000517799.5, TCF7-207, 570; ENST00000522375.5, TCF7-221, 557; ENST00000519037.5, TCF7-212, 547; ENST00000521639.5, TCF7-219, 539; ENST00000520699.1, TCF7-217, 459; ENST00000517741.5, TCF7-206, 796; ENST00000520652.5, TCF7-216, 651; ENST00000519447.5, TCF7-215, 553; ENST00000517478.1, TCF7-205, 572; ENST00000522653.5, TCF7-223, 5340; ENST00000524342.5, TCF7-224, 3366; ENST00000519238.1, TCF7-214, 1965; ENST00000519165.1, TCF7-213, 1137; ENST00000522561.5, TCF7-222, 769; ENST00000521970.1, TCF7-220, 602"	MPQLDSGGGGAGGGDDLGAPDELLAFQDEGEEQDDKSRDSAAGPERDLAELKSSLVNESEGAAGGAGIPGVPGAGAGARGEAEALGREHAAQRLFPDKLPEPLEDGLKAPECTSGMYKETVYSAFNLLMHYPPPSGAGQHPQPQPPLHKANQPPHGVPQLSLYEHFNSPHPTPAPADISQKQVHRPLQTPDLSGFYSLTSGSMGQLPHTVSWFTHPSLMLGSGVPGHPAAIPHPAIVPPSGKQELQPFDRNLKTQAESKAEKEAKKPTIKKPLNAFMLYMKEMRAKVIAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKRRSREKHQESTTETNWPRELKDGNGQESLSMSSSSSPA	chr5:134114681-134151865[+]	"Transcriptional activator involved in T-cell lymphocyte differentiation. Necessary for the survival of CD4(+) CD8(+) immature thymocytes. Isoforms lacking the N-terminal CTNNB1 binding domain cannot fulfill this role. Binds to the T-lymphocyte-specific enhancer element (5'-WWCAAAG-3') found in the promoter of the CD3E gene. Represses expression of the T-cell receptor gamma gene in alpha-beta T-cell lineages (By similarity). Required for the development of natural killer receptor-positive lymphoid tissue inducer T-cells (By similarity). TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by TCF7 and CTNNB1.May also act as feedback transcriptional repressor of CTNNB1 and TCF7L2 target genes."	.	HGNC:11639	TCF7_HUMAN	Reviewed	ENSG00000081059	.	.	.	.	.
Mol00665	Protein	Translationally-controlled tumor protein (TCTP)	TCTP; Fortilin; Histamine-releasing factor; HRF; p23	TPT1	7178	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000530705.6, TPT1-212, 4548; ENST00000616577.4, TPT1-214, 4814; ENST00000379056.5, TPT1-203, 1101; ENST00000379055.5, TPT1-202, 948; ENST00000309246.9, TPT1-201, 1008; ENST00000379060.8, TPT1-204, 764; ENST00000528619.5, TPT1-209, 731; ENST00000527226.2, TPT1-208, 613; ENST00000530245.5, TPT1-211, 530; ENST00000529421.5, TPT1-210, 801; ENST00000490277.1, TPT1-207, 1851; ENST00000442760.2, TPT1-205, 902; ENST00000484604.5, TPT1-206, 794; ENST00000533567.5, TPT1-213, 594"	MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC	chr13:45333471-45341284[-]	Involved in calcium binding and microtubule stabilization.	PDB: 1YZ1; PDB: 2HR9; PDB: 3EBM; PDB: 4Z9V; PDB: 5O9L; PDB: 5O9M; PDB: 6IZB; PDB: 6IZE	HGNC:12022	TCTP_HUMAN	Reviewed	ENSG00000133112	.	.	.	.	.
Mol00666	Protein	Telomerase reverse transcriptase (TERT)	HEST2; Telomerase catalytic subunit; Telomerase-associated protein 2; TP2; EST2; TCS1; TRT	TERT	7015	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000310581.10, TERT-201, 4039; ENST00000334602.10, TERT-202, 3210; ENST00000656021.1, TERT-206, 5289; ENST00000460137.6, TERT-203, 2992; ENST00000667927.1, TERT-207, 493; ENST00000484238.6, TERT-204, 2422; ENST00000503656.1, TERT-205, 406"	MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD	chr5:1253147-1295068[-]	"Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis."	PDB: 2BCK; PDB: 4B18; PDB: 4MNQ; PDB: 5MEN; PDB: 5MEO; PDB: 5MEP; PDB: 5MEQ; PDB: 5MER; PDB: 5UGW; PDB: 7BG9	HGNC:11730	TERT_HUMAN	Reviewed	ENSG00000164362	.	.	.	.	.
Mol00667	Protein	Transcription factor A (TFAM)	mtTFA; Mitochondrial transcription factor 1; MtTF1; Transcription factor 6; TCF-6; Transcription factor 6-like 2; TCF6; TCF6L2	TFAM	7019	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000487519.6, TFAM-204, 5025; ENST00000373895.7, TFAM-201, 973; ENST00000395377.2, TFAM-203, 663; ENST00000373899.3, TFAM-202, 1121"	MAFLRSMWGVLSALGRSGAELCTGCGSRLRSPFSFVYLPRWFSSVLASCPKKPVSSYLRFSKEQLPIFKAQNPDAKTTELIRRIAQRWRELPDSKKKIYQDAYRAEWQVYKEEISRFKEQLTPSQIMSLEKEIMDKHLKRKAMTKKKELTLLGKPKRPRSAYNVYVAERFQEAKGDSPQEKLKTVKENWKNLSDSEKELYIQHAKEDETRYHNEMKSWEEQMIEVGRKDLLRRTIKKQRKYGAEEC	chr10:58385345-58399220[+]	"Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation. Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA. In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand. Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase. Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites. Is able to unwind DNA. Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes. Required for maintenance of normal levels of mitochondrial DNA. May play a role in organizing and compacting mitochondrial DNA."	PDB: 3FGH; PDB: 3TMM; PDB: 3TQ6; PDB: 4NNU; PDB: 4NOD; PDB: 6ERP; PDB: 6ERQ; PDB: 6HB4; PDB: 6HC3	HGNC:11741	TFAM_HUMAN	Reviewed	ENSG00000108064	.	.	.	.	.
Mol00668	Protein	Protransforming growth factor alpha (TGFA)	TGF-alpha; EGF-like TGF; ETGF; TGF type 1	TGFA	7039	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000295400.11, TGFA-201, 4117; ENST00000418333.6, TGFA-203, 1225; ENST00000444975.5, TGFA-205, 985; ENST00000450929.5, TGFA-207, 950; ENST00000445399.5, TGFA-206, 812; ENST00000419940.5, TGFA-204, 681; ENST00000394241.3, TGFA-202, 568; ENST00000460808.5, TGFA-208, 470; ENST00000474101.1, TGFA-209, 147"	MVPSAGQLALFALGIVLAACQALENSTSPLSADPPVAAAVVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALICRHEKPSALLKGRTACCHSETVV	chr2:70447284-70554193[-]	TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar.	PDB: 1GK5; PDB: 1MOX; PDB: 1YUF; PDB: 1YUG; PDB: 2TGF; PDB: 3E50; PDB: 3TGF; PDB: 4TGF; PDB: 5KN5	HGNC:11765	TGFA_HUMAN	Reviewed	ENSG00000163235	.	.	.	.	.
Mol00669	Protein	Transforming growth factor beta-2 proprotein (TGFB2)	Cetermin; Glioblastoma-derived T-cell suppressor factor; G-TSF; LAP; TGF-beta-2	TGFB2	7042	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000366930.9, TGFB2-202, 5868; ENST00000366929.4, TGFB2-201, 5053; ENST00000479322.1, TGFB2-203, 1508; ENST00000488793.1, TGFB2-204, 405"	MHYCVLSAFLILHLVTVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPEEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPPFFPSENAIPPTFYRPYFRIVRFDVSAMEKNASNLVKAEFRVFRLQNPKARVPEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVHEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYTSGDQKTIKSTRKKNSGKTPHLLLMLLPSYRLESQQTNRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASASPCCVSQDLEPLTILYYIGKTPKIEQLSNMIVKSCKCS	chr1:218345336-218444619[+]	"Transforming growth factor beta-2 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively."	PDB: 1TFG; PDB: 2TGI; PDB: 4KXZ; PDB: 5TX4; PDB: 5TY4; PDB: 6I9J; PDB: 6XM2; PDB: 7RCO	HGNC:11768	TGFB2_HUMAN	Reviewed	ENSG00000092969	.	.	.	.	.
Mol00670	Protein	TGF-beta receptor type I (TGFBR1)	TGFR-1; Activin A receptor type II-like protein kinase of 53kD; Activin receptor-like kinase 5; ALK-5; ALK5; Serine/threonine-protein kinase receptor R4; SKR4; TGF-beta type I receptor; Transforming growth factor-beta receptor type I; TGF-beta receptor type I; TbetaR-I; ALK5; SKR4	TGFBR1	7046	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374994.9, TGFBR1-202, 6492; ENST00000552516.5, TGFBR1-209, 5933; ENST00000374990.6, TGFBR1-201, 5720; ENST00000550253.1, TGFBR1-208, 1538; ENST00000549021.5, TGFBR1-206, 680; ENST00000548365.5, TGFBR1-205, 582; ENST00000546584.1, TGFBR1-203, 565; ENST00000547314.5, TGFBR1-204, 533; ENST00000552573.6, TGFBR1-210, 526; ENST00000549766.5, TGFBR1-207, 1678"	MEAAVAAPRPRLLLLVLAAAAAAAAALLPGATALQCFCHLCTKDNFTCVTDGLCFVSVTETTDKVIHNSMCIAEIDLIPRDRPFVCAPSSKTGSVTTTYCCNQDHCNKIELPTTVKSSPGLGPVELAAVIAGPVCFVCISLMLMVYICHNRTVIHHRVPNEEDPSLDRPFISEGTTLKDLIYDMTTSGSGSGLPLLVQRTIARTIVLQESIGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNGTWTQLWLVSDYHEHGSLFDYLNRYTVTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESFKRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVCEQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLSQQEGIKM	chr9:99104038-99154192[+]	"Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation."	PDB: 1B6C; PDB: 1IAS; PDB: 1PY5; PDB: 1RW8; PDB: 1VJY; PDB: 2L5S; PDB: 2PJY; PDB: 2WOT; PDB: 2WOU; PDB: 2X7O; PDB: 3FAA; PDB: 3GXL; PDB: 3HMM; PDB: 3KCF; PDB: 3KFD; PDB: 3TZM; PDB: 4X0M; PDB: 4X2F; PDB: 4X2G; PDB: 4X2J; PDB: 4X2K; PDB: 4X2N; PDB: 5E8S; PDB: 5E8T; PDB: 5E8U; PDB: 5E8W; PDB: 5E8X; PDB: 5E8Z; PDB: 5E90; PDB: 5FRI; PDB: 5QIK; PDB: 5QIL; PDB: 5QIM; PDB: 5QTZ; PDB: 5QU0; PDB: 5USQ; PDB: 6B8Y; PDB: 6MAC	HGNC:11772	TGFR1_HUMAN	Reviewed	ENSG00000106799	.	.	.	.	.
Mol00671	Protein	"Fructose-2,6-bisphosphatase TIGAR (TIGAR)"	TP53-induced glycolysis and apoptosis regulator; TP53-induced glycolysis regulatory phosphatase; C12orf5	TIGAR	57103	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000179259.6, TIGAR-201, 8209; ENST00000635110.1, TIGAR-204, 3633; ENST00000537251.1, TIGAR-202, 527; ENST00000539671.1, TIGAR-203, 160"	MARFALTVVRHGETRFNKEKIIQGQGVDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERSKFCKDMTVKYDSRLRERKYGVVEGKALSELRAMAKAAREECPVFTPPGGETLDQVKMRGIDFFEFLCQLILKEADQKEQFSQGSPSNCLETSLAEIFPLGKNHSSKVNSDSGIPGLAASVLVVSHGAYMRSLFDYFLTDLKCSLPATLSRSELMSVTPNTGMSLFIINFEEGREVKPTVQCICMNLQDHLNGLTETR	chr12:4307763-4360028[+]	"Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate. Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production. Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death. Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity. In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3. Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage. Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation. Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions. Protects glioma cells from hypoxia- and ROS-induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1-dependent and p53/TP53-independent manner. Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses. Involved in intestinal tumor progression."	PDB: 3DCY	HGNC:1185	TIGAR_HUMAN	Reviewed	ENSG00000078237	.	.	.	.	.
Mol00672	Protein	Metalloproteinase inhibitor 1 (TIMP1)	Erythroid-potentiating activity; EPA; Fibroblast collagenase inhibitor; Collagenase inhibitor; Tissue inhibitor of metalloproteinases 1; TIMP-1; CLGI; TIMP	TIMP1	7076	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000218388.9, TIMP1-201, 769; ENST00000456754.6, TIMP1-205, 1095; ENST00000377017.5, TIMP1-202, 626; ENST00000445623.1, TIMP1-204, 595; ENST00000441738.1, TIMP1-203, 341"	MAPFEPLASGILLLLWLIAPSRACTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLRSQIA	chrX:47582408-47586789[+]	"Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors."	PDB: 1D2B; PDB: 1OO9; PDB: 1UEA; PDB: 2J0T; PDB: 3MA2; PDB: 3V96; PDB: 6MAV; PDB: 6N9D	HGNC:11820	TIMP1_HUMAN	Reviewed	ENSG00000102265	.	.	.	.	.
Mol00673	Protein	Toll-like receptor 3 (TLR3)	.	TLR3	7098	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000296795.8, TLR3-201, 6015; ENST00000504367.1, TLR3-202, 2310; ENST00000513189.1, TLR3-205, 1156; ENST00000508051.1, TLR3-203, 628; ENST00000512264.1, TLR3-204, 2942"	MRQTLPCIYFWGGLLPFGMLCASSTTKCTVSHEVADCSHLKLTQVPDDLPTNITVLNLTHNQLRRLPAANFTRYSQLTSLDVGFNTISKLEPELCQKLPMLKVLNLQHNELSQLSDKTFAFCTNLTELHLMSNSIQKIKNNPFVKQKNLITLDLSHNGLSSTKLGTQVQLENLQELLLSNNKIQALKSEELDIFANSSLKKLELSSNQIKEFSPGCFHAIGRLFGLFLNNVQLGPSLTEKLCLELANTSIRNLSLSNSQLSTTSNTTFLGLKWTNLTMLDLSYNNLNVVGNDSFAWLPQLEYFFLEYNNIQHLFSHSLHGLFNVRYLNLKRSFTKQSISLASLPKIDDFSFQWLKCLEHLNMEDNDIPGIKSNMFTGLINLKYLSLSNSFTSLRTLTNETFVSLAHSPLHILNLTKNKISKIESDAFSWLGHLEVLDLGLNEIGQELTGQEWRGLENIFEIYLSYNKYLQLTRNSFALVPSLQRLMLRRVALKNVDSSPSPFQPLRNLTILDLSNNNIANINDDMLEGLEKLEILDLQHNNLARLWKHANPGGPIYFLKGLSHLHILNLESNGFDEIPVEVFKDLFELKIIDLGLNNLNTLPASVFNNQVSLKSLNLQKNLITSVEKKVFGPAFRNLTELDMRFNPFDCTCESIAWFVNWINETHTNIPELSSHYLCNTPPHYHGFPVRLFDTSSCKDSAPFELFFMINTSILLIFIFIVLLIHFEGWRISFYWNVSVHRVLGFKEIDRQTEQFEYAAYIIHAYKDKDWVWEHFSSMEKEDQSLKFCLEERDFEAGVFELEAIVNSIKRSRKIIFVITHHLLKDPLCKRFKVHHAVQQAIEQNLDSIILVFLEEIPDYKLNHALCLRRGMFKSHCILNWPVQKERIGAFRHKLQVALGSKNSVH	chr4:186069155-186088073[+]	"Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response."	PDB: 1ZIW; PDB: 2A0Z; PDB: 2MK9; PDB: 2MKA; PDB: 3ULU; PDB: 3ULV; PDB: 5GS0; PDB: 7C76	HGNC:11849	TLR3_HUMAN	Reviewed	ENSG00000164342	.	.	.	.	.
Mol00674	Protein	Transmembrane emp24 domain-containing protein 3 (TMED3)	Membrane protein p24B; p24 family protein gamma-4; p24gamma4; p26; C15orf22; UNQ5357/PRO1078	TMED3	23423	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000299705.10, TMED3-201, 1418; ENST00000424155.6, TMED3-202, 16555; ENST00000536821.5, TMED3-203, 2265; ENST00000543455.1, TMED3-204, 1483; ENST00000558562.1, TMED3-205, 938"	MGSTVPRSASVLLLLLLLRRAEQPCGAELTFELPDNAKQCFHEEVEQGVKFSLDYQVITGGHYDVDCYVEDPQGNTIYRETKKQYDSFTYRAEVKGVYQFCFSNEFSTFSHKTVYFDFQVGDEPPILPDMGNRVTALTQMESACVTIHEALKTVIDSQTHYRLREAQDRARAEDLNSRVSYWSVGETIALFVVSFSQVLLLKSFFTEKRPISRAVHS	chr15:79311112-79427432[+]	"Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network."	.	HGNC:28889	TMED3_HUMAN	Reviewed	ENSG00000166557	.	.	.	.	.
Mol00675	Protein	Transmembrane protein 54 (TMM54)	Beta-casein-like protein; Protein CAC-1; BCLP; CAC1	TMEM54	113452	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373463.8, TMEM54-202, 1030"	MCLRLGGLSVGDFRKVLMKTGLVLVVLGHVSFITAALFHGTVLRYVGTPQDAVALQYCVVNILSVTSAIVVITSGIAAIVLSRYLPSTPLRWTVFSSSVACALLSLTCALGLLASIAMTFATQGKALLAACTFGSSELLALAPDCPFDPTRIYSSSLCLWGIALVLCVAENVFAVRCAQLTHQLLELRPWWGKSSHHMMRENPELVEGRDLLSCTSSEPLTL	chr1:32894594-32901438[-]	.	.	HGNC:24143	TMM54_HUMAN	Reviewed	ENSG00000121900	.	.	.	.	.
Mol00676	Protein	Tumor necrosis factor ligand superfamily member 13B (TNFSF13B)	.	TNFSF13B	10673	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375887.9, TNFSF13B-201, 2576; ENST00000430559.5, TNFSF13B-202, 2614; ENST00000542136.1, TNFSF13B-206, 495; ENST00000479435.1, TNFSF13B-203, 637; ENST00000493765.1, TNFSF13B-205, 507; ENST00000486502.1, TNFSF13B-204, 395"	MDDSTEREQSRLTSCLKKREEMKLKECVSILPRKESPSVRSSKDGKLLAATLLLALLSCCLTVVSFYQVAALQGDLASLRAELQGHHAEKLPAGAGAPKAGLEEAPAVTAGLKIFEPPAPGEGNSSQNSRNKRAVQGPEETVTQDCLQLIADSETPTIQKGSYTFVPWLLSFKRGSALEEKENKILVKETGYFFIYGQVLYTDKTYAMGHLIQRKKVHVFGDELSLVTLFRCIQNMPETLPNNSCYSAGIAKLEEGDELQLAIPRENAQISLDGDVTFFGALKLL	chr13:108251240-108308484[+]	"Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response."	PDB: 1JH5; PDB: 1KD7; PDB: 1KXG; PDB: 1OQD; PDB: 1OQE; PDB: 1OSG; PDB: 3V56; PDB: 4V46; PDB: 4ZCH; PDB: 5Y9J; PDB: 6FXN	HGNC:11929	TN13B_HUMAN	Reviewed	ENSG00000102524	.	.	.	.	.
Mol00677	Protein	Tumor necrosis factor alpha-induced protein 3 (TNFAIP3)	TNF alpha-induced protein 3; OTU domain-containing protein 7C; Putative DNA-binding protein A20; Zinc finger protein A20; OTUD7C	TNFAIP3	7128	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000612899.5, TNFAIP3-206, 4665; ENST00000237289.8, TNFAIP3-201, 4432; ENST00000420009.5, TNFAIP3-202, 698; ENST00000433680.1, TNFAIP3-204, 465; ENST00000421450.1, TNFAIP3-203, 421; ENST00000485192.1, TNFAIP3-205, 604"	MAEQVLPQALYLSNMRKAVKIRERTPEDIFKPTNGIIHHFKTMHRYTLEMFRTCQFCPQFREIIHKALIDRNIQATLESQKKLNWCREVRKLVALKTNGDGNCLMHATSQYMWGVQDTDLVLRKALFSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLIKMASTDTPMARSGLQYNSLEEIHIFVLCNILRRPIIVISDKMLRSLESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSHHFVPLVTLKDSGPEIRAVPLVNRDRGRFEDLKVHFLTDPENEMKEKLLKEYLMVIEIPVQGWDHGTTHLINAAKLDEANLPKEINLVDDYFELVQHEYKKWQENSEQGRREGHAQNPMEPSVPQLSLMDVKCETPNCPFFMSVNTQPLCHECSERRQKNQNKLPKLNSKPGPEGLPGMALGASRGEAYEPLAWNPEESTGGPHSAPPTAPSPFLFSETTAMKCRSPGCPFTLNVQHNGFCERCHNARQLHASHAPDHTRHLDPGKCQACLQDVTRTFNGICSTCFKRTTAEASSSLSTSLPPSCHQRSKSDPSRLVRSPSPHSCHRAGNDAPAGCLSQAARTPGDRTGTSKCRKAGCVYFGTPENKGFCTLCFIEYRENKHFAAASGKVSPTASRFQNTIPCLGRECGTLGSTMFEGYCQKCFIEAQNQRFHEAKRTEEQLRSSQRRDVPRTTQSTSRPKCARASCKNILACRSEELCMECQHPNQRMGPGAHRGEPAPEDPPKQRCRAPACDHFGNAKCNGYCNECFQFKQMYG	chr6:137867214-137883312[+]	"Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of proinflammatory cytokines and IFN beta in LPS-tolerized macrophages."	PDB: 2EQE; PDB: 2EQF; PDB: 2EQG; PDB: 2VFJ; PDB: 3DKB; PDB: 3OJ3; PDB: 3OJ4; PDB: 3VUW; PDB: 3VUX; PDB: 3VUY; PDB: 3ZJD; PDB: 3ZJE; PDB: 3ZJF; PDB: 3ZJG; PDB: 5LRX; PDB: 5V3B; PDB: 5V3P	HGNC:11896	TNAP3_HUMAN	Reviewed	ENSG00000118503	.	.	.	.	.
Mol00678	Protein	Tumor necrosis factor ligand superfamily member 10 (TNFSF10)	.	TNFSF10	8743	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000241261.7, TNFSF10-201, 1876; ENST00000420541.6, TNFSF10-202, 1619; ENST00000430881.1, TNFSF10-203, 467; ENST00000466777.1, TNFSF10-204, 1326; ENST00000494851.5, TNFSF10-206, 572; ENST00000472804.1, TNFSF10-205, 566"	MAMMEVQGGPSLGQTCVLIVIFTVLLQSLCVAVTYVYFTNELKQMQDKYSKSGIACFLKEDDSYWDPNDEESMNSPCWQVKWQLRQLVRKMILRTSEETISTVQEKQQNISPLVRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG	chr3:172505508-172523475[-]	"Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis."	PDB: 1D0G; PDB: 1D2Q; PDB: 1D4V; PDB: 1DG6; PDB: 1DU3; PDB: 4N90; PDB: 5CIR	HGNC:11925	TNF10_HUMAN	Reviewed	ENSG00000121858	.	.	.	.	.
Mol00679	Protein	Tumor necrosis factor (TNF)	Cachectin; TNF-alpha; Tumor necrosis factor ligand superfamily member 2; TNF-a; N-terminal fragment; NTF; ICD1; ICD2; TNFA; TNFSF2	TNF	7124	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000449264.3, TNF-208, 1678"	MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL	chr6:31575565-31578336[+]	"Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Up-regulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective. Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line. Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance. Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6."	PDB: 1A8M; PDB: 1TNF; PDB: 2AZ5; PDB: 2E7A; PDB: 2TUN; PDB: 2ZJC; PDB: 2ZPX; PDB: 3ALQ; PDB: 3IT8; PDB: 3L9J; PDB: 3WD5; PDB: 4G3Y; PDB: 4TSV; PDB: 4TWT; PDB: 4Y6O; PDB: 5M2I; PDB: 5M2J; PDB: 5M2M; PDB: 5MU8; PDB: 5TSW; PDB: 5UUI; PDB: 5WUX; PDB: 5YOY; PDB: 6OOY; PDB: 6OOZ; PDB: 6OP0; PDB: 6RMJ; PDB: 6X81; PDB: 6X82; PDB: 6X83; PDB: 6X85; PDB: 6X86; PDB: 7ASY; PDB: 7AT7; PDB: 7ATB; PDB: 7JRA; PDB: 7KP9; PDB: 7KPA; PDB: 7KPB	HGNC:11892	TNFA_HUMAN	Reviewed	ENSG00000232810	.	.	.	.	.
Mol00680	Protein	Target of Myb protein 1 (TOM1)	.	TOM1	10043	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000449058.7, TOM1-209, 2278; ENST00000411850.5, TOM1-203, 2390; ENST00000447733.5, TOM1-208, 2317; ENST00000425375.5, TOM1-205, 2252; ENST00000456128.5, TOM1-211, 1133; ENST00000443206.2, TOM1-207, 567; ENST00000608749.5, TOM1-218, 553; ENST00000608674.5, TOM1-217, 541; ENST00000404284.6, TOM1-202, 2622; ENST00000424387.5, TOM1-204, 2211; ENST00000439512.5, TOM1-206, 800; ENST00000449508.1, TOM1-210, 593; ENST00000395736.7, TOM1-201, 560; ENST00000492723.1, TOM1-215, 2568; ENST00000491987.1, TOM1-214, 852; ENST00000487670.1, TOM1-213, 849; ENST00000465529.1, TOM1-212, 555; ENST00000497448.1, TOM1-216, 438"	MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDALRAVKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHVLVASQDFVESVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVTIYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETQSGQDSVGTDSSQQEDSGQHAAPLPAPPILSGDTPIAPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQAEPADLELLQELNRTCRAMQQRVLELIPQIANEQLTEELLIVNDNLNNVFLRHERFERFRTGQTTKAPSEAEPAADLIDMGPDPAATGNLSSQLAGMNLGSSSVRAGLQSLEASGRLEDEFDMFALTRGSSLADQRKEVKYEAPQATDGLAGALDARQQSTGAIPVTQACLMEDIEQWLSTDVGNDAEEPKGVTSEEFDKFLEERAKAADRLPNLSSPSAEGPPGPPSGPAPRKKTQEKDDDMLFAL	chr22:35299275-35347992[+]	May be involved in intracellular trafficking. Probable association with membranes.	.	HGNC:11982	TOM1_HUMAN	Reviewed	ENSG00000100284	.	.	.	.	.
Mol00681	Protein	DNA topoisomerase 1 (TOP1)	DNA topoisomerase I	TOP1	7150	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361337.3, TOP1-201, 3734; ENST00000680945.1, TOP1-202, 2532; ENST00000681113.1, TOP1-204, 3938; ENST00000681058.1, TOP1-203, 8092; ENST00000681392.1, TOP1-205, 4782; ENST00000681884.1, TOP1-206, 4736"	MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF	chr20:41028822-41124487[+]	"Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter."	PDB: 1A31; PDB: 1A35; PDB: 1A36; PDB: 1EJ9; PDB: 1K4S; PDB: 1K4T; PDB: 1LPQ; PDB: 1NH3; PDB: 1R49; PDB: 1RR8; PDB: 1RRJ; PDB: 1SC7; PDB: 1SEU; PDB: 1T8I; PDB: 1TL8	HGNC:11986	TOP1_HUMAN	Reviewed	ENSG00000198900	.	.	.	.	.
Mol00682	Protein	DNA topoisomerase 2-beta (TOP2B)	DNA topoisomerase II; beta isozyme	TOP2B	7155	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264331.9, TOP2B-201, 5814; ENST00000435706.6, TOP2B-204, 5389; ENST00000424225.1, TOP2B-203, 3525; ENST00000413971.5, TOP2B-202, 2049; ENST00000475717.1, TOP2B-206, 540; ENST00000491510.1, TOP2B-207, 584; ENST00000470132.1, TOP2B-205, 451"	MAKSGGCGAGAGVGGGNGALTWVTLFDQNNAAKKEESETANKNDSSKKLSVERVYQKKTQLEHILLRPDTYIGSVEPLTQFMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKVSIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEAKIKHFDGEDYTCITFQPDLSKFKMEKLDKDIVALMTRRAYDLAGSCRGVKVMFNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHELANERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFINCLIENPTFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIVESILNWVKFKAQTQLNKKCSSVKYSKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHIENQKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEKAAEEDETQNQHDDSSSDSGTPSGPDFNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPSDLWKEDLAAFVEELDKVESQEREDVLAGMSGKAIKGKVGKPKVKKLQLEETMPSPYGRRIIPEITAMKADASKKLLKKKKGDLDTAAVKVEFDEEFSGAPVEGAGEEALTPSVPINKGPKPKREKKEPGTRVRKTPTSSGKPSAKKVKKRNPWSDDESKSESDLEETEPVVIPRDSLLRRAAAERPKYTFDFSEEEDDDADDDDDDNNDLEELKVKASPITNDGEDEFVPSDGLDKDEYTFSPGKSKATPEKSLHDKKSQDFGNLFSFPSYSQKSEDDSAKFDSNEEDSASVFSPSFGLKQTDKVPSKTVAAKKGKPSSDTVPKPKRAPKQKKVVEAVNSDSDSEFGIPKKTTTPKGKGRGAKKRKASGSENEGDYNPGRKTSKTTSKKPKKTSFDQDSDVDIFPSDFPTEPPSLPRTGRARKEVKYFAESDEEEDDVDFAMFN	chr3:25597984-25664907[-]	"Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand."	PDB: 3QX3; PDB: 4G0U; PDB: 4G0V; PDB: 4G0W; PDB: 4J3N; PDB: 5GWI; PDB: 5GWJ; PDB: 5ZAD; PDB: 5ZEN; PDB: 5ZQF; PDB: 5ZRF	HGNC:11990	TOP2B_HUMAN	Reviewed	ENSG00000077097	.	.	.	.	.
Mol00683	Protein	Zinc finger protein RFP (TRIM27)	RING finger protein 76; RING-type E3 ubiquitin transferase TRIM27; Ret finger protein; Tripartite motif-containing protein 27; RFP; RNF76	TRIM27	5987	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377199.4, TRIM27-202, 2963; ENST00000377194.7, TRIM27-201, 2686; ENST00000414543.5, TRIM27-203, 1813; ENST00000498117.1, TRIM27-207, 728; ENST00000496091.1, TRIM27-206, 687; ENST00000467742.1, TRIM27-204, 541; ENST00000481474.5, TRIM27-205, 7006"	MASGSVAECLQQETTCPVCLQYFAEPMMLDCGHNICCACLARCWGTAETNVSCPQCRETFPQRHMRPNRHLANVTQLVKQLRTERPSGPGGEMGVCEKHREPLKLYCEEDQMPICVVCDRSREHRGHSVLPLEEAVEGFKEQIQNQLDHLKRVKDLKKRRRAQGEQARAELLSLTQMEREKIVWEFEQLYHSLKEHEYRLLARLEELDLAIYNSINGAITQFSCNISHLSSLIAQLEEKQQQPTRELLQDIGDTLSRAERIRIPEPWITPPDLQEKIHIFAQKCLFLTESLKQFTEKMQSDMEKIQELREAQLYSVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLGSPCFIAGRHYWEVEVGDKAKWTIGVCEDSVCRKGGVTSAPQNGFWAVSLWYGKEYWALTSPMTALPLRTPLQRVGIFLDYDAGEVSFYNVTERCHTFTFSHATFCGPVRPYFSLSYSGGKSAAPLIICPMSGIDGFSGHVGNHGHSMETSP	chr6:28903002-28923988[-]	"E3 ubiquitin-protein ligase that mediates ubiquitination of PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-linked polyubiquitin chains; the function inhibits CD4 T-cell activation. Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly. Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA."	.	HGNC:9975	TRI27_HUMAN	Reviewed	ENSG00000204713	.	.	.	.	.
Mol00684	Protein	E3 ubiquitin-protein ligase TRIM31 (TRIM31)	RING-type E3 ubiquitin transferase TRIM31; Tripartite motif-containing protein 31; C6orf13; RNF	TRIM31	11074	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000376734.4, TRIM31-210, 2027; ENST00000485864.5, TRIM31-215, 620; ENST00000471695.1, TRIM31-212, 1223; ENST00000493404.1, TRIM31-216, 613; ENST00000480808.1, TRIM31-213, 593; ENST00000468264.1, TRIM31-211, 517; ENST00000484583.1, TRIM31-214, 510"	MASGQFVNKLQEEVICPICLDILQKPVTIDCGHNFCLKCITQIGETSCGFFKCPLCKTSVRKNAIRFNSLLRNLVEKIQALQASEVQSKRKEATCPRHQEMFHYFCEDDGKFLCFVCRESKDHKSHNVSLIEEAAQNYQGQIQEQIQVLQQKEKETVQVKAQGVHRVDVFTDQVEHEKQRILTEFELLHQVLEEEKNFLLSRIYWLGHEGTEAGKHYVASTEPQLNDLKKLVDSLKTKQNMPPRQLLEDIKVVLCRSEEFQFLNPTPVPLELEKKLSEAKSRHDSITGSLKKFKDQLQADRKKDENRFFKSMNKNDMKSWGLLQKNNHKMNKTSEPGSSSAGGRTTSGPPNHHSSAPSHSLFRASSAGKVTFPVCLLASYDEISGQGASSQDTKTFDVALSEELHAALSEWLTAIRAWFCEVPSS	chr6:30102897-30113090[-]	Regulator of Src-induced anchorage independent cell growth (By similarity). May have E3 ubiquitin-protein ligase activity.	PDB: 2YSJ; PDB: 2YSL	HGNC:16289	TRI31_HUMAN	Reviewed	ENSG00000204616	.	.	.	.	.
Mol00685	Protein	Short transient receptor potential channel 5 (TRPC5)	TrpC5; Transient receptor protein 5; TRP-5; hTRP-5; hTRP5; TRP5	TRPC5	7224	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262839.3, TRPC5-201, 12143"	MAQLYYKKVNYSPYRDRIPLQIVRAETELSAEEKAFLNAVEKGDYATVKQALQEAEIYYNVNINCMDPLGRSALLIAIENENLEIMELLLNHSVYVGDALLYAIRKEVVGAVELLLSYRRPSGEKQVPTLMMDTQFSEFTPDITPIMLAAHTNNYEIIKLLVQKRVTIPRPHQIRCNCVECVSSSEVDSLRHSRSRLNIYKALASPSLIALSSEDPILTAFRLGWELKELSKVENEFKAEYEELSQQCKLFAKDLLDQARSSRELEIILNHRDDHSEELDPQKYHDLAKLKVAIKYHQKEFVAQPNCQQLLATLWYDGFPGWRRKHWVVKLLTCMTIGFLFPMLSIAYLISPRSNLGLFIKKPFIKFICHTASYLTFLFMLLLASQHIVRTDLHVQGPPPTVVEWMILPWVLGFIWGEIKEMWDGGFTEYIHDWWNLMDFAMNSLYLATISLKIVAYVKYNGSRPREEWEMWHPTLIAEALFAISNILSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYETRAIDEPNNCKGIRCEKQNNAFSTLFETLQSLFWSVFGLLNLYVTNVKARHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFDEGGTLPPPFNIIPSPKSFLYLGNWFNNTFCPKRDPDGRRRRRNLRSFTERNADSLIQNQHYQEVIRNLVKRYVAAMIRNSKTHEGLTEENFKELKQDISSFRYEVLDLLGNRKHPRSFSTSSTELSQRDDNNDGSGGARAKSKSVSFNLGCKKKTCHGPPLIRTMPRSSGAQGKSKAESSSKRSFMGPSLKKLGLLFSKFNGHMSEPSSEPMYTISDGIVQQHCMWQDIRYSQMEKGKAEACSQSEINLSEVELGEVQGAAQSSECPLACSSSLHCASSICSSNSKLLDSSEDVFETWGEACDLLMHKWGDGQEEQVTTRL	chrX:111768011-112082776[-]	Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective (By similarity). May also be activated by intracellular calcium store depletion. Mediates calcium-dependent phosphatidylserine externalization and apoptosis in neurons via its association with PLSCR1 (By similarity).	PDB: 6YSN; PDB: 7D4P; PDB: 7D4Q; PDB: 7E4T	HGNC:12337	TRPC5_HUMAN	Reviewed	ENSG00000072315	.	.	.	.	.
Mol00686	Protein	Tetraspanin-12 (TSN12)	Tspan-12; Tetraspan NET-2; Transmembrane 4 superfamily member 12; NET2; TM4SF12; UNQ774/PRO1568	TSPAN12	23554	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000222747.8, TSPAN12-201, 2585; ENST00000415871.5, TSPAN12-202, 1495; ENST00000430985.1, TSPAN12-204, 693; ENST00000424710.5, TSPAN12-203, 569; ENST00000441017.5, TSPAN12-206, 551; ENST00000433758.5, TSPAN12-205, 551; ENST00000450414.5, TSPAN12-207, 1167"	MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL	chr7:120787320-120858402[-]	"Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activate the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity."	.	HGNC:21641	TSN12_HUMAN	Reviewed	ENSG00000106025	.	.	.	.	.
Mol00687	Protein	Tumor suppressor candidate 3 (TUSC3)	Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3; Oligosaccharyl transferase subunit TUSC3; Magnesium uptake/transporter TUSC3; Protein N33; N33	TUSC3	7991	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000503731.6, TUSC3-203, 3697; ENST00000382020.8, TUSC3-201, 3683; ENST00000506802.5, TUSC3-204, 1546; ENST00000509380.5, TUSC3-209, 1266; ENST00000511783.2, TUSC3-212, 1203; ENST00000515859.5, TUSC3-213, 1627; ENST00000510836.5, TUSC3-210, 1452; ENST00000503191.5, TUSC3-202, 731; ENST00000507400.1, TUSC3-206, 727; ENST00000508446.1, TUSC3-207, 457; ENST00000507316.1, TUSC3-205, 573; ENST00000511342.1, TUSC3-211, 555; ENST00000509177.1, TUSC3-208, 493"	MGARGAPSRRRQAGRRLRYLPTGSFPFLLLLLLLCIQLGGGQKKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSVCRQANEEYQILANSWRYSSAFCNKLFFSMVDYDEGTDVFQQLNMNSAPTFMHFPPKGRPKRADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRPPNYSGTIALALLVSLVGGLLYLRRNNLEFIYNKTGWAMVSLCIVFAMTSGQMWNHIRGPPYAHKNPHNGQVSYIHGSSQAQFVAESHIILVLNAAITMGMVLLNEAATSKGDVGKRRIICLVGLGLVVFFFSFLLSIFRSKYHGYPYSDLDFE	chr8:15417215-15766649[+]	Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition.	PDB: 4M8G; PDB: 4M90; PDB: 4M91; PDB: 4M92	HGNC:30242	TUSC3_HUMAN	Reviewed	ENSG00000104723	.	.	.	.	.
Mol00688	Protein	Twinfilin-1 (TWF1)	Protein A6; Protein tyrosine kinase 9; PTK9	TWF1	5756	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000395510.7, TWF1-201, 2987; ENST00000548315.5, TWF1-207, 1170; ENST00000552521.5, TWF1-211, 3012; ENST00000546662.5, TWF1-203, 925; ENST00000546506.5, TWF1-202, 582; ENST00000548403.1, TWF1-208, 396; ENST00000547459.5, TWF1-204, 3320; ENST00000550371.1, TWF1-209, 612; ENST00000547564.1, TWF1-205, 558; ENST00000551789.1, TWF1-210, 617; ENST00000547961.1, TWF1-206, 455"	MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVGVDTKHQTLQGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNTELKDLPKRIPKDSARYHFFLYKHSHEGDYLESIVFIYSMPGYTCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNGDELTADFLYEEVHPKQHAHKQSFAKPKGPAGKRGIRRLIRGPAETEATTD	chr12:43793723-43806328[-]	"Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles (By similarity)."	PDB: 7CCC	HGNC:9620	TWF1_HUMAN	Reviewed	ENSG00000151239	.	.	.	.	.
Mol00689	Protein	Twist-related protein 1 (TWST1)	Class A basic helix-loop-helix protein 38; bHLHa38; H-twist; BHLHA38; TWIST	TWIST1	7291	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000242261.6, TWIST1-201, 1630; ENST00000354571.5, TWIST1-202, 589; ENST00000443687.5, TWIST1-203, 527"	MMQDVSSSPVSPADDSLSNSEEEPDRQQPPSGKRGGRKRRSSRRSAGGGAGPGGAAGGGVGGGDEPGSPAQGKRGKKSAGCGGGGGAGGGGGSSSGGGSPQSYEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH	chr7:19020991-19117636[-]	"Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer (By similarity)."	PDB: 2MJV	HGNC:12428	TWST1_HUMAN	Reviewed	ENSG00000122691	.	.	.	.	.
Mol00690	Protein	Transcriptional repressor protein YY1 (TYY1)	Delta transcription factor; INO80 complex subunit S; NF-E1; Yin and yang 1; YY-1; INO80S	YY1	7528	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262238.10, YY1-201, 6534; ENST00000554804.1, YY1-205, 1114; ENST00000554371.1, YY1-203, 636; ENST00000553625.5, YY1-202, 422; ENST00000651219.1, YY1-207, 931; ENST00000623799.1, YY1-206, 2742; ENST00000554579.1, YY1-204, 826"	MASGDTLYIATDGSEMPAEIVELHEIEVETIPVETIETTVVGEEEEEDDDDEDGGGGDHGGGGGHGHAGHHHHHHHHHHHPPMIALQPLVTDDPTQVHHHQEVILVQTREEVVGGDDSDGLRAEDGFEDQILIPVPAPAGGDDDYIEQTLVTVAAAGKSGGGGSSSSGGGRVKKGGGKKSGKKSYLSGGAGAAGGGGADPGNKKWEQKQVQIKTLEGEFSVTMWSSDEKKDIDHETVVEEQIIGENSPPDYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARMKPRKIKEDDAPRTIACPHKGCTKMFRDNSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPYVCPFDGCNKKFAQSTNLKSHILTHAKAKNNQ	chr14:100238298-100282788[+]	"Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Plays a role in regulating enhancer activation."	PDB: 1UBD; PDB: 1ZNM; PDB: 4C5I	HGNC:12856	TYY1_HUMAN	Reviewed	ENSG00000100811	.	.	.	.	.
Mol00691	Protein	Ubiquitin-conjugating enzyme E2 C (UBE2C)	(E3-independent) E2 ubiquitin-conjugating enzyme C; E2 ubiquitin-conjugating enzyme C; UbcH10; Ubiquitin carrier protein C; Ubiquitin-protein ligase C; UBCH10	UBE2C	11065	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356455.9, UBE2C-204, 777; ENST00000372568.4, UBE2C-205, 914; ENST00000335046.7, UBE2C-202, 737; ENST00000617055.4, UBE2C-208, 705; ENST00000352551.9, UBE2C-203, 665; ENST00000405520.5, UBE2C-206, 641; ENST00000243893.10, UBE2C-201, 476; ENST00000496085.1, UBE2C-207, 518"	MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP	chr20:45812576-45816957[+]	"Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit."	PDB: 1I7K; PDB: 4YII; PDB: 5A31; PDB: 5KHR; PDB: 5L9U	HGNC:15937	UBE2C_HUMAN	Reviewed	ENSG00000175063	.	.	.	.	.
Mol00692	Protein	Ubiquitin carboxyl-terminal hydrolase 14 (USP14)	Deubiquitinating enzyme 14; Ubiquitin thioesterase 14; Ubiquitin-specific-processing protease 14; TGT	USP14	9097	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261601.8, USP14-201, 4972; ENST00000582707.5, USP14-208, 1803; ENST00000383589.6, USP14-202, 2168; ENST00000400266.7, USP14-203, 1681; ENST00000581983.1, USP14-207, 503; ENST00000580410.5, USP14-206, 474; ENST00000583119.5, USP14-209, 578; ENST00000578942.5, USP14-205, 3189; ENST00000578786.1, USP14-204, 1104"	MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ	chr18:158383-214629[+]	Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation.	PDB: 2AYN; PDB: 2AYO; PDB: 5GJQ; PDB: 6IIK; PDB: 6IIL; PDB: 6IIM; PDB: 6IIN; PDB: 6LVS	HGNC:12612	UBP14_HUMAN	Reviewed	ENSG00000101557	.	.	.	.	.
Mol00693	Protein	Ubiquitin carboxyl-terminal hydrolase 22 (USP22)	Deubiquitinating enzyme 22; Ubiquitin thioesterase 22; Ubiquitin-specific-processing protease 22; KIAA1063; USP3L	USP22	23326	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261497.9, USP22-201, 5189; ENST00000537526.6, USP22-206, 4976; ENST00000476111.5, USP22-204, 573; ENST00000584538.1, USP22-211, 554; ENST00000582335.1, USP22-210, 306; ENST00000579645.5, USP22-209, 1906; ENST00000455117.6, USP22-202, 677; ENST00000577610.5, USP22-207, 564; ENST00000478443.1, USP22-205, 1071; ENST00000578446.1, USP22-208, 605; ENST00000463692.1, USP22-203, 355"	MVSRPEPEGEAMDAELAVAPPGCSHLGSFKVDNWKQNLRAIYQCFVWSGTAEARKRKAKSCICHVCGVHLNRLHSCLYCVFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCFLCQDYIYDKDMEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSEGNVVNGESHVSGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQFLEYE	chr17:20999596-21043760[-]	"Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression."	.	HGNC:12621	UBP22_HUMAN	Reviewed	ENSG00000124422	.	.	.	.	.
Mol00694	Protein	Mitochondrial uncoupling protein 2 (UCP2)	UCP 2; Solute carrier family 25 member 8; UCPH; SLC25A8	UCP2	7351	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000663595.2, UCP2-211, 1644; ENST00000310473.9, UCP2-201, 1675; ENST00000536983.5, UCP2-202, 1413; ENST00000539764.1, UCP2-204, 464; ENST00000545212.1, UCP2-209, 389; ENST00000542615.5, UCP2-206, 538; ENST00000541027.5, UCP2-205, 536; ENST00000544615.5, UCP2-208, 1004; ENST00000539330.1, UCP2-203, 608; ENST00000543714.5, UCP2-207, 567; ENST00000545562.2, UCP2-210, 344"	MVGFKATDVPPTATVKFLGAGTAACIADLITFPLDTAKVRLQIQGESQGPVRATASAQYRGVMGTILTMVRTEGPRSLYNGLVAGLQRQMSFASVRIGLYDSVKQFYTKGSEHASIGSRLLAGSTTGALAVAVAQPTDVVKVRFQAQARAGGGRRYQSTVNAYKTIAREEGFRGLWKGTSPNVARNAIVNCAELVTYDLIKDALLKANLMTDDLPCHFTSAFGAGFCTTVIASPVDVVKTRYMNSALGQYSSAGHCALTMLQKEGPRAFYKGFMPSFLRLGSWNVVMFVTYEQLKRALMAACTSREAPF	chr11:73974672-73982843[-]	"UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat."	.	HGNC:12518	UCP2_HUMAN	Reviewed	ENSG00000175567	.	.	.	.	.
Mol00695	Protein	Tyrosine-protein kinase UFO (AXL)	AXL oncogene; UFO	AXL	558	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000301178.9, AXL-201, 4717; ENST00000359092.7, AXL-202, 3206; ENST00000593513.1, AXL-203, 2557; ENST00000594880.1, AXL-204, 543; ENST00000599659.5, AXL-205, 1708"	MAWRCPRMGRVPLAWCLALCGWACMAPRGTQAEESPFVGNPGNITGARGLTGTLRCQLQVQGEPPEVHWLRDGQILELADSTQTQVPLGEDEQDDWIVVSQLRITSLQLSDTGQYQCLVFLGHQTFVSQPGYVGLEGLPYFLEEPEDRTVAANTPFNLSCQAQGPPEPVDLLWLQDAVPLATAPGHGPQRSLHVPGLNKTSSFSCEAHNAKGVTTSRTATITVLPQQPRNLHLVSRQPTELEVAWTPGLSGIYPLTHCTLQAVLSDDGMGIQAGEPDPPEEPLTSQASVPPHQLRLGSLHPHTPYHIRVACTSSQGPSSWTHWLPVETPEGVPLGPPENISATRNGSQAFVHWQEPRAPLQGTLLGYRLAYQGQDTPEVLMDIGLRQEVTLELQGDGSVSNLTVCVAAYTAAGDGPWSLPVPLEAWRPGQAQPVHQLVKEPSTPAFSWPWWYVLLGAVVAAACVLILALFLVHRRKKETRYGEVFEPTVERGELVVRYRVRKSYSRRTTEATLNSLGISEELKEKLRDVMVDRHKVALGKTLGEGEFGAVMEGQLNQDDSILKVAVKTMKIAICTRSELEDFLSEAVCMKEFDHPNVMRLIGVCFQGSERESFPAPVVILPFMKHGDLHSFLLYSRLGDQPVYLPTQMLVKFMADIASGMEYLSTKRFIHRDLAARNCMLNENMSVCVADFGLSKKIYNGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQPADCLDGLYALMSRCWELNPQDRPSFTELREDLENTLKALPPAQEPDEILYVNMDEGGGYPEPPGAAGGADPPTQPDPKDSCSCLTAAEVHPAGRYVLCPSTTPSPAQPADRGSPAAPGQEDGA	chr19:41219223-41261766[+]	"Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, AXL binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response."	PDB: 2C5D; PDB: 4RA0; PDB: 5U6B; PDB: 5VXZ	HGNC:905	UFO_HUMAN	Reviewed	ENSG00000167601	.	.	.	.	.
Mol00696	Protein	Serine/threonine-protein kinase ULK1 (ULK1)	Autophagy-related protein 1 homolog; ATG1; hATG1; Unc-51-like kinase 1; KIAA0722	ULK1	8408	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000321867.6, ULK1-201, 5322; ENST00000540568.1, ULK1-203, 2145; ENST00000544718.1, ULK1-207, 1678; ENST00000541761.2, ULK1-205, 1262; ENST00000540647.5, ULK1-204, 1211; ENST00000537421.5, ULK1-202, 959; ENST00000542313.2, ULK1-206, 307"	MEPGRGGTETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAMRTLSEDTIRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPNSIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPTIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASPSVRKSPPVPVPSYPSSGSGSSSSSSSTSHLASPPSLGEMQQLQKTLASPADTAGFLHSSRDSGGSKDSSCDTDDFVMVPAQFPGDLVAEAPSAKPPPDSLMCSGSSLVASAGLESHGRTPSPSPPCSSSPSPSGRAGPFSSSRCGASVPIPVPTQVQNYQRIERNLQSPTQFQTPRSSAIRRSGSTSPLGFARASPSPPAHAEHGGVLARKMSLGGGRPYTPSPQVGTIPERPGWSGTPSPQGAEMRGGRSPRPGSSAPEHSPRTSGLGCRLHSAPNLSDLHVVRPKLPKPPTDPLGAVFSPPQASPPQPSHGLQSCRNLRGSPKLPDFLQRNPLPPILGSPTKAVPSFDFPKTPSSQNLLALLARQGVVMTPPRNRTLPDLSEVGPFHGQPLGPGLRPGEDPKGPFGRSFSTSRLTDLLLKAAFGTQAPDPGSTESLQEKPMEIAPSAGFGGSLHPGARAGGTSSPSPVVFTVGSPPSGSTPPQGPRTRMFSAGPTGSASSSARHLVPGPCSEAPAPELPAPGHGCSFADPITANLEGAVTFEAPDLPEETLMEQEHTEILRGLRFTLLFVQHVLEIAALKGSASEAAGGPEYQLQESVVADQISLLSREWGFAEQLVLYLKVAELLSSGLQSAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDRIHSITAERLIFSHAVQMVQSAALDEMFQHREGCVPRYHKALLLLEGLQHMLSDQADIENVTKCKLCIERRLSALLTGICA	chr12:131894622-131923150[+]	"Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation. May also phosphorylate SESN2 and SQSTM1 to regulate autophagy. Phosphorylates FLCN, promoting autophagy. Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation. Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B."	PDB: 4WNO; PDB: 4WNP; PDB: 5CI7; PDB: 6HYO; PDB: 6MNH; PDB: 6QAS	HGNC:12558	ULK1_HUMAN	Reviewed	ENSG00000177169	.	.	.	.	.
Mol00697	Protein	Urokinase-type plasminogen activator (PLAU)	U-plasminogen activator; uPA	PLAU	5328	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000372764.4, PLAU-201, 2343; ENST00000446342.5, PLAU-202, 2658; ENST00000481390.5, PLAU-203, 468; ENST00000494287.1, PLAU-204, 750; ENST00000496926.1, PLAU-205, 160"	MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKLLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL	chr10:73909177-73917496[+]	Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.	PDB: 1C5W; PDB: 1C5X; PDB: 1C5Y; PDB: 1C5Z; PDB: 1EJN; PDB: 1F5K; PDB: 1F5L; PDB: 1F92; PDB: 1FV9; PDB: 1GI7; PDB: 1GI8; PDB: 1GI9; PDB: 1GJ7; PDB: 1GJ8; PDB: 1GJ9; PDB: 1GJA; PDB: 1GJB; PDB: 1GJC; PDB: 1GJD; PDB: 1KDU; PDB: 1LMW; PDB: 1O3P; PDB: 1O5A; PDB: 1O5B; PDB: 1O5C; PDB: 1OWD; PDB: 1OWE; PDB: 1OWH; PDB: 1OWI; PDB: 1OWJ; PDB: 1OWK; PDB: 1SC8; PDB: 1SQA; PDB: 1SQO; PDB: 1SQT; PDB: 1U6Q; PDB: 1URK; PDB: 1VJ9; PDB: 1VJA; PDB: 1W0Z; PDB: 1W10; PDB: 1W11; PDB: 1W12; PDB: 1W13; PDB: 1W14; PDB: 2FD6; PDB: 2I9A; PDB: 2I9B; PDB: 2NWN; PDB: 2O8T; PDB: 2O8U; PDB: 2O8W; PDB: 2R2W; PDB: 2VIN; PDB: 2VIO; PDB: 2VIP; PDB: 2VIQ; PDB: 2VIV; PDB: 2VIW; PDB: 2VNT; PDB: 3BT1; PDB: 3BT2; PDB: 3IG6; PDB: 3KGP; PDB: 3KHV; PDB: 3KID; PDB: 3M61; PDB: 3MHW; PDB: 3MWI; PDB: 3OX7; PDB: 3OY5; PDB: 3OY6; PDB: 3PB1; PDB: 3QN7; PDB: 3U73; PDB: 4DVA; PDB: 4DW2; PDB: 4FU7; PDB: 4FU8; PDB: 4FU9; PDB: 4FUB; PDB: 4FUC; PDB: 4FUD; PDB: 4FUE; PDB: 4FUF; PDB: 4FUG; PDB: 4FUH; PDB: 4FUI; PDB: 4FUJ; PDB: 4GLY; PDB: 4H42; PDB: 4JK5; PDB: 4JK6; PDB: 4K24; PDB: 4MNV; PDB: 4MNW; PDB: 4MNX; PDB: 4MNY; PDB: 4OS1; PDB: 4OS2; PDB: 4OS4; PDB: 4OS5; PDB: 4OS6; PDB: 4OS7; PDB: 4X0W; PDB: 4X1N; PDB: 4X1P; PDB: 4X1Q; PDB: 4X1R; PDB: 4X1S; PDB: 4XSK; PDB: 4ZHL; PDB: 4ZHM; PDB: 4ZKN; PDB: 4ZKO; PDB: 4ZKR; PDB: 4ZKS; PDB: 5HGG; PDB: 5WXF; PDB: 5WXO; PDB: 5WXP; PDB: 5WXQ; PDB: 5WXR; PDB: 5WXS; PDB: 5WXT; PDB: 5XG4; PDB: 5YC6; PDB: 5YC7; PDB: 5Z1C; PDB: 5ZA7; PDB: 5ZA8; PDB: 5ZA9; PDB: 5ZAE; PDB: 5ZAF; PDB: 5ZAG; PDB: 5ZAH; PDB: 5ZAJ; PDB: 5ZC5; PDB: 6AG2; PDB: 6AG3; PDB: 6AG7; PDB: 6AG9; PDB: 6JYP; PDB: 6JYQ; PDB: 6L04; PDB: 6L05; PDB: 6NMB; PDB: 6XVD; PDB: 7DZD	HGNC:9052	UROK_HUMAN	Reviewed	ENSG00000122861	.	.	.	.	.
Mol00698	Protein	Vitamin D3 receptor (VDR)	VDR; 1;25-dihydroxyvitamin D3 receptor; Nuclear receptor subfamily 1 group I member 1; NR1I1	VDR	7421	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000549336.6, VDR-206, 4616; ENST00000395324.6, VDR-202, 4762; ENST00000550325.5, VDR-208, 3925; ENST00000229022.9, VDR-201, 3404; ENST00000546653.5, VDR-203, 937; ENST00000548664.1, VDR-205, 596; ENST00000550314.5, VDR-207, 562; ENST00000547065.1, VDR-204, 1782"	MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS	chr12:47841537-47943048[-]	"Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes. Plays a central role in calcium homeostasis."	PDB: 1DB1; PDB: 1IE8; PDB: 1IE9; PDB: 1KB2; PDB: 1KB4; PDB: 1KB6; PDB: 1S0Z; PDB: 1S19; PDB: 1TXI; PDB: 1YNW; PDB: 2HAM; PDB: 2HAR; PDB: 2HAS; PDB: 2HB7; PDB: 2HB8; PDB: 3A2I; PDB: 3A2J; PDB: 3A3Z; PDB: 3A40; PDB: 3A78; PDB: 3AUQ; PDB: 3AUR; PDB: 3AX8; PDB: 3AZ1; PDB: 3AZ2; PDB: 3AZ3; PDB: 3B0T; PDB: 3CS4; PDB: 3CS6; PDB: 3KPZ; PDB: 3M7R; PDB: 3OGT; PDB: 3P8X; PDB: 3TKC; PDB: 3VHW; PDB: 3W0A; PDB: 3W0C; PDB: 3W0Y; PDB: 3WGP; PDB: 3WWR; PDB: 3X31; PDB: 3X36; PDB: 4G2I; PDB: 4ITE; PDB: 4ITF; PDB: 5GT4; PDB: 5V39; PDB: 5YSY; PDB: 5YT2	HGNC:12679	VDR_HUMAN	Reviewed	ENSG00000111424	.	.	.	.	.
Mol00699	Protein	Vascular endothelial growth factor C (VEGFC)	VEGF-C; Flt4 ligand; Flt4-L; Vascular endothelial growth factor-related protein; VRP	VEGFC	7424	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000618562.2, VEGFC-202, 2259; ENST00000507638.1, VEGFC-201, 759"	MHLLGFFSVACSLLAAALLPGPREAPAAAAAFESGLDLSDAEPDAGEATAYASKDLEEQLRSVSSVDELMTVLYPEYWKMYKCQLRKGGWQHNREQANLNSRTEETIKFAAAHYNTEILKSIDNEWRKTQCMPREVCIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGLQCMNTSTSYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLDVYRQVHSIIRRSLPATLPQCQAANKTCPTNYMWNNHICRCLAQEDFMFSSDAGDDSTDGFHDICGPNKELDEETCQCVCRAGLRPASCGPHKELDRNSCQCVCKNKLFPSQCGANREFDENTCQCVCKRTCPRNQPLNPGKCACECTESPQKCLLKGKKFHHQTCSCYRRPCTNRQKACEPGFSYSEEVCRCVPSYWKRPQMS	chr4:176683538-176792922[-]	"Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors."	PDB: 2X1W; PDB: 2X1X; PDB: 4BSK; PDB: 6TJT	HGNC:12682	VEGFC_HUMAN	Reviewed	ENSG00000150630	.	.	.	.	.
Mol00700	Protein	Vimentin (VIM)	.	VIM	7431	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000544301.7, VIM-209, 2154; ENST00000224237.9, VIM-201, 1868; ENST00000478746.1, VIM-204, 757; ENST00000497849.1, VIM-208, 634; ENST00000469543.5, VIM-203, 2666; ENST00000487938.5, VIM-206, 2272; ENST00000485947.1, VIM-205, 1139; ENST00000637053.1, VIM-210, 508; ENST00000495528.1, VIM-207, 962; ENST00000421459.2, VIM-202, 753"	MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE	chr10:17228241-17237593[+]	"Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally."	PDB: 1GK4; PDB: 1GK6; PDB: 1GK7; PDB: 3G1E; PDB: 3KLT; PDB: 3S4R; PDB: 3SSU; PDB: 3SWK; PDB: 3TRT; PDB: 3UF1; PDB: 4MCY; PDB: 4MCZ; PDB: 4MD0; PDB: 4MD5; PDB: 4MDI; PDB: 4MDJ; PDB: 4YPC; PDB: 4YV3; PDB: 5WHF; PDB: 6ATF; PDB: 6ATI; PDB: 6BIR; PDB: 6YXK	HGNC:12692	VIME_HUMAN	Reviewed	ENSG00000026025	.	.	.	.	.
Mol00701	Protein	Wee1-like protein kinase (WEE1)	WEE1hu; Wee1A kinase	WEE1	7465	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000450114.7, WEE1-202, 3588; ENST00000299613.10, WEE1-201, 3436; ENST00000681684.1, WEE1-210, 2777; ENST00000530712.6, WEE1-207, 2488; ENST00000524612.5, WEE1-204, 573; ENST00000527848.1, WEE1-205, 465; ENST00000680141.1, WEE1-209, 3687; ENST00000530175.5, WEE1-206, 838; ENST00000524549.1, WEE1-203, 5187; ENST00000532275.1, WEE1-208, 582"	MSFLSRQQPPPPRRAGAACTLRQKLIFSPCSDCEEEEEEEEEEGSGHSTGEDSAFQEPDSPLPPARSPTEPGPERRRSPGPAPGSPGELEEDLLLPGACPGADEAGGGAEGDSWEEEGFGSSSPVKSPAAPYFLGSSFSPVRCGGPGDASPRGCGARRAGEGRRSPRPDHPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIDSSSVKLRGSSLFMDTEKSGKREFDVRQTPQVNINPFTPDSLLLHSSGQCRRRKRTYWNDSCGEDMEASDYELEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAKAAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVSLTIY	chr11:9573670-9593457[+]	"Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation."	PDB: 1X8B; PDB: 2IN6; PDB: 2IO6; PDB: 2Z2W; PDB: 3BI6; PDB: 3BIZ; PDB: 3CQE; PDB: 3CR0; PDB: 5V5Y; PDB: 5VC3; PDB: 5VC4; PDB: 5VC5; PDB: 5VC6; PDB: 5VD2; PDB: 5VD4; PDB: 5VD5; PDB: 5VD7; PDB: 5VD8; PDB: 5VD9; PDB: 5VDA; PDB: 7N3U	HGNC:12761	WEE1_HUMAN	Reviewed	ENSG00000166483	.	.	.	.	.
Mol00702	Protein	Wnt inhibitory factor 1 (WIF1)	WIF-1; UNQ191/PRO217	WIF1	11197	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000286574.9, WIF1-201, 1977; ENST00000546001.1, WIF1-203, 568; ENST00000543094.1, WIF1-202, 429"	MARRSAFPAAALWLWSILLCLLALRAEAGPPQEESLYLWIDAHQARVLIGFEEDILIVSEGKMAPFTHDFRKAQQRMPAIPVNIHSMNFTWQAAGQAEYFYEFLSLRSLDKGIMADPTVNVPLLGTVPHKASVVQVGFPCLGKQDGVAAFEVDVIVMNSEGNTILQTPQNAIFFKTCQQAECPGGCRNGGFCNERRICECPDGFHGPHCEKALCTPRCMNGGLCVTPGFCICPPGFYGVNCDKANCSTTCFNGGTCFYPGKCICPPGLEGEQCEISKCPQPCRNGGKCIGKSKCKCSKGYQGDLCSKPVCEPGCGAHGTCHEPNKCQCQEGWHGRHCNKRYEASLIHALRPAGAQLRQHTPSLKKAEERRDPPESNYIW	chr12:65050626-65121305[-]	Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation.	PDB: 2D3J; PDB: 2YGN; PDB: 2YGO; PDB: 2YGP; PDB: 2YGQ	HGNC:18081	WIF1_HUMAN	Reviewed	ENSG00000156076	.	.	.	.	.
Mol00703	Protein	Protein wntless homolog (WLS)	Integral membrane protein GPR177; Protein evenness interrupted homolog; EVI; Putative NF-kappa-B-activating protein 373; C1orf139; GPR177; UNQ85/PRO18667	WLS	79971	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262348.9, WLS-201, 2716; ENST00000370976.7, WLS-205, 2332; ENST00000354777.6, WLS-202, 2037; ENST00000530486.5, WLS-212, 1056; ENST00000370971.1, WLS-203, 700; ENST00000534713.5, WLS-214, 600; ENST00000370973.2, WLS-204, 572; ENST00000471243.2, WLS-206, 555; ENST00000533537.5, WLS-213, 524; ENST00000491076.1, WLS-207, 779; ENST00000527864.1, WLS-211, 570; ENST00000491811.5, WLS-208, 1041; ENST00000497187.5, WLS-209, 747; ENST00000498615.1, WLS-210, 745"	MAGAIIENMSTKKLCIVGGILLVFQIIAFLVGGLIAPGPTTAVSYMSVKCVDARKNHHKTKWFVPWGPNHCDKIRDIEEAIPREIEANDIVFSVHIPLPHMEMSPWFQFMLFILQLDIAFKLNNQIRENAEVSMDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLEKVIFALGISMTFINIPVEWFSIGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHMMDQHERNHIAGYWKQVGPIAVGSFCLFIFDMCERGVQLTNPFYSIWTTDIGTELAMAFIIVAGICLCLYFLFLCFMVFQVFRNISGKQSSLPAMSKVRRLHYEGLIFRFKFLMLITLACAAMTVIFFIVSQVTEGHWKWGGVTVQVNSAFFTGIYGMWNLYVFALMFLYAPSHKNYGEDQSNGDLGVHSGEELQLTTTITHVDGPTEIYKLTRKEAQE	chr1:68098473-68233120[-]	"Regulates Wnt proteins sorting and secretion in a feedback regulatory mechanism. This reciprocal interaction plays a key role in the regulation of expression, subcellular location, binding and organelle-specific association of Wnt proteins. Plays also an important role in establishment of the anterior-posterior body axis formation during development (By similarity)."	PDB: 7DRT; PDB: 7KC4	HGNC:30238	WLS_HUMAN	Reviewed	ENSG00000116729	.	.	.	.	.
Mol00704	Protein	Protein Wnt-10b (WNT10B)	Protein Wnt-12; WNT12	WNT10B	7480	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000301061.9, WNT10B-201, 2246; ENST00000403957.5, WNT10B-202, 1817; ENST00000407467.5, WNT10B-203, 1802; ENST00000413630.1, WNT10B-204, 623; ENST00000420388.1, WNT10B-205, 559; ENST00000475740.1, WNT10B-206, 429"	MLEEPRPRPPPSGLAGLLFLALCSRALSNEILGLKLPGEPPLTANTVCLTLSGLSKRQLGLCLRNPDVTASALQGLHIAVHECQHQLRDQRWNCSALEGGGRLPHHSAILKRGFRESAFSFSMLAAGVMHAVATACSLGKLVSCGCGWKGSGEQDRLRAKLLQLQALSRGKSFPHSLPSPGPGSSPSPGPQDTWEWGGCNHDMDFGEKFSRDFLDSREAPRDIQARMRIHNNRVGRQVVTENLKRKCKCHGTSGSCQFKTCWRAAPEFRAVGAALRERLGRAIFIDTHNRNSGAFQPRLRPRRLSGELVYFEKSPDFCERDPTMGSPGTRGRACNKTSRLLDGCGSLCCGRGHNVLRQTRVERCHCRFHWCCYVLCDECKVTEWVNVCK	chr12:48965340-48971735[-]	"Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Acts in the immune system, mammary gland, adipose tissue, bone and skin."	.	HGNC:12775	WN10B_HUMAN	Reviewed	ENSG00000169884	.	.	.	.	.
Mol00705	Protein	Int-1-related protein (WNT2)	Int-1-like protein 1; Int-1-related protein; IRP; INT1L1; IRP	WNT2	7472	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265441.8, WNT2-201, 3856; ENST00000491214.1, WNT2-204, 513; ENST00000647844.1, WNT2-205, 4205; ENST00000449446.5, WNT2-202, 1768; ENST00000461427.1, WNT2-203, 571"	MNAPLGGIWLWLPLLLTWLTPEVNSSWWYMRATGGSSRVMCDNVPGLVSSQRQLCHRHPDVMRAISQGVAEWTAECQHQFRQHRWNCNTLDRDHSLFGRVLLRSSRESAFVYAISSAGVVFAITRACSQGEVKSCSCDPKKMGSAKDSKGIFDWGGCSDNIDYGIKFARAFVDAKERKGKDARALMNLHNNRAGRKAVKRFLKQECKCHGVSGSCTLRTCWLAMADFRKTGDYLWRKYNGAIQVVMNQDGTGFTVANERFKKPTKNDLVYFENSPDYCIRDREAGSLGTAGRVCNLTSRGMDSCEVMCCGRGYDTSHVTRMTKCGCKFHWCCAVRCQDCLEALDVHTCKAPKNADWTTAT	chr7:117275451-117323152[-]	Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons.	.	HGNC:12780	WNT2_HUMAN	Reviewed	ENSG00000105989	.	.	.	.	.
Mol00706	Protein	Protein Wnt-5a (WNT5A)	.	WNT5A	7474	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264634.9, WNT5A-201, 5841; ENST00000474267.5, WNT5A-202, 6042; ENST00000497027.5, WNT5A-205, 1299; ENST00000482079.1, WNT5A-203, 959; ENST00000493406.1, WNT5A-204, 521; ENST00000624674.1, WNT5A-207, 493; ENST00000497817.1, WNT5A-206, 661"	MKKSIGILSPGVALGMAGSAMSSKFFLVALAIFFSFAQVVIEANSWWSLGMNNPVQMSEVYIIGAQPLCSQLAGLSQGQKKLCHLYQDHMQYIGEGAKTGIKECQYQFRHRRWNCSTVDNTSVFGRVMQIGSRETAFTYAVSAAGVVNAMSRACREGELSTCGCSRAARPKDLPRDWLWGGCGDNIDYGYRFAKEFVDARERERIHAKGSYESARILMNLHNNEAGRRTVYNLADVACKCHGVSGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMRLNSRGKLVQVNSRFNSPTTQDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQTERCHCKFHWCCYVKCKKCTEIVDQFVCK	chr3:55465715-55490539[-]	"Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression. Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells. Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes."	.	HGNC:12784	WNT5A_HUMAN	Reviewed	ENSG00000114251	.	.	.	.	.
Mol00707	Protein	Protein Wnt-6 (WNT6)	.	WNT6	7475	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000233948.4, WNT6-201, 1719; ENST00000486233.1, WNT6-202, 408"	MLPPLPSRLGLLLLLLLCPAHVGGLWWAVGSPLVMDPTSICRKARRLAGRQAELCQAEPEVVAELARGARLGVRECQFQFRFRRWNCSSHSKAFGRILQQDIRETAFVFAITAAGASHAVTQACSMGELLQCGCQAPRGRAPPRPSGLPGTPGPPGPAGSPEGSAAWEWGGCGDDVDFGDEKSRLFMDARHKRGRGDIRALVQLHNNEAGRLAVRSHTRTECKCHGLSGSCALRTCWQKLPPFREVGARLLERFHGASRVMGTNDGKALLPAVRTLKPPGRADLLYAADSPDFCAPNRRTGSPGTRGRACNSSAPDLSGCDLLCCGRGHRQESVQLEENCLCRFHWCCVVQCHRCRVRKELSLCL	chr2:218859805-218874233[+]	Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. Together with CAV1 may promote chemoresistance of gastric cancer cells to DNA-damaging anthracycline drugs through the activation of the canonical Wnt receptor signaling pathway.	.	HGNC:12785	WNT6_HUMAN	Reviewed	ENSG00000115596	.	.	.	.	.
Mol00708	LncRNA	WT1 antisense RNA (WT1-AS)	WIT-1; WIT11; WT1AS; WT1-AS	WT1-AS	51352	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000702558.1,WT1-AS-212,1357; ENST00000691801.1,WT1-AS-211,542; ENST00000690579.1,WT1-AS-210,931; ENST00000687964.1,WT1-AS-209,460; ENST00000687495.1,WT1-AS-208,618; ENST00000686872.1,WT1-AS-207,1254; ENST00000525436.1,WT1-AS-206,1254; ENST00000494911.5,WT1-AS-205,1320; ENST00000478367.5,WT1-AS-204,561; ENST00000459866.1,WT1-AS-203,328; ENST00000442957.1,WT1-AS-202,482; ENST00000395900.1,WT1-AS-201,3828"	.	"chr11:32,435,518-32,500,632[+]"	.	.	HGNC:18135	.	.	ENSG00000183242	.	.	.	.	.
Mol00709	Protein	Cystine/glutamate transporter (SLC7A11)	Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT	SLC7A11	23657	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000280612.9, SLC7A11-201, 9645; ENST00000509248.1, SLC7A11-202, 797"	MVRKPVVSTISKGGYLQGNVNGRLPSLGNKEPPGQEKVQLKRKVTLLRGVSIIIGTIIGAGIFISPKGVLQNTGSVGMSLTIWTVCGVLSLFGALSYAELGTTIKKSGGHYTYILEVFGPLPAFVRVWVELLIIRPAATAVISLAFGRYILEPFFIQCEIPELAIKLITAVGITVVMVLNSMSVSWSARIQIFLTFCKLTAILIIIVPGVMQLIKGQTQNFKDAFSGRDSSITRLPLAFYYGMYAYAGWFYLNFVTEEVENPEKTIPLAICISMAIVTIGYVLTNVAYFTTINAEELLLSNAVAVTFSERLLGNFSLAVPIFVALSCFGSMNGGVFAVSRLFYVASREGHLPEILSMIHVRKHTPLPAVIVLHPLTMIMLFSGDLDSLLNFLSFARWLFIGLAVAGLIYLRYKCPDMHRPFKVPLFIPALFSFTCLFMVALSLYSDPFSTGIGFVITLTGVPAYYLFIIWDKKPRWFRIMSEKITRTLQIILEVVPEEDKL	chr4:138164097-138242349[-]	"Sodium-independent, high-affinity exchange of anionic amino acids with high specificity for anionic form of cystine and glutamate."	PDB: 7CCS	HGNC:11059	XCT_HUMAN	Reviewed	ENSG00000151012	.	.	.	.	.
Mol00710	Protein	DNA repair endonuclease XPF (ERCC4)	DNA excision repair protein ERCC-4; DNA repair protein complementing XP-F cells; Xeroderma pigmentosum group F-complementing protein; ERCC11; XPF	ERCC4	2072	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000311895.8, ERCC4-201, 6764; ENST00000682617.1, ERCC4-211, 6918; ENST00000575156.5, ERCC4-207, 2073; ENST00000682826.1, ERCC4-212, 4351; ENST00000683962.1, ERCC4-216, 3925; ENST00000462862.1, ERCC4-203, 721; ENST00000574194.1, ERCC4-205, 583; ENST00000682568.1, ERCC4-210, 2161; ENST00000574781.1, ERCC4-206, 638; ENST00000682909.1, ERCC4-213, 6447; ENST00000683277.1, ERCC4-214, 5930; ENST00000683407.1, ERCC4-215, 2803; ENST00000389138.7, ERCC4-202, 2106; ENST00000682552.1, ERCC4-209, 1254; ENST00000576348.1, ERCC4-208, 604; ENST00000573018.1, ERCC4-204, 523"	MESGQPARRIAMAPLLEYERQLVLELLDTDGLVVCARGLGADRLLYHFLQLHCHPACLVLVLNTQPAEEEYFINQLKIEGVEHLPRRVTNEITSNSRYEVYTQGGVIFATSRILVVDFLTDRIPSDLITGILVYRAHRIIESCQEAFILRLFRQKNKRGFIKAFTDNAVAFDTGFCHVERVMRNLFVRKLYLWPRFHVAVNSFLEQHKPEVVEIHVSMTPTMLAIQTAILDILNACLKELKCHNPSLEVEDLSLENAIGKPFDKTIRHYLDPLWHQLGAKTKSLVQDLKILRTLLQYLSQYDCVTFLNLLESLRATEKAFGQNSGWLFLDSSTSMFINARARVYHLPDAKMSKKEKISEKMEIKEGEETKKELVLESNPKWEALTEVLKEIEAENKESEALGGPGQVLICASDDRTCSQLRDYITLGAEAFLLRLYRKTFEKDSKAEEVWMKFRKEDSSKRIRKSHKRPKDPQNKERASTKERTLKKKKRKLTLTQMVGKPEELEEEGDVEEGYRREISSSPESCPEEIKHEEFDVNLSSDAAFGILKEPLTIIHPLLGCSDPYALTRVLHEVEPRYVVLYDAELTFVRQLEIYRASRPGKPLRVYFLIYGGSTEEQRYLTALRKEKEAFEKLIREKASMVVPEEREGRDETNLDLVRGTASADVSTDTRKAGGQEQNGTQQSIVVDMREFRSELPSLIHRRGIDIEPVTLEVGDYILTPEMCVERKSISDLIGSLNNGRLYSQCISMSRYYKRPVLLIEFDPSKPFSLTSRGALFQEISSNDISSKLTLLTLHFPRLRILWCPSPHATAELFEELKQSKPQPDAATALAITADSETLPESEKYNPGPQDFLLKMPGVNAKNCRSLMHHVKNIAELAALSQDELTSILGNAANAKQLYDFIHTSFAEVVSKGKGKK	chr16:13920138-13952348[+]	"Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair, and which is essential for nucleotide excision repair (NER) and interstrand cross-link (ICL) repair."	PDB: 1Z00; PDB: 2A1J; PDB: 2AQ0; PDB: 2KN7; PDB: 2MUT; PDB: 6SXA; PDB: 6SXB	HGNC:3436	XPF_HUMAN	Reviewed	ENSG00000175595	.	.	.	.	.
Mol00711	Protein	DNA repair protein XRCC3 (XRCC3)	X-ray repair cross-complementing protein 3	XRCC3	7517	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000555055.6, XRCC3-211, 2567; ENST00000553264.5, XRCC3-202, 3018; ENST00000352127.11, XRCC3-201, 2563; ENST00000554913.5, XRCC3-209, 2539; ENST00000556980.5, XRCC3-217, 801; ENST00000553361.5, XRCC3-204, 746; ENST00000554974.5, XRCC3-210, 575; ENST00000554170.1, XRCC3-206, 572; ENST00000555964.5, XRCC3-215, 562; ENST00000553332.5, XRCC3-203, 560; ENST00000556682.5, XRCC3-216, 535; ENST00000557439.5, XRCC3-218, 2599; ENST00000555832.1, XRCC3-214, 632; ENST00000555451.1, XRCC3-213, 409; ENST00000554811.5, XRCC3-208, 3668; ENST00000555231.5, XRCC3-212, 582; ENST00000553807.1, XRCC3-205, 568; ENST00000554774.1, XRCC3-207, 510"	MDLDLLDLNPRIIAAIKKAKLKSVKEVLHFSGPDLKRLTNLSSPEVWHLLRTASLHLRGSSILTALQLHQQKERFPTQHQRLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQFPRQHGGLEAGAVYICTEDAFPHKRLQQLMAQQPRLRTDVPGELLQKLRFGSQIFIEHVADVDTLLECVNKKVPVLLSRGMARLVVIDSVAAPFRCEFDSQASAPRARHLQSLGATLRELSSAFQSPVLCINQVTEAMEEQGAAHGPLGFWDERVSPALGITWANQLLVRLLADRLREEEAALGCPARTLRVLSAPHLPPSSCSYTISAEGVRGTPGTQSH	chr14:103697609-103715504[-]	"Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD21 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C."	.	HGNC:12830	XRCC3_HUMAN	Reviewed	ENSG00000126215	.	.	.	.	.
Mol00712	Protein	DNA repair protein XRCC4 (XRCC4)	hXRCC4; X-ray repair cross-complementing protein 4; XRCC4/C	XRCC4	7518	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000396027.9, XRCC4-203, 1602; ENST00000282268.7, XRCC4-201, 1696; ENST00000511817.1, XRCC4-205, 1636; ENST00000338635.10, XRCC4-202, 1579; ENST00000509268.1, XRCC4-204, 1567; ENST00000542685.5, XRCC4-206, 1243"	MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKENSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI	chr5:83077498-83353787[+]	"[DNA repair protein XRCC4]: DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination. Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors. Plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed. XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity. Binding of the LIG4-XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. Promotes displacement of PNKP from processed strand break termini."	PDB: 1FU1; PDB: 1IK9; PDB: 3II6; PDB: 3MUD; PDB: 3Q4F; PDB: 3RWR; PDB: 3SR2; PDB: 3W03; PDB: 4XA4; PDB: 5CHX; PDB: 5CJ0; PDB: 5CJ4; PDB: 5E50; PDB: 5WJ7; PDB: 5WLZ; PDB: 6ABO; PDB: 7LSY; PDB: 7LT3; PDB: 7M3P; PDB: 7NFC; PDB: 7NFE	HGNC:12831	XRCC4_HUMAN	Reviewed	ENSG00000152422	.	.	.	.	.
Mol00713	Protein	Y-box-binding protein 1 (YBX1)	YB-1; CCAAT-binding transcription factor I subunit A; CBF-A; DNA-binding protein B; DBPB; Enhancer factor I subunit A; EFI-A; Nuclease-sensitive element-binding protein 1; Y-box transcription factor; NSEP1; YB1	YBX1	4904	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000321358.12, YBX1-201, 2979; ENST00000436427.1, YBX1-203, 1524; ENST00000332220.10, YBX1-202, 776; ENST00000467957.1, YBX1-204, 770"	MSSEAETQQPPAAPPAAPALSAADTKPGTTGSGAGSGGPGGLTSAAPAGGDKKVIATKVLGTVKWFNVRNGYGFINRNDTKEDVFVHQTAIKKNNPRKYLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVQGSKYAADRNHYRRYPRRRGPPRNYQQNYQNSESGEKNEGSESAPEGQAQQRRPYRRRRFPPYYMRRPYGRRPQYSNPPVQGEVMEGADNQGAGEQGRPVRQNMYRGYRPRFRRGPPRQRQPREDGNEEDKENQGDETQGQQPPQRRYRRNFNYRRRRPENPKPQDGKETKAADPPAENSSAPEAEQGGAE	chr1:42682418-42703805[+]	"DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing, DNA repair and transcription regulation. Predominantly acts as a RNA-binding protein: binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting the mRNA stability maintainer ELAVL1, thereby preventing mRNA decay. Component of the CRD-mediated complex that promotes MYC mRNA stability. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors. Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs. Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs. Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs. Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection. Also able to bind DNA: regulates transcription of the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair. The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation."	PDB: 1H95; PDB: 5YTS; PDB: 5YTT; PDB: 5YTV; PDB: 5YTX; PDB: 6A6L; PDB: 6KTC; PDB: 6KUG; PDB: 6LMR; PDB: 6LMS	HGNC:8014	YBOX1_HUMAN	Reviewed	ENSG00000065978	.	.	.	.	.
Mol00714	Protein	Tyrosine-protein kinase Yes (YES1)	Proto-oncogene c-Yes; p61-Yes; YES	YES1	7525	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000314574.5, YES1-201, 4605; ENST00000584307.5, YES1-205, 4639; ENST00000577961.5, YES1-203, 4554; ENST00000577611.1, YES1-202, 568; ENST00000581960.1, YES1-204, 487"	MGCIKSKENKSPAIKYRPENTPEPVSTSVSHYGAEPTTVSPCPSSSAKGTAVNFSSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPAGLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQPGENL	chr18:721588-812546[-]	"Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis."	PDB: 2HDA	HGNC:12841	YES_HUMAN	Reviewed	ENSG00000176105	.	.	.	.	.
Mol00715	Protein	YEATS domain-containing protein 4 (YEATS4)	Glioma-amplified sequence 41; Gas41; NuMA-binding protein 1; NuBI-1; NuBI1; GAS41	YEATS4	8089	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000247843.7, YEATS4-201, 1468; ENST00000548020.5, YEATS4-202, 1100; ENST00000549685.5, YEATS4-203, 884; ENST00000552955.1, YEATS4-205, 827; ENST00000552949.1, YEATS4-204, 428"	MFKRMAEFGPDSGGRVKGVTIVKPIVYGNVARYFGKKREEDGHTHQWTVYVKPYRNEDMSAYVKKIQFKLHESYGNPLRVVTKPPYEITETGWGEFEIIIKIFFIDPNERPVTLYHLLKLFQSDTNAMLGKKTVVSEFYDEMIFQDPTAMMQQLLTTSRQLTLGAYKHETEFAELEVKTREKLEAAKKKTSFEIAELKERLKASRETINCLKNEIRKLEEDDQAKDI	chr12:69359710-69390870[+]	"Chromatin reader component of the NuA4 histone acetyltransferase (HAT) complex, a complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. Specifically recognizes and binds acylated histone H3, with a preference for histone H3 diacetylated at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac). Also able to recognize and bind crotonylated histone H3. May also recognize and bind histone H3 succinylated at 'Lys-122' (H3K122succ); additional evidences are however required to confirm this result in vivo. Plays a key role in histone variant H2AZ1/H2A.Z deposition into specific chromatin regions: recognizes and binds H3K14ac and H3K27ac on the promoters of actively transcribed genes and recruits NuA4-related complex to deposit H2AZ1/H2A.Z. H2AZ1/H2A.Z deposition is required for maintenance of embryonic stem cell."	PDB: 5R68; PDB: 5R69; PDB: 5VNA; PDB: 5VNB; PDB: 5XTZ; PDB: 5Y8V; PDB: 7JFY	HGNC:24859	YETS4_HUMAN	Reviewed	ENSG00000127337	.	.	.	.	.
Mol00716	Protein	Zinc finger and BTB domain-containing protein 7A (ZBTB7A)	Factor binding IST protein 1; FBI-1; Factor that binds to inducer of short transcripts protein 1; HIV-1 1st-binding protein 1; Leukemia/lymphoma-related factor; POZ and Krueppel erythroid myeloid ontogenic factor; POK erythroid myeloid ontogenic factor; Pokemon; Pokemon 1; TTF-I-interacting peptide 21; TIP21; Zinc finger protein 857A; FBI1; LRF; ZBTB7; ZNF857A	ZBTB7A	51341	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000322357.9, ZBTB7A-201, 6437; ENST00000601588.1, ZBTB7A-202, 2083"	MAGGVDGPIGIPFPDHSSDILSGLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEIDFVSAEALTALMDFAYTATLTVSTANVGDILSAARLLEIPAVSHVCADLLDRQILAADAGADAGQLDLVDQIDQRNLLRAKEYLEFFQSNPMNSLPPAAAAAAASFPWSAFGASDDDLDATKEAVAAAVAAVAAGDCNGLDFYGPGPPAERPPTGDGDEGDSNPGLWPERDEDAPTGGLFPPPVAPPAATQNGHYGRGGEEEAASLSEAAPEPGDSPGFLSGAAEGEDGDGPDVDGLAASTLLQQMMSSVGRAGAAAGDSDEESRADDKGVMDYYLKYFSGAHDGDVYPAWSQKVEKKIRAKAFQKCPICEKVIQGAGKLPRHIRTHTGEKPYECNICKVRFTRQDKLKVHMRKHTGEKPYLCQQCGAAFAHNYDLKNHMRVHTGLRPYQCDSCCKTFVRSDHLHRHLKKDGCNGVPSRRGRKPRVRGGAPDPSPGATATPGAPAQPSSPDARRNGQEKHFKDEDEDEDVASPDGLGRLNVAGAGGGGDSGGGPGAATDGNFTAGLA	chr19:4043303-4066899[-]	"Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation. Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating the organization of chromatin and through the direct recruitment of transcription factors to gene regulatory regions. Negatively regulates SMAD4 transcriptional activity in the TGF-beta signaling pathway through these two mechanisms. That is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the recruitment of the transcriptional activators CREBBP and EP300. Collaborates with transcription factors like RELA to modify the accessibility of gene transcription regulatory regions to secondary transcription factors. Also directly interacts with transcription factors like SP1 to prevent their binding to DNA. Functions as an androgen receptor/AR transcriptional corepressor by recruiting NCOR1 and NCOR2 to the androgen response elements/ARE on target genes. Thereby, negatively regulates androgen receptor signaling and androgen-induced cell proliferation. Involved in the switch between fetal and adult globin expression during erythroid cells maturation. Through its interaction with the NuRD complex regulates chromatin at the fetal globin genes to repress their transcription. Specifically represses the transcription of the tumor suppressor ARF isoform from the CDKN2A gene. Efficiently abrogates E2F1-dependent CDKN2A transactivation. Regulates chondrogenesis through the transcriptional repression of specific genes via a mechanism that also requires histone deacetylation. Regulates cell proliferation through the transcriptional regulation of genes involved in glycolysis. Involved in adipogenesis through the regulation of genes involved in adipocyte differentiation. Plays a key role in the differentiation of lymphoid progenitors into B and T lineages. Promotes differentiation towards the B lineage by inhibiting the T-cell instructive Notch signaling pathway through the specific transcriptional repression of Notch downstream target genes. Also regulates osteoclast differentiation. May also play a role, independently of its transcriptional activity, in double-strand break repair via classical non-homologous end joining/cNHEJ. Recruited to double-strand break sites on damage DNA, interacts with the DNA-dependent protein kinase complex and directly regulates its stability and activity in DNA repair. May also modulate the splicing activity of KHDRBS1 toward BCL2L1 in a mechanism which is histone deacetylase-dependent and thereby negatively regulates the pro-apoptotic effect of KHDRBS1."	PDB: 2IF5; PDB: 2NN2; PDB: 7EYI; PDB: 7N5S; PDB: 7N5T	HGNC:18078	ZBT7A_HUMAN	Reviewed	ENSG00000178951	.	.	.	.	.
Mol00717	Protein	Zinc finger E-box-binding homeobox 1 (ZEB1)	NIL-2-A zinc finger protein; Negative regulator of IL2; Transcription factor 8; TCF-8; AREB6; TCF8	ZEB1	6935	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000424869.6, ZEB1-202, 5937; ENST00000446923.7, ZEB1-204, 6250; ENST00000320985.14, ZEB1-201, 5423; ENST00000560721.6, ZEB1-217, 3368; ENST00000542815.7, ZEB1-207, 3217; ENST00000561212.5, ZEB1-220, 1500; ENST00000558440.5, ZEB1-210, 886; ENST00000437844.6, ZEB1-203, 6246; ENST00000559858.5, ZEB1-215, 2745; ENST00000561061.5, ZEB1-219, 970; ENST00000493835.5, ZEB1-206, 683; ENST00000606671.5, ZEB1-223, 571; ENST00000558832.5, ZEB1-212, 570; ENST00000606161.1, ZEB1-222, 482; ENST00000488625.6, ZEB1-205, 6026; ENST00000542879.5, ZEB1-208, 3645; ENST00000558655.5, ZEB1-211, 2773; ENST00000561304.5, ZEB1-221, 1383; ENST00000559496.5, ZEB1-214, 1381; ENST00000558863.5, ZEB1-213, 1355; ENST00000560196.5, ZEB1-216, 1014; ENST00000557827.5, ZEB1-209, 877; ENST00000560909.2, ZEB1-218, 564"	MADGPRCKRRKQANPRRNNVTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDRKEGQEILGPEAQADEAGCTVKDDECESDAENEQNHDPNVEEFLQQQDTAVIFPEAPEEDQRQGTPEASGHDENGTPDAFSQLLTCPYCDRGYKRFTSLKEHIKYRHEKNEDNFSCSLCSYTFAYRTQLERHMTSHKSGRDQRHVTQSGCNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECPNCKKRFSHSGSYSSHISSKKCISLIPVNGRPRTGLKTSQCSSPSLSASPGSPTRPQIRQKIENKPLQEQLSVNQIKTEPVDYEFKPIVVASGINCSTPLQNGVFTGGGPLQATSSPQGMVQAVVLPTVGLVSPISINLSDIQNVLKVAVDGNVIRQVLENNQANLASKEQETINASPIQQGGHSVISAISLPLVDQDGTTKIIINYSLEQPSQLQVVPQNLKKENPVATNSCKSEKLPEDLTVKSEKDKSFEGGVNDSTCLLCDDCPGDINALPELKHYDLKQPTQPPPLPAAEAEKPESSVSSATGDGNLSPSQPPLKNLLSLLKAYYALNAQPSAEELSKIADSVNLPLDVVKKWFEKMQAGQISVQSSEPSSPEPGKVNIPAKNNDQPQSANANEPQDSTVNLQSPLKMTNSPVLPVGSTTNGSRSSTPSPSPLNLSSSRNTQGYLYTAEGAQEEPQVEPLDLSLPKQQGELLERSTITSVYQNSVYSVQEEPLNLSCAKKEPQKDSCVTDSEPVVNVIPPSANPINIAIPTVTAQLPTIVAIADQNSVPCLRALAANKQTILIPQVAYTYSTTVSPAVQEPPLKVIQPNGNQDERQDTSSEGVSNVEDQNDSDSTPPKKKMRKTENGMYACDLCDKIFQKSSSLLRHKYEHTGKRPHECGICKKAFKHKHHLIEHMRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEERDSTEQEEAGPEILSNEHVGARASPSQGDSDERESLTREEDEDSEKEEEEEDKEMEELQEEKECEKPQGDEEEEEEEEEVEEEEVEEAENEGEEAKTEGLMKDDRAESQASSLGQKVGESSEQVSEEKTNEA	chr10:31318495-31529814[+]	Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting microRNAs.	PDB: 2E19	HGNC:11642	ZEB1_HUMAN	Reviewed	ENSG00000148516	.	.	.	.	.
Mol00718	Protein	Zinc finger protein with KRAB and SCAN domains 1 (ZKSCAN1)	Zinc finger protein 139; Zinc finger protein 36; Zinc finger protein KOX18; KOX18; ZNF139; ZNF36	ZKSCAN1	7586	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000324306.11, ZKSCAN1-201, 9403; ENST00000620510.1, ZKSCAN1-206, 9192; ENST00000535170.5, ZKSCAN1-205, 8758; ENST00000426572.5, ZKSCAN1-202, 2011; ENST00000432317.1, ZKSCAN1-203, 573; ENST00000482979.5, ZKSCAN1-204, 1449"	MMTAESREATGLSPQAAQEKDGIVIVKVEEEDEEDHMWGQDSTLQDTPPPDPEIFRQRFRRFCYQNTFGPREALSRLKELCHQWLRPEINTKEQILELLVLEQFLSILPKELQVWLQEYRPDSGEEAVTLLEDLELDLSGQQVPGQVHGPEMLARGMVPLDPVQESSSFDLHHEATQSHFKHSSRKPRLLQSRALPAAHIPAPPHEGSPRDQAMASALFTADSQAMVKIEDMAVSLILEEWGCQNLARRNLSRDNRQENYGSAFPQGGENRNENEESTSKAETSEDSASRGETTGRSQKEFGEKRDQEGKTGERQQKNPEEKTRKEKRDSGPAIGKDKKTITGERGPREKGKGLGRSFSLSSNFTTPEEVPTGTKSHRCDECGKCFTRSSSLIRHKIIHTGEKPYECSECGKAFSLNSNLVLHQRIHTGEKPHECNECGKAFSHSSNLILHQRIHSGEKPYECNECGKAFSQSSDLTKHQRIHTGEKPYECSECGKAFNRNSYLILHRRIHTREKPYKCTKCGKAFTRSSTLTLHHRIHARERASEYSPASLDAFGAFLKSCV	chr7:100015572-100041689[+]	May be involved in transcriptional regulation.	.	HGNC:13101	ZKSC1_HUMAN	Reviewed	ENSG00000106261	.	.	.	.	.
Mol00719	Protein	Zinc finger protein 217 (ZNF217)	ZABC1	ZNF217	7764	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371471.7, ZNF217-202, 5790; ENST00000302342.3, ZNF217-201, 5633; ENST00000431687.5, ZNF217-203, 779; ENST00000437222.1, ZNF217-204, 746; ENST00000540425.1, ZNF217-205, 568"	MQSKVTGNMPTQSLLMYMDGPEVIGSSLGSPMEMEDALSMKGTAVVPFRATQEKNVIQIEGYMPLDCMFCSQTFTHSEDLNKHVLMQHRPTLCEPAVLRVEAEYLSPLDKSQVRTEPPKEKNCKENEFSCEVCGQTFRVAFDVEIHMRTHKDSFTYGCNMCGRRFKEPWFLKNHMRTHNGKSGARSKLQQGLESSPATINEVVQVHAAESISSPYKICMVCGFLFPNKESLIEHRKVHTKKTAFGTSSAQTDSPQGGMPSSREDFLQLFNLRPKSHPETGKKPVRCIPQLDPFTTFQAWQLATKGKVAICQEVKESGQEGSTDNDDSSSEKELGETNKGSCAGLSQEKEKCKHSHGEAPSVDADPKLPSSKEKPTHCSECGKAFRTYHQLVLHSRVHKKDRRAGAESPTMSVDGRQPGTCSPDLAAPLDENGAVDRGEGGSEDGSEDGLPEGIHLDKNDDGGKIKHLTSSRECSYCGKFFRSNYYLNIHLRTHTGEKPYKCEFCEYAAAQKTSLRYHLERHHKEKQTDVAAEVKNDGKNQDTEDALLTADSAQTKNLKRFFDGAKDVTGSPPAKQLKEMPSVFQNVLGSAVLSPAHKDTQDFHKNAADDSADKVNKNPTPAYLDLLKKRSAVETQANNLICRTKADVTPPPDGSTTHNLEVSPKEKQTETAADCRYRPSVDCHEKPLNLSVGALHNCPAISLSKSLIPSITCPFCTFKTFYPEVLMMHQRLEHKYNPDVHKNCRNKSLLRSRRTGCPPALLGKDVPPLSSFCKPKPKSAFPAQSKSLPSAKGKQSPPGPGKAPLTSGIDSSTLAPSNLKSHRPQQNVGVQGAATRQQQSEMFPKTSVSPAPDKTKRPETKLKPLPVAPSQPTLGSSNINGSIDYPAKNDSPWAPPGRDYFCNRSASNTAAEFGEPLPKRLKSSVVALDVDQPGANYRRGYDLPKYHMVRGITSLLPQDCVYPSQALPPKPRFLSSSEVDSPNVLTVQKPYGGSGPLYTCVPAGSPASSSTLEGKRPVSYQHLSNSMAQKRNYENFIGNAHYRPNDKKT	chr20:53567071-53609907[-]	Binds to the promoters of target genes and functions as repressor. Promotes cell proliferation and antagonizes cell death. Promotes phosphorylation of AKT1 at 'Ser-473'.	PDB: 2HU2; PDB: 3UK3; PDB: 4F2J; PDB: 4IS1	HGNC:13009	ZN217_HUMAN	Reviewed	ENSG00000171940	.	.	.	.	.
Mol00720	Protein	E3 ubiquitin-protein ligase ZNRF3 (ZNRF3)	RING finger protein 203; RING-type E3 ubiquitin transferase ZNRF3; Zinc/RING finger protein 3; KIAA1133; RNF203	ZNRF3	84133	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000544604.7, ZNRF3-203, 6872; ENST00000406323.3, ZNRF3-202, 2878; ENST00000402174.5, ZNRF3-201, 2667"	MRPRSGGRPGATGRRRRRLRRRPRGLRCSRLPPPPPLPLLLGLLLAAAGPGAARAKETAFVEVVLFESSPSGDYTTYTTGLTGRFSRAGATLSAEGEIVQMHPLGLCNNNDEEDLYEYGWVGVVKLEQPELDPKPCLTVLGKAKRAVQRGATAVIFDVSENPEAIDQLNQGSEDPLKRPVVYVKGADAIKLMNIVNKQKVARARIQHRPPRQPTEYFDMGIFLAFFVVVSLVCLILLVKIKLKQRRSQNSMNRLAVQALEKMETRKFNSKSKGRREGSCGALDTLSSSSTSDCAICLEKYIDGEELRVIPCTHRFHRKCVDPWLLQHHTCPHCRHNIIEQKGNPSAVCVETSNLSRGRQQRVTLPVHYPGRVHRTNAIPAYPTRTSMDSHGNPVTLLTMDRHGEQSLYSPQTPAYIRSYPPLHLDHSLAAHRCGLEHRAYSPAHPFRRPKLSGRSFSKAACFSQYETMYQHYYFQGLSYPEQEGQSPPSLAPRGPARAFPPSGSGSLLFPTVVHVAPPSHLESGSTSSFSCYHGHRSVCSGYLADCPGSDSSSSSSSGQCHCSSSDSVVDCTEVSNQGVYGSCSTFRSSLSSDYDPFIYRSRSPCRASEAGGSGSSGRGPALCFEGSPPPEELPAVHSHGAGRGEPWPGPASPSGDQVSTCSLEMNYSSNSSLEHRGPNSSTSEVGLEASPGAAPDLRRTWKGGHELPSCACCCEPQPSPAGPSAGAAGSSTLFLGPHLYEGSGPAGGEPQSGSSQGLYGLHPDHLPRTDGVKYEGLPCCFYEEKQVARGGGGGSGCYTEDYSVSVQYTLTEEPPPGCYPGARDLSQRIPIIPEDVDCDLGLPSDCQGTHSLGSWGGTRGPDTPRPHRGLGATREEERALCCQARALLRPGCPPEEAGAVRANFPSALQDTQESSTTATEAAGPRSHSADSSSPGA	chr 22: 28883572-29057488 [+] 	"E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone. Along with RSPO2 and RNF43, constitutes a master switch that governs limb specification."	.	HGNC:18126	ZNRF3_HUMAN	Reviewed	ENSG00000183579	.	.	.	.	.
Mol00723	Protein	Dihydropteroate synthase (SUL)	Dihydropteroate pyrophosphorylase type I; Dihydropteroate synthase type I; DHPS; sul1	sul1/sul2/ sul3	67375551	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives (By similarity). It is implicated in resistance to sulfonamide. The type II enzyme is stable whereas type I DHPS loses its activity rapidly."	.	.	DHP1_ECOLX/Q6UUU7_ECOLX /Q6RSI4_ECOLX	.	.	.	.	.	.	.
Mol00724	Protein	Pleiotropic ABC efflux transporter of multiple drugs CDR /Multidrug resistance protein 1 (CDR1/ABCB1)	.	BCR/ABL	.	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	.	.	.	.	.	CDR1_CANAL/MDR1_CANAL	.	.	.	.	.	.	.
Mol00725	Protein	DUF2154 domain-containing protein/Glycerophosphoryl diester phosphodiesterase family protein (LIAF/GDPD)	.	EF_0779	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	.	.	.	.	.	A0A6I4XRK1_ENTFL/Q837Q4_ENTFA	.	.	.	.	.	.	.
Mol00726	Protein	Catalase isozyme A/Tetracycline efflux MFS transporter/Dihydropteroate synthase (CATA1/TETB/SUL)	.	catA1 / tetB/ sul1/ sul2	.	Salmonella enterica subsp. enterica serovar Agona	58095	Salmonella enterica subsp. enterica serovar Agona	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	A0A516IHW8_SALET/A0A3S8XDC0_SALET/ H9TJU7_SALET	.	.	.	.	.	.	.
Mol00727	Protein	Dihydrofolate reductase/DNA-directed RNA polymerase subunit beta (DHFR/RPOB)	.	DHFR/RPOB	.	Mycobacterium leprae	1769	Mycobacterium leprae	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	.	.	.	.	.	DHPS1_MYCLE/RPOB_MYCLE	.	.	.	.	.	.	.
Mol00728	Protein	Dihydrofolate reductase/DNA gyrase subunit A/DNA gyrase subunit B (DHFR/GYRA/GYRB)	.	DHFR/GYRA/GYRB	887105; 66672403; 948211	Mycobacterium leprae	1769	Mycobacterium leprae	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	.	.	.	.	.	DHPS1_MYCLE/GYRA_MYCLE/GYRB_MYCLE	.	.	.	.	.	.	.
Mol00729	Protein	Protein tcr3 (TCR3)	tcr3; Tcr3 protein	tcr3	.	Streptomyces aureofaciens	1894	Kitasatospora aureofaciens	Kitasatospora	2063	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MGMANATSQTGEAVADEAGGPAGFTHRQIITALSGLLLAVLLAALDQTIVSTALRTIGDQLHGQTVQAWVITGYLVSSTIAMPFYGKLSDIYGRKPLYLAAIAVFIVGSAACAMANSMETLAIARVLQGFGGAGLMSLPTAVIADLAPVRERGRYFSYLMMAWVAASVLGPLVGGLFAGAGEILGVTGWRWAFLINVPLGLVALLSVRKALNLPHRRVDHPIDFRGALTLALCLVPLLIVAEEGLDWGWGSARSLTLFAVSLIGLVLFVLAERARGLEAMVPLRLFRRGGITMATAVNFTIGVGIFGTVSTLPLFLQLVQGRSATVAGLVIIPVMTGAIVSQTICAKIIKKWNRYKKPAIVGLGSMAGALLSLSAAGADTPLAVIVVIAAWLGFGIGLSQTVITLAIQSSAPKSELGVANAASGLFRQLGGTSGAAVFMSVLFGVAAGRLDGADPDEAVRRALSDPGSTGGLSASAVDAFTSGFDTMFLVGGLILAVGFLLTFPLRELRDEE	.	.	.	.	Q53769_KITAU	Unreviewed	.	.	.	.	.	.
Mol00730	Protein	Protein pexA (PEXA)	pexA; AKSOIL_0345; PexA	pexA	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKKFVLFCERNGIALIPIVLILLGCGLWPEMELLVPSLPDMQRAFNIQDAQIQQLLTANFVGFLIGVLFAGPLCDSAGRRTVMMIGTIGYLVSSVLCPFCNDFVLLMIARFFQGLFMTGPVIAGGVLLMEATEGVKQIFWMSIGNAAITFCMAAGPIVGSWINTGFGYVGNLWSILILGLIGCLPALFLVPESLPVEKRAAFHPKLLFKGYFALLKDFRFMCLAIPMCALAAAYWIYVGVSALYMVNQLGIAQEMFGRYQGPIVGCFSIISLGSSKLLQRFGLMKCLRAGIVSMFTGMLLLLGMSILSLDHAVATTVFMMFFVGGMAPICSMLFPYALGHLPVDLKGNAQAMVQAIRLFFASIGTSLVGVFYKSAFLPVALIMFAILLFSCYFLWKGRRYLKEGLGADHILSVGH	.	.	.	.	D9MX76_9BACT	Unreviewed	.	.	.	.	.	.
Mol00731	Protein	Epidermal growth factor receptor/Protein Mdm4 (EGFR/MDM4)	.	EGFR/MDM4	1956; 4194	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	EGFR_HUMAN/MDM4_HUMAN	.	.	.	.	.	.	.
Mol00732	Protein	Efflux pump membrane transporter MdsA (MDSA)	sat4; Streptothricin acetyltransferase	MdsA	.	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRRTFKIMLIAGVIAAIGGVIYMAGEALWDKDNAVGPPASAPPPPSVPVAKALSRTLAPTAEFTGFLAAPETVELRSRVGGTLDAVSVPEGRLVSRGQLLFQIDPRPFEVALDTAVAQLRQAEVLARQAQADFDRIQRLVASGAVSRKNADDVTATRNARQAQMQSAKAAVAAARLELSWTRITAPIAGRVDRILVTRGNLVSGGVAGNATLLTTIVSHNPMYVYFDIDEATWLKALRHTRSDKNPPVVNMGLTTDNGLPYQGVLDFMGNQMNRSTGTIRARAVIPDPDGMLSPGLFARISLPIGEPRETVLIDDLAVSADQGKNYVLIVGKENQVEYRPVELGQMVDGLRVVTQGVQPGEKIILKGLVRPGMTVAPRLVPMRQNVTDKQTATLTKADGDSASKAVRQ	.	.	.	.	A0A736DX09_SALTM	Unreviewed	.	.	.	.	.	.
Mol00733	Protein	Efflux pump membrane transporter MdsB (MDSB)	sat4; Streptothricin acetyltransferase	MdsB	.	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKFTHFFIARPIFAIVLSLLMLLAGAIAFLKLPLSEYPAVTPPTVQVSASYPGANPQVIADTVAAPLEQVINGVDGMLYMNTQMAIDGRMVISIAFEQGTDPDMAQIQVQNRVSRALPRLPEEVQRIGVVTEKTSPDMLMVVHLVSPQKRYDSLYLSNFAIRQVRDELARLPGVGDVLVWGAGEYAMRVWLDPAKIANRGLTASDIVTALREQNVQVAAGSVGQQPEASAAFQMTVNTLGRLTSEEQFGEIVVKIGADGEVTRLRDVARVTLGADAYTLRSLLNGEAAPALQIIQSPGANAIDVSNAIRGKMDELQQNFPQDIEYRIAYDPTVFVRASLQSVAITLLEALVLVVLVVVMFLQTWRASIIPLVAVPVSLVGTFALMHLFGFSLNTLSLFGLVLSIGIVVDDAIVVVENVERHISQGKSPGEAAKKAMDEVTGPILSITSVLTAVFIPSAFLAGLQGEFYRQFALTIAISTILSAINSLTLSPALAAILLRPHHDTAKADWLTRLMGTVTGGFFHRFNRFFDSASNRYVSAVRRAVRGSVIVMVLYAGFVGLTWLGFHQVPNGFVPAQDKYYLVGIAQLPSGASLDRTEAVVKQMSAIALAEPGVESVVVFPGLSVNGPVNVPNSALMFAMLKPFDEREDPSLSANAIAGKLMHKFSHIPDGFIGIFPPPPVPGLGATGGFKLQIEDRAELGFEAMTKVQSEIMSKAMQTPELANMLASFQTNAPQLQVDIDRVKAKSMGVSLTDIFETLQINLGSLYVNDFNRFGRAWRVMAQADAPFRMQQEDIGLLKVRNAKGEMIPLSAFVTIMRQSGPDRIIHYNGFPSVDISGGPAPGFSSGQATDAIEKIVRETLPEGMVFEWTDLVYQEKQAGNSALAIFALAVLLAFLILAAQYNSWSLPFAVLLIAPMSLLSAIVGVWVSGGDNNIFTQIGFVVLVGLAAKNAILIVEFARAKEHDGADPLTAVLEASRLRLRPILMTSFAFIAGVVPLVLATGAGAEMRHAMGIAVFAGMLGVTLFGLLLTPVFYVVVRRMALKRENRVDSHDQQA	.	.	.	.	A0A0D6HCN1_SALTM	Unreviewed	.	.	.	.	.	.
Mol00734	Protein	Efflux pump membrane transporter MdsC (MDSC)	sat4; Streptothricin acetyltransferase	MdsC	.	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKITFTGYRQTATLATLAFVTTLAGCTMAPKHERPASPTAMVYPYATSTVSGAPDAADIGWRDFFHDPLLQELIAIALRNNRDLRKAGLNVEAARALYRIQRAEMLPTLGIATAMDASRTPADLSVMDESEINRRYEAAGATTAWELDLWGRVRSLSDQALAAYMALDETYIAARMSLVSEVASAWLTLRADRELLRLTEDTLAAQKSSYTLTTQLARTGNATQLDLRMAEIALRSAEINRAAYTRQLARDRNALELLLGQPLTPELSRRLNEAVTLTEGAIPTTLPGGLPSDLLVRRPDIRAAEYRLRGANARIGAARAAFFPTISLTGSAGTASASLSGLFEPGSGSWRFLPQITLPLFHGGALRADLDRAHVQKQIEIARYENVIQQAFRDVADGLAGQRTLNDQVQSEQRAVEASQIAYELAGLRFQEGVDDYLTLLDTHRMLYGAQQRLVRTRLMQQLNIINLYKALGGGWREYSEKKQG	.	.	.	.	A0A0D6HCR2_SALTM	Unreviewed	.	.	.	.	.	.
Mol00735	Protein	Aminoglycoside 6-adenylyltransferase AadS (AAADS)	.	F3F51_25225	.	Bacteroides ovatus	28116	Bacteroides ovatus	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MKVREEKLRTIIEWSEKNEDVRVLLLTSSLVNPLALVDEFSDLDIEFVFEDNTNYISDKSWTLKFGNPIAMIEEDESCFNHKHAMKMLLYEDGVKVDFKLYSKSKFIKETQEKELPEDWDIGYKILIDKDGITKQMLKPTYQISIIKKPSEKEFQNLINDFWWDTTYVAKCLVRDEIFYAKFMSETVIRTEYLIPLIEWHIASEHNWNITTNKYGRLFKKYLNQEMWAKTEQTFSGSDIKENWTALFSMTDLVSEIGTELSKKLEYKYPDKLENDIRKYLAGLKPKT	.	.	.	.	A0A6N3V4B7_BACOV	Unreviewed	.	.	.	.	.	.
Mol00736	Protein	Multidrug export protein EmrA (EMRA)	.	emrA	947166	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSANAEIQTPQQPAKKKGKRKTALLLLTLLFVIIAVAYGIYWFLVLRHIEETDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVKEGDVLVTLDQTDAKQAFEKAKTALASSVRQTHQLMINSKQLQANIDVQKTALAQAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYNANQAMILNSNLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATDLWVDANFKETQLANMRIGQPVTVITDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRVELDARQLEQHPLRIGLSTLVTVDTANRDGQVLASQVRTTPVAESNAREINLAPVNKLIDDIVQANAG	.	"Part of the tripartite efflux system EmrAB-TolC, which confers resistance to antibiotics such as CCCP, FCCP, 2,4-dinitrophenol and nalidixic acid. EmrA is a drug-binding protein that provides a physical link between EmrB and TolC."	.	.	Q8ZMK9_SALTY	Unreviewed	.	.	.	.	.	.
Mol00737	Protein	Multidrug export protein EmrB (EMRB)	.	emrB	947167	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MQQQKPLEGAQLVIMTIALSLATFMQVLDSTIANVAIPTIAGNLGSSLSQGTWVITSFGVANAISIPLTGWLAKRFGEVKLFMWSTVAFAAASWACGVSSSLNMLIFFRVVQGVVAGPLIPLSQSLLLNNYPPAKRSIALALWSMTVIVAPICGPILGGYISDNYHWGWIFFINVPIGIAVVLMTLHTLRGRETHTERRRIDAVGLALLVIGIGSLQIMLDRGKELDWFSSQEIIILTVVAVIAISFLIVWELTDDHPIVDLSLFKSRNFTIGCLCISLAYMLYFGAIVLLPQLLQEVYGYTATWAGLASAPVGIIPVILSPIIGRFAHKLDMRRLVTFSFIMYAVCFYWRAWTFEPGMDFGASAWPQFIQGFAVACFFMPLTTITLSGLPPERLAAASSLSNFTRTLAGSIGTSITTTMWTDRESLHHAQLTESVTAYNPNAQTMYDKLEGLGMTHQQASGWIAQQITNQGLIISANEIFWMSAGIFLVLLGLVWFAKPPFGAGGGGGGAH	.	"Part of the tripartite efflux system EmrAB-TolC, which confers resistance to antibiotics such as CCCP, FCCP, 2,4-dinitrophenol and nalidixic acid."	.	.	Q8ZMK8_SALTY	Unreviewed	.	.	.	.	.	.
Mol00738	Protein	Tiamulin efflux ATP-binding protein (TAEA)	taeA; AK95_19955; Tiamulin efflux ATP-binding protein	taeA	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNILTVEQVTKSYGDKILFQDASFGMEDQDKIGIIGVNGTGKSTFLRVIAGLEPPDSGKISMGNRIRVRYLAQNPEFDPDKTVLQQVFEGDLPEMKAVREYTETMELLELHPSHEELQQKLLKLNQTLETLQAWQLESDAKTILSKLGIRNYEAKMGTLSGGQRKRVALAAALIQPSDLLILDEPTNHIDNESVAWLEQYLQKRRGALLMITHDRYFLDRVANVMLELDHGRLFRYEANYSRFLELKAEREEREAASEQKRQNLLRSELAWIRRGAKARTTKQKARIERFEKLKDQEMVHSSGELDVSVASTRLGRKILEIEGLRMKIDDKTLIQDLSYIAVPEDRIGIVGPNGSGKSTLLNLIAGRIQPGGGEVVLGPTVKLGYFTQEHQEMDGSQRVIEYIKDEAEVVRTADGSAITAAQMLERFLFPPALQWTPIAKLSGGEKRRLYLLRVLMSAPNVLLLDEPTNDLDIQTLSVLEQYLDEFPGVCIVVSHDRFFLDRTVDKIMAFEGDGQIRVHVGSYSEYAEWMQRHGGEASGSKAEASIAKSASGSSDGTDSDSAKEAPRERLKFSYKEQREFDQIDGLIEDTESKLASIQSEMETAGSDAARLQELMKAQEETERELEHLMERWTYLNELAEKIEQSKKS	.	.	.	.	A0A1I9ZKK9_9BACL	Unreviewed	.	.	.	.	.	.
Mol00739	Protein	Transcriptional regulatory protein (PHOP)	phoP; PhoP	phoP	.	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRVLVVEDNALLRHHLKVQLQELGHQVDAAEDAREADYYLGEHLPDIAIVDLGLPDEDGLSLIRRWRSHDVSLPVLVLTAREGWQDKVEVLSAGADDYVTKPFHIEEVAARMQALLRRNSGLASQVISLPPFQVDLSRRELSVNDQPIKLTAFEYTIMETLIRNRGKVVSKDSLMLQLYPDAELRESHTIYVLMGRLRKKIQAEYPQDVITTVRGQGYLFELR	.	.	.	.	A0A139ZN42_KLEPN	Unreviewed	.	.	.	.	.	.
Mol00740	Protein	Multidrug resistance protein MdtC (MDTC)	.	mdtA	946604	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKGSNTFRWAIAIGVVVAAAAFWFWHSRSESPTAAPGVAAQAPHTASAGRRGMRDGPLAPVQAATATTQAVPRYLSGLGTVTAANTVTVRSRVDGQLIALHFQEGQQVNAGDLLAQIDPSQFKVALAQAQGQLAKDNATLANARRDLARYQQLAKTNLVSRQELDAQQALVNETQGTIKADEANVASAQLQLDWSRITAPVSGRVGLKQVDVGNQISSSDTAGIVVITQTHPIDLIFTLPESDIATVVQAQKAGKALVVEAWDRTNSHKLSEGVLLSLDNQIDPTTGTIKIKARFTNQDDTLFPNQFVNARMLVDTEQNAVVVPAAAVQMGNEGHFVWVLNDENNVSKKRVKIGIQDNRNVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQTTVADEKSPSRHEGQKGARA	.	The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.	.	.	A0A0D6FFV8_SALTM	Unreviewed	.	.	.	.	.	.
Mol00741	Protein	Multidrug resistance protein MdtB (MDTB)	.	mdtB	946606	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MQVLPPGSTGGPSRLFILRPVATTLLMAAILLAGIIGYRFLPVAALPEVDYPTIQVVTLYPGASPDVMTSAVTAPLERQFGQMSGLKQMSSQSSGGASVVTLQFQLTLPLDVAEQEVQAAINAATNLLPSDLPNPPIYSKVNPADPPIMTLAVTSNSMPMTQVEDMVETRVAQKISQVSGVGLVTLAGGQRPAVRVKLNAQAVAALGLTSETVRTAITGANVNSAKGSLDGPERAVTLSANDQMQSADEYRRLIIAYQNGAPVRLGDVATVEQGAENSWLGAWANQAPAIVMNVQRQPGANIIATADSIRQMLPQLTESLPKSVKVTVLSDRTTNIRASVRDTQFELMLAIALVVMIIYLFLRNIPATIIPGVAVPLSLIGTFAVMVFLDFSINNLTLMALTIATGFVVDDAIVVIENISRYIEKGEKPLAAALKGAGEIGFTIISLTFSLIAVLIPLLFMGDIVGRLFREFAVTLAVAILISAVVSLTLTPMMCARMLSQQSLRKQNRFSRACERMFDRVIASYGRGLAKVLNHPWLTLSVAFATLLLSVMLWIVIPKGFFPVQDNGIIQGTLQAPQSSSYASMAQRQRQVAERILQDPAVQSLTTFVGVDGANPTLNSARLQINLKPLDARDDRVQQVISRLQTAVATIPGVELYLQPTQDLTIDTQVSRTQYQFTLQATTLDALSHWVPKLQNALQSLPQLSEVSSDWQDRGLAAWVNVDRDSASRLGISMADVDNALYNAFGQRLISTIYTQANQYRVVLEHNTASMPGLAALETIRLTSRDGGTVPLSAIARIEQRFAPLSINHLDQFPVTTFSFNVPESYSLGDAVQAILDTEKTLALPADITTQFQGSTLAFQAALGSTVWLIVAAVVAMYIVLGVLYESFIHPITILSTLPTAGVGALLALIIAGSELDIIGIILLIGIVKKNAIMMIDFALAAEREQGMSPRDAIFQACLLRFRPILMTTLAALLGALPLMLSTGVGTELRRPLGIAMVGGLLVSQVLTLFTTPVIYLLFDRLSLYVKSRFPRHKEEA	.	The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.	.	.	A0A752NKJ0_SALTM	Unreviewed	.	.	.	.	.	.
Mol00742	Protein	Multidrug resistance protein MdtA (MDTA)	.	mdC	946608	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRFFALFIYRPVATILIAAAITLCGILGFRLLPVAPLPQVDFPVIMVSASLPGASPETMASSVATPLERSLGRIAGVNEMTSSSSLGSTRIILEFNFDRDINGAARDVQAAINAAQSLLPGGMPSRPTYRKANPSDAPIMILTLTSESWSQGKLYDFASTQLAQTIAQIDGVGDVDVGGSSLPAVRVGLNPQALFNQGVSLDEVREAIDSANVRRPQGAIEDSVHRWQIQTNDELKTAAEYQPLIIHYNNGAAVRLGDVASVTDSVQDVRNAGMTNAKPAILLMIRKLPEANIIQTVDGIRAKLPELRAMIPAAIDLQIAQDRSPTIRASLQEVEETLAISVALVILVVFLFLRSGRATLIPAVAVPVSLIGTFAAMYLCGFSLNNLSLMALTIATGFVVDDAIVVLENIARHLEAGMKPLQAALQGTREVGFTVISMSLSLVAVFLPLLLMGGLPGRLLREFAVTLSVAIGISLVVSLTLTPMMCGWMLKSSKPRTQPRKRGVGRLLVALQQGYGTSLKWVLNHTRLVGVVFLGTVALNIWLYIAIPKTFFPEQDTGVLMGGIQADQSISFQAMRGKLQDFMKIIRDDPAVNNVTGFTGGSRVNSGMMFITLKPRGERKETAQQIIDRLRVKLAKEPGARLFLMAVQDIRVGGRQANASYQYTLLSDSLAALREWEPKIRKALSALPQLADVNSDQQDNGAEMNLIYDRDTMSRLGIDVQAANSLLNNAFGQRQISTIYQPMNQYKVVMEVDPRYSQDISALEKMFVINRDGKAIPLSYFAQWRPANAPLSVNHQGLSAASTIAFNLPTGTSLSQATEAINRTMTQLGVPSTVRGSFSGTAQVFQQTMNSQLILIVAAIATVYIVLGILYESYVHPLTILSTLPSAGVGALLALELFNAPFSLIALIGIMLLIGIVKKNAIMMVDFALEAQRSGGLTPEQAIFQACLLRFRPIMMTTLAALFGALPLVLSGGDGSELRQPLGITIVGGLVMSQLLTLYTTPVVYLFFDRLRLRFSRKNSKPVVEI	.	The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. MdtABC requires TolC for its function.	.	.	A0A0D6FGF2_SALTM	Unreviewed	.	.	.	.	.	.
Mol00743	Protein	Protein QacZ (QACZ)	qacZ; QacZ	qacZ	.	Enterococcus faecium	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MPYLYLLLAIVSEVIGSAFLKSSDGFSKLYPTITTIISYLISFYFLSKTMQHLPLNIAYASWSGLGLVLTTIVSVLIFKEQINLISIISIILIIFGVVLLNTFGSSH	.	.	.	.	A0A088SHQ9_ENTFC	Unreviewed	.	.	.	.	.	.
Mol00744	Protein	Gentamicin 3'-acetyltransferase (AACC1)	RCS36_PI-II0023	aacC1	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MGIIRTCRLGPDQVKSMRAALDLFGREFGDVATYSQHQPDSDYLGNLLRSKTFIALAAFDQEAVVGALAAYVLPKFEQPRSEIYIYDLAVSGEHRRQGIATALINLLKHEANALGAYVIYVQADYGDDPAVALYTKLGIREEVMHFDIDPSTAT	.	.	.	.	D3VY99_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00745	Protein	Aminoglycoside acetyltransferase (AAC)	aac(3)-Ic; aac(3)Ic; acc(3)Ic; Aminoglycoside acetyltransferase	aac(3)-Ic	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MISTQTKITRLNSQDVGVMRAMLGMFGEAFEDAENYCRAQPSDSYLQDLLCGSGFIAIAALQGQEVIGGLAAYVLPKFEQQRKEIYIYDLGVQGAYRRRGIATALINELQRIAHDIGAYVIFVQADYGDDPAVALYTKLGIREDVMHFDIEPQPAA	.	.	.	.	Q83V16_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00746	Protein	AAC(6')-Ib family aminoglycoside 6'-N-acetyltransferase (AAC6IB)	aac(6')-Ib; EYB64_20715; 6')-Ib family aminoglycoside 6'-N-acetyltransferase	aac(6')-Ib	.	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTNSNDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDGWWEEETDPGVRGIDQLLANASQLGKGLGTKLVRALVELLFNDPEVTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPDGPAVYMVQTRQAFERTRSVA	.	.	.	.	A0A7Z7VKB5_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00747	Protein	AAC(6')-Ib family aminoglycoside 6'-N-acetyltransferase (AAC6IB)	aac(3)-Ib/aac(6')-Ib; Aminoglycoside 3-N-acetyltransferase/aminoglycoside 6'-N-acetyltransferase fusion protein	aac(6')-Ib	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTNSNDSVTLRLMTEHDLAMLYEWLNRSHIVEWWGGEEARPTLADVQEQYLPSVLAQESVTPYIAMLNGEPIGYAQSYVALGSGDGWWEEETDPGVRGIDQSLANASQLG KGLGTKLVRALVELLFNDPE VTKIQTDPSPSNLRAIRCYEKAGFERQGTVTTPDGPAVYMVQTRQAFERTRSDA	.	.	.	.	Q7BM49_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00748	Protein	16S rRNA (adenine(1408)-N(1))-methyltransferase (KAMB)	16S rRNA m1A1408 methyltransferase; Kanamycin-apramycin resistance methylase	kamB	.	Streptoalloteichus tenebrarius	1933	Streptoalloteichus tenebrarius	Streptoalloteichus	2016	Pseudonocardiaceae	2070	Pseudonocardiales	85010	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MRRVVGKRVQEFSDAEFEQLRSQYDDVVLDVGTGDGKHPYKVARQNPSRLVVALDADKSRMEKISAKAAAKPAKGGLPNLLYLWATAERLPPLSGVGELHVLMPWGSLLRGVLGSSPEMLRGMAAVCRPGASFLVALNLHAWRPSVPEVGEHPEPTPDSADEWLAPRYAEAGWKLADCRYLEPEEVAGLETSWTRRLHSSRDRFDVLALTGTISP	.	"Specifically methylates the N(1) position of adenine 1408 in 16S rRNA. Confers resistance to various aminoglycosides, including kanamycin, neomycin and apramycin."	PDB: 3MQ2	.	KAMB_STRSD	Reviewed	.	.	.	.	.	.
Mol00749	Protein	16S rRNA (guanine(1405)-N(7))-methyltransferase (RMTA)	16S rRNA m7G1405 methyltransferase; Sisomicin-gentamicin resistance methylase Sgm	sgm	.	Micromonospora zionensis	1879	Micromonospora zionensis	Micromonospora	1873	Micromonosporaceae	28056	Micromonosporales	85008	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTAPAADDRIDEIERAITKSRRYQTVAPATVRRLARAALVAARGDVPDAVKRTKRGLHEIYGAFLPPSPPNYAALLRHLDSAVDAGDDEAVRAALLRAMSVHISTRERLPHLDEFYRELFRHLPRPNTLRDLACGLNPLAAPWMGLPAETVYIASDIDARLVGFVDEALTRLNVPHRTNVADLLEDRLDEPADVTLLLKTLPCLETQQRGSGWEVIDIVNSPNIVVTFPTKSLGQRSKGMFQNYSQSFESQARERSCRIQRLEIGNELIYVIQK	.	"Specifically methylates the N(7) position of guanine 1405 in 16S rRNA. Confers resistance to various aminoglycosides, including gentamicin, kanamycin and sisomicin."	PDB: 3LCU; PDB: 3LCV	.	SGM_MICZI	Reviewed	.	.	.	.	.	.
Mol00750	Protein	16S rRNA (guanine(1405)-N(7))-methyltransferase (RMTA)	16S rRNA m7G1405 methyltransferase	rmtA	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSFDDALASILSSKKYRSLCPDTVRRILDQEWGRHKSPKLAVEATRTRLHGICGAYVTPESLKAAAAALSVGDVQKALSLHASTKERLAELDCLYDFIFSGGVPHRVLDIACGLNPLALFIRDITSVWACDIHQGLGDVITPFAHHQGLDFTFALQDVMCTPPTETGDLALVFKLLPLLEREQAGAAMALLQALATPRIAVSFPTRSLGGRGKGMEANYSAWFEGALPDEFEIEDTKTIGIELVYMIKRNK	.	.	.	.	Q8GRA1_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00751	Protein	23S ribosomal RNA methyltransferase Erm (ERM39)	erm(39); 23S ribosomal RNA methyltransferase Erm	erm(39)	.	Mycobacterium fortuitum	1766	Mycolicibacterium fortuitum	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSSAHHGRHENGQNFLRDRRVVGDIIRMVSHTTGPIVEIGAGDGALTLPLQRLGRPLTAIEIDLHRARRLADRTTAEVVATDFLRYRLPRTPHVVVGNLPFHLTTAILRRLLHENGWTDATLLVQWEVARRRAGVGGATMMTAQWWPWFEFGLARKVSADAFRPRPSVDAGLLTIQRRAEPLLPWADHRAYQALVHRVFTGRGRGLAQILRPHVHPRWLSTNGIHPSALPRALTAQQWVALFEAAG	.	.	.	.	A0A481WX14_MYCFO	Unreviewed	.	.	.	.	.	.
Mol00752	Protein	23S ribosomal RNA methyltransferase Erm36 (ERM36)	ermML; erm36; 23S ribosomal RNA methyltransferase ErmML	ermML	.	Micrococcus luteus	1270	Micrococcus luteus	Micrococcus	1269	Micrococcaceae	1268	Micrococcales	85006	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MPTYRGGRHEHGQNFLTDHTTIDRLSRLVGDSTGPIVEIGPGQGRLTRELQKLGRSLTAVEIDSRLADRLASASQFREQKHVTVVNADFLHWPLPTTPYVVVGNVPFHLTTAILRRLLHDGAWTQVVLLVQWEVARRRAGIGGSSMMTAQWWPWIDFSLHGRVPRSAFKPAPSVDGGLLEMTRRPDPLLSPDARESYRQFVHDVFTSRGRGIGEILANVSSSLGKRGALQLLKSEGIRSSSLPKDLSAEQWARLFTSASPTKSAKTGRNAHPAHSARRQGR	.	.	.	.	Q8VQ13_MICLU	Unreviewed	.	.	.	.	.	.
Mol00753	Protein	23S rRNA (Adenine(2503)-C(8))-methyltransferase ClbA (CIBA)	KM843_02845; 8))-methyltransferase ClbA	KM843_02845	.	Bacillus amyloliquefaciens	1390	Bacillus amyloliquefaciens	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MQQKNKYIRIQEFLKQNKFPDFRMNQIKNAVFQGRINHFNEITVLPKSLRKLLIEEFGESILNIAPLKVQHSEQVTKVLFEISGDEKIETVNMKYKAGWESFCISSQCGCHFGCKFCATGDIGLKRNLTSDEMTDQILYFHLKGHSIDSISFMGMGEALANVQVFDALHVLTNPELFALSPRRLSISTIGIIPGIKKITQDYPQVNLTFSLHSPFNEQRSKLMPINERYPLLEVMDTLDEHIRVTSRKVYIAYIMLPGVNDSIDHANEVVNLLRSRYKRGNLFHVNIIRYNPTVSSPMRFEEVNEKQVVNFYKKLKSAGINVTVRSQFGIDIDAACGQLYGNYQKNKNQ	.	.	.	.	A0A8F0JTM7_9BACI	Unreviewed	.	.	.	.	.	.
Mol00754	Protein	23S rRNA (adenosine(1067)-2'-O)-methyltransferase (TSNR)	23S rRNA [AM1067] 2'-O-methyltransferase; 23S rRNA methylase; Thiostrepton-resistance methylase; rRNA (adenosine-2'-O)-methyltransferase	tsnR	.	Streptomyces laurentii	39478	Streptomyces laurentii	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MANLDVIVDRSDPAVQRIVDVTKHSRSVVRTVLIEDIEPLTQSIRAGVEFTEVYGLDTVPFPGDLLAACEKRGIRVRLLSAAVANQVFKTEKKPKVFGIAKVPPAGRFADLESLSGDVVLLDGVKIVGNIGAIVRTRSALGAAGIVLVDSGLGTIADRRLIRASRGYVFSLPIVLATRDEALAFFRDGGMRPVVFEADGKLSIGELDGIDERLVLVFGSEKTGPSGEFAGVATESVSIPMNPAAESLNVSVSAGIALHRRARRNLSRPRG	.	Specifically methylates the adenosine-1067 in 23S ribosomal RNA. Confers resistance to antibiotic thiostrepton.	.	.	TSNR_STRLU	Reviewed	.	.	.	.	.	.
Mol00755	Protein	23S rRNA (adenosine(1067)-2'-O)-methyltransferase (TSNR)	23S rRNA [AM1067] 2'-O-methyltransferase; 23S rRNA methylase; Thiostrepton-resistance methylase; rRNA (adenosine-2'-O)-methyltransferase; tsr	tsnR	.	Streptomyces azureus	146537	Streptomyces azureus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTELDTIANPSDPAVQRIIDVTKPSRSNIKTTLIEDVEPLMHSIAAGVEFIEVYGSDSSPFPSELLDLCGRQNIPVRLIDSSIVNQLFKGERKAKTFGIARVPRPARFGDIASRRGDVVVLDGVKIVGNIGAIVRTSLALGASGIILVDSDITSIADRRLQRASRGYVFSLPVVLSGREEAIAFIRDSGMQLMTLKADGDISVKELGDNPDRLALLFGSEKGGPSDLFEEASSASVSIPMMSQTESLNVSVSLGIALHERIDRNLAANR	.	Specifically methylates the adenosine-1067 in 23S ribosomal RNA. Confers resistance to antibiotic thiostrepton.	PDB: 3GYQ	.	TSNR_STRAJ	Reviewed	.	.	.	.	.	.
Mol00756	Protein	30S ribosomal protein S12 (RPSL)	rps12; Rv0682; MTV040.10	rpsL	45424644	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MPTIQQLVRKGRRDKISKVKTAALKGSPQRRGVCTRVYTTTPKKPNSALRKVARVKLTSQVEVTAYIPGEGHNLQEHSMVLVRGGRVKDLPGVRYKIIRGSLDTQGVKNRKQARSRYGAKKEKG	.	"Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity)."	.	.	RS12_MYCTU	Reviewed	.	.	.	.	.	.
Mol00757	Protein	AacA43 aminoglycoside (AACA43)	aacA43; 6') acetyltransferase	aacA43	.	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MIYNIINIADSEKNKEDAARILYSAFRGKGKDAWPTLDSAREEIAECIASPNICLGITLDDRLVGWGGLRPMYETTWELHPLVIDPDYQGNGLGRLLLSKIESTATTNRIIGIMLGTDDETLSTSLSMTDIDESNIFQEIKNIINIKNHPFEFYKKCGYIIVGIVPNANGYRKPDIWMWKNLEKKSG	.	.	.	.	F2WU95_KLEPN	Unreviewed	.	.	.	.	.	.
Mol00758	Protein	AADA2 protein (AADA2)	aadA2; Fragment	aadA2	.	Pseudomonas fluorescens	294	Pseudomonas fluorescens	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRVAVTIEISNQLSEVLSVIERHLESTLLAVHLYGSA	.	.	.	.	Q57405_PSEFL	Unreviewed	.	.	.	.	.	.
Mol00759	Protein	AADA9 protein (AADA9)	aadA9; AADA9 protein	aadA9	.	Corynebacterium glutamicum	1718	Corynebacterium glutamicum	Corynebacterium	1716	Corynebacteriaceae	1653	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSNSIHTGISRQLSQARDVIKRHLASTLKAIHLYGSAIDGGLKPYSDIDLLVTVDARLDEATRRSLMLDFLNISAPPCESSILRPLEVTVVACNEVVPWRYPARRELQFGEWLREDILEGVFEPAALDADLAILITKARQHSIALVGPVAQKVFMPVPEHDFLQVLSDTLKLWNTHEDWENEERNIVLTLARIWYSTETGGIVPKDVAAEWVLERLPAEHKPILVEARQAYLGLCKDSLALRADETSAFIGYAKSAVADLLEKRKSQTSHICDGAKNV	.	.	.	.	Q8VVI9_CORGT	Unreviewed	.	.	.	.	.	.
Mol00760	Protein	ABC superfamily ATP binding cassette transporter (ABCCT)	sal(A); ABC superfamily ATP binding cassette transporter	sal(A)	.	Staphylococcus sciuri	1296	Mammaliicoccus sciuri	Mammaliicoccus	2803850	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MLFLFEEKALEVEHKVLIPELTFSIEDHEHLAIVGVNGVGKSTLLKVIHQDQSVDSAMMEQDLTPYYDWTVMDYIIESYPEIAKIRLQLNHTDMINKYIELDGYIIEGEIVTEAKKLGIKEEQLEQKISTLSGGEQTKVSFLKVKMSKASLLLIDEPTNHMDLEMKEWLTKAFKQEQRAILFVSHDRTFLNETPDAILELSLDGAKKYIGKYDKYKQQKDIEHETLKLQYEKQQKEQAAIEETIKKYKAWYQKAEQSASVRSPYQQKQLSKLAKRFKSKEQQLNRKLDQEHIPNPHKKEKTFSIQHHNFKSHYLVQFNHVSFAYDNRKIFDDVSFYIKRNQNVIVEGRNGTGKSTLIKLILGELEPTKGDITVHPELEIGYFSQDFENLNMHHTVLDEILEIPEMKEADARTILASFYFDKDRINDVVETLSMGEKCRLQFVKLYFSNPHIMILDEPTNYFDIGMQENIIQLIQSFQGSVLIVSHDNYFKSQIKDQTWTIKNHQMTHENVQVKDPINTESMKHHLKELEQYTDERNRETEF	.	.	.	.	T1RRK4_MAMSC	Unreviewed	.	.	.	.	.	.
Mol00761	Protein	ABC transporter (ABCT)	pgh1; Fragment	pgh1	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFINSLAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGKLMSLKGDSENAKLSFEKYYPLMIRKSNIDVRDDGGIRINKNLIKGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFQDYQNNNNNSLVLKNVNEFSNQSGSAEDYTVFNNNGEILLDDINICDYNLRDLRNLFSIVSQ	.	.	.	.	G3LT32_PLAFA	Unreviewed	.	.	.	.	.	.
Mol00762	Protein	ABC transporter (ABCT)	msrE; msr(E); Macrolide efflux protein	msrE	64224022	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSLIIKARNIRLDYAGRDVLDIDELEIHSYDRIGLVGDNGAGKSSLLKVLNGEIVLAEATLQRFGDFAHISQLGGIEIETVEDRAMLSRLGVSNVQNDTMSGGEETRAKIAAAFSQQVHGILADEPTSHLDLNGIDLLIGQLKAFDGALLVISHDRYFLDMVVDKIWELKDGKITEYWGGYSDYLRQKEEERQHQAVEYELMMKERERLESAVQEKRQQANRLDNKKKGEKSKNSTESAGRLGHAKMTGTKQRKLYQAAKSMEKRLAALEDIQAPEHLRSIRFRQSSALELHNKFPITADGLSLKFGSRTIFDDANFIIPLGAKVAITGSNGTGKTSLLKMISERADGLTISPKAEIGYFTQTGYKFNTHKSVLSFMQEECEYTVAEIRAVLASMGIGANDIQKNLSDLSGGEIIKLLLSKMLLGKYNILLMDEPGNYLDLKSIAALETMMKSYAGTIIFVSHDKQLVDNIADIIYEIKDHKIIKTFERDC	.	.	.	.	F6M9M9_PASMD	Unreviewed	.	.	.	.	.	.
Mol00763	Protein	ABC transporter ATPase subunit (ABCS)	mel; yheS_2; yheS_3; ERS022181_01535; SAMEA3390019_00884; SAMEA3714416_01732; Mel; Mel efflux pump protein; Mel protein; Putative integrative and conjugative element protein; Ribose import ATP-binding protein rbsA; EC 3.6.3.17	mel	61401270	Streptococcus pneumoniae	1313	Streptococcus pneumoniae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MELILKAKDIRVEFKGRDVLDINELEVYDYDRIGLVGANGAGKSTLLRVLLGELTPPGCKMNRLGELAYIPQLDEVTLQEEKDFALVGKLGVEQLNIQTMSGGEETRLKIAQALSAQVHGILADEPTSHLDREGIDFLIGQLKYFTGALLVISHDRYFLDEIVDKIWELKDGKITEYWGNYSDYLRQKEEERKSQAAEYEQFIAERARLERAAEEKRKQARKIEQKAKGSSKKKSTEDGGRLAHQKSIGSKEKKMYNAAKTLEHRIAALGKVEAPEGIRRIRFRQSKALELHNPYPIVGAEINKVFGDKALFENASFQIPLGAKVALTGGNGIGKTTLIQMILNHEEGISISPKAKIGYFAQNGYKYNSNQNVMEFMQKDCDYNISEIRSVLASMGFKQNDIGKSLSVLSGGEIIKLLLAKMLMGRYNILIMDEPSNFLDIPSLEALEILMKEYTGTIVFITHDKRLLENVADVVYEIRDKKINLKH	.	.	.	.	Q93QE4_STREE	Unreviewed	.	.	.	.	.	.
Mol00764	Protein	ABC transporter ATP-binding protein (ABCP)	B1P95_04040; B4W81_01075; BU194_12630; DKP91_00610; DPX29_03150; DTPHA_1400158; GBM44_03070; GBM73_06715; A); Lsa family ABC-F type ribosomal protection protein	B1P95_04040	66453566	Enterococcus faecium	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MSKIEIKNLTFGYDSQGTLLFEQANLNFDTQWKLGLIGRNGRGKTTLLNILQNKLPYQGQVIHQQEFAYFPQQTKDKERLTYYVLNDITDFEIWEIERELQLMQTDPEILWREFSTLSGGEKTKVLLALLFVDDTHFPLIDEPTNHLDISGRKQVAAYLKKKKQGFIVVSHDRGFIDEVVDHVLAIEKSQLELYQGNFSIYEEQKKLRDEFEMAQNEKLKKEVSRLKKTAAEKAEWSRSREGDKTKKQVGFIDTESRRVNKGAVGADAARTMKRSKAIVNRMETQISEKEKLLKDIEYIDSLTMNSQASHHKRLLSVEDLQLGYENLLFEPIHFTIEPHQRVAISGPNGAGKSSIIHYLLGAFNGKVIGEKYQPKHLSISYASQNYEDNRGTLAEFAEKNQVDYQAFLNNLRKLGMERDVFHNKIEQMSMGQRKKVELAKSLSQPAELYTWDEPLNYLDVFNQEQLEQLILNVKPAMLLVEHDQTFLDKVSTEIISLERI	.	.	.	.	S5FVG4_ENTFC	Unreviewed	.	.	.	.	.	.
Mol00765	Protein	ABC transporter ATP-binding/permease protein YojI (YOJI)	yojJ; b2211; JW2199	yojI	946705	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MELLVLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITIAFVRLPELVQGIILTIGSAAYLWMLSGKMLLVTAIWMAITIWGGFVLVARVYKHMATLRETEDKLYTDFQTVLEGRKELTLNRERAEYVFNNLYIPDAQEYRHHIIRADTFHLSAVNWSNIMMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLTAQVAFNKLNKFALAPFKAEFPRPQAFPNWQTLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQLLGPEGKPANPQLVEKWLAQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVARTA	.	"Mediates resistance to the antibacterial peptide microcin J25, when expressed from a multicopy vector. Functions as an efflux pump for microcin J25, with the help of the outer membrane channel TolC."	.	.	YOJI_ECOLI	Reviewed	.	.	.	.	.	.
Mol00766	Protein	Tetracycline resistance protein class A (TETA)	tetA; TetA	tetA	.	Corynebacterium striatum	43770	Corynebacterium striatum	Corynebacterium	1716	Corynebacteriaceae	1653	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MKTYSWFVPPAPPADDPARLHPARWSSGNRVVRDMVGAYPGVLVLHILSYLIGSGISAFVPVVVGMIVDGLVGEEKFNAWWLFAVLVGIFIIQFIGEATGDGLATASVRRVTHNAQQHLSSGVLRRGAGAMSPGTVLNTIDADANTVGRYRELLSFPLMAIGYAVCAMVAMWSVSPWISLAIPASALIIALFAAWTAGPVTRVSLKRRAAEADVAGLATDASQGIRTVKGLGAGATVATRFHAETAKANGLMLTHLRVEVWLGFARFCVAWLCNLGIVGLSAWMTLRGEITPGQLTSVALLVQPALTMAGLAFGDLASGWGRAVASGQRIEQLHHAGDDAAGPEPTDTPVPGAGLWILEPAERSYATAAAWAQRADVLFPPHTVNVFEGTIADNVNPRGDVPEDVVKQALAAAHCQDILRRLGGINEAGELPDAPLGEAGLNLSGGQRQRVALARALAADPEVLILDDPTTGLDSVTQADVVAAVAALRADKTTVVITGNAAWQHAGTELEVA	.	.	.	.	Q9Z4Q1_CORST	Unreviewed	.	.	.	.	.	.
Mol00767	Protein	ABC transporter (ABCT)	AFR1; ABC-transporter	AFR1	.	Cryptococcus neoformans	5207	Cryptococcus neoformans	Cryptococcus	5206	Cryptococcaceae	1884633	Tremellales	5234	Tremellomycetes	155616	Basidiomycota	5204	Fungi	4751	.	MSATGVPAELNNLGAPITATTQNPSGLANSQVTSGPASSATQHDEHRSSAGNTLADEENDKAVESEKAEVIDAAADGKQKRLAADSSENIVTELEPHHVSIHRGKEEFAALERRYSTLSQQSQHELHRPTTRHSVRSSFSRKDRVVSRLTQDDAEKAKEGEGEFNLVDVLRSGRENQDEAGIKRKAVGVIWEDLEVIGAGGMRINIRNFSSAIIEQFMMPAFKILSIFGVNPFAPKPKAILHPSSGLLKPGEMCLVLGRPGAGCTTFLKTITNQRAGFMEIKGNVEYAGVGWKEMRKRYGGEVVYNQEDDDHLPTLTVAQTIRFAPATKTPKKKIPGVSAKQFQDDMLDLLLSMLNIKHTANTIVGNAYVRGVSGGERKRVSIAEMFCSGATVCSWDNSTRGLDASTALDYAKSLRLLTDIMGQTTFVSLYQAGEGIYDQFDKVLVLNEGHVAYFGPAKEARQYMIGLGYRDLPRQTTADYLSGCTDVNERRFADGRDETNVPATPEEMDKAYKESEVCARMTREREEYKQLMAEDATAREDFRQAVLEQKHKGVSKKSPYTVSFLQQVFIIFKRQLRLKFQDHFGISTGYATAIISALIVGSVYFRLPETASGAFTRGGLLFLGLLFNALTSFSELPSQMLGRSVLYRQNEYRFYRPAAFALAAVLADVPYNASVIFLFSIVLYFMGGLYSSGGAFFMFFLFVFLTFMVMSAFFRTLGVATSDYNVAARLASVLISFMVTYTGYMIPVQRMKRWLFWIFYLNPLSYGYEAIFANEFSRINLTCDSSYTIPRNIPEAGITGYPDTLGPNQMCSIFGSTPGDPNVSGSDYMATGYSYYKAHIWRNFGILLGFFAFFMFLQMLFIEVLEQGAKHFSINVYKKEDKDLKAKNERLAERLEAFRAGELEQDLSELKMRPEPFTWEVLNYTVPVPGGHRQLLNDIYGYVKPGSLTALMGASGAGKTTVLDVRASRKNIGVIEGDVLMNGRPIGTGFQRGCGYAEQQDTHEWTTTVREALRYSAYLRQPQHVPKQEKDDYVEDIIELLELQELADAMIGFPGYGLSVEARKRVTIGVELAAKPELLLFLDEPTSGLDGQSAYNIVRFLKKLCAAGQKILCTIHQPNALLFQSFDRLLLLQRGGECVYFGDIGPDSKVLIDYLERNGAKVPHDANPAEFMLEAIGAGSRKRIGSDWGEKWRNSPEFAEVKREIQELKAEALAKPVEEKSNRTEYATSFFFQLKTVLRRTNVALWRNADYQWTRLFAHLAIGLIVTLTFLQLDNSVQSLQYRVFAIFFATVLPALILAQIEPQYIMSRMTFNREASSKMYSSTVFALTQLLSEMPYSLGCAVSFFLLLYYGVGFPYASSRAGYFFLMILVTEVYAVTLGQAVAALSPTILIAALFNPFLLVLFSIFCGVTAPPPTLPYFWRKWMWPLDPFTRLISGLVSTVLQDQEVVCKDGEYQVFPAPSGQTCQQWAGAFAEAIGGYINNPDSTGDCQFCQYRTGQAFFTPLEISFSTRWRDFGIFICYVVFNILVLLIAARFLKWQRR	.	.	.	.	Q8X0Z3_CRYNE	Unreviewed	.	.	.	.	.	.
Mol00768	Protein	Alpha-enolase (ENO1)	2-phospho-D-glycerate hydro-lyase; C-myc promoter-binding protein; Enolase 1; MBP-1; MPB-1; Non-neural enolase; NNE; Phosphopyruvate hydratase; Plasminogen-binding protein; ENO1L1; MBPB1; MPB1	ENO1	2023	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000234590.10, ENO1-201, 1781; ENST00000647408.1, ENO1-216, 1782; ENST00000497492.1, ENO1-207, 647; ENST00000489867.2, ENO1-205, 637; ENST00000646156.1, ENO1-211, 622; ENST00000646660.1, ENO1-213, 581; ENST00000643438.1, ENO1-208, 569; ENST00000646906.1, ENO1-215, 548; ENST00000646370.2, ENO1-212, 1837; ENST00000646680.1, ENO1-214, 557; ENST00000414948.1, ENO1-202, 744; ENST00000645600.1, ENO1-209, 605; ENST00000464920.2, ENO1-203, 2548; ENST00000645609.1, ENO1-210, 1819; ENST00000492343.2, ENO1-206, 1247; ENST00000486051.5, ENO1-204, 536"	MSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK	chr1:8861000-8879190[-]	"Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production."	PDB: 2PSN; PDB: 3B97; PDB: 5JLZ; PDB: 5LAX; PDB: 5NI9; PDB: 5NIG; PDB: 5OCK	HGNC:3350	ENOA_HUMAN	Reviewed	ENSG00000074800	.	.	.	.	.
Mol00769	Protein	Alternative penicillin-binding protein 2a (MECD)	mecD; mec; CW686_07055; PBP2a family beta-lactam-resistant peptidoglycan transpeptidase MecD	mecD	.	Macrococcus caseolyticus	69966	Macrococcus caseolyticus	Macrococcus	69965	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKNIKVKILIVCSLCLISFFLYNLLKENEIDKIFSSIENRNVDEINENITFLSRNTFSKKQRYDRMNHIDNSLGIKKVNITDIKLLEEIVDTRKYSANMHYDSKFGKFTKKGYFEFEKNGESKRWELNWTPEVIIPGLTATNEVRVEELKSSRGEIVDRNGIPLAIDGEHYQVGIDPKNYNKKDSKQIAKLLNINESTLKNKLKQSWVKDGVFVPIKSYVELSDEIKNKIPEYGLSVNKIKGRTYPLKEASAHLLGYIGEINADELNDPKFKGYDSHSIVGKTGIEYMYDKELQNRDGLIVYITDDDGLTDSKEILVHKKPKNGKKIVLSIDSRVQNSIYNHLKDDNGSGTAMNPKTGELLALVSYPSFNPYDFMFGISNKKYQALLNDKKAPLLNKFQELTSPGSTQKLLTSIIGLNNGVINESKSYEINGKGWRKDGSWGGYKVTRFEVVNGRIDLEKAIAHSDNIFFARTTLEMGGKKFVRGMKDLGVGEETPSDYPVRTGQIANKINLERNLNNDILLADSGYGQGEILVNPIHILSIYSSLVNEGNMMAPKLNMEHKSKVWKKHITSQKNIDILTSSMRKVVTGTHKLDTERNYANFAGKTGTAELKMTQNEGLGTQIGWFVGYDQQNPNMMLAINVKNVEDKGMSSYNAQKFAQVMDDLYEHGARTYEPDSE	.	.	.	.	A0A1S7BGS4_9STAP	Unreviewed	.	.	.	.	.	.
Mol00770	Protein	Aminocyclitol acetyltransferase ApmA (APMA)	apmA; Aminocyclitol acetyltransferase ApmA	apmA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKTRLEQVLERYLNGREVAVWGVPTRRLLRALKPFKFHTADRVDPQYHYVVAVTDDDLTDFLSDEQSKSFQYANDYLTFDDEGGELPFERMCFNVPVGRQTYFGDGVVGACENGYIKSIGQFTSINGTAEIHANHQLNMTFVSDDIQNFFNEESMAVFQEKLRKDPKHPYAYSKEPMTIGSDVYIGAHAFINASTVTSIGDGAIIGSGAVVLENVPPFAVVVGVPARIKRYRFSKEMIETLLRVKWWDWSIEEINENVDALISPELFMKKYGSL	.	.	PDB: 7JM0; PDB: 7JM1; PDB: 7JM2	.	A0A1D0AST6_STAAU	Unreviewed	.	.	.	.	.	.
Mol00771	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	Aminoglycoside 3''-adenylyltransferase; AAD(3'') (9) adenylyltransferase; Streptomycin 3''-adenylyltransferase	aadA	31892376	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MREAVIAEVSTQLSEVVGVIERHLEPTLLAVHLYGSAVDGGLKPHSDIDLLVTVTVRLDETTRRALINDLLETSASPGESEILRAVEVTIVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPATIDIDLAILLTKAREHSVALVGPAAEELFDPVPEQDLFEALNETLTLWNSPPDWAGDERNVVLTLSRIWYSAVTGKIAPKDVAADWAMERLPAQYQPVILEARQAYLGQEEDRLASRADQLEEFVHYVKGEITKVVGK	.	Mediates bacterial resistance to the antibiotics streptomycin and spectinomycin.	.	.	S3AD_ECOLX	Reviewed	.	.	.	.	.	.
Mol00772	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	aadA; APX88_23745; APX88_23750; DAH22_24350; GFY34_19935; GFY34_26370; IT029_005230; IT029_005519	aadA7	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSEKVPAEISVQLSQALNVIGRHLESTLLAVHLYGSALDGGLKPYSDIDLLVTVAAPLNDAVRQALLVDLLEVSASPGQNKALRALEVTIVVHSDIVPWRYPARRELQFGEWQRKDILAGIFEPATTDSDLAILLTKAKQHSVVLAGSAAKDLFSSVPESDLFKALADTLKLWNSPPDWAGDERNVVLTLSRIWYTAATGKIAPKDVAATWAMARLPAQHQPILLNAKRAYLGQEEDYLPARADQVAALIKFVKYEAVKLLGASQ	.	.	.	.	Q9L799_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00773	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	.	aadA21	.	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRVAVTIEISNQLSEVLSVIERHLESTLLAVHLYGSAVDGGLKPYSDIDLLVTVTVRLDETTRRALINDLLETSASPGESEILRAVEVTIVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPATIDIDLAILLTKAREHSVALVGPAAEELFDPVPEQDLFEALNETLTLWNSPPDWAGDERNVVLTLSRIWYSAVTGKIAPKDVARDWAMERLPAQYQPVILEARQAYLGQEEDRLASRADQLEEFVHYVKGEITKVVGK	.	.	.	.	Q8GCH1_SALTM	Unreviewed	.	.	.	.	.	.
Mol00774	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	aadA; aadA1b; aadA1d; aadA2; aadAI; BO068_004688; BO068_005462; BON66_04400; BON68_01140; BON70_24900; BON72_22960; BON94_27315; BTQ06_25060; CQP61_00015; DAH50_23555; DKP82_26115; GF147_27240; GF147_27245; GQW07_24995; GQW07_26760; GQW07_26780; GRO95_25260; GRO95_26815; GRO95_26835; pO103_87	aadA1	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MREAVIAEVSTQLSEVVGVIERHLEPTLLAVHLYGSAVDGGLKPHSDIDLLVTVTVRLDETTRRALINDLLETSASPGESEILRAVEVTIVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPATIDIDLAILLTKAREHSVALVGPAAEELFDPVPEQDLFEALNETLTLWNSPPDWAGDERNVVLTLSRIWYSAVTGRIAPKDVAADWAMERLPAQYQPVILEARQAYLGQEEDRLASRADQLEEFVHYVKGEITKVVGK	.	.	.	.	Q79JG0_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00775	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	.	aadA1	31892376	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MREAVIAEVSTQLSEVVGVIERHLEPTLLAVHLYGSAVDGGLKPHSDIDLLVTVTVRLDETTRRALINDLLETSASPGESEILRAVEVTIVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPATIDIDLAILLTKAREHSVALVGPAAEELFDPVPEQDLFEALNETLTLWNSPPDWAGDERNVVLTLSRIWYSAVTGKIAPKDVAADWAMERLPAQYQPVILEARQAYLGQEEDRLASRADQLEEFVHYVKGEITKVVGK	.	.	.	.	Q6YLY2_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00776	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	.	aadA14	.	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTNKPPESIAEQVSEARSILENHLETIQAIHLFGSAVDGGLKPFSDIDLLVTVGTPLNESTRAALMSDLLAVSAFPGTDSKRRALEVTVLTQEDVVPWRYPAKRQMQFGEWLRDDINARIFEPALMDHDLAILLTKVRRHSVALYGPAAHEFFDEIPVVDVQRSLLETLTLWTTEADWKGDERNIVLALVRIWYTAMTGEITSKVAAADWALQRLPREIKSVVIAARDAYLGLEAADLAAYPKERADLRNHIHSSVTAKLQ	.	.	.	.	Q5DUB9_PASMD	Unreviewed	.	.	.	.	.	.
Mol00777	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	aadA; aadA1; aadA2a; aadA_2; ant1_1; ant1_2; AOY10_00066; BANRA_05017; BANRA_05549; BGZ_05257; BGZ_05467; ExPECSC038_05202; JFD_05362; NDM1Dok01_N0149; SAMEA3472044_03633; SAMEA3472056_05572; SAMEA3472080_04508; TUM18780_18820	aadA2	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTIEISNQLSEVLSVIERHLESTLLAVHLYGSAVDGGLKPYSDIDLLVTVAVKLDETTRRALLNDLMEASAFPGESETLRAIEVTLVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPAMIDIDLAILLTKAREHSVALVGPAAEEFFDPVPEQDLFEALRETLKLWNSQPDWAGDERNVVLTLSRIWYSAITGKIAPKDVAADWAIKRLPAQYQPVLLEAKQAYLGQKEDHLASRADHLEEFIRFVKGEIIKSVGK	.	.	.	.	Q51348_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00778	Protein	Aminoglycoside (AADB)	aadB; pRCADGH-2_024; 2') adenyltransferase	aadB	67369350	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MDTTQVTLIHKILAAADERNLPLWIGGGWAIDARLGRVTRKHDDIDLTFPGERRGELEAIVEMLGGRVMEELDYGFLAEIGDELLDCEPAWWADEAYEIAEAPQGSCPEAAEGVIAGRPVRCNSWEAIIWDYFYYADEVPPVDWPTKHIESYRLACTSLGAEKVEVLRAAFRSRYAA	.	.	.	.	A0A1X9ZE10_PASMD	Unreviewed	.	.	.	.	.	.
Mol00779	Protein	Aminoglycoside 2'-N-acetyltransferase (A2NA)	AAC(2')-Ia	aac	.	Providencia stuartii	588	Providencia stuartii	Providencia	586	Morganellaceae	1903414	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MGIEYRSLHTSQLTLSEKEALYDLLIEGFEGDFSHDDFAHTLGGMHVMAFDQQKLVGHVAIIQRHMALDNTPISVGYVEAMVVEQSYRRQGIGRQLMLQTNKIIASCYQLGLLSASDDGQKLYHSVGWQIWKGKLFELKQGSYIRSIEEEGGVMGWKADGEVDFTASLYCDFRGGDQW	.	Catalyzes the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. It confers resistance to aminoglycosides.	PDB: 5US1; PDB: 6VOU; PDB: 6VR2; PDB: 6VR3; PDB: 6VTA; PDB: 7JZS	.	AAC2_PROST	Reviewed	.	.	.	.	.	.
Mol00780	Protein	Aminoglycoside 2'-N-acetyltransferase (A2NA)	AAC(2')-Id; MSMEG_0434; MSMEI_0423	aac	66738619	Mycolicibacterium smegmatis	1772	Mycolicibacterium smegmatis	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MLTQHVSEARTRGAIHTARLIHTSDLDQETRDGARRMVIEAFRDPSGDSDFTDDFTDDDWDHALGGMHALISHHGALIAHGAVVQRRLMYRGPDGRGHALRCGYVEAVAVREDRRGDGLGTAVLDALEQVIRGAYQIGALSASDIARPMYIARGWLSWEGPTSVLTPTEGIVRTPEDDRSLFVLPVDLPDGLELDTAREITCDWRSGDPW	.	Catalyzes the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. It confers resistance to aminoglycosides.	PDB: 7CRM; PDB: 7CS0; PDB: 7CS1; PDB: 7CSI; PDB: 7CSJ	.	AAC2_MYCS2	Reviewed	.	.	.	.	.	.
Mol00781	Protein	Aminoglycoside 2'-N-acetyltransferase (A2NA)	AAC(2')-Ib	aac	29426913	Mycolicibacterium fortuitum	1766	Mycolicibacterium fortuitum	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MPFQDVSAPVRGGILHTARLVHTSDLDQETREGARRMVIEAFEGDFSDADWEHALGGMHAFICHHGALIAHAAVVQRRLLYRDTALRCGYVEAVAVREDWRGQGLATAVMDAVEQVLRGAYQLGALSASDTARGMYLSRGWLPWQGPTSVLQPAGVTRTPEDDEGLFVLPVGLPAGMELDTTAEITCDWRDGDVW	.	"Confers resistance to gentamicin, tobramycin, dibekacin, netilmicin, and 6'-N-ethylnetilmicin."	.	.	AAC2_MYCFO	Reviewed	.	.	.	.	.	.
Mol00782	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	C2800_11465	strA	60604314	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNRTNIFFGESHSDWLPVRGGESGDFVFRRGDGHAFAKIAPASRRGELAGERDRLIWLKGRGVACPEVINWQEEQEGACLVITAIPGVPAADLSGADLLKAWPSMGQQLGAVHSLSVDQCPFERRLSRMFGRAVDVVSRNAVNPDFLPDEDKSTPQLDLLARVERELPVRLDQERTDMVVCHGDPCMPNFMVDPKTLQCTGLIDLGRLGTADRYADLALMIANAEENWAAPDEAERAFAVLFNVLGIEAPDRERLAFYLRLDPLTWG	.	.	.	.	Q79C26_PASMD	Unreviewed	.	.	.	.	.	.
Mol00783	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	APH(3'); Kanamycin kinase; Ribostamycin phosphotransferase	rph	.	Streptomyces ribosidificus	80859	Streptomyces ribosidificus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MESTLRRTYPHHTWHLVNEGDSGAFVYRLTGHGPELYAKIAPRTPENSAFHLDGEADRLDWLARHGISVPRVVERGADDTTAWLVTEAVPGAAASEEWPEDERAAVVDAIAEMARTLHELPVSECPFDRRLDVTGEARHNVREGLVDLDDLQEEPAGWTGDQLLAELDLTRPEKEDLVVCHGDLCPNNVLLDPETHRITGLIDVGRLRLATCHADLALAARELAIDEDPWFGPAYAERFLERYGAHHVDQEKMAFYQLLDEFF	.	"Resistance to kanamycin and structurally-related aminoglycosides, including amikacin."	.	.	KKA9_STRRI	Reviewed	.	.	.	.	.	.
Mol00784	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	APH(3')VII; Kanamycin kinase; type VII; Neomycin-kanamycin phosphotransferase type VII	aphA-7	.	Campylobacter jejuni	197	Campylobacter jejuni	Campylobacter	194	Campylobacteraceae	72294	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MKYIDEIQILGKCSEGMSPAEVYKCQLKNTVCYLKKIDDIFSKTTYSVKREAEMMMWLSDKLKVPDVIEYGVREHSEYLIMSELRGKHIDCFIDHPIKYIECLVNALHQLQAIDIRNCPFSSKIDVRLKELKYLLDNRIADIDVSNWEDTTEFDDPMTLYQWLCENQPQEELCLSHGDMSANFFVSHDGIYFYDLARCGVADKWLDIAFCVREIREYYPDSDYEKFFFNMLGLEPDYKKINYYILLDEMF	.	"Resistance to kanamycin and structurally-related aminoglycosides, including amikacin."	.	.	KKA7_CAMJU	Reviewed	.	.	.	.	.	.
Mol00785	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	APH(3')VI; Kanamycin kinase; type VI; Neomycin-kanamycin phosphotransferase type VI	aphA-6	.	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MELPNIIQQFIGNSVLEPNKIGQSPSDVYSFNRNNETFFLKRSSTLYTETTYSVSREAKMLSWLSEKLKVPELIMTFQDEQFEFMITKAINAKPISALFLTDQELLAIYKEALNLLNSIAIIDCPFISNIDHRLKESKFFIDNQLLDDIDQDDFDTELWGDHKTYLSLWNELTETRVEERLVFSHGDITDSNIFIDKFNEIYFLDLGRAGLADEFVDISFVERCLREDASEETAKIFLKHLKNDRPDKRNYFLKLDELN	.	"Resistance to kanamycin and structurally-related aminoglycosides, including amikacin."	.	.	KKA6_ACIBA	Reviewed	.	.	.	.	.	.
Mol00786	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	APH(3')IV; Butirosin resistance protein A; Kanamycin kinase; type IV; Neomycin-kanamycin phosphotransferase type IV; aph; butA	aphA4	.	Bacillus circulans	1397	Niallia circulans	Niallia	2837506	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNESTRNWPEELLELLGQTELTVNKIGYSGDHVYHVKEYRGTPAFLKIAPSVWWRTLRPEIEALAWLDGKLPVPKILYTAEHGGMDYLLMEALGGKDGSHETIQAKRKLFVKLYAEGLRSVHGLDIRECPLSNGLEKKLRDAKRIVDESLVDPADIKEEYDCTPEELYGLLLESKPVTEDLVFAHGDYCAPNLIIDGEKLSGFIDLGRAGVADRYQDISLAIRSLRHDYGDDRYKALFLELYGLDGLDEDKVRYYIRLDEFF	.	"Resistance to butirosin and structurally-related aminoglycosides, including kanamycin and amikacin."	.	.	KKA4_NIACI	Reviewed	.	.	.	.	.	.
Mol00787	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	APH(3')III; Kanamycin kinase; type III; Neomycin-kanamycin phosphotransferase type III	aphA	63968956	Streptococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MAKMRISPELKKLIEKYRCVKDTEGMSPAKVYKLVGENENLYLKMTDSRYKGTTYDVEREKDMMLWLEGKLPVPKVLHFERHDGWSNLLMSEADGVLCSEEYEDEQSPEKIIELYAECIRLFHSIDISDCPYTNSLDSRLAELDYLLNNDLADVDCENWEEDTPFKDPRELYDFLKTEKPEEELVFSHGDLGDSNIFVKDGKVSGFIDLGRSGRADKWYDIAFCVRSIREDIGEEQYVELFFDLLGIKPDWEKIKYYILLDELF	.	"Resistance to kanamycin and structurally-related aminoglycosides, including amikacin."	PDB: 1J7I; PDB: 1J7L; PDB: 1J7U; PDB: 1L8T; PDB: 2B0Q; PDB: 2BKK; PDB: 3Q2J; PDB: 3TM0	.	KKA3_ENTFL	Reviewed	.	.	.	.	.	.
Mol00788	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	APH(3')-II; APH(3')II; Kanamycin kinase; type II; Neomycin-kanamycin phosphotransferase type II; kan; nptII	neo	61686716	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MIEQDGLHAGSPAAWVERLFGYDWAQQTIGCSDAAVFRLSAQGRPVLFVKTDLSGALNELQDEAARLSWLATTGVPCAAVLDVVTEAGRDWLLLGEVPGQDLLSSHLAPAEKVSIMADAMRRLHTLDPATCPFDHQAKHRIERARTRMEAGLVDQDDLDEEHQGLAPAELFARLKARMPDGEDLVVTHGDACLPNIMVENGRFSGFIDCGRLGVADRYQDIALATRDIAEELGGEWADRFLVLYGIAAPDSQRIAFYRLLDEFF	.	"Resistance to kanamycin, neomycin, paromomycin, ribostamycin, butirosin and gentamicin B."	PDB: 1ND4	.	KKA2_KLEPN	Reviewed	.	.	.	.	.	.
Mol00789	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	.	aph(3')-IIc	.	Stenotrophomonas maltophilia	40324	Stenotrophomonas maltophilia	Stenotrophomonas	40323	Xanthomonadaceae	32033	Xanthomonadales	135614	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MEASNPFTDGLRLPRAWQEALADAHIERQSIGVSRADVARVHRPGQTDAFLKSEVIDAFSELGDEIARLRWLQAQGQSAPTVIATTEEGGRRWLLMSALPGRDLASSPELAPRRVAELLADALRGLHAVPVANCPFDQQLASRLQAAQARVEAGLVDADDFDDERLGQSPQQVFAELRATRPAHEDLVVSQGDACLPNLTVTDGRFTGFIDCGRLGVADRYQDLALAARSLVHNFGESRCVAALFQRYGAVPDERRLAFYRLLDEFF	.	.	.	.	E5LCR3_STEMA	Unreviewed	.	.	.	.	.	.
Mol00790	Protein	Aminoglycoside 6-adenylyltransferase (A6AD)	6-O-adenyl-transferase; AAD(6); ANT(6); Aminoglycoside inactivating enzyme; Sm inactivating enzyme; Streptomycin 6-adenylyltransferase; BSU26790; HIR78_15755	aadK	938061	Bacillus subtilis	1423	Bacillus subtilis	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MRSEQEMMDIFLDFALNDERIRLVTLEGSRTNRNIPPDNFQDYDISYFVTDVESFKENDQWLEIFGKRIMMQKPEDMELFPPELGNWFSYIILFEDGNKLDLTLIPIREAEDYFANNDGLVKVLLDKDSFINYKVTPNDRQYWIKRPTAREFDDCCNEFWMVSTYVVKGLARNEILFAIDHLNEIVRPNLLRMMAWHIASQKGYSFSMGKNYKFMKRYLSNKEWEELMSTYSVNGYQEMWKSLFTCYALFRKYSKAVSEGLAYKYPDYDEGITKYTEGIYCSVK	.	"Mediates bacterial resistance to streptomycin. Adenylates streptomycin on the O-6 residue. Adenylates streptidine on the O-6 residue. Does not act on spectinomycin, neomycin-B or kanamycin (Ref.5984036). Specific for ATP and GTP nucleotides incorporating a purine ring. No reaction with CTP or UTP."	PDB: 2PBE	.	AADK_BACSU	Reviewed	.	.	.	.	.	.
Mol00791	Protein	Aminoglycoside acetyltransferase (AAC)	aac(6')-Im; Aminoglycoside acetyltransferase	aac(6')-Im	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MLEKKRVSFRPMNEDDLVLMLKWLTDDRVLEFYDGRDKKHTQKTIREHYTEQWADEIYRVIIEYDTIPIGYAQIYRIQGELFDEYNYHETEEKIYAMDQFIGEPEYWNMGIGAEYCRVVCQYLRTEMDADAVILDPRKNNLRAVRAYQKAGFKIIKELPEHELHEGKKEDCVLMEWRV	.	.	PDB: 6BFF; PDB: 6BFH	.	Q93ET8_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00792	Protein	Aminoglycoside acetyltransferase (AAC)	aac(3)-Id; Aminoglycoside acetyltransferase	aac(3)-Id	.	Vibrio fluvialis	676	Vibrio fluvialis	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSVEIIHLTGNDVALLQSINAMFGEAFNDQDSYARNKPSSSYLQKLLSTSSFIALAAVDEQKVIGAIAAYELQKFEQQRSEIYIYDLAVAATRRREGIATALIKKLKAIGAARGAYVIYVQADKGVEDQPAIELYKKLGTIEDVFHFDIAVEQSKNHA	.	.	.	.	Q766H0_VIBFL	Unreviewed	.	.	.	.	.	.
Mol00793	Protein	Aminoglycoside adenyltransferase 2''-Ia (ANT2I)	AAD(2''); Aminoglycoside adenyltransferase 2''-Ia; ANT(2'')-Ia; Gentamicin 2''-nucleotidyltransferase; Gentamicin resistance protein	aadB	67369350	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MDTTQVTLIHKILAAADERNLPLWIGGGWAIDARLGRVTRKHDDIDLTFPGERRGELEAIVEMLGGRVMEELDYGFLAEIGDELLDCEPAWWADEAYEIAEAPQGSCPEAAEGVIAGRPVRCNSWEAIIWDYFYYADEVPPVDWPTKHIESYRLACTSLGAEKVEVLRAAFRSRYAA	.	"Mediates bacterial resistance to kanamycin, gentamicin, dibekacin, sisomicin and tobramycin by adenylating the 2''-hydroxyl group of these antibiotics."	PDB: 4WQK; PDB: 4WQL; PDB: 5KQJ	.	AADB1_KLEPN	Reviewed	.	.	.	.	.	.
Mol00794	Protein	Aminoglycoside adenylyltransferase (AAD5)	aadA5; Aminoglycoside adenylyltransferase	aadA5	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MLDLLKVSSPPGDGGTWRPLELTVVARSEVVPWRYPARRELQFGEWLRHDILSGTFEPAVLDHDLAILLTKARQHSLALLGPSAATFFEPVPKEHFSKALFDTIAQWNAESDWKGDERNVVLALARIWYSASTGLIAPKDVAAAWVSERLPAEHRPLICKARAAYLGSEDDDLAMRVEETAAFVRYAKATIERILRCAARAASASTPWRGHRSHRSAFKRRGSAVRSNMS	.	.	.	.	A0A896ZCC3_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00795	Protein	Aminoglycoside N(3)-acetyltransferase (A3AC)	yokD_2; NCTC13033_06639	kan	6215660	Streptomyces griseus	1911	Streptomyces griseus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MDETELLRRSDGPVTRDRIRHDLAALGLVPGDTVMFHTRLSAIGYVSGGPQTVIDALLDVVGPTGTLLVTCGWNDAPPYDFTDWPPAWQEAVRAHHPAFDPRTSEAEHANGRLPEALRRRPGAVRSRHPDVSLAALGASAPALMDAHPWDDPHGPGSPLARLVALGGRVLLLGAPRDTMTLLHHAEALAQAPGKRFVTYEQPIEVAGERVWRTFRDIDSEHGAFDYSSAVPEGQDPFAVIVGSMLAAGIGREGFVGAARSRLFDAAPAVEFGVRWIEEHLNRDR	.	.	PDB: 7LAP	.	Q54216_STRGR	Unreviewed	.	.	.	.	.	.
Mol00796	Protein	Aminoglycoside N(3)-acetyltransferase (A3AC)	.	aac	.	Enterobacter cloacae	550	Enterobacter cloacae	Enterobacter	547	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTDPRKNGDLHEPATAPATPWSKSELVRQLRDLGVRSGDMVMPHVSLRAVGPLADGPQTLVDALIEAVGPTGNILAFVSWRDSPYEQTLGHDAPPAAIAQSWPAFDPDHAPAYPGFGAINEFIRTYPGCRRTAHPDASMAAIGPDAAWLVAPHEMGAAYGPRSPIARFLAHAGKILSIGAGPDAVTALHYAEAVARIEGKRRVTYSMPLLREGKRVWVTTSDWDSNGILDEYAAPDGPDAVERIARDYLARTRVAQGPVGGAQSRLIDAADIVSFGIEWLEARHAAPAAAALKPKQRRD	.	"Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin."	PDB: 6BBR; PDB: 6BBZ; PDB: 6BC2; PDB: 6BC3; PDB: 6BC4; PDB: 6BC5; PDB: 6BC6; PDB: 6BC7; PDB: 6NP1; PDB: 6NP2; PDB: 6NP3; PDB: 6NP4; PDB: 6NP5; PDB: 6O5U	.	Q47030_ENTCL	Unreviewed	.	.	.	.	.	.
Mol00797	Protein	Aminoglycoside N(3)-acetyltransferase (A3AC)	aac(3); aac(3)-IV; aac(3)-IVa; aac(3)IV; aac3-VI; BJJ90_27515; BMC79_004910; BMC79_005421; BVL39_27730; BZL69_29365; CDC27_25895; CR538_26885; CWS33_26775; D0X26_29340; D9D77_25705; D9D77_28900; D9E49_23800; D9E49_28790; E4K51_25065; F3N40_24255; F3N40_27730; GTP88_26100; GTP88_26800; HNC66_26125; HNC66_27870; HND12_28675; HND12_30655; HVX16_26725; J0541_005607; J0541_005921; pEC012_00026; SAMEA3472080_05397	aacC4	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MQYEWRKAELIGQLLNLGVTPGGVLLVHSSFRSVRPLEDGPLGLIEALRAALGPGGTLVMPSWSGLDDEPFDPATSPVTPDLGVVSDTFWRLPNVKRSAHPFAFAAAGPQAEQIISDPLPLPPHSPASPVARVHELDGQVLLLGVGHDANTTLHLAELMAKVPYGVPRHCTILQDGKLVRVDYLENDHCCERFALADRWLKEKSLQKEGPVGHAFARLIRSRDIVATALGQLGRDPLIFLHPPEAGCEECDAARQSIG	.	"Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin."	PDB: 6MN3; PDB: 6MN4; PDB: 6MN5	.	Q306W4_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00798	Protein	Aminoglycoside N(3)-acetyltransferase III (A3AC3)	ACC(3)-III; Aminocyclitol 3-N-acetyltransferase type III; Gentamicin-(3)-N-acetyl-transferase	aac3-Vb	.	Serratia marcescens	1823	Nocardia otitidiscaviarum	Nocardia	1817	Nocardiaceae	85025	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MNTIESITADLHGLGVRPGDLIMVHASLKAVGPVEGGAASVVSALRAAVGSAGTLMGYASWDRSPYEETLNGARMDEELRRRWPPFDLATSGTYPGFGLLNRFLLEAPDARRSAHPDASMVAVGPLAATLTEPHRLGQALGEGSPLERFVGHGGKVLLLGAPLDSVTVLHYAEAIAPIPNKRRVTYEMPMLGPDGRVRWELAEDFDSNGILDCFAVDGKPDAVETIAKAYVELGRHREGIVGRAPSYLFEAQDIVSFGVTYLEQHFGAP	.	"Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin."	PDB: 7LAO	.	AAC3_SERMA	Reviewed	.	.	.	.	.	.
Mol00799	Protein	Aminoglycoside N(3)-acetyltransferase IX (A3AC9)	ACC(3)-IX; Aminocyclitol 3-N-acetyltransferase type IX	aacC9	.	Micromonospora chalcea	1874	Micromonospora chalcea	Micromonospora	1873	Micromonosporaceae	28056	Micromonosporales	85008	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MEEMSLLNHSGGPVTRSRIKHDLADLGLKDGDVVIFHTRMSAIGYVAGGTQTIIGALLDVVGARGTLMVPCGWNNAPPYDFLDWPRDWQDALRAEHPAYDPDLSEADYNNGRLPEALPRWPGAIRSRHPDASFAALGPAAAELMAEHPWDHPHGPDTPLARLIAHSGRVLLLGAPLDTMTLLHHAEALADVRSKRFVTYEQPILVNGQRVWRQFRDIDSEEGAFDYSTVRRGVEPFEAIARDMLSAGIGRQGRVGAADSYLFDAGPVFNFAINWIEAKLKR	.	Resistance to neomycin.	.	.	AACC9_MICCH	Reviewed	.	.	.	.	.	.
Mol00800	Protein	Aminoglycoside N(3)-acetyltransferase VIII (A3AC8)	ACC(3)-VIII; Aminocyclitol 3-N-acetyltransferase type VIII	aacC8	.	Streptomyces fradiae	1906	Streptomyces fradiae	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MDEKELIERAGGPVTRGRLVRDLEALGVGAGDTVMVHTRMSAIGYVVGGPQTVIDAVRDAVGADGTLMAYCGWNDAPPYDLAEWPPAWREAARAEWPAYDPLLSEADRGNGRVPEALRHQPGAVRSRHPDASFVAVGPAAHPLMDDHPWDDPHGPDSPLARLAGAGGRVLLLGAPLDTLTLLHHAEARAEAPGKRFVAYEQPVTVGGRRVWRRFRDVDTSRGVPYGRVVPEGVVPFTVIAQDMLAAGIGRTGRVAAAPVHLFEAADVVRFGVEWIESRMGGAAGGA	.	Resistance to neomycin.	.	.	AACC8_STRFR	Reviewed	.	.	.	.	.	.
Mol00801	Protein	Aminoglycoside N(6')-acetyltransferase type 1 (A6AC1)	Aminoglycoside resistance protein	aac(6')	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSKLGPTKPAPSMANTPVGNVVPCKTPDHPGWLELRLQLWPDGSTEEFLPEMAAACAEPDRFGQFLFLSPGGLAEGLVEVALRTDYVNGTESSPVAFLEGVFVVPASRGLGIARALVAAAEGWARDRGCTEFASDAEVSNVGSHAMHAALGFVETERVVFFRKVVAP	.	.	.	.	S6CFI8_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00802	Protein	Aminoglycoside phosphotransferase (APH)	aph(2')-Ib; Aminoglycoside phosphotransferase	aph(2')-Ib	.	Enterococcus faecium	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MVNLDAEIYEHLNKQIKINELRYLSSGDDSDTFLCNEQYVVKVPKRDSVRISQKREFELYRFLENCKLSYQIPAVVYQSDRFNIMKYIKGERITYEQYHKLSEKEKDALAYDEATFLKELHSIEIDCSVSLFSDALVNKKDKFLQDKKLLISILEKEQLLTDEMLEHIETIYENILNNAVLFKYTPCLVHNDFSANNMIFRNNRLFGVIDFGDFNVGDPDNDFLCLLDCSTDDFGKEFGRKVLKYYQHKAPEVAERKAELNDVYWSIDQIIYGYERKDREMLIKGVSELLQTQAEMFIF	.	.	PDB: 3HAM; PDB: 3HAV	.	Q9EVD7_ENTFC	Unreviewed	.	.	.	.	.	.
Mol00803	Protein	ARE-ABC-F family resistance factor PoxtA (POXTA)	poxtA; ARE-ABC-F family resistance factor PoxtA	poxtA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKGKNMNLAFGLEEIYEDAEFQIGDLDKVGIVGVNGAGKTTLFRLLLGELELDNGSLTSGNARIGYLPQEIVLEDEDITVWDFLFEGRPIKKYEQELEEIYKKLETAVNAEQEALLARMGTLQERLEYFDFYEAETILLEFADKMSIDAELYHRPMRELSGGQKSKMAFARLLYSKPEILLLDEPTNHLDVSTKDFVIKYLKNYRGSVLIISHDIDFLNRIINKIMYINKATHKISVYDGDYYIYKKKYAEEQRIREMAIVQQEKEIKELSDFVQKAKQASQTNHHLKRMGQERALRLDKKRGELQKRNRLYKRVKMDIRPKREGAQVPLEVENITFHYSGYPTLYQNLSFQINGRERFLVVGENGVGKSTLLKLMMGILSPDEGCIRFNQKTDIAYYAQELEQLDENKTVIDNVESEGYTPWQIRAVLSNFLFYDDDVNKKVSVLSPGEKARVALCKILLQKANLLILDEPTNHLDPETQKIIGGNFNLFEGTIIAVSHNPSFVEQIGISRMLILPSGRIEPYSRELLEYYYEINGSVAKF	.	.	.	.	A0A2R3EPU8_STAAU	Unreviewed	.	.	.	.	.	.
Mol00804	Protein	Arylamine N-acetyltransferase 1 (NAT1)	NAT	nat	.	Mycolicibacterium smegmatis	1772	Mycolicibacterium smegmatis	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAMDLGGYLTRIGLDGRPRPDLGTLHAIVAAHNRSIPFENLDPLLGIPVADLSAEALFAKLVDRRRGGYCYEHNGLLGYVLEELGFEVERLSGRVVWMRADDAPLPAQTHNVLSVAVPGADGRYLVDVGFGGQTLTSPIRLEAGPVQQTRHEPYRLTRHGDDHTLAAQVRGEWQPLYTFTTEPRPRIDLEVGSWYVSTHPGSHFVTGLTVAVVTDDARYNLRGRNLAVHRSGATEHIRFDSAAQVLDAIVNRFGIDLGDLAGRDVQARVAEVLDT	.	"Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines. Substrates include isoniazid, anisidine, and 4-aminoveratrole, and to a much lesser extent, p-aminobenzoic acid."	PDB: 1GX3; PDB: 1W5R; PDB: 1W6F	.	NAT_MYCSM	Reviewed	.	.	.	.	.	.
Mol00805	Protein	ATP-binding cassette sub-family B5 (ABCB5)	ABCB5 P-gp; P-glycoprotein ABCB5	Abcb5	77706	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000035515.5, Abcb5-201, 3876; ENSMUST00000100982.5, Abcb5-202, 1591; ENSMUST00000177311.8, Abcb5-203, 463"	MANSERTNGLQETNQRYGPLQEQVPKVGNQAVGPIEIFRFADNLDIVLMTLGILASMINGATVPLMSLVLGEISDHLINGCLVQTNRTKYQNCSQTQEKLNEDIIVLTLYYIGIGAAALIFGYVQISFWVITAARQTTRIRKQFFHSILAQDISWFDGSDICELNTRMTGDINKLCDGIGDKIPLMFQNISGFSIGLVISLIKSWKLSLVVLSTSPLIMASSALCSRMIISLTSKELDAYSKAGAVAEEALSSIQTVTAFGAQEKEIQRYTQHLKDAKDAGIKRATASKLSLGAVYFFMNGAYGLAFWYGTSLIFGGEPGYTIGTILAVFFSVIHSSYCIGSVAPHLETFTVARGAAFNIFQVIDKKPNIDNFSTAGFVPECIEGNIEFKNVSFSYPSRPSAKVLKGLNLKIKAGETVALVGPSGSGKSTTVQLLQRLYDPEDGCITVDENDIRAQNVRHYREQIGVVRQEPVLFGTTIGNNIKFGREGVGEKEMEQAAREANAYDFIMAFPKKFNTLVGEKGAQMSGGQKQRIAIARALVRNPKILILDEATSALDTESESLVQTALEKASKGRTTIVVAHRLSTIRGADLIVTMKDGMVVEKGTHAELMAKQGLYYSLAMAQDIKKVDEQMESRTCSTAGNASYGSLCDVNSAKAPCTDQLEEAVHHQKTSLPEVSLLKIFKLSKSEWPFVVLGTLASALNGSVHPVFSIIFGKLVTMFEDKNKATLKQDAELYSMMLVVLGIVALVTYLMQGLFYGRAEENLAMRLRHSAFKAMLYQDMAWYDDKENNTGALTTTLAVDVAQIQGAATSRLGIVTQDVSNMSLSILISFIYGWEMTLLILSFAPVLAVTGMIQTAAMAGFANRDKQALKRAGKIATEAVENIRTVVSLTRERAFEQMYEETLQTQHRNALKRAHITGCCYAVSHAFVHFAHAAGFRFGAYLIQAGRMMPEGMFIVFTAIAYGAMAIGETLVWAPEYSKAKAGASHLFALLKNKPTINSCSQSGEKPDTCEGNLEFREVSFVYPCRPEVPVLQNMSLSIEKGKTVAFVGSSGCGKSTCVQLLQRFYDPMKGQVLLDGVDVKELNVQWLRSQTAIVSQEPVLFNCSIAENIAYGDNSRMVPLEEIKEVADAANIHSFIEGLPRKYNTLVGLRGVQLSGGQKQRLAIARALLRKPKILLLDEATSALDNESEKVVQQALDKARRGKTCLVVAHRLSTIQNADMIVVLQNGSIKEQGTHQELLRNGDTYFKLVAAH	chr 12: 118831559-118930156[-] 	"Energy-dependent efflux transporter responsible for decreased drug accumulation in multidrug-resistant cells. Specifically present in limbal stem cells, where it plays a key role in corneal development and repair."	.	.	ABCB5_MOUSE	Reviewed	ENSMUSG00000072791	.	.	.	.	.
Mol00806	Protein	ATP-binding cassette sub-family C11(ABCC11)	Multidrug resistance-associated protein 8; MRP8	ABCC11	85320	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356608.7, ABCC11-202, 5894; ENST00000394747.5, ABCC11-203, 4862; ENST00000394748.5, ABCC11-204, 4576; ENST00000353782.9, ABCC11-201, 4463; ENST00000569991.1, ABCC11-209, 582; ENST00000565329.1, ABCC11-205, 1813; ENST00000565487.1, ABCC11-206, 671; ENST00000569172.1, ABCC11-208, 556; ENST00000567385.5, ABCC11-207, 3601"	MTRKRTYWVPNSSGGLVNRGIDIGDDMVSGLIYKTYTLQDGPWSQQERNPEAPGRAAVPPWGKYDAALRTMIPFRPKPRFPAPQPLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRRGIEKASVLLVMLRFQRTRLIFDALLGICFCIASVLGPILIIPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEKLIQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPSKALVFEEATLSWQQTCPGIVNGALELERNGHASEGMTRPRDALGPEEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQLTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYMKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALMATATSSLR	chr16:48165773-48247568[-]	"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Participates in physiological processes involving bile acids, conjugated steroids and cyclic nucleotides. Stimulates the ATP-dependent uptake of a range of physiological lipophilic anions, including the glutathione S-conjugates leukotriene C4 and dinitrophenyl S-glutathione, steroid sulfates such as dehydroepiandrosterone 3-sulfate (DHEAS) and estrone 3-sulfate, glucuronides such as estradiol 17-beta-D-glucuronide (E(2)17betaG), the monoanionic bile acids glycocholate and taurocholate, and methotrexate. Enhances also the cellular extrusion of cAMP and cGMP. Confers resistance to anticancer drugs, such as 5-fluorouracil (5-FU) and methotrexate. Probably functions to secrete earwax. Required for the secretion of components contributing to axillary odor formation."	.	HGNC:14639	MRP8_HUMAN	Reviewed	ENSG00000121270	.	.	.	.	.
Mol00807	Protein	ATP-binding cassette transporter A (ABCA)	abcA; AbcA	abcA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKRENPLFFLFKKLSWPVGLIVAAITISSLGSLSGLLVPLFTGRIVDKFSVSHINWNLIALFGGIFVINALLSGLGLYLLSKIGEKIIYRIRSVLWEHIIQLKMPFFDKNESGQLMSRLTDDTKVINEFISQKLPNLLPSIVTLVGSLIMLFILDWKMTLLTFITIPIFVLIMIPLGRIMQKISTSTQSEIANFSGLLGRVLTEMRLVKISNTERLELDNAHKNLNEIYKLGLKQAKIAAVVQPISGIVMLLTIAIILGFGALEIATGAITAGTLIAMIFYVIQLSMPLINLSTLVTDYKKAVGASSRIYEIMQEPIEPTEALEDSENVLIDDGVLSFEHVDFKYDVKKILDDVSFQIPQGQVSAFVGPSGSGKSTIFNLIERMYEIESGDIKYGLESVYDIPLSKWRRKIGYVMQSNSMMSGTIRDNILYGINRHVSDEELINYAKLANCHDFIMQFDEGYDTLVGERGLKLSGGQRQRIDIARSFVKNPDILLLDEATANLDSESELKIQEALETLMEGRTTIVIRDRLSTLKKPVKLCGLDKGQVTGKGTHSELMASHAKYKNFVVSQKLTD	.	May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation.	.	.	Q53614_STAAU	Unreviewed	.	.	.	.	.	.
Mol00808	Protein	ATP-binding protein (ABP)	oleC-ORF4; ATP-binding protein	oleC-ORF4	.	Streptomyces antibioticus	1890	Streptomyces antibioticus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTVRGLVKHYGETKALDGVDLDVREGTVMGVLGPNGAGKTTLVRILSTLITPDSGQATVAGYDVVRQPRQLRRVIGLTGQYASVDEKLPGWENLYLIGRLLDLSRKEARARADELLERFSLTEAARRPAGTYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVKAMVGDGVTVLLTTQYMEEAEQLASELTVVDRGRVIAKGGIEELKARVGGRTLRVRPVDPLQLRPLAGMLDELGITGLASTTVDTETGALLVPILSDEQLTAVVGAVTARGITLSSITTELPSLDEVFLSLTGHRASAPQDAEPARQEVAV	.	.	.	.	Q53716_STRAT	Unreviewed	.	.	.	.	.	.
Mol00809	Protein	ATP-binding protein (ABP)	oleB; ATP-binding protein	oleB	.	Streptomyces antibioticus	1890	Streptomyces antibioticus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MQNAHRSDTGAAALTGTPEKLLPTQPETGSFQVVLDDVVRAPGGRPLLDGVNQSVALGERVGIIGENGSGKSTLLRMLAGVDRPDGGQVLVRAPGGCGYLPQTPDLPPEDTVQDAIDHALAELRSLERGLREAEQALAGAEPEELEGLLGAYGDLLEAFEARDGYAADARVDAAMHGLGLAGITGDRRLGSLSGGEQARLNLACLLAASPQLMLLDEPTNHLDVGALEWLEERLRAHRGSVLVVSHDRVFLERVATALWEVDGERRTVNRHGGGYAGYLQAKAAARRRWEQAYQDWLEDLARQRELARSAADHLATGPRRNTERSNQRHQRNVEKQISARVRNAKERVRRLEENPVPRPPQPMRFRARVEGGGTVGRGGALAELYKVTVGTRLDVPSFTVDPGERILITGHNGAGKSTLLRVLAGDLAPDQGECERPERIGWLPQETEITDRQQSLLAAFAAGLPGIAEEHRGALLGFGLFRPSALGTAVGDLSTGQLRRLALARLLRDPADLLLLDEPTNHLSPALVEDLEEALAHYRGALVVVSHDRMFAQRFTGRRMHMEGGRFVE	.	.	.	.	Q53712_STRAT	Unreviewed	.	.	.	.	.	.
Mol00810	Protein	ATP-dependent protease subunit HslV (HSlV)	PA5053	hslV	881049	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTTIVSVRRNGKVVMGGDGQVSLGNTVMKGNAKKVRRLYHGQVLAGFAGATADAFTLFERFEQQLEKHQGHLVRAAVELAKDWRTDRSLSRLEAMLAVANKDASLIITGNGDVVEPEHGLIAMGSGGGFAQAAALALLQHNAELSAREVAETALNIAGSICVFTNQNLTIEELDSAV	.	Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.	.	.	HSLV_PSEAE	Reviewed	.	.	.	.	.	.
Mol00811	Protein	Bacitracin transport ATP-binding protein BcrA (BCRA)	.	bcrA	.	Bacillus licheniformis	1402	Bacillus licheniformis	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MSTIIKTTDLTKMYGSQKSVDHLNINVKQGDIYGFLGRNGAGKTTTIRMLLGLIKPTSGQIEIFGENFFKNKKEILRRIGSIVEVPGFYANLTARENLLINAKIIGIHKKNAIDEVLEIVGLQHETKKLVGKFSLGMKQRLGIARALLHYPELLILDEPTNGLDPIGIKEMRRLIHSLAKERNITIFISSHILSEIEQLVDHVGIIHEGKLLEEIPFDHLKKRNRKYLEFQLSDQNKAVVLMEQHFDIHDYEVHQDGIIRVYSHLGQQGKLNKLFVENGIDVLKITMSEDSLEDYFVKLIGGGTIG	.	Part of the binding-protein-dependent transport system for bacitracin that confer resistance to this antibiotic. Probably responsible for energy coupling to the transport system (By similarity).	.	.	BCRA_BACLI	Reviewed	.	.	.	.	.	.
Mol00812	Protein	Bacitracin transport permease protein BCRB (BCRB)	.	bcrB	.	Bacillus licheniformis	1402	Bacillus licheniformis	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MAKKAKYPDVPIRFSETFSDTNLYIVLLIGVPLYGVITSYLFNREYAESTLKNLLTIPVSRISLIVSKLVLLLIWIMMLTLIAWVLTLLFGLIGQFEGLSSAVLIEGFKQFMIGGALLFFLVSPIIFVTLLFKNYVPTIIFTIIISMVSIMVYGTEYSALFPWSAVWVIASGTFFPEYPPEYSFISVAATTVLGLAATIVYFKKIDIH	.	Part of the binding-protein-dependent transport system for bacitracin that confer resistance to this antibiotic; probably responsible for the translocation of the substrate across the membrane.	.	.	BCRB_BACLI	Reviewed	.	.	.	.	.	.
Mol00813	Protein	Bcr/CflA family efflux transporter (BCML)	.	cmlB	.	Klebsiella aerogenes	548	Klebsiella aerogenes	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRSKNCNWRYSLAVTVLLLSPFDLLASLGMDMYLPAVPFMPHALGTTAGTIQLTLTTYLVMIGAGQLLFGPLSDRLGRRPVLLAGGAAYVAASIGLVVTSSAGVFLGFRILQACGASACLVATFATVRDIYAGRKESNVIYGLLGSMLAMVPAIGPLLGAVIDTWFGWRAIFAFLGLGMIAALTAAWRLWPETRVQRPAALQWSQLLLPIKHLNFWLYTVCYAAGMGSFFVFFSIAPGLMMGRQGMSQFGFSLLFATVAIAMMLAARFMGRVIAKWGSLSALRMGMGCLIAGAVLLVITELWIPQSVLGFIAPMWLVGVGVATAVSVAPNGALRGFDHIAGAVTAVYFCLGGLLLGSVGTLIISLLPRDTAWPVIAYCLVLATIVLGLSCVSRARDLRGHGEYDAVART	.	.	.	.	Q9X2P0_KLEAE	Unreviewed	.	.	.	.	.	.
Mol00814	Protein	Bcr/CflA family efflux transporter (BCML)	.	cmlA4	.	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRSKNFSWRYSLAATVLLLSPFDLLASLGMDMYLPAVPFMPNALGTTASTVQLTLATYLVMIGAGQLLFGPLSDRLGRRPVLLGGGLAYVVASMGLAFTSLAEVFLGLRILQACGASACLVSTFATVRDIYAGREESNVIYGILGSMLAMVPAVGPLLGALVDMWLGWRAIFAFLGLGMIAASAAAWRFWPETRVQRVTGLQWSQLLLPVKCLNFWLYTLCYAAGMGSFFVFFFIAPGLIMGRQGVSQLGFSLLFATVAIAMVFTARFMGRVIPKWGSPSVLRMGMGCLIAGAVLLAITEIWASQSVLGFIAPMWLVGIGVATAVSVAPNGALQGFDHVAGTVTAVYFCLGGVLLGSIGTLIISLLPRNTAWPVVVYCLTLATVVLGLSCVSRAKGSRGQGEHDVVALQSAESTSNPNR	.	.	.	.	Q9KJY5_KLEPN	Unreviewed	.	.	.	.	.	.
Mol00815	Protein	Bcr/CflA family efflux transporter (BCML)	cmlA1; cmlA6; IPC1317_27175	CmlA6	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRSKNFSWRYSLAATVLLLSPFDLLASLGMDMYLPAVPFMPNALGTTASTIQLTLTTYLVMIGAGQLLFGPLSDRLGRRPVLLGGGLAYVVASMGLALTSSAEVFLGLRILQACGASACLVSTFATVRDIYAGREESNVIYGILGSMLAIVPAVGPLLGALVDMWLGWRAIFAFLGLGMIAASAAAWRFWPETRVQRVAGLQWSQLLLPVKCLNFWLYTLCYAAGMGSFFVFFSIAPGLMMGRQGVSQLGFSLLFATVAIAMVFTARFMGRVIPKWGSPSVLRMGMGCLIAGAVLLAITEIWALQSVLGFIAPMWLVGIGVATAVSVAPNGALRGFDHVAGTVTAVYFCLGGVLLGSIGTLIISLLPRNTAWPVVVYCLTLATVVLGLSCVSRVKGSRGQGEHDVVALQSAESTSNPNR	.	.	.	.	Q933G9_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00816	Protein	Bcr/CflA family efflux transporter (BCML)	SCH_052	cmlA	.	Salmonella(Salmonella choleraesuis)	28901	Salmonella enterica	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSSKNFSWRYSLAATVLLLSPFDLLASLGMDMYLPAVPFMPNALGTTASTIQLTLTTYLVMIGAGQLLFGPLSDRLGRRPVLLGGGLAYVVASMGLALTSSAEVFLGLRILQACGASACLVSTFATVRDIYAGREESNVIYGILGSMLAMVPAVGPLLGALVDMWLGWRAIFAFLGLGMIAASAAAWRFWPETRVQRVAGLQWSQLLLPVKCLNFWLYTLCYAAGMGSFFVFFSIAPGLMMGRQGVSQLGFSLLFATVAIAMVFTARFMGRVIPKWGSPSVLRMGMGCLIAGAVLLAITEIWALQSVLGFIAPMWLVGIGVATAVSVAPNGALRGFDHVAGTVTAVYFCLGGVLLGSIGTLIISLLPRNTAWPVVVYCLTLATVVLGLSCVSRVKGSRGQGEHDVVALQSAESTSNPNR	.	.	.	.	Q5J429_SALCH	Unreviewed	.	.	.	.	.	.
Mol00817	Protein	Bcr/CflA family efflux transporter (BCML)	.	floR	.	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTTTRPAWAYTLPAALLLMAPFDILASLAMDIYLPVVPAMPGILNTTPAMIQLTLSLYMVMLGVGQVIFGPLSDRIGRRPILLAGATAFVIASLGAAWSSTAPAFVAFRLLQAVGASAMLVATFATVRDVYANRPEGVVIYGLFSSMLAFVPALGPIAGALIGEFLGWQAIFITLAILAMLALLNAGFRWHETRPLDQVKTRRSVLPIFASPAFWVYTVGFSAGMGTYFVFFSTAPRVLLGQAEYSEIGFSFAFATVALVMIVTTRFAKSFVARWGIAGCVARGMALLVCGAVLLGIGELYGSPSFLTFILPMWVVAVGIVFTVSVTANGALAEFDDIAGSAVAFYFCVQSLIVSIVGTLAVALLNGDTAWPVICYATAMAVLVSLGLVLLRLRGAATEKSPVV	.	.	.	.	B6ET84_PASMD	Unreviewed	.	.	.	.	.	.
Mol00818	Protein	Bcr/CflA family efflux transporter (BCML)	.	floR	.	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTTTRPAWAYTLPAALLLMAPFDILASLAMDIYLPVVPAMPGILNTTPAMIQLTLSLYMVMLGVGQVIFGPLSDRIGRRPILLAGATAFVIASLGAAWSSTAPAFVAFRLLQAVGASAMLVATFATVRDVYANRPEGVVIYGLFSSMLAFVPALGPIAGALIGEFLGWQAIFITLAILAMLALLNAGFRWHETRPLDQVKTRRSVLPIFASPAFWVYTVGFSAGMGTFFVFFSTAPRVLIGQAEYSEIGFSFAFATVALVMIVTTRFAKSFVARWGIAGCVARGMALLVCGAVLLGIGELYGSPSFLTFILPMWVVAVGIVFTVSVTANGALAEFDDIAGSAVAFYFCVQSLIVSIVGTLAVALLNGDTAWPVICYATAMAVLVSLGLVLLRLRGAATEKSPVV	.	.	.	.	A0A1Y0F4T3_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00819	Protein	BCR-ABL1 e8a2 variant (BCR-ABL1)	BCR-ABL1; Fragment	BCR-ABL1	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	QNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGELLNRKDKTTFEKLDYLMSKEDNYKRTREYIRSLKMVPSIPYLEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGE	.	.	.	.	E7E8T7_HUMAN	Unreviewed	.	.	.	.	.	.
Mol00820	Protein	Beta-lactamase (BLA)	FX155_06310	aci1	.	Acidaminococcus fermentans	905	Acidaminococcus fermentans	Acidaminococcus	904	Acidaminococcaceae	909930	Acidaminococcales	1843488	Negativicutes	909932	Firmicutes	1239	.	.	.	MKKFCFLFLIICGLMVFCLQDCQARQKLNLADLENKYNAVIGVYAVDMENGKKICYKPDTRFSYCSTHKVFTAAELLRQKNTSDLNEIRKFSAEDILSYAPITKDHVADGMTLAEICSASLRWSDNTAANLILQEIGGVENFKVALKNIGDKTTKPARNEPELNLFNPKDNRDTSTPRQMVKNLQVYIFGDILSDDKKKLLIDWMSDNSITDTLIKAETPQGWKVIDKSGSGDYGARNDIAVIYPPNRKPIVMAIMSRRTEKNAKSDDAMIAEAAKRIFDNLVF	.	.	.	.	Q9XBM2_ACIFE	Unreviewed	.	.	.	.	.	.
Mol00821	Protein	Beta-lactamase (BLA)	bla; bla CTX-M-15; bla CTXM-15; bla_1; bla_2; bla_3; blaCTX-M; blaCTX-M-15; blaCTX-M15; CTX-M-15; A9X72_26855; ACN68_29740; AWP47_17965; BANRA_05422; BJI68_26810; C2121_004650; C2121_005381; CO706_01125; CY655_16075; E3O05_17770; E5P22_18740; E5P33_09365; E5P39_23850; E5P41_23530; E5P42_20460; E5P43_23600; E5P44_23710; E5P45_23695; E5P46_23480; E5P47_23815; E5P48_23485; E5P49_23765; E5P50_24275; E5P51_02965; EA435_19100; EBP16_19885; EBP16_24990; ELT22_08720; ELT25_03215; ELT31_23875; ELT40_25155; ELT41_23005; ELT44_26705; ELT46_06805; ELT48_21595; ELT48_27155; ELT49_23685; ELT54_13870; ELT60_26675; ELT61_26075; ELU83_06515; ELU96_05460; ELU97_00005; ELV01_27290; ELV02_26600; ELV03_26255; ELV04_25750; ELV07_26450; ELV11_23415; ELV13_26970; ELV16_12500; ELV21_22135; ELV23_26085; ELX56_25110; ELX56_26475; ELX70_23835; ELX76_26235; ELX76_27770; ELX79_26345; ELX83_26200; ELX83_26525; ELY24_26875; ELY36_26165; EVY14_26065; EXX13_27820; F0L67_27800; F9B07_28185; FEJ01_19840; FEJ01_27020; G3565_28475; G5603_26845; G5632_10280; G9448_24215; GQE64_24895; GQW07_24060; GQW07_26690; GRO95_23990; GRO95_26745; GRW77_24730; HL601_21620; HL601_27220; HMJ82_28240; HMJ82_29040; HMU48_14165; HMU48_30490; IH772_23850; RCS105_pI0076; RCS46_P0095; RCS53_P0006; RCS57_p0080; RCS59_P0138; RCS67_P0011; SAMEA4363221_00081; SAMEA4370330_00042; SAMEA4370365_00031; SAMEA4370386_00071; SAMEA4370473_00021	blaUOE-1	58463765	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MVKKSLRQFTLMATATVTLLLGSVPLYAQTADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAAAAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAALQYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDPRDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPASWVVGDKTGSGGYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVLASAAKIVTDGL	.	.	PDB: 4HBT; PDB: 4HBU; PDB: 5FA7; PDB: 5FAO; PDB: 5FAP	.	Q9EXV5_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00822	Protein	Beta-lactamase (BLA)	CTX-M-27; BHS81_28690; E2646_25290; E5P24_23885; E5P25_24685; ELT16_25615; ELT17_24970; ELT17_25950; ELT24_25425; ELT28_24375; ELT30_25285; ELT33_25580; ELT34_25190; ELT35_24930; ELT50_25655; ELT51_25275; ELT52_25075; ELT56_26135; ELT59_25810; ELT63_26730; ELT72_26015; ELU07_25785; ELU85_24945; ELU88_25405; ELU89_26185; ELU94_24395; ELU95_24935; ELU98_24760; ELU99_26765; ELV00_25900; ELV10_25555; ELV12_25315; ELV15_26115; ELV22_25665; ELV22_26040; ELV26_26000; ELV28_26965; ELV29_23540; ELX68_25300; ELX68_25610; ELX69_25215; ELX69_26380; ELX96_26110; ELX96_28025; ELY23_25275; ELY23_26125; ELY32_26250; ELY32_27450; ELY41_26420; ELY41_28245; ELY48_26225; ELY48_27465; ELY50_26145; ELY50_26870; GRC73_24255; GRC73_24680; HLV18_24285; HLV18_24805	blaCTX-M-27	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTVGDKTGSGGYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL	.	.	PDB: 1YLP	.	Q840M4_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00823	Protein	Beta-lactamase (BLA)	bla SHV-12; shv5; BANRA_05004; F2N31_20430; F2N31_29225; RCS28_PI0048; RCS35_PII0006; RCS37_PII0024; RCS49_PIII0007; RCS49_PIV0001	blaSHV-12	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRYIRLCIISLLATLPLAVHASPQPLEQIKQSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGASKRGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR	.	.	.	.	Q7X574_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00824	Protein	Beta-lactamase (BLA)	blaCTX-M; blaSHV; blaSHV-5a; blaSHV12; SHV-12; BANRA_05658; BANRA_05677; BANRA_05967; BL124_00006465; C3F39_28925; DN601_29505; IPF_343; IPF_8; pCRE380_11; pCT-KPC_120	blaSHV-12	.	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRYIRLCIISLLATLPLAVHASPQPLEQIKQSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGASKRGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR	.	.	.	.	Q79TB3_KLEPN	Unreviewed	.	.	.	.	.	.
Mol00825	Protein	Beta-lactamase (BLA)	bla_4; blaOXA-48; G5637_27540; GPZ86_28000; KPE71T_00045; SAMEA3727643_05844	bla	.	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRVLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASTFKIPNSLIALDLGVVKDEHQVFKWDGQTRDIATWNRDHNLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATEQISFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYSTRIEPKIGWWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP	.	.	PDB: 3HBR; PDB: 4S2J; PDB: 4S2K; PDB: 4S2N; PDB: 4S2P; PDB: 4WMC; PDB: 5DTK; PDB: 5DTS; PDB: 5DTT; PDB: 5DVA; PDB: 5FAQ; PDB: 5FAS; PDB: 5FAT; PDB: 5HAP; PDB: 5HAQ; PDB: 5OFT; PDB: 5QA4; PDB: 5QA5; PDB: 5QA6; PDB: 5QA7; PDB: 5QA8; PDB: 5QA9; PDB: 5QAA; PDB: 5QAB; PDB: 5QAC; PDB: 5QAD; PDB: 5QAE; PDB: 5QAF; PDB: 5QAG; PDB: 5QAH; PDB: 5QAI; PDB: 5QAJ; PDB: 5QAK; PDB: 5QAL; PDB: 5QAM; PDB: 5QAN; PDB: 5QAO; PDB: 5QAP; PDB: 5QAQ; PDB: 5QAR; PDB: 5QAS; PDB: 5QAT; PDB: 5QAU; PDB: 5QAV; PDB: 5QAW; PDB: 5QAX; PDB: 5QAY; PDB: 5QAZ; PDB: 5QB0; PDB: 5QB1; PDB: 5QB2; PDB: 5QB3; PDB: 5QB4; PDB: 6GOA; PDB: 6HOO; PDB: 6I5D; PDB: 6P96; PDB: 6P97; PDB: 6P98; PDB: 6P99; PDB: 6P9C; PDB: 6PK0; PDB: 6PQI; PDB: 6PSG; PDB: 6PT1; PDB: 6PT5; PDB: 6PTU; PDB: 6PXX; PDB: 6Q5B; PDB: 6Q5F; PDB: 6RJ7; PDB: 6UVK; PDB: 6V1O; PDB: 6ZRJ; PDB: 6ZRP; PDB: 6ZXI; PDB: 7ASS; PDB: 7AUX; PDB: 7AW5; PDB: 7KH9; PDB: 7KHQ	.	Q6XEC0_KLEPN	Unreviewed	.	.	.	.	.	.
Mol00826	Protein	Beta-lactamase (BLA)	bla; bla TEM-1; bla_1; bla_2; blaTEM; BlaTEM-1; blaTEM-1; blaTEM-116; blaTEM-1B; blaTEM-1b; blaTEM-1D; blaTEM1; blaTEM1D; blaTEM1E; blaTEM1F; A2F99_004554; A2F99_004666; A9X72_26835; AWP47_17940; AWP93_00390; B6R12_004739; B6R12_005526; B6R15_005206; B6R15_005523; BANRA_04773; BANRA_05427; BFL24_24620; BG944_002911; BG944_005713; BHS81_30510; BIZ41_10685; BJI68_26345; BO068_005319; BO068_005477; BON66_02690; BON67_03845; BON68_19145; BON69_00465; BON70_01975; BON71_00055; BON72_28760; BON75_23670; BON76_21975; BON81_25130; BON82_05385; BON83_24205; BON86_07485; BON88_06945; BON89_06025; BON94_02815; BON96_02690; BON97_18680; BON98_03600; BSR05_26525; BVL39_07935; BVL39_07960; BXT93_06865; C2121_004654; C2121_005384; CCS08_09025; CDL36_20780; CG831_004349; CG831_004504; CO706_01105; CO706_17370; CQP61_30495; CWS33_22125; CX692_004596; CX692_004719; CX693_004596; CX693_004721; CX699_004527; CX699_004672; CXJ73_005347; CXJ73_006204; CY655_27570; D3822_31045; D3C88_10830; D3G36_26695; D3G36_27505; D4U49_22295; D4U49_28905; D9C02_24990; D9D77_20430; D9D77_28935; D9J61_26735; D9J61_26740; D9J61_26745; D9J61_26750; D9J61_26755; D9J61_26760; DAH37_27405; DAH50_26125; DKP82_25825; DNX30_29295; DNX30_30505; DU321_26460; DXT70_23345; E2114_26540; E2115_26450; E2116_26650; E2118_26645; E2120_26945; E2122_14285; E2123_26540; E2124_26660; E2125_26620; E2128_25025; E2130_26595; E2131_25090; E2135_22030; E2136_26925; E5P22_20565; E5P23_12820; E5P23_13380; E5P24_23910; E5P25_24710; E5P30_23990; E5P37_17910; E5P51_01875; E5P52_21745; E5S34_22695; E5S35_22580; E5S39_22165; E5S43_22320; EA435_26350; EHH55_26375; EI021_25945; EIZ93_28475; EKI52_29585; ELT20_23760; ELT22_24990; ELT25_25950; ELT26_23465; ELT31_25650; ELT31_26030; ELT32_25300; ELT36_25095; ELT36_25560; ELT39_25205; ELT40_25345; ELT48_24185; ELT48_26800; ELT49_23665; ELT55_26225; ELT56_21465; ELU91_25690; ELU97_22830; ELV10_25830; ELV12_25815; ELV20_25130; ELV21_27315; ELV23_25740; ELV24_24545; ELV24_25955; ELV28_24995; ELV28_29525; ELV29_22900; ELX56_24795; ELX56_26000; ELX68_15695; ELX68_26135; ELY05_22530; ELY05_24915; EPS76_27635; ERS085406_05171; ETECE562_05056; ETN48_p0069; EVY14_27485; EXX13_05385; EYV18_22010; F9B07_25495; FDM60_13440; FDM60_28130; FE587_19010; FE587_27705; FEJ01_26155; FEJ01_27540; FGG80_21220; FJQ51_26745; FJQ51_27795; FTV92_27545; FTV93_29765; FWK02_02110; FY127_09010; FZN31_00540; G4A38_27760; G9448_23805; G9448_25615; GF147_26500; GF147_27220; GFY34_25275; GFY34_26415; GKE84_18035; GLW94_27210; GLW94_28255; GP650_26385; GP979_22355; GQE64_24875; GQW07_26790; GQW68_26185; GQW68_27145; GQW80_26180; GQW80_27605; GRO95_26845; GRW05_13885; GRW57_26480; GRW77_24710; GTP88_26265; GTP88_26850; HHH44_005310; HHH44_005312; HJS37_003877; HJS37_005198; HKA49_005153; HKA49_005608; HLZ50_24695; HLZ50_26680; HMJ82_29245; HMJ82_29250; HMJ82_29255; HMJ82_29260; HMU06_23660; HMU06_28740; HMV95_25095; HMV95_26455; HNC36_28295; HNC36_29435; HNC59_27740; HNC59_29670; HNC66_22940; HNC66_27545; HNC99_29675; HND12_30830; HVX16_26760; HX136_25470; HX136_25960; IH768_20880; IPF_160; IT029_005376; IT029_005543; JE86ST02C_05370; JE86ST05C_05430; JNP96_28840; JNP96_30605; NCTC12950_01033; NDM1Dok01_N0178; O2R_124; pEC012_00011; pEC012_00036; pG5A4Y217_19; pHN3A11_016; pHN7A8_020; pHNFP460_046; pOLA52_03; R6K_0002; RCS30_P0189; RCS35_PII0008; RCS37_PI0008; RCS39_P0009; RCS49_PIII0009; RCS55_PI0069; RCS57_p0075; RCS57TR364_P0005; RCS59_P0142; RCS65_P0143; rpec180_8; SAMEA3472056_05622; SAMEA3472080_04547; SAMEA3751407_05223; SAMEA3752557_04872; SAMEA4363221_00075; SAMEA4370473_00028; TUM18780_19120; TUM18780_46010	TEM-1	67514328	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW	.	.	.	.	Q6SJ61_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00827	Protein	Beta-lactamase (BLA)	blaOxa-50c; blaOXA-50b; blaOXA-50g; IPC1494_23315; IPC152_19190; IPC1595_21065; IPC57_19425; IPC607_22635; EC 3.5.2.6; OXA-50 family oxacillin-hydrolyzing class D beta-lactamase OXA-488; Oxacillinase	blaOxa-50c	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRPLLFSALLLLSGHAQASEWNDSRAVDKLFGAAGVKGTFVLYDVQRQRYVGHDRERAETRFVPASTYKVANSLIGLSTGAVRSADEVLPYGGKPQRFKAWEHDMSLRDAIKASNVPVYQELARRIGLERMRANVSRLGYGNAEIGQVVDNFWLVGPLKISAMEQTRFLLRLAQGELPFPAPVQSTVRAMTLLESGPGWELHGKTGWCFDCTPELGWWVGWVKRNERLYGFALNIDMPGGEADIGKRVELGKASLKALGILP	.	.	.	.	Q6JTT6_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00828	Protein	Beta-lactamase (BLA)	blaCMY-2	bla	39514982	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MMKKSLCCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAVIYQGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDAIARGEIKLSDPVTKYWPELTGKQWQGIRLLHLATYTAGGLPLQIPDDVRDKAALLHFYQNWQPQWTPGAKRLYANSSIGLFGALAVKPSGMSYEEAMTRRVLQPLKLAHTWITVPQNEQKDYAWGYREGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIALAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPVRVEAAWRILEKLQ	.	This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.	PDB: 1ZC2	.	Q48434_KLEPN	Unreviewed	.	.	.	.	.	.
Mol00829	Protein	Beta-lactamase (BLA)	RSP_3749	ampC	.	Rhodobacter sphaeroides	1063	Cereibacter sphaeroides	Cereibacter	1653176	Rhodobacteraceae	31989	Rhodobacterales	204455	Alphaproteobacteria	28211	Proteobacteria	1224	.	.	.	MKHLSPLSILLMVGALTPALAQDTTPSFESAAAAAFESVIEEHDIPGLVVGVTHGGRHSFYQTGLASREDQQPVTPDTLFELGSISKIFNVTLAALAEERGALSLDAPVADYLPSLRGSPAGELTLIDLATHHTGGLPLQVPDEVADVDRLVDWLRSWRPPEPGTRSYSNISIGLLGHITAGVLGMSYADASQTVIFPALGLKSTWIDVPTDAMGRYAFGYDRKTDAPTRVTPGVLDDEAYGVKSSARDMLTLLDLELGTGTASPEVQTAVATTQEGRFQTRLYTQAMIWEAYPWPVDPERLVEGNGYDFILQPQPVDEVDTTPDRRVILNKTGSTNGFGGYIAIVPSEDLGVVVLANRNYPNEARVRATYDLITHILAE	.	.	PDB: 7MQN	.	Q3IVS9_CERS4	Unreviewed	.	.	.	.	.	.
Mol00830	Protein	Beta-lactamase (BLA)	.	blaTEM-1b	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASWQQLIDWVEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIK	.	.	.	.	Q1WBW3_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00831	Protein	Beta-lactamase (BLA)	bla; bla_1; blaCTX-M; blaCTX-M-15; blaCTX-M-3; CTX-M-57; BJJ90_28645; BK383_23175; BVL39_25925; C5Y87_27520; CDL36_28010; D9C02_24490; DM870_24300; DS732_31125; EAI46_08065; EIA08_20890; EIZ93_26440; ELT20_21470; ELT21_22800; ELT36_16845; ELT58_24780; ELV05_08105; ELV08_25910; ELV40_24885; ELY02_21550; ELY05_21460; ELY05_24820; FKO60_26825; HHH44_004851; HHH44_005271; HLZ50_25860; HLZ50_26760; HNC59_29660; HNC99_27310; HNC99_29655; JFD_05359; M55_021; pHNFP460_058; TUM18780_46190	blaCTX-M-55	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MVKKSLRQFTLMATATVTLLLGSVPLYAQTADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAVAAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAALQYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDPRDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPASWVVGDKTGSGGYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVLASAAKIVTDGL	.	.	.	.	Q0GA57_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00832	Protein	Beta-lactamase (BLA)	bla CTX-M-3; blaCTX-M-3; blaCTX-M3; AN672_26965	bla	.	Citrobacter freundii	546	Citrobacter freundii	Citrobacter	544	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MVKKSLRQFTLMATATVTLLLGSVPLYAQTADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAAAAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAALQYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDPRDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPASWVVGDKTGSGDYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVLASAAKIVTDGL	.	.	.	.	O52904_CITFR	Unreviewed	.	.	.	.	.	.
Mol00833	Protein	Beta-lactamase (BLA)	bla(SHV-12); SHV-12; EVY09_23940; pCRE727_11; pYQ13500_012; STN0717ENT73_P11400	blaSHV-12	.	Enterobacter cloacae	550	Enterobacter cloacae	Enterobacter	547	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRYIRLCIISLLATLPLAVHASPQPLEQIKQSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGASKRGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR	.	.	.	.	O06025_ENTCL	Unreviewed	.	.	.	.	.	.
Mol00834	Protein	Beta-lactamase (BLA)	A7B01_09155; A7B01_20130; A7B01_25230	blaOXA-181	.	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRVLALSAVFLVASIIGMPAVAKEWQENKSWNAHFTEHKSQGVVVLWNENKQQGFTNNLKRANQAFLPASTFKIPNSLIALDLGVVKDEHQVFKWDGQTRDIAAWNRDHDLITAMKYSVVPVYQEFARQIGEARMSKMLHAFDYGNEDISGNVDSFWLDGGIRISATQQIAFLRKLYHNKLHVSERSQRIVKQAMLTEANGDYIIRAKTGYSTRIEPKIGWWVGWVELDDNVWFFAMNMDMPTSDGLGLRQAITKEVLKQEKIIP	.	.	PDB: 5OE0	.	G5CKK8_KLEPN	Unreviewed	.	.	.	.	.	.
Mol00835	Protein	Beta-lactamase (BLA)	blaNDM-5; blaNDM; C5N07_29035; CWS33_26475; D0X26_01580; D0X26_30180; EI021_24930; EIZ93_26035; EYV17_23675; EYV18_23855; G5632_22505; pEC1929_0014; TUM18780_51250; Beta-lactamase II; Class B carbapenemase NDM-5; Class B metallo-beta-lactamase NDM-5; Metallo-beta-lactamase NDM-5; NDM-5; NDM-5 metallo-beta-lactamase; New Delhi Metallo carbapenemase protein; New Delhi metallo beta lactamase 5; Subclass B1 metallo-beta-lactamase NDM-5	blaNDM-5	39459987	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR	.	.	PDB: 4TZE	.	G3K399_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00836	Protein	Beta-lactamase (BLA)	.	blaCMY-61	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MMNRYAAALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAVIYQGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDAIARGEIKLSDPVTKYWPELTGKQWQGIRLLHLATYTAGGLPLQIPDDVRDKAALLHFYQNWQPQWTPGAKRLYANSSIGLFGALAVKPSGMSYEEAMTRRVLQPLKLAHTWITVPQNEQKDYAWGYREGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIALAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPVRVEAAWRILEKLQ	.	This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.	PDB: 6G9T	.	G3F7G9_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00837	Protein	Beta-lactamase (BLA)	blaCMY-42; G5603_25265; pCMY42_EC8_00033	CMY-42	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MMKKSLCCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAVIYQGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDAIARGEIKLSDPVTKYWPELTGKQWQGIRLLHLATYTAGGLPLQIPDDVRDKAALLHFYQNWQPQWTPGAKRLYANSSIGLFGALAVKPSGMSYEEAMTRRVLQPLKLAHTWITVPQNEQKDYAWGYREGKPVHSSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIALAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPVRVEAAWRILEKLQ	.	This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.	.	.	F4YXC2_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00838	Protein	Beta-lactamase (BLA)	Penicillinase; oxa2	bla	67369352	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MAIRIFAILFSIFSLATFAHAQEGTLERSDWRKFFSEFQAKGTIVVADERQADRAMLVFDPVRSKKRYSPASTFKIPHTLFALDAGAVRDEFQIFRWDGVNRGFAGHNQDQDLRSAMRNSTVWVYELFAKEIGDDKARRYLKKIDYGNADPSTSNGDYWIEGSLAISAQEQIAFLRKLYRNELPFRVEHQRLVKDLMIVEAGRNWILRAKTGWEGRMGWWVGWVEWPTGSVFFALNIDTPNRMDDLFKREAIVRAILRSIEALPPNPAVNSDAAR	.	This is an oxacillin-hydrolyzing beta-lactamase.	.	.	BLO2_ECOLX	Reviewed	.	.	.	.	.	.
Mol00839	Protein	Beta-lactamase (BLA)	Penicillinase; oxa1	bla	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKNTIHINFAIFLIIANIIYSSASASTDISTVASPLFEGTEGCFLLYDASTNAEIAQFNKAKCATQMAPDSTFKIALSLMAFDAEIIDQKTIFKWDKTPKGMEIWNSNHTPKTWMQFSVVWVSQEITQKIGLNKIKNYLKDFDYGNQDFSGDKERNNGLTEAWLESSLKISPEEQIQFLRKIINHNLPVKNSAIENTIENMYLQDLDNSTKLYGKTGAGFTANRTLQNGWFEGFIISKSGHKYVFVSALTGNLGSNLTSSIKAKKNAITILNTLNL	.	This is an oxacillin-hydrolyzing beta-lactamase.	PDB: 1M6K; PDB: 3ISG; PDB: 4MLL	.	BLO1_ECOLX	Reviewed	.	.	.	.	.	.
Mol00840	Protein	Beta-lactamase (BLA)	IRT-4; Penicillinase; TEM-1; TEM-16/CAZ-7; TEM-2; TEM-24/CAZ-6; TEM-3; TEM-4; TEM-5; TEM-6; TEM-8/CAZ-2	bla;	67514328	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW	.	"TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors."	PDB: 1AXB; PDB: 1BT5; PDB: 1BTL; PDB: 1CK3; PDB: 1ERM; PDB: 1ERO; PDB: 1ERQ; PDB: 1ESU; PDB: 1FQG; PDB: 1JTD; PDB: 1JTG; PDB: 1JVJ; PDB: 1JWP; PDB: 1JWV; PDB: 1JWZ; PDB: 1LHY; PDB: 1LI0; PDB: 1LI9; PDB: 1M40; PDB: 1NXY; PDB: 1NY0; PDB: 1NYM; PDB: 1NYY; PDB: 1PZO; PDB: 1PZP; PDB: 1S0W; PDB: 1TEM; PDB: 1XPB; PDB: 1XXM; PDB: 1YT4; PDB: 1ZG4; PDB: 1ZG6; PDB: 2B5R; PDB: 2V1Z; PDB: 2V20; PDB: 3C7U; PDB: 3C7V; PDB: 3CMZ; PDB: 3DTM; PDB: 3JYI; PDB: 3TOI; PDB: 4DXB; PDB: 4DXC; PDB: 4GKU; PDB: 4IBR; PDB: 4IBX; PDB: 4ID4; PDB: 4MEZ; PDB: 4QY5; PDB: 4QY6; PDB: 4R4R; PDB: 4R4S; PDB: 4RVA; PDB: 4RX2; PDB: 4RX3; PDB: 4ZJ1; PDB: 4ZJ2; PDB: 4ZJ3; PDB: 5HVI; PDB: 5HW1; PDB: 5HW5; PDB: 5I52; PDB: 5I63; PDB: 5IQ8; PDB: 5KKF; PDB: 5KPU; PDB: 5NPO; PDB: 6APA; PDB: 6AYK; PDB: 6B2N	.	BLAT_ECOLX	Reviewed	.	.	.	.	.	.
Mol00841	Protein	Beta-lactamase (BLA)	Penicillinase	blaF	.	Mycolicibacterium fortuitum	1766	Mycolicibacterium fortuitum	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTGLSRRNVLIGSLVAAAAVGAGVGGAAPAFAAPIDDQLAELERRDNVLIGLYAANLQSGRRITHRLDEMFAMCSTFKGYAAARVLQMAEHGEISLDNRVFVDADALVPNSPVTEARAGAEMTLAELCQAALQRSDNTAANLLLKTIGGPAAVTAFARSVGDERTRLDRWEVELNSAIPGDPRDTSTAAALAVGYRAILAGDALSPPQRGLLEDWMRANQTSSMRAGLPEGWTTADKTGSGDYGSTNDAGIAFGPDGQRLLLVMMTRSQAHDPKAENLRPLIGELTALVLPSLL	.	.	PDB: 2CC1	.	BLAF_MYCFO	Reviewed	.	.	.	.	.	.
Mol00842	Protein	Beta-lactamase (BLA)	.	cfxA	.	Bacteroides vulgatus	821	Phocaeicola vulgatus	Phocaeicola	909656	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNKSQASQYVAHISAVVYSLLMQTSVKS	.	"Can hydrolyze cephalosporins, penicillins and also cefoxitin; but at a slow rate."	.	.	BLAC_PHOVU	Reviewed	.	.	.	.	.	.
Mol00843	Protein	Beta-lactamase (BLA)	PIT-2; shv1	bla	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRYIRLCIISLLATLPLAVHASPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR	.	.	.	.	BLA1_ECOLX	Reviewed	.	.	.	.	.	.
Mol00844	Protein	Beta-lactamase (BLA)	bla_SHV-12	blaSHV-12	.	Salmonella enterica serotype wien	149391	Salmonella enterica subsp. enterica serovar Braenderup	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRYIRLCIISLLATLPLAVHASPQPLEQIKQSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGASKRGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR	.	.	.	.	B1NX62_SALET	Unreviewed	.	.	.	.	.	.
Mol00845	Protein	Beta-lactamase (BLA)	Cephalosporinase; PA4110	ampC	878149	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRVTPETLFEIGSVSKTFTATLAGYALTQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR	.	.	PDB: 2WZX; PDB: 2WZZ; PDB: 3S1Y; PDB: 3S22; PDB: 4GZB; PDB: 4HEF; PDB: 4NK3; PDB: 4OOY; PDB: 4WYY; PDB: 4WZ4; PDB: 4X68; PDB: 6UQS; PDB: 6UQT; PDB: 6UQU; PDB: 6UR3	.	AMPC_PSEAE	Reviewed	.	.	.	.	.	.
Mol00846	Protein	Beta-lactamase-like protein (VARG)	D6U24_07385; ERS013186_01425; ERS013199_01612; ERS013207_02023	varG	57740219	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKLSTLALAPITAALLTFNASAKGHDHDNQRAIFFPGETVQDTVKVEVEPSATQSLKLGQKINNLYERQFDNSQATVQKLGKNTYWIGVNYYNATVVVNEDSVLLIDPLGDGRIDALFKGVQSITNKPITTIMYSHYHLDHLGGGNQLVDLIKKNYPKVDKIRVIASQTVADKINQHAEVGENGVKTPKVPAPNDIYDLTKPQTVQFGSMKIKMMAPKGSGHTPDNTMILIPSDRVLHFADMINPDQLPFYNFAGAEHFHGYEEDLQSLLSKPLSKQWDFINGGHGNIGSKQDVKDLLEYIADIRTEVGKQLEVAPYTPVLSDGNHFVWFKRWQDEITNNVHTALANKYGHMYGFDSGVVETHAAMILADMIDH	.	.	.	.	A0A655YL50_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00847	Protein	Beta-lactam-inducible penicillin-binding protein (MECA)	mecA; ftsI_1; pbp; AS852_00205; BN1321_10005; BSZ10_12685; SAMEA70245418_00035; ZH16; PBP2'; PBP2a; EC 3.4.16.4; Penicillin-binding protein 2; Penicillin-binding protein 2 prime; Penicillin-binding protein MecA; EC 2.4.1.129; Penicillin-binding protein PBP2a	mecA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKKIKIVPLILIVVVVGFGIYFYASKDKEINNTIDAIEDKNFKQVYKDSSYISKSDNGEVEMTERPIKIYNSLGVKDINIQDRKIKKVSKNKKRVDAQYKIKTNYGNIDRNVQFNFVKEDGMWKLDWDHSVIIPGMQKDQSIHIENLKSERGKILDRNNVELANTGTAYEIGIVPKNVSKKDYKAIAKELSISEDYIKQQMDQNWVQDDTFVPLKTVKKMDEYLRDFAKKFHLTTNETESRNYPLGKATSHLLGYVGPINSEELKQKEYKGYKDDAVIGKKGLEKLYDKKLQHEDGYRVTIVDDNSNTIAHTLIEKKKKDGKDIQLTIDAKVQKSIYNNMKNDYGSGTAIHPQTGELLALVSTPSYDVYPFMYGMSNEEYNKLTEDKKEPLLNKFQITTSPGSTQKILTAMIGLNNKTLDDKTSYKIDGKGWQKDKSWGGYNVTRYEVVNGNIDLKQAIESSDNIFFARVALELGSKKFEKGMKKLGVGEDIPSDYPFYNAQISNKNLDNEILLADSGYGQGEILINPVQILSIYSALENNGNINAPHLLKDTKNKVWKKNIISKENINLLTDGMQQVVNKTHKEDIYRSYANLIGKSGTAELKMKQGETGRQIGWFISYDKDNPNMMMAINVKDVQDKGMASYNAKISGKVYDELYENGNKKYDIDE	.	.	.	.	Q6I7E7_STAAU	Unreviewed	.	.	.	.	.	.
Mol00848	Protein	Bifunctional AAC/APH (AAC/APH)	AAC(6'); 2''-aminoglycoside phosphotransferase; APH(2''); R015; VRA0030	aacA-aphD	58049990	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNIVENEICIRTLIDDDFPLMLKWLTDERVLEFYGGRDKKYTLESLKKHYTEPWEDEVFRVIIEYNNVPIGYGQIYKMYDELYTDYHYPKTDEIVYGMDQFIGEPNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHELHEGKKEDCYLMEYRYDDNATNVKAMKYLIEHYFDNFKVDSIEIIGSGYDSVAYLVNNEYIFKTKFSTNKKKGYAKEKAIYNFLNTNLETNVKIPNIEYSYISDELSILGYKEIKGTFLTPEIYSTMSEEEQNLLKRDIASFLRQMHGLDYTDISECTIDNKQNVLEEYILLRETIYNDLTDIEKDYIESFMERLNATTVFEGKKCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTNFGEDILRMYGNIDIEKAKEYQDIVEEYYPIETIVYGIKNIKQEFIENGRKEIYKRTYKD	.	"Involved in resistance to gentamicin, tobramycin, and kanamycin. Tobramycin and kanamycin resistance is due to the ACC activity, specified by N-terminal region. The C-terminal region is a kinase that phosphorylates several 4,6-disubstituted aminoglycosides."	PDB: 4ORK; PDB: 5BYL; PDB: 5IQA; PDB: 5IQB; PDB: 5IQC; PDB: 5IQD; PDB: 5IQE; PDB: 5IQF; PDB: 5IQG; PDB: 5IQH; PDB: 5IQI; PDB: 6C5U; PDB: 6CAV; PDB: 6CEY; PDB: 6CGD; PDB: 6CGG; PDB: 6CH4	.	AACA_STAAU	Reviewed	.	.	.	.	.	.
Mol00849	Protein	Bifunctional AAC/APH (AAC/APH)	aph(2'')	aac(6')	.	Campylobacter jejuni	197	Campylobacter jejuni	Campylobacter	194	Campylobacteraceae	72294	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MEIVQDKIRIRTLTNDDFPLMLKWLTDDRVLEFYGGRDKKYTLESLKEHYTEKWEDEVFRVIIEYDNVPIGYGQVYKMYDELYSDYHYPKTNEIVYGMDQFIGEPEYWSKGIGSKYTKMIFEFLKKERNANAVILDPHKNNPRAIRSYQKSGFRIIEDLPEHELHEGKKEDCYLMEYRYDDNVTNVKAMKYLIEHYFEDFKVESIKVIGSGYDSVAYLVNGEYIFKTKFSANKKKGYEKEKAIYDFLNQRLNTNIKIPNVKYSYFSDNISILGYKEIKGTFLTPEIYFALSKEKQELLKQDIAMFLRQMHDLDYSEISLYTIDNKQNVLEEYQLLKDTIYDSLTDIEKQYVEDFMQRLHSTTIFDGKKCLCHNDFSCNHLLLDDENRLCGVIDFGDSGIIDEYCDFIYLLEDSEEEIGVSFGEDILRLYGNIDISKAKEYQDVVEQYYPIETIVYGIKNNRPDFIEKGRKEIYIRTRKDEKLRK	.	"Involved in resistance to gentamicin, tobramycin, and kanamycin. Tobramycin and kanamycin resistance is due to the ACC activity, specified by N-terminal region. The C-terminal region is a kinase that phosphorylates several 4,6-disubstituted aminoglycosides."	.	.	A0A075C639_CAMJU	Unreviewed	.	.	.	.	.	.
Mol00850	Protein	Brefeldin A resistance protein (BFR1)	hba2; SPCC18B5.01c; SPCPJ732.04c	bfr1	2539195	Schizosaccharomyces pombe	4896	Schizosaccharomyces pombe	Schizosaccharomyces	4895	Schizosaccharomycetaceae	4894	Schizosaccharomycetales	34346	Schizosaccharomycetes	147554	Ascomycota	4890	Fungi	4751	.	MNQNSDTTHGQALGSTLNHTTEVTRISNSSDHFEDSSSNVDESLDSSNPSSNEKASHTNEEYRSKGNQSYVPSSSNEPSPESSSNSDSSSSDDSSVDRLAGDPFELGENFNLKHYLRAYKDSLQRDDIITRSSGVCMRDHSVYGVGSGYEFLKTFPDIFLQPYRAITEKQVVEKAILSHCHALANAGELVMVLGQPGSGCSTFLRSVTSDTVHYKRVEGTTHYDGIDKADMKKFFPGDLLYSGENDVHFPSLTTAETLDFAAKCRTPNNRPCNLTRQEYVSRERHLIATAFGLTHTFNTKVGNDFVRGVSGGERKRVTISEGFATRPTIACWDNSTRGLDSSTAFEFVNVLRTCANELKMTSFVTAYQASEKIYKLFDRICVLYAGRQIYYGPADKAKQYFLDMGFDCHPRETTPDFLTAISDPKARFPRKGFENRVPRTPDEFEQMWRNSSVYADLMAEMESYDKRWTETTPASSEAPEKDNFGSDISATTKHELYRQSAVAEKSKRVKDTSPYTVTFSQQLWYCLARSWERYINDPAYIGSMAFAFLFQSLIIGSIFYDMKLNTVDVFSRGGVLFFSILFCALQSLSEIANMFSQRPIIAKHRASALYHPAADVISSLIVDLPFRFINISVFSIVLYFLTNLKRTAGGFWTYFLFLFIGATCMSAFFRSLAGIMPNVESASALGGIGVLAIAIYTGYAIPNIDVGWWFRWIAYLDPLQFGFESLMINEFKARQFECSQLIPYGSGYDNYPVANKICPVTSAEPGTDYVDGSTYLYISFNYKTRQLWRNLAIIIGYYAFLVFVNIVASETLNFNDLKGEYLVFRRGHAPDAVKAAVNEGGKPLDLETGQDTQGGDVVKESPDNEEELNKEYEGIEKGHDIFSWRNLNYDIQIKGEHRRLLNGVQGFVVPGKLTALMGESGAGKTTLLNVLAQRVDTGVVTGDMLVNGRGLDSTFQRRTGYVQQQDVHIGESTVREALRFSAALRQPASVPLSEKYEYVESVIKLLEMESYAEAIIGTPGSGLNVEQRKRATIGVELAAKPALLLFLDEPTSGLDSQSAWSIVCFLRKLADAGQAILCTIHQPSAVLFDQFDRLLLLQKGGKTVYFGDIGEHSKTLLNYFESHGAVHCPDDGNPAEYILDVIGAGATATTNRDWHEVWNNSEERKAISAELDKINASFSNSEDKKTLSKEDRSTYAMPLWFQVKMVMTRNFQSYWREPSILMSKLALDIFAGLFIGFTFYNQGLGVQNIQNKLFAVFMATVLAVPLINGLQPKFIELRNVFEVREKPSNIYSWVAFVFSAIIVEIPFNLVFGTLFFLCWFYPIKFYKHIHHPGDKTGYAWLLYMFFQMYFSTFGQAVASACPNAQTASVVNSLLFTFVITFNGVLQPNSNLVGFWHWMHSLTPFTYLIEGLLSDLVHGLPVECKSHEMLTINPPSGQTCGEYMSAFLTNNTAAGNLLNPNATTSCSYCPYQTADQFLERFSMRYTHRWRNLGIFVGYVFFNIFAVLLLFYVFRVMKLRSTWLGKKITGTG	.	"Confers hyper-resistance to brefeldin A (BFA), an inhibitor of intracellular protein transport. Could serve as an efflux pump of various antibiotics."	.	.	BFR1_SCHPO	Reviewed	.	.	.	.	.	.
Mol00851	Protein	CAM-1 carbapenemase (CAM1)	ICEPACAM-1_00375	blaCAM-1	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKSTAIILFLLVFSLGVFGQTGDALKISQLSGDFYIFTTYQTYKDAKVSANGMYVVTDEGVVLIDTPWDETQLQPLLNYIKEKHNKDVVMSVSTHFHEDRTNGIEFLRTKGVKTYTTKKTDELSQKKGYERAEFLLEKDTEFKIGQYKFQTYYPGEGHAPDNIVVWFPNERILYGGCFIKSTEAEDIGNLSDANIDEWSNSIKNVQKKFKNPKFVIPGHDGWASTKSLKHTLKLIKKTRKK	.	.	.	.	A0A2R4PHC7_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00852	Protein	Capreomycin acetyltransferase (CPAA)	cpaA; AK95_27390; CpaA	cpaA	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MPLRITAMTETYADQIMQWSYEPPYDFYNSEPDEEFRKELLECSYYAILDKEGQLFGFCCTGSSAQIPIAIPLGAYDEDLLDFGLGMKPESTGQCRGKEFLSFVLASIAEFHKRQSFRLTVAKFNERAIRLYTQLGFSEVATFDYGGTTFITMIKKPGSGL	.	.	.	.	A0A1I9ZKK5_9BACL	Unreviewed	.	.	.	.	.	.
Mol00853	Protein	Carboxymethylenebutenolidase (CLCD)	CLHOM_33680	clcD	.	Clostridium homopropionicum	36844	Clostridium homopropionicum	Clostridium	1485	Clostridiaceae	31979	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKIINNSDSVIIVLHEIYGINQHIRMACEKFSTNGYDIICPNLIHVNQPFSYDLQEEAYRHFINNIGFYSATKQVKQLILEAKEKYNHVYLLGYSIGATIAWLCSNGENMCDGIIGYYGSRIRDYMNITPKCPALLIFPTEEKSFNVQELVDSLGKCNIDAFILNGKHGFSDPFSENYCAQSFEKAERLVSNFLKK	.	.	.	.	A0A0L6Z678_9CLOT	Unreviewed	.	.	.	.	.	.
Mol00854	Protein	Cardiolipin synthase (CLS)	CL synthase; cls; CWC53_05265; GBM73_14260; SMVRE20_01891	clsA	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MKIIVDNFFTILLIMNILLSFIIVFRERKETAQTWAWLLVLMFIPVVGFILYIFLGRGISKEKIFDLKIQGKIGKNLEIEEDKQALMRGLYPHPPTGQVDVKQLIYMLTVFESTLYTTKNEITLFTDGREKFDALIEDIKQAEDHIHFQYYIYRSDALGEEVRDALTEAARRGVKVRVLLDAWGSTQVSSSFFQNLKKAGGEIAFFFPLFVPYINPRINYRNHRKIVVIDGKIGYTGGFNVGNEYLGLVKKFGYWRDNHLRIYGEAVYILQNRFLMDWNSQHTKEVGYSPKFFPSIHSTGDIAVQIVTSGPDTEHEQIKMTYLKMISLAKREILIQTPYYIPDGSIHEALKLALLSGVKVHIQIPNKPDHLLVYWATYSFAAELIEYGARIETYENGFIHAKTMIIDGGIVSVGSANIDVRSFRLDFEVNTLIYDERMASRVRKAFFEDSKISTHLTKEMYENRGIIIKMKEGLARLISPLL	.	Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.	.	.	A0A455TTM7_ENTFC	Unreviewed	.	.	.	.	.	.
Mol00855	Protein	Cardiolipin synthase 2 (CLS2)	CL synthase 2; SACOL2079	cls2	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MIELLSIALKHSNIILNSIFIGAFILNLLFAFTIIFMERRSANSIWAWLLVLVFLPLFGFILYLLLGRQIQRDQIFKIDKEDKKGLELIVDEQLAALKNENFSNSNYQIVKFKEMIQMLLYNNAAFLTTDNDLKIYTDGQEKFDDLIQDIRNATDYIHFQYYIIQNDELGRTILNELGKKAEQGVEVKILYDDMGSRGLRKKGLRPFRNKGGHAEAFFPSKLPLINLRMNNRNHRKIVVIDGQIGYVGGFNVGDEYLGKSKKFGYWRDTHLRIVGDAVNALQLRFILDWNSQATRDHISYDDRYFPDVNSGGTIGVQIASSGPDEEWEQIKYGYLKMISSAKKSIYIQSPYFIPDQAFLDSIKIAALGGVDVNIMIPNKPDHPFVFWATLKNAASLLDAGVKVFHYDNGFLHSKTLVIDDEIASVGTANMDHRSFTLNFEVNAFIYDQQIAKKLKQAFIDDLAVSSELTKARYAKRSLWIKFKEGISQLLSPIL	.	Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.	.	.	CLS2_STAAC	Reviewed	.	.	.	.	.	.
Mol00856	Protein	Catalase-peroxidase (KATG)	CP; Peroxidase/catalase; Rv1908c; MTCY180.10	katG	885638	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGAAFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRGGAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKTFGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPDPMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGWKSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAGAGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDMGPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAASSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSFADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGKGNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVNLLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKFVQDFVAAWDKVMNLDRFDVR	.	"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity, oxidizing various electron donors including NADP(H). Protects M.tuberculosis against toxic reactive oxygen species (ROS) including hydrogen peroxide as well as organic peroxides and thus contributes to its survival within host macrophages by countering the phagocyte oxidative burst. Also displays efficient peroxynitritase activity, which may help the bacterium to persist in macrophages."	.	.	KATG_MYCTU	Reviewed	.	.	.	.	.	.
Mol00857	Protein	CATB10-Ib variant (CATB10)	catB10; CatB10	catB10	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTNYFESPFKGKLLADQVKNPNIKVGRYSYYSGYYHGHSFDECARFLLPDRNDIDQLIVGSFCSIGTGASFIMAGNQGHRYDWASSFPFFYMKEEPAFSGALDAFQKAGDTVIGSDVWIGSEAMIMPGINVGHGAVIGSRALVTKDVEPYTIVGGNPAKPIKKRFSDEEIAMLLKMNWWDWPTEKIEEAMPLLCSSNIVGLHRYWQGFAV	.	.	.	.	B8Y897_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00858	Protein	CATB6 chloramphenicol acetyltransferase (CATB6)	catB6; CatB6 protein	catB6	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MENYFDSPFKGKLLSEQVTNRNIKVGRYSYYSGYYHGHSFDDCARYLLPDRDDVDKLIIGSFCSIGSGASFIMAGNQGHRHDWVTSFPFFYMQEEPAFSSSTDAFQKAGDTIVGNDVWIGSEAMIMPGIKIGDGAVIGSRSLVTRDVEPYTIIGGNPAKQIKKRFSDEEISLLMEMEWWNWPLDKIKTAMPLLCSSDIFGLHRHWRGIAV	.	.	.	.	Q9R818_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00859	Protein	CCAAT-binding factor complex subunit (HAPE)	hapE; CCAAT-binding transcription factor complex subunit	hapE	.	Aspergillus fumigatus	746128	Aspergillus fumigatus	Aspergillus	5052	Aspergillaceae	1131492	Eurotiales	5042	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MEQSSQSTAQQQGRQQPVYDTRNGGHYGASAALSAQGYAPVAELYTGTWANVNQGLQGTARDILTTYWQHIINHLESDNHDYKIHQLPLARIKKVMKADPEVKMISAEAPILFAKGCDIFITELTMRAWIHAEDNKRRTLQRSDIAAALSKSDMFDFLIDIVPREEATSHAKRSSQTTAGAAGSSAATGAQLPPSQHGVQHPPHHMGPPDYGSLGQHGMGQDQEYRQPTMYGGAVQSDPTAAYGQPQSQIFEGMYNPYPHLPPQQVCQNSS	.	.	.	.	A0A1Y0LW31_ASPFM	Unreviewed	.	.	.	.	.	.
Mol00860	Protein	Chaperone protein ClpB (CLPB)	PA4542	clpB	879457	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRIDRLTSKLQLALSDAQSLAVGHDHPAIEPVHLLSALLEQQGGSIKPLLMQVGFDIAALRSGLNKELDALPKIQSPTGDVNLSQDLARLLNQADRLAQQKGDQFISSELVLLAAMDENTRLGKLLLGQGVSRKALENAVANLRGGEAVNDPNVEESRQALDKYTVDMTKRAEEGKLDPVIGRDDEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPDGLKDKRLLALDMGALIAGAKFRGEFEERLKAVLNELGKQEGRVILFIDELHTMVGAGKAEGAMDAGNMLKPALARGELHCVGATTLDEYRQYIEKDAALERRFQKVLVDEPSEEDTIAILRGLKERYEVHHGVSITDGAIIAAAKLSHRYITDRQLPDKAIDLIDEAASRIRMEIDSKPEELDRLDRRLIQLKIEREALKKEDDEATRKRLAKLEEDIVKLEREYADLEEIWKSEKAEVQGSAQIQQKIEQAKQEMEAARRKGDLESMARIQYQTIPDLERSLQMVDQHGKTENQLLRNKVTDEEIAEVVSKWTGIPVSKMLEGEREKLLRMEQELHRRVIGQDEAVVAVSNAVRRSRAGLADPNRPSGSFLFLGPTGVGKTELCKALAEFLFDTEEALVRIDMSEFMEKHSVARLIGAPPGYVGFEEGGYLTEAIRRKPYSVVLLDEVEKAHPDVFNILLQVLEDGRLTDSHGRTVDFRNTVVVMTSNLGSAQIQELAGDREAQRAAVMDAVNAHFRPEFINRIDEVVVFEPLAREQIAGIAEIQLGRLRKRLAERELSLELSQEALDKLIAVGFDPVYGARPLKRAIQRWIENPLAQLILAGKFAPGASISAKVEGDEIVFA	.	"Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity)."	.	.	CLPB_PSEAE	Reviewed	.	.	.	.	.	.
Mol00861	Protein	Chloramphenicol 3-O phosphotransferase (CH3OP)	CPT; SVEN_4064	SVEN_4064	.	Streptomyces venezuelae	54571	Streptomyces venezuelae	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTTRMIILNGGSSAGKSGIVRCLQSVLPEPWLAFGVDSLIEAMPLKMQSAEGGIEFDADGGVSIGPEFRALEGAWAEGVVAMARAGARIIIDDVFLGGAAAQERWRSFVGDLDVLWVGVRCDGAVAEGRETARGDRVAGMAAKQAYVVHEGVEYDVEVDTTHKESIECAWAIAAHVVP	.	Inactivates chloramphenicol by catalyzing the transfer of the gamma-phosphate of ATP to the antibiotic's C-3' hydroxyl group.	PDB: 1GRQ; PDB: 1GRR; PDB: 1QHN; PDB: 1QHS; PDB: 1QHX; PDB: 1QHY	.	CPT_STRVP	Reviewed	.	.	.	.	.	.
Mol00862	Protein	Chloramphenicol acetyltransferase (CAT)	.	catIII	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNYTKFDVKNWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPVMIYLIAQAVNQFDELRMAIKDDELIVWDSVDPQFTVFHQETETFSALSCPYSSDIDQFMVNYLSVMERYKSDTKLFPQGVTPENHLNISALPWVNFDSFNLNVANFTDYFAPIITMAKYQQEGDRLLLPLSVQVHHAVCDGFHVARFISRLQELCNSKLK	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	Q7B0A8_9BACT	Unreviewed	.	.	.	.	.	.
Mol00863	Protein	Chloramphenicol acetyltransferase (CAT)	.	cat-TC	.	Lactobacillus reuteri	1598	Limosilactobacillus reuteri	Limosilactobacillus	2742598	Lactobacillaceae	33958	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNFNKIDLDNWKRKEIFNHYLNQQTTFSITTEIDISVLYRNIKQEGYKFYPAFIFLVTRVINSNTAFRTGYNSDGELGYWDKLEPLYTIFDGVSKTFSGIWTSVKNDFKEFYDLYLSDVEKYNGSGKLFPKTPIPENAFSLSIIPWTSFTGFNLNINNNSNYLLPIITAGKFINKGNSIYLPLSLQVHHSVCDGYHAGLFMNSIRNCQIGLMTGFYNIDKPTVLFTVGFLMSLTCPLI	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	P94902_LIMRT	Unreviewed	.	.	.	.	.	.
Mol00864	Protein	Chloramphenicol acetyltransferase (CAT)	Atu4738; AGR_L_286	cat	.	Agrobacterium tumefaciens	358	Agrobacterium tumefaciens	Agrobacterium	357	Rhizobiaceae	82115	Hyphomicrobiales	356	Alphaproteobacteria	28211	Proteobacteria	1224	.	.	.	MENYFESPFRGITLDKQVKSPNLVVGKYSYYSGYYHGHSFEDCARYLLPDEGADRLVIGSFCSIGSGAAFIMAGNQGHRNEWISTFPFFFMPEVPEFENAANGYLPAGDTVIGNDVWIGSEAIIMPGITVGDGAVIGTRALVTKDVEPYAIVGGNPAKTIRKRFDDDSIALLLEMKWWGWPAERLKAAMPLMTSGNVAALYRFWRSDSL	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT4_AGRFC	Reviewed	.	.	.	.	.	.
Mol00865	Protein	Chloramphenicol acetyltransferase (CAT)	CAT	catQ	.	Clostridium perfringens	1502	Clostridium perfringens	Clostridium	1485	Clostridiaceae	31979	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKFNLIDIEDWNRKPYFEHYLNAVRCTYSMTANIEITGLLREIKLKGLKLYPTLIYIITTVVNRHKEFRTCFDQKGKLGYWDSMNPSYTVFHKDNETFSSIWTEYDENFPRFYYNYLEDIRNYSDVLNFMPKTGEPANTINVSSIPWVNFTGFNLNIYNDATYLIPIFTLGKYFQQDNKILLPMSVQVHHAVCDGYHISRFFNEAQELASNYETWLGEK	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT1_CLOPF	Reviewed	.	.	.	.	.	.
Mol00866	Protein	Chloramphenicol acetyltransferase (CAT)	CAT	cat	.	Vibrio anguillarum	55601	Vibrio anguillarum	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MEFRLVDLKTWKRKEYFTHYFESVPCTYSMTVKLDITTIKTGKAKLYPALLYAVSTVVNRHEEFRMTVDDEGQIGIFSEMMPCYTIFQKDTEMFSNIWTEYIGDYTEFCKQYEKDMQQYGENKGMMAKPNPPVNTFPVSMIPWTTFEGFNLNLQKGYGYLLPIFTFGRYYEENGKYWIPLSIQVHHAVCDGFHTCRFINELQDVIQSLQNHGGDEE	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT_VIBAN	Reviewed	.	.	.	.	.	.
Mol00867	Protein	Chloramphenicol acetyltransferase (CAT)	CAT	cat	.	Staphylococcus intermedius	1285	Staphylococcus intermedius	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MTFNIIKLENWDRKEYFEHYFNQQTTYSITKEIDITLFKDMIKKKGYEIYPSLIYAIMEVVNKNKVFRTGINSENKLGYWDKLNPLYTVFNKQTEKFTNIWTESDNNFTSFYNNYKNDLFEYKDKEEMFPKKPIPENTIPISMIPWIDFSSFNLNIGNNSSFLLPIITIGKFYSENNKIYIPVALQLHHAVCDGYHASLFINEFQDIIKKVDDWI	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT_STAIN	Reviewed	.	.	.	.	.	.
Mol00868	Protein	Chloramphenicol acetyltransferase (CAT)	CAT	catB	.	Clostridium butyricum	1492	Clostridium butyricum	Clostridium	1485	Clostridiaceae	31979	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MNFNLIDINHWSRKPYFEHYLNNVKCTYSMTANIEITDLLYEIKLKNIKFYPTLIYMIATVVNNHKEFRICFDHKGSLGYWDSMNPSYTIFHKENETFSSIWTEYNKSFLRFYSDYLDDIKNYGNIMKFTPKSNEPDNTFSVSSIPWVSFTGFNLNVYNEGTYLIPIFTAGKYFKQENKIFIPISIQVHHAICDGYHASRFINEMQELAFSFQEWLENK	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT_CLOBU	Reviewed	.	.	.	.	.	.
Mol00869	Protein	Chloramphenicol acetyltransferase (CAT)	CAT	CAT	.	Campylobacter coli	195	Campylobacter coli	Campylobacter	194	Campylobacteraceae	72294	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MQFTKIDINNWTRKEYFDHYFGNTPCTYSMTVKLDISKLKKDGKKLYPTLLYGVTTIINRHEEFRTALDENGQVGVFSEMLPCYTVFHKETETFSSIWTEFTADYTEFLQNYQKDIDAFGERMGMSAKPNPPENTFPVSMIPWTSFEGFNLNLKKGYDYLLPIFTFGKYYEEGGKYYIPLSIQVHHAVCDGFHVCRFLDELQDLLNK	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT_CAMCO	Reviewed	.	.	.	.	.	.
Mol00870	Protein	Chloramphenicol acetyltransferase (CAT)	CAT; Cat-86	cat86	.	Bacillus pumilus	1408	Bacillus pumilus	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MFKQIDENYLRKEHFHHYMTLTRCSYSLVINLDITKLHAILKEKKLKVYPVQIYLLARAVQKIPEFRMDQVNDELGYWEILHPSYTILNKETKTFSSIWTPFDENFAQFYKSCVADIETFSKSSNLFPKPHMPENMFNISSLPWIDFTSFNLNVSTDEAYLLPIFTIGKFKVEEGKIILPVAIQVHHAVCDGYHAGQYVEYLRWLIEHCDEWLNDSLHIT	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT_BACPU	Reviewed	.	.	.	.	.	.
Mol00871	Protein	Chloramphenicol acetyltransferase (CAT)	CEP63_016285	catA	.	Proteus mirabilis	1885	Streptomyces actuosus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MNYEKINLEQWNRKEHFLHYRHNLQCGFSLTTKIDITVLKTVLAKNNLKLYPAMIYLIAKTVNSYSESRMAIKDDELVIWDYINPVYTIFHPETETFSELWSEYVEDWHSFLEGYNQDYQKYKDNLSLSAKSNFPENHFCISMIPWISFDGFNLNVANVKDYFPPIFTMGKYTQQSDNFLLPISIQVHHATCDGFHIARMINKLQELCDGFSG	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	A0A2J9LAW3_PROMI	Unreviewed	.	.	.	.	.	.
Mol00872	Protein	Chloramphenicol acetyltransferase (CAT)	.	catV	.	Brevibacillus brevis	1393	Brevibacillus brevis	Brevibacillus	55080	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKFQRIDLDNWSRRSYFEHYLNRVNCTFSMTANIDITELLPALRQKEMKLYPAFLYMVTNAVNAHREFRTSFHADGELGYWESMIPSYTFFHQDDQTFSTMWTEFADEFPVFYQNYVADMKKYGDNKGLVAKELEPPYTFPVSCIPWVSFSGFNLNISGDGRYLLPIITSGKYFGQEGKTLLPVSLQVHHAVCDGYHASLFIHDLQKWATNYKEWLGVE	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	A0A291R8R6_BREBE	Unreviewed	.	.	.	.	.	.
Mol00873	Protein	Chloramphenicol acetyltransferase (CAT)	CGZ46_14915; EY666_15625	catA	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MTFNIINLETWDRKEYFNHYFNQQTTFSVTKEFDITLLKSMIKNKGYKLYPALIYIIVNIINQNKVFRTGINSEGNLGYWDKLNPLYTVFNKETEKFSNIWTESNVSFNSFYNSYKSDLLEYKDKNEMFPKKPIPENTVPISMIPWIDFSSFNLNIGNNSRFLLPIITMGKFYSKNNKIYLPVSLQVHHAVCDGYHASLFMSEFQNMVDSVNEWI	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	A0A1J6XFK8_ENTFL	Unreviewed	.	.	.	.	.	.
Mol00874	Protein	Chloramphenicol acetyltransferase (CAT)	AK95_11695	catU	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKFHIINVEEWTRKPYYEHYLRSNKCTFSITVDIDITRLLYSLKANGFKLYPAFIYMVTRVVNDRVEFKTSFSPEGELGYWDRMTPSYTFFHNDDHTFSCLWTAFSNDFYRFHDHYEQDMEQYRDTKGLFVKENPPPNTFPISMIPWTSFSGFNLNIVNEADYLLPIITGGKYTEQGGRVLLPVSLQVHHAVCDGYHASMFFKELQSLADSFEDWLT	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	A0A1I9ZKK1_9BACL	Unreviewed	.	.	.	.	.	.
Mol00875	Protein	Chloramphenicol acetyltransferase 2 (CATII)	Chloramphenicol acetyltransferase II; CAT-II	cat-IIH	.	Haemophilus influenzae	727	Haemophilus influenzae	Haemophilus	724	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNFTRIDLNTWNRREHFALYRQQIKCGFSLTTKLDITAFRTALAETDYKFYPVMIYLISRVVNQFPEFRMAMKDNALIYWDQTDPVFTVFHKETETFSALFCRYCPDISEFMAGYNAVMAEYQHNTALFPQGALPENHLNISSLPWVSFDGFNLNITGNDDYFAPVFTMAKFQQEDNRVLLPVSVQVHHAVCDGFHAARFINTLQMMCDNILK	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT2_HAEIF	Reviewed	.	.	.	.	.	.
Mol00876	Protein	Chloramphenicol acetyltransferase 2 (CATII)	Chloramphenicol acetyltransferase II; CAT-II	cmlA	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNFTRIDLNTWNRREHFALYRQQIKCGFSLTTKLDITALRTALAETGYKFYPLMIYLISRAVNQFPEFRMALKDNELIYWDQSDPVFTVFHKETETFSALSCRYFPDLSEFMAGYNAVTAEYQHDTRLFPQGNLPENHLNISSLPWVSFDGFNLNITGNDDYFAPVFTMAKFQQEGDRVLLPVSVQVHHAVCDGFHAARFINTLQLMCDNILK	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT2_ECOLX	Reviewed	.	.	.	.	.	.
Mol00877	Protein	Chloramphenicol acetyltransferase gene (CATS)	CATS; Fragment	CATS	.	Streptococcus pyogenes	1314	Streptococcus pyogenes	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	FTNIPCTYSMTVKLDITQIKKKRMKLYPAMLYYLATIVNRHSEFRTAINQEGELGIYDEMIPSYTIFHEDTETFSNLWTPYIPDFEAFSMAYANDMQRYGSNYGMIGKPDIPENVFNVSMIPWSTFDSFNLNLQKGYDYLIPIFTMGKYYRDDEKIILPLAIQV	.	.	.	.	Q54803_STRPY	Unreviewed	.	.	.	.	.	.
Mol00878	Protein	Chloramphenicol resistance protein (CMX)	cmx; Fragment	cmx	.	Corynebacterium glutamicum	1718	Corynebacterium glutamicum	Corynebacterium	1716	Corynebacteriaceae	1653	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	FSLLLITRVLSALANTGFLAVALSTATTLVPANQKGRALSILLSGTTIATVVGVPAGALLGTALGWRTTFWAIAILCIPAAVGVIRGVTNNVGRSETSATSPRLRVELSQLATPRLILAMALGALINGGTFAAFTFLAPIVTETAGLAEAWVSVALVMFGIGSFLGVTIAGRLSDQRPGLVLAVGGPLLLTGWIVLAV	.	.	.	.	A0A345Z5Q8_CORST	Unreviewed	.	.	.	.	.	.
Mol00879	Protein	Chloroquine resistance transporter (CRT)	PfCRT	CRT	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MKFASKKNNQKNSSKNDERYRELDNLVQEGNGSRLGGGSCLGKCAHVFKLIFKEIKDNIFIYILSIIYLSVCVMNKIFAKRTLNKIGNYSFVTSETHNFICMIMFFIVYSLFGNKKGNSKERHRSFNLQFFAISMLDACSVILAFIGLTRTTGNIQSFVLQLSIPINMFFCFLILRYRYHLYNYLGAVIIVVTIALVEMKLSFETQEENSIIFNLVLISALIPVCFSNMTREIVFKKYKIDILRLNAMVSFFQLFTSCLILPVYTLPFLKQLHLPYNEIWTNIKNGFACLFLGRNTVVENCGLGMAKLCDDCDGAWKTFALFSFFNICDNLITSYIIDKFSTMTYTIVSCIQGPAIAIAYYFKFLAGDVVREPRLLDFVTLFGYLFGSIIYRVGNIILERKKMRNEENEDSEGELTNVDSIITQ	.	May regulate endogenous transporter.	.	.	CRT_PLAFA	Reviewed	.	.	.	.	.	.
Mol00880	Protein	Chloroquine resistance transporter (CRT)	CRT	CRT	.	Toxoplasma gondii	5811	Toxoplasma gondii	Toxoplasma	5810	Sarcocystidae	5809	Eucoccidiorida	75739	Conoidasida	1280412	Apicomplexa	5794	.	.	.	MPPAHHGSGGRRRPGRGNKGKRDTEAGMTASPDPGYMRPETHAAPSQQTDVRSPASAREHRNADVGVAAPDALTPNAGEQKEVEGVAKVNVAVSSDQPPDWAPSQSDLPPSLSPTTASRPATSSRSPRARSRHSPVASSSAFSSPAPSASALTSASGVPEAPLAAPELKHTLAADEGNPEPRLEGPVERLHARQENPLTDSSDGSYILLEEGESQRACLDRKNRHLRQTTPPGVWTTADLASQNSHSASFASGFRRALLPSGGSGDHDEQASDCRASLRGMQRPCFGSPSTDTRMGAAEGLPLASRRRRQHWRRELRAFGAVALACLRASWHGMKRARLRATRWIDRNAATVRVACYTFLLLVTSTGNTICFKKMIDKMPNYSPCLTQVTTVVFVPVFFALSLYTDYAGGLPQEMADFPKRNFAVMGFLDSFSGVMAIIGAVHTTGTTQVVLQQSCIVFSLLASIVMLRKRFHAAHYLGALVIILGVLVVKLPDLLHPSSDGGGDVFVFNLLYLLSNLPTAVSCVYKEVAFRGVEMGTNYLQAWVALFQFLIGFLVLPLNALPVLGPQRVPLAELPASLWNGTRCLFGFNTIVTNCGGAGNMESPCDNCEGAWKYVGMYLSFNLLYNMFIIFVVKSGGAALTFLVSTLRLPVTALAFCSRAIMGDRAVPPKATDFYGLLVLILGLVIYRAGGIMKRRAQRRAVAAARGHTSSPMMLTPREEEQIGTIFVEEVFAAGELEDGGVTEEDETDDDTSEVEVHPVFSSVVASEPPHVYVHTKRHSHSDGGYHKLPACGSSPAAFTPFTQRMPGTGSESCSRRRNRDGDDERSPRSHACSFDEETGFAGGTGTGRHFSSPGTALSPNRVGGYEPPSMHAVQPAVIGKSRANNGCI	.	.	.	.	A0A059XKS9_TOXGO	Unreviewed	.	.	.	.	.	.
Mol00881	Protein	Cholinesterase (BCHE)	Acylcholine acylhydrolase; Butyrylcholine esterase; Choline esterase II; Pseudocholinesterase; CHE1	BCHE	590	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000264381.8, BCHE-201, 2405; ENST00000488954.1, BCHE-204, 739; ENST00000479451.5, BCHE-202, 702; ENST00000482958.1, BCHE-203, 2527; ENST00000497011.5, BCHE-205, 2522"	MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL	chr3:165772904-165837462[-]	Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.	PDB: 1P0I; PDB: 1P0M; PDB: 1P0P; PDB: 1P0Q; PDB: 1XLU; PDB: 1XLV; PDB: 1XLW; PDB: 2J4C; PDB: 2PM8; PDB: 2WID; PDB: 2WIF; PDB: 2WIG; PDB: 2WIJ; PDB: 2WIK; PDB: 2WIL; PDB: 2WSL; PDB: 2XMB; PDB: 2XMC; PDB: 2XMD; PDB: 2XMG; PDB: 2XQF; PDB: 2XQG; PDB: 2XQI; PDB: 2XQJ; PDB: 2XQK; PDB: 2Y1K; PDB: 3DJY; PDB: 3DKK; PDB: 3O9M; PDB: 4AQD; PDB: 4AXB; PDB: 4B0O; PDB: 4B0P; PDB: 4BBZ; PDB: 4BDS; PDB: 4TPK; PDB: 4XII; PDB: 5DYT; PDB: 5DYW; PDB: 5DYY; PDB: 5K5E; PDB: 5LKR; PDB: 5NN0; PDB: 6EMI; PDB: 6EP4; PDB: 6EQP; PDB: 6EQQ; PDB: 6ESJ; PDB: 6ESY; PDB: 6EUL; PDB: 6EYF; PDB: 6EZ2; PDB: 6F7Q; PDB: 6I0B; PDB: 6I0C; PDB: 6I2T; PDB: 6QAA; PDB: 6QAB; PDB: 6QAC; PDB: 6QAD; PDB: 6QAE; PDB: 6R6V; PDB: 6R6W; PDB: 6RUA; PDB: 6SAM; PDB: 6T9P; PDB: 6T9S; PDB: 6XTA; PDB: 6ZWI; PDB: 7AIY; PDB: 7AMZ; PDB: 7AWG; PDB: 7AWH; PDB: 7AWI; PDB: 7BGC	HGNC:983	CHLE_HUMAN	Reviewed	ENSG00000114200	.	.	.	.	.
Mol00882	Protein	Copper-translocating P-type ATPase (COPA)	D806_060860	D806_060860	.	Mycolicibacterium smegmatis	1772	Mycolicibacterium smegmatis	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTTSTPVPAASIELQIGGMTCASCANRIERRLNKLDGVIASVNYATEKATVAVPDGYDPADLISAVEATGYTASLPATSAPAREDTSPAAHDDPELDALRHRLLGSTVLSIPVIAMAMIPALQFTYWQWASLTLAAPVVIWAAWPFHRAAWANLRHGSATMDTLISMGTLAAFLWSLYALFLGTAGTAGMTHPFALALTPSHGAANIYLEVAAGVTTFILAGRYFEKRSKRQAGAALRALLELGAKEVSVLRDGAETKIPVDRLAVGDEFVVRPGEKIATDGVVVSGTSAVDASMLTGESIPVDVGVGDTVVGATVNAGGRLVVRASRVGSDTQLAQMAQLVENAQTGKAQVQRLADRISGVFVPIVIAVAVITLGAWLGAGYPAAAAFTAAVAVLVIACPCALGLATPTALLVGTGRGAQMGILIKGPEVLESTRTVDTVVLDKTGTVTTGKMALVDVRTIPGTQRRDLLRLAGALEDASEHPIARAIATAARDEVGVLPTVEDFANAEGEGVHGVVDGHAVVVGRESLLTDWAQHLDTDLAQAKQHAEAEGKTVVTVGWDGTARGILIIADTVKPTSAQAITELKELGLTPILLTGDNDAVARRIATDVGIDTVIAEVMPEGKVQAITILQSQGKTVAMIGDGVNDAAALAQADLGLAMGTGTDVAIEASDITLVRGDLRSAVDAIRLSRKTLSTIKTNLFWAFAYNVAAVPVAALGMLNPMLAGAAMAFSSVFVVGNSLRLRGFTSTFTDRKDNGHE	.	.	.	.	A0A2U9PZ75_MYCSE	Unreviewed	.	.	.	.	.	.
Mol00883	Protein	Cytidine deaminase (CDA)	Cytidine aminohydrolase; CDD	CDA	978	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375071.4, CDA-201, 809; ENST00000461985.1, CDA-202, 762"	MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ	chr1:20589086-20618903[+]	This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.	PDB: 1MQ0	HGNC:1712	CDD_HUMAN	Reviewed	ENSG00000158825	.	.	.	.	.
Mol00884	Protein	Cytochrome P450 sterol 14 alpha-demethylase (CYP51)	CYP51; I7I51_04085; Cytochrome P450 sterol 14 alpha-demethylase	CYP51	.	Histoplasma capsulatum	5037	Histoplasma capsulatum	Histoplasma	5036	Ajellomycetaceae	299071	Onygenales	33183	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MSWFTIGTFGVLAFVAAVTLNLVYQLLFRFLNKTRPPLVFHWIPFLGSTIRYRTDPYKFFFSCRQKEASRLFQHGDIFTFVLLGRPTTVYLGIKGNEFILNGKLKDVNAEEVYGPLTTPVFGPDVVYDCPNSKLIEQKKFIKYGLTQAALESHVPLIEKEVMDYLDSSPNFLGASGEVDISAVMAEITIFTAGSALQGEEVRSKLTTEFAVLYHDLDKGFSPINFMLPWAPLPHNKKRDAAHTLMHAIYLDIIEKRRRAARNANGSQTQDMIENLMQCTYKNGQKLPDKEIANIMISLLMAGQHSSSTTSSWIMLHLASEPAVVEQLYQEQLDNLPRTGPNGSLGPLQYGDLNRLPLHRNVIRETLRLHTSIHSLLRKVMNPMPVAGTPYVIPPSHVVLSAPGVTALSDEYFPNPTMWDPNRWETQEPKVDEKEDMVDYGYGTISKGTSSPYLPFGAGRHRCIGEKFAYVNLTVIVAIMVRHLQFSNIGGKTGVPRTDYSSMFSAPMKPARINWKRRTAKSG	.	.	.	.	A0A8A1M600_AJECA	Unreviewed	.	.	.	.	.	.
Mol00885	Protein	Cytotoxic T-lymphocyte protein 4 (CTLA4)	.	CTLA4	1493	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000648405.2, CTLA4-204, 1997; ENST00000295854.10, CTLA4-201, 525; ENST00000696479.1, CTLA4-207, 2039; ENST00000696049.1, CTLA4-206, 1168; ENST00000487393.1, CTLA4-203, 214; ENST00000427473.3, CTLA4-202, 874; ENST00000650075.1, CTLA4-205, 740"	MACLGFQRHKAQLNLATRTWPCTLLFFLLFIPVFCKAMHVAQPAVVLASSRGIASFVCEYASPGKATEVRVTVLRQADSQVTEVCAATYMMGNELTFLDDSICTGTSSGNQVNLTIQGLRAMDTGLYICKVELMYPPPYYLGIGNGTQIYVIDPEPCPDSDFLLWILAAVSSGLFFYSFLLTAVSLSKMLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN	chr2:203853888-203873965[+]	"Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28."	PDB: 1AH1; PDB: 1H6E; PDB: 1I85; PDB: 1I8L; PDB: 2X44; PDB: 3BX7; PDB: 3OSK; PDB: 5GGV; PDB: 5TRU; PDB: 5XJ3; PDB: 6RP8; PDB: 6RPJ; PDB: 6RQM; PDB: 6XY2; PDB: 7CIO; PDB: 7ELX	HGNC:2505	CTLA4_HUMAN	Reviewed	ENSG00000163599	.	.	.	.	.
Mol00886	Protein	"D-glucan-1,3-beta--UDP glucosyltransferase (FKS1)"	FKS	FKS	.	Aspergillus fumigatus	746128	Aspergillus fumigatus	Aspergillus	5052	Aspergillaceae	1131492	Eurotiales	5042	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MSGYQQGGGHYNDGYGHQEHGDSFYQDEHGQAYYDHDYGDGYYDRSGYYGPDGNHNQQEGGYYDAGQPHDDYYGDHYYDQGNGQQGYDNRGRRRGDSEEDSETFSDFTMRSETARAADMDYYGRGDERYNSYADSQYGGRGYGYRPPSSQISYGANRSSGASTPVYGMDYGNALPAGQRSREPYPAWASDGQVPVSKEEIEDIFLDLVNKFGFQRDSMRNMYDHLMTMLDSRASRMTPNQALLSLHADYIGGDNANYRRWYFAAHLDLDDAVGFANMKLGKADRKTRKARKAAKKAAQQNPENVEETLEALEGDNSLEAAEYRWKTRMNKMSQHDRVRQLALFLLCWGEANQVRFLPECLCFIFKCADDYYNSPECQNRVEPVEEFTYLNEIITPLYQYCRDQGYEIVDGKYVRRERDHNQIIVSDMNQLFWYPEGIERIALEDKTRLVDIPPAERWTKLKDVVWKKAFFKTYKETRSWFHMITNFNRIWVIHLGAFWFFTAFNAQSLYTDNYQQQVNNKPPGYRIWSAVGFGGALSSFIQIAATICEWMYVPRRWAGAQHLTKRLMFLILVFVINLAPGVFVFAYSKSMGISKTIPLIVGIVHFFVALATFVFFSVMPLGGLFGSYLKKHGRQYVASQTFTASFPRLHGNDMWMSYGLWVCVFGAKLAESYFFLTLSFKDPIRILSPMQIHQCAGVKYIGNVLCHKQPQILLGLMFFMDLTLFFLDSYLWYIICNTVFSVARSFYLGVSIWSPWRNIFSRLPKRIYSKVLATTDMEIKYKPKVLISQVWNAIIISMYREHLLAIDHVQKLLYHQVPSEQEGKRTLRAPTFFVSQEDQSFKTEFFPPGSEAERRISFFAQSLSTPMPEPLPVDNMPTFTVLIPHYSEKILLSLREIIREDEPYSRVTLLEYLKQLHPHEWDCFVKDTKILADETSQFNGEPEKSEKDVAKSKIDDLPFYCIGFKSAAPEYTLRTRIWSSLRSQTLYRTVSGFMNYSRAIKLLYRVENPEVVQMFGGNSEKLERELERMARRKFKIVVSMQRYAKFNKEERENTEFLLRAYPDLQIAYLDEEPPVNEGEEPRLYSALIDGHCELLENGMRKPKFRIQLSGNPILGDGKSDNQNHSIIFYRGEYIQVIDANQDNYLEECLKIRSVLAEFEELTTDNVSPYTPGIPSTNTNPVAILGAREYIFSENIGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFLNGIFMTTRGGISKAQKGLHLNEDIYAGMNAMIRGGRIKHCEYYQCGKGRDLGFGSILNFTTKIGTGMGEQMLSREYYYLGTQLPLDRFLSFYYAHPGFHINNMFIMLSVQMFMIVLINLGALKHETITCRYNPDLPITDPLRPTYCANLTPIVDWVNRCIISIFIVFFISFVPLAVQELTERGVWRMAMRLAKHFGSVSFMFEVFVCQIYANAVHQNLSFGGARYIGTGRGFATARIPFGVLYSRFAGPSIYAGARSLLMLLFATSTVWTAALIWFWVSLLALCISPFLFNPHQFAWNDFFIDYRDYLRWLSRGNSRSHASSWIGFCRLSRTRITGYKRKLLGVPSEKGSGDVPRARLTNIFFSEIIAPLVLVAVTLVPYLYINSRTGVRDNPETTDAILRLAIVAAGPIAINAGVAGVFFGMACCMGPIFSMCCKKFGAVLAAIAHAIAVIVLLAIFEVMFFLESWSWPRMLIGMIAAAAIQRFIYKLIIALALTREFKHDQSNIAWWTGKWYNMGWHSMSQPGREFLCKITELGYFSADFVLGHVLLFAMLPALCVPFIDKFHSVMLFWLRPSRQIRPPIYSLKQSKLRKRRVIRFAILYFGMLILFLVLLIAPLVVRSMGLVKTPNLPFNLLQPLDKDNNDTMVTYTGNNIPAGFEPVESASSVATATS	.	.	.	.	P87204_ASPFM	Unreviewed	.	.	.	.	.	.
Mol00887	Protein	"D-glucan-1,3-beta--UDP glucosyltransferase (FKS1)"	GSC1; EC 2.4.1.34	GSC1	.	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSYNDNNNHYYDPNQQGGMPPHQGGEGYYQQQYDDMGQQPHQQDYYDPNAQYQQQPYDMDGYQDQANYGGQPMNAQGYNADPEAFSDFSYGGQTPGTPGYDQYGTQYTPSQMSYGGDPRSSGASTPIYGGQGQGYDPTQFNMSSNLPYPAWSADPQAPIKIEHIEDIFIDLTNKFGFQRDSMRNMFDYFMTLLDSRSSRMSPAQALLSLHADYIGGDNANYRKWYFSSQQDLDDSLGFANMTLGKIGRKARKASKKSKKARKAAEEHGQDVDALANELEGDYSLEAAEIRWKAKMNSLTPEERVRDLALYLLIWGEANQVRFTPECLCYIYKSATDYLNSPLCQQRQEPVPEGDYLNRVITPLYRFIRSQVYEIYDGRFVKREKDHNKVIGYDDVNQLFWYPEGISRIIFEDGTRLVDIPQEERFLKLGEVEWKNVFFKTYKEIRTWLHFVTNFNRIWIIHGTIYWMYTAYNSPTLYTKHYVQTINQQPLASSRWAACAIGGVLASFIQILATLFEWIFVPREWAGAQHLSRRMLFLVLIFLLNLVPPVYTFQITKLVIYSKSAYAVSIVGFFIAVATLVFFAVMPLGGLFTSYMNKRSRRYIASQTFTANYIKLKGLDMWMSYLLWFLVFLAKLVESYFFSTLSLRDPIRNLSTMTMRCVGEVWYKDIVCRNQAKIVLGLMYLVDLLLFFLDTYMWYIICNCIFSIGRSFYLGISILTPWRNIFTRLPKRIYSKILATTEMEIKYKPKVLISQIWNAIVISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRNSEAERRISFFAQSLATPMPEPLPVDNMPTFTVFTPHYSEKILLSLREIIREDDQFSRVTLLEYLKQLHPVEWDCFVKDTKILAEETAAYENGDDSEKLSEDGLKSKIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTVSGFMNYARAIKLLYRVENPELVQYFGGDPEGLELALERMARRKFRFLVSMQRLSKFKDDEMENAEFLLRAYPDLQIAYLDEEPALNEDEEPRVYSALIDGHCEMLENGRRRPKFRVQLSGNPILGDGKSDNQNHAVIFHRGEYIQLIDANQDNYLEECLKIRSVLAEFEEMNVEHVNPYAPNLKSEDNNTKKDPVAFLGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFLNATFMLTRGGVSKAQKGLHLNEDIYAGMNAMMRGGKIKHCEYYQCGKGRDLGFGSILNFTTKIGAGMGEQMLSREYFYLGTQLPLDRFLSFYYGHPGFHINNLFIQLSLQVFILVLGNLNSLAHEAIMCSYNKDVPVTDVLYPFGCYNIAPAVDWIRRYTLSIFIVFFISFIPLVVQELIERGVWKAFQRFVRHFISMSPFFEVFVAQIYSSSVFTDLTVGGARYISTGRGFATSRIPFSILYSRFADSSIYMGARLMLILLFGTVSHWQAPLLWFWASLSALMFSPFIFNPHQFAWEDFFLDYRDFIRWLSRGNTKWHRNSWIGYVRLSRSRITGFKRKLTGDVSEKAAGDASRAHRSNVLFADFLPTLIYTAGLYVAYTFINAQTGVTSYPYEINGSTDPQPVNSTLRLIICALAPVVIDMGCLGVCLAMACCAGPMLGLCCKKTGAVIAGVAHGVAVIVHIIFFIVMWVTEGFNFARLMLGIATMIYVQRLLFKFLTLCFLTREFKNDKANTAFWTGKWYNTGMGWMAFTQPSREFVAKIIEMSEFAGDFVLAHIILFCQLPLLFIPLVDRWHSMMLFWLKPSRLIRPPIYSLKQARLRKRMVRKYCVLYFAVLILFIVIIVAPAVASGQIAVDQFANIGGSGSIADGLFQPRNVSNNDTGNHRPKTYTWSYLSTRFTGSTTPYSTNPFRV	.	.	.	.	O13428_CANAX	Unreviewed	.	.	.	.	.	.
Mol00888	Protein	"D-glucan-1,3-beta--UDP glucosyltransferase (FKS1)"	1;3-beta-D-glucan-UDP glucosyltransferase; Calcineurin dependent protein 1; Calcofluor white hypersensitivity protein 53; Echinocandin target gene protein 1; FK506 sensitivity protein 1; Glucan synthase of cerevisiae protein 1; Papulacandin B resistance protein 1; CND1; CWH53; ETG1; GLS1; GSC1; PBR1; YLR342W; L8300.6	FKS1	851055	Saccharomyces cerevisiae	4932	Saccharomyces cerevisiae	Saccharomyces	4930	Saccharomycetaceae	4893	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MNTDQQPYQGQTDYTQGPGNGQSQEQDYDQYGQPLYPSQADGYYDPNVAAGTEADMYGQQPPNESYDQDYTNGEYYGQPPNMAAQDGENFSDFSSYGPPGTPGYDSYGGQYTASQMSYGEPNSSGTSTPIYGNYDPNAIAMALPNEPYPAWTADSQSPVSIEQIEDIFIDLTNRLGFQRDSMRNMFDHFMVLLDSRSSRMSPDQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMSLGKLSRKARKAKKKNKKAMEEANPEDTEETLNKIEGDNSLEAADFRWKAKMNQLSPLERVRHIALYLLCWGEANQVRFTAECLCFIYKCALDYLDSPLCQQRQEPMPEGDFLNRVITPIYHFIRNQVYEIVDGRFVKRERDHNKIVGYDDLNQLFWYPEGIAKIVLEDGTKLIELPLEERYLRLGDVVWDDVFFKTYKETRTWLHLVTNFNRIWVMHISIFWMYFAYNSPTFYTHNYQQLVDNQPLAAYKWASCALGGTVASLIQIVATLCEWSFVPRKWAGAQHLSRRFWFLCIIFGINLGPIIFVFAYDKDTVYSTAAHVVAAVMFFVAVATIIFFSIMPLGGLFTSYMKKSTRRYVASQTFTAAFAPLHGLDRWMSYLVWVTVFAAKYSESYYFLVLSLRDPIRILSTTAMRCTGEYWWGAVLCKVQPKIVLGLVIATDFILFFLDTYLWYIIVNTIFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQVWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAAYEGNENEAEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNAEGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLTEGEEPRIYSALIDGHCEILDNGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNVEQVNPYAPGLRYEEQTTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLSQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAMLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPVDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLSSLAHESIMCIYDRNKPKTDVLVPIGCYNFQPAVDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFCHLLSLSPMFEVFAGQIYSSALLSDLAIGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGARSMLMLLFGTVAHWQAPLLWFWASLSSLIFAPFVFNPHQFAWEDFFLDYRDYIRWLSRGNNQYHRNSWIGYVRMSRARITGFKRKLVGDESEKAAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDDDRVNSVLRIIICTLAPIAVNLGVLFFCMGMSCCSGPLFGMCCKKTGSVMAGIAHGVAVIVHIAFFIVMWVLESFNFVRMLIGVVTCIQCQRLIFHCMTALMLTREFKNDHANTAFWTGKWYGKGMGYMAWTQPSRELTAKVIELSEFAADFVLGHVILICQLPLIIIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQTRLRKRMVKKYCSLYFLVLAIFAGCIIGPAVASAKIHKHIGDSLDGVVHNLFQPINTTNNDTGSQMSTYQSHYYTHTPSLKTWSTIK	.	"Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Involved in cell wall synthesis, maintenance and cell wall remodeling."	.	.	FKS1_YEAST	Reviewed	.	.	.	.	.	.
Mol00889	Protein	"D-glucan-1,3-beta--UDP glucosyltransferase (FKS1)"	FKS2; AO440_003426; EC 2.4.1.34	FKS2	.	Candida glabrata	5478	Candida glabrata	Nakaseomyces	374468	Saccharomycetaceae	4893	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSYDQGGNGNWQNTDPNGNYYYNGAENNEFYDQDYASQQPEQQQGGEGYYDEYGQPNYNYMNDPQQGQMPQQQPGGYDNDGYYDSYYNNQMNAGVGNGLGPDQTNFSDFSSYGPPPFQNNQANYTPSQLSYSNNGMGSNGMNMSGSSTPVYGNYDPNAIAMTLPNDPYPAWTADPQSPVSIEQIEDVFIDLTNKFGFQRDSMRNIFDLFMTLLDSRTSRMSPDQALLSVHADYIGGDTANYKKWYFAAQLDMDDEVGFRNMNLGKLSRKARKAKKKNKKAMEEANPEDAAEVLNKIEGDNSLEASDFRWKTKMNMLTPIERVRQVALYMLIWGEANQVRFTSECLCFIYKCASDYLESPLCQQRTEPIPEGDYLNRVITPIYQFIRNQVYEIVDGRYVKREKDHNKIIGYDDVNQLFWYPEGITKIVLEDGTKLTDIPSEERYLRLGEVAWNDVFFKTYKETRTWLHLVTNFNRIWIMHVSVYWMYVAYNSPTFYTHNYQQLVNNQPVPAYRWASAALAGTVASAIQLFATVCEWWFVPRKWAGAQHLSRRFWFLCGILGVNLGPLIFVFAYEKDTVQSKAGHAVAAVTFFIAVATVLFFSIMPLGGLFTSYMQKSSRRYVASQTFTASFAPLQGLDRWLSYLVWVTVFAAKYSESYFFLILSLRDPIRILSTTTMRCTGEYWWGSKLCRHQSKIVLGFMIATDFILFFLDTYLWYIVVNTVFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQIWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRNSEAERRISFFAQSLATPMPEPLPVDNMPTFTVLTPHYSERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAAYENEEPQDPEKSDALKTQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTVSGFMNYARAIKLLYRVENPEIVQMFGGNAEGLERELEKMARRKFKFLVSMQRLAKFKPHELENTEFLLRAYPDLQIAYLDEEPPLNEGEEPRIYSALIDGHCEMLENGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNAEPVYPYTPGVKYEDQKTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFINATFMTTRSGLSKAQKGLHLNEDIYAGMNALLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPVDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLHALAHESILCIYDRNKPKTDVLYPIGCYNFSPAIDWIRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFRHILSLSPMFEVFAGQIYSAALLSDMTVGGARYISTGRGFATSRIPFSILYSRFASSAIYMGARSMLMLLFGTVAHWQAPLLWFWASLSALLFSPFIFNPHQFSWEDFFLDYRDYIRWLSRGNNKYHKNSWIGYVRMARSRITGFKRKLIGDDSEKAAGDANRAHRTNLILAELIPTAINAGSCFIGFTFINAQTGVKATDDDRVNSVLRVVLCTLGPIAVDVGVLFFCLGMSCCSGPLFGMCCKKTGAVMAAVAHGVSVVIHIGFFIVMWVLEGFNFTRMLVGVATVIQCQRFIFQLMTILLLTREFKNDHANTAFWTGKWYGSGFGYMAWTQPMRELTAKVIEMSEFAADFVLGHVILFAQFPVLCIPAIDKFHSIMLFWLKPSRHIRPPIYSLKQSRLRKRMVKRYLTLYIIIFLVFAGAIVGPAVAASHVPQDIGHTLTGPFHNIVQPRNKSNNDTGLQISTYSNHYYTHTPSLKTWSTIK	.	.	.	.	F5BCZ9_CANGB	Unreviewed	.	.	.	.	.	.
Mol00890	Protein	"D-glucan-1,3-beta--UDP glucosyltransferase (FKS1)"	FKS1; fks1; AO440_001525; EC 2.4.1.34	FKS1	2888318	Candida glabrata	5478	Candida glabrata	Nakaseomyces	374468	Saccharomycetaceae	4893	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSYNNNGQQMSDQGYYDNNQGYYQPEDQQNGQAMYGDEGYYDPNISGGDYYNQPPPPPNMMGQDMENFSDFSSYGPPGVQGYDYQNMNQSGQYTPSQMSYNGDPNSGSSTPIYGNGMSAYDPNAIAMALPNDPYPAWTADSQSPVPIEQIEDVFIDLTNKFGFQRDSMRNMFDHFMTLLDSRTSRMAPDQALLSLHADYIGGDTANYKKWYFAAQLDMDDEVGFRNMSLGKLSRKARKAKKKNKKAMEEANPEDAEDILNKLEGDNSLEAADFRWKTKMNALTPIERVRQIALYLLIWGEANQVRFTSECLCFIYKCATDYLNSPLCQQRTEPMPEGDYLNRVITPLYRFIRNQVYEIVDGRYVKREKDHHKVIGYDDVNQLFWYPEGIAKIVFEDSTKLIEIPAEERYLRLGEVSWDDVFFKTYKETRSWFHMITNFNRIWIMHVTIFWMYVAYNSPTFYTHNYQQLVNNQPPAAYKWASAALGGTVASFIQLLATICEWSFVPRKWAGAQHLSRRFWFLCLIFAVNLGPIIFVFAYEKDTVQSKAGHAVAAVMFFVAVATLLFFSVMPLGGLFTSYMQKSTRRYVASQTFTASFAPLHGLDRWLSYLVWVTVFAAKYAESYYFLILSLRDPIRILSTTTMRCTGEYWWGSKLCRHQSKIVLGLMIATDFILFFLDTYLWYIVVNTVFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQVWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRNSEAERRISFFAQSLATPMPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAAYEGMDDQDPEKEDALKNQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTVSGFMNYARAIKLLYRVENPEIVQMFGGNAEGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLNEGEEPRIYSALIDGHCEILENGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNAEQVYPYSPGVKYEDQNTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFINATFMTTRGGISKAQKGLHLNEDIYAGMNALLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPIDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLHALAHESIICIYDKNKPKTDVLYPIGCYNFSPAIDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFRHILSLSPMFEVFAGQIYSSALLSDLTVGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGARSMLMLLFGTVAHWQAPLLWFWASLSALLFSPFIFNPHQFSWEDFFLDYRDYIRWLSRGNSKYHRNSWIGYVRMARSRITGFKRKLVGDESEKAAGDASRAHRTNLILAEIIPNAIYAAGCFVGFTFINAQTGVKTTDDDRVNSVLRIIICTLAPIVIDIGVLFFVLGMSCCSGPLFGMCCKRTGSVMAGFAHGIAVIVHIGFFIVMWVLEGFNFTRMLLGVVTMIQCQRLIFQCMTVLMLTREFKNDHANTAFWTGKWYGSGFGYMAWTQPTRELTAKVIELSEFAADFVLGHVILFAQFPVLCIPAIDKFHSIMLFWLKPSRQIRPPIYSLKQSRLRKRMVKRYLTLYIIVFLVFAGCIVGPAVASSHVAKDLGHQLTGTFHNLVQPRNVSNNDTGFGISTYSNHYYTHTPSLKTWSTIK	.	.	.	.	E2GKZ4_CANGB	Unreviewed	.	.	.	.	.	.
Mol00891	Protein	"D-glucan-1,3-beta--UDP glucosyltransferase (FKS1)"	FKS1; EC 2.4.1.34	FKS1	.	Candida parapsilosis	5480	Candida parapsilosis	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSYNDNNHNYYDPNQQGGGVPNDGYYQQPYDMNQQQQQQQQQPYDDMNQQPQHQDYYDPNAQYHQQPYDMDGYNDPNQYGGHPMNAQGYNADPEAFSDFSYNGQAPGTPGYDQYGTQYTPSQMSYGGDPRSSGASTPIYGVQGQGYDPTQFQVSSNLPYPAWSADPQAPIKIEHIEDIFIDLTNKFGFQRDSMRNMFDYFMTLLDSRSSRMAPAQALLSLHADYIGGDNANYRKWFFSSQQDLDDTLGFANMTLGKIGRKARKASKKSKKARKAAEEHGEDVDALANELEGDYSLEAAEIRWKAKMNTLTPEERVRDIALYLLLWGEANQVRFTPECLCYLYKTAVDYLESPLCQQRQEPVPEGDYLNRVITPLYRFLRSQVYEIYEGRFVKREKDHNKVIGYDDVNQLFWYPEGVSRIIFTDGTRLIDIPKEERYLRLGEVEWSNVFFKTYKEIRTWLHFVTNFNRIWIIHGSIYWMYTAYNSPTLYTKNYVQTINQQPLASSRWAACAIGGIIAAFLQILATIFEWMFVPREWAGAQHLTRRLMFLILIFLVNLAPVVYTFKVAGLTLYSKSSYALSVVGFFIAVATLVFFAVMPLGGLFTSYMNKRSRRYISSHTFTANFVKLRGLDMWMSYLLWVLVFLAKLVESYFFLTLSLRDAIRNLSKTTMRCTGEVWYGDIVCRQQAKIVLGLMYAVDLLLFFLDTYLWYIICNCIFSIGRSFYLGISILTPWRNIFTRLPKRIYSKILATTEMEIKYKPKVLISQIWNAIVISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFASQDDNNFETEFFPRNSEAERRISFFAQSLATPMPEPVPVDNMPTFTVFTPHYSEKILLSLREIIREDDQFSRVTLLEYLKQLHPVEWECFVKDTKILAEETAAYENGEDAEKASEDGLKSKIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTVSGFMNYARAIKLLYRVENPELVQYFGGDPEGLELALEKMARRKFRFLVSMQRLSKFKDDEMENAEFLLRAYPDLQIAFLDEEPALNEDEEPRVYSSLIDGHCEMLENGRRRPKFRVQLSGNPILGDGKSDNQNHAIIFHRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNVEHVNPYSPDLKSENPLHEKKAPVAILGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFLNATFMLTRGGVSKAQKGLHLNEDIYAGMNAMMRGGKIKHCEYYQCGKGRDMGFGSILNFTTKIGAGMGEQMLSREYYYLSTQLPLDRFLSFYYGHPGFHINNLFIQLSLQVFMLVLANLNSLAHESIICSYDRDVPVTDVLYPFGCYNIAPAVDWIRRYTLSIFIVFFISFIPLVVQELIERGVWKACQRFVRHFISLSPMFEVFVAQIYSSSVFTDLTVGGARYISTGRGFATSRIPFSILYSRFADSSIYMGARLMLILLFGTVAHWQAPLLWFWASLSSLMFSPFIFNPHQFAWEDFFIDYRDFIRWLSRGNTKWHRNSWIGYVRLSRSRITGFKRKLTGDISEKAAGDASRAHRSNILFADFLPTLIYTAGLYVAFTFINAQTGVTQYPYEIDGSTDVQEVNSVLRLIVCSLAPVVIDCGVLFGCVGMACCAGPMMGLCCKKTGAVIAGIAHGIAVIVHIVFFIVMWVMEGFNFARMLLGFATMIYVQRLLFKFLTLAFLTREFKNDKANTAFWTGKWYNTGMGWMAFTQPSREFVAKIVEMSEFAGDFMLAHIILFCQLPILAVPLIDRWHSMMLFWLKPSRLIRPPIYSLKQARLRKRMVRKYVTLYFAVLLLFVVIIAAPAAASGSIKVDQFADIGSKGSIAYGLFQPRNVSNNDTGPTNRPKSYTWSYLSEKYSGHTTAYSTNAFR	.	.	.	.	A9YLC3_CANPA	Unreviewed	.	.	.	.	.	.
Mol00892	Protein	"D-glucan-1,3-beta--UDP glucosyltransferase (FKS1)"	FKS1; B9J08_000964; CA7LBN_002502; EC 2.4.1.34	FKS1	.	Candida auris	498019	Candida auris	.	.	Metschnikowiaceae	27319	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSYDNNHNYYDPNQQQGGQPGGEYYQQGAYDEMGQPVNYDQAGDYYDPNQQYQQQPYDMDGYQNYGQQGAAGYSADPEAFSDFSYGGGHAPGTPGYDQYGAQYTPSQMSYAGARSSGASTPIYGANPNYDPSQFQLSSNLPYPAWSADPQAPIKIEHIEDIFIDLTNKFGFQRDSMRNMFDYFMTLLDSRSSRMSPAQALLSLHADYIGGDNANYKKWFFASQQDLDESIGFANMNLGKIGRKARKASKKSKKARKAAEEHGQDIDALNNELEGDYSMEAANIRWKAKMNVLTPEERVRDIALYLLLWGEANQVRFTPELICFIFKTALDYLNSPQCQQRQEPVPEGDYLNRIITPIYRFIRSQVYEIYEGRFVKREKDHNKVIGYDDVNQLFWYPEGISRIIFNDGTRLVDIPMEERYMRLGEVEWQNIFFKTYKEVRTWLHLVTNFNRIWIIHVTIYWMYTAYNSPTLYTQDYVQTINNRPTASSQWSAPAMGGMIASFIEVMATVFEWMFVPREWAGAQHLSRRLVFLIIILVINIVPFAYSFYWAGLSAISKSAHAVSIVGFFIAVATLLFFAIMPLGGLFTSYMNRRSRKYVASQIFTANFHSLRGLDMWMSYLLWVTVFAAKLAESYFFLTLSLRDPIRNLSTMTMRCNGEQWFGDTLCKHQAKIVLGLMLLVDLFLFFLDTYMWYIICNCVFSIGRSFYLGISILTPWRNIFTRLPKRIYSKILATTEMEIKYKPKVLISQVWNAIVISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRNSEAERRISFFAQSLATPILEPLPVDNMPTFTVFTPHYSEKILLSLREIIREDDQFSRVTLLEYLKQLHPVEWDCFVKDTKILAEETAAYENADEEERSNEDGLKAKIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTVSGFMNYARAIKLLYRVENPELVQYFGGDPEGLELALEKMARRKFKFVVSMQRLAKFKEDEMENAEFLLRAYPDLQIAYLDEEPPLNEDEEPRVYSALIDGHCEVLDNGRRRPKFRVQLSGNPILGDGKSDNQNHAIIFHRGEYIQLIDANQDNYLEECLKIRSVLAEFEELNVEHVNPYAPGLKNNNDEKPAPVAILGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFLNATFMLTRGGVSKAQKGLHLNEDIYAGMTAMLRGGRIKHCEYYQCGKGRDMGFGSICNFTTKIGAGMGEQMLSREYYYLSTQLPLDRFLSFYYGHPGFHINNLFIQLSLQTFMLVLANLNSLAHESILCDYDRNVPITDPLRPFGCYNLSPAIDWIRRYTLSIFIVFWISFIPLVVQELIERGLWKATQRFFRHFISLSPMFEVFLAQIYSNSLFTDLTVGGARYISTGRGFATSRIPFSILFSRFADSAIYMGSRSMLILLFGSVAHWQAPLLWFWASLSALMFSPFLFNPHQFAWEDFFIDYRDFIRWLSRGNTKWHRNSWIGYIKLSRSRVTGFKRKLTGDISEKSAGDASRAHRSNVFMADFLPCLFYAAGLFVAYTYVNAQTGVTRWSVDGRDSTEPIKVNSVVRIVICALAPVVIDIGCLGVCLGMACCAGPMLGLCCKKTGAVIAGVAHGVAVIVHLVFFIVMWVLEGFNFARMLLGIVTMIYIQRVLFKILTLLFLTREFKNDKSNTAFWTGKWYNTGMGYMAATQPAREFVAKIIEMSEFAGDFILAHLILFIQLPILCIPLIDRWHSTMLFWLKPSRLIRPPIYSLKQAKLRKRIVRKYCTLYFAILVLFIVIIAAPAVAGRFIADNLGANMSGTFEGLFQPRKVKNNDTGKVSSWWSTSDVKITFWSFTPTTSNVYTTKAF	.	.	.	.	A0A2H1A4W2_CANAR	Unreviewed	.	.	.	.	.	.
Mol00893	Protein	Dihydrofolate reductase (DHFR)	.	DHFR	.	Pneumocystis jirovecii	42068	Pneumocystis jirovecii	Pneumocystis	4753	Pneumocystidaceae	44281	Pneumocystidales	37987	Pneumocystidomycetes	147553	Ascomycota	4890	Fungi	4751	.	MDWQKSLTLIVALTLSRGIGLKNDLPWKLKSDMMFFSRVTSGLLVTRSTGQMNVVLMGRKTWESLPAHSRPLKNRINVVISRQEVLDLGGGAYHARSLDDALALLSQIYDSTSKIQLNRVFVIGGGELYKAAMEHSRLNRIIATVIHNEVDCDVFFPIDFRSSQSCLPWRKQDHSVLEAWVGSKVPQGKINENGFIYEFEMWIRDI	.	.	.	.	Q9UUP5_PNEJI	Unreviewed	.	.	.	.	.	.
Mol00894	Protein	Dihydrofolate reductase (DHFR)	dhfR18; D6U24_19495	dfr18	.	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNKEIQFSMIVARGVNGEIGQDGDLPWHVEGVRLKEDLKRFKAITMGKTLVMGRKTFESIPNGLPGRNVIVLTREPYDKADITERGDGTFVAWGNSCHLFEVAEHLGVTEIIVAGGAEIYNLHKDVITKVFETKVLRAYPAADTHVDVFWESPGYDTEGRQWRVTSRGHIIENGSFTIATTYER	.	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis."	.	.	Q8VVN6_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00895	Protein	Dihydrofolate reductase (DHFR)	DHPS; Dihydropteroate pyrophosphorylase; folP; sul2; D6U24_19945; VC1786ICE_13; Vcrx029	sulII	64223951	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNKSLIIFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKADGIPVSLDSYQPATQAYALSRGVAYLNDIRGFPDAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGAGIKRNRLVLDPGMGFFLGAAPETSLSVLARFDELRLRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGADFIRTHEPRPLRDGLAVLAALKETARIR	.	"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives."	.	.	Q7DFV9_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00896	Protein	Dihydrofolate reductase (DHFR)	dfr17; dfrA; dhfr17; dhfrA17; AKG29_00690; BON71_09100; BON81_06950; BON82_23795; BON83_00130; BON86_00200; BON87_24910; BVL39_07840; C5N07_28340; CDC27_27020; CDL36_28485; CDL37_03930; CWS33_26355; D0X26_01220; D0X26_28460; E2646_24960; E5P27_23655; E5P44_22195; E5P45_23940; E5P46_21200; E5P47_22545; E5P49_22525; E5P50_23750; EAN77_29860; EAN77_31025; EHH55_26460; EIZ93_24725; ELT16_24660; ELT17_24370; ELT17_26535; ELT20_22050; ELT24_24270; ELT30_23905; ELT31_25005; ELT31_26075; ELT32_25290; ELT33_25145; ELT34_24315; ELT35_24175; ELT39_24930; ELT50_25070; ELT51_25310; ELT52_24415; ELT55_25070; ELT59_24930; ELT61_25350; ELT63_25360; ELT72_24990; ELU07_24215; ELU88_24760; ELU89_23625; ELU91_25280; ELU94_23205; ELU98_22920; ELV00_24845; ELV02_25915; ELV03_25830; ELV04_25175; ELV07_26135; ELV08_25745; ELV09_26230; ELV12_23125; ELV13_25085; ELV15_23990; ELV20_24985; ELV22_23800; ELV22_25890; ELV24_24250; ELV24_25715; ELV26_25060; ELV28_26305; ELV28_27750; ELV29_24420; ELX68_23645; ELX68_25470; ELX76_26265; ELX76_27795; ELX79_23870; ELX79_27590; ELX83_25375; ELX83_26555; ELX96_23205; ELX96_27870; ELY23_24500; ELY23_26210; ELY32_25885; ELY32_27300; ELY41_22960; ELY41_28095; ELY48_25510; ELY48_27265; ELY50_25030; ELY50_27010; EXX13_27085; F0L67_27205; FKO60_26910; FZC17_05390; G3565_28015; GLW94_27755; GLW94_28285; GRC73_23675; GRC73_24560; HL601_26105; HL601_27185; HLV18_23895; HLV18_24740; HMV95_21525; HMV95_26380; RCS76_PICDS8925D; RCS78_P0020	dfrA17	58463194	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKISLISAVSENGVIGSGPDIPWSVKGEQLLFKALTYNQWLLVGRKTFDSMGVLPNRKYAVVSKNGISSSNENVLVFPSIENALKELSKVTDHVYVSGGGQIYNSLIEKADIIHLSTVHVEVEGDIKFPIMPENFNLVFEQFFMSNINYTYQIWKKG	.	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis."	.	.	Q7BPP7_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00897	Protein	Dihydrofolate reductase (DHFR)	.	dfrA15	.	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKLSLMAAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFESMGALPNRKYAVVTRSSFTSSDENVLVFPSIDEALNHLKTITDHVIVSGGGEIYKSLIDKVDTLHISTIDIEPEGDVYFPEIPSSFRPVFSQDFVSNINYSYQIWQKG	.	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis."	.	.	Q7BN39_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00898	Protein	Dihydrofolate reductase (DHFR)	dhfR; dhfrI; ERS013198_02214; ERS013202_02356; ERS013206_02102; ERS013207_02168; VC1786ICE_93	dfrA1	58164746	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKLSLMVAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFESMGALPNRKYAVVTRSSFTSDNENVLIFPSIKDALTNLKKITDHVIVSGGGEIYKSLIDQVDTLHISTIDIEPEGDVYFPEIPSNFRPVFTQDFASNINYSYQIWQKG	.	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis."	.	.	Q7B9D5_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00899	Protein	Dihydrofolate reductase (DHFR)	dfrA; dhfr; dhfr12; dhfrA12; dhfrXII; AOY10_00067; B6R12_004225; B6R12_005492; B6R15_004946; B6R15_005525; BANRA_05018; BANRA_05550; BHS81_30685; BJI68_09275; BJJ90_26820; BK292_28535; BK383_28330; BVL39_27785; CA593_26965; CR538_27010; CR538_27775; CR539_26880; D9C02_25135; E2117_19040; E2133_22650; E4K51_27155; E5P24_23220; E5P25_24335; E5S34_22245; EA239_25350; EI021_22810; EIZ93_23115; ELT27_22805; ELT29_23875; ELT56_25010; ELU90_23320; ELV08_25350; ELX61_23120; ELX85_17445; F3N40_24870; F3N40_27900; FTV93_26310; G5603_27160; G5632_22460; HHH44_004744; HHH44_005252; HMU48_23540; HMU48_30935; HNC36_27120; HNC36_29310; HNC99_24940; HNC99_29620; HND12_29345; HND12_30765; HND12_30780; HND12_30795; HND12_30810; HVX16_27030; HVX16_27860; J0541_005704; J0541_005934; NDM1Dok01_N0147; RCS28_PI0034; RCS40_P0057; RCS51_P0085; RCS55_PI0020; SAMEA3472044_03632; SAMEA3472080_05518; TUM18780_18810	dfrA12	61419540	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNSESVRIYLVAAMGANRVIGNGPNIPWKIPGEQKIFRRLTEGKVVVMGRKTFESIGKPLPNRHTLVISRQANYRATGCVVVSTLSHAIALASELGNELYVAGGAEIYTLALPHAHGVFLSEVHQTFEGDAFFPMLNETEFELVSTETIQAVIPYTHSVYARRNG	.	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis."	.	.	Q79DQ2_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00900	Protein	Dihydrofolate reductase (DHFR)	DHPS; Dihydropteroate pyrophosphorylase; folP; ML0224; MLCB2548.07c	folP1	.	Mycobacterium leprae	1769	Mycobacterium leprae	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSLAPVQVIGVLNVTDNSFSDGGRYLDPDDAVQHGLAMVAEGAAIVDVGGESTRPGAIRTDPRVELSRIVPVVKELAAQGITVSIDTTRADVARAALQSGARIVNDVSGGRADPAMAPLVAEAGVAWVLMHWRLMSAERPYEAPNYRDVVAEVRADLLAGVDQAVAAGVDPGSLVIDPGLGFAKTGQHNWALLNALPELVATGVPILLGASRKRFLGRLLAGADGAVRPPDGRETATAVISALAALHGAWGVRVHDVRASVDALKVVGAWLHAGPQIEKVRCDG	.	"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate, the immediate precursor of folate derivatives."	.	.	DHPS1_MYCLE	Reviewed	.	.	.	.	.	.
Mol00901	Protein	Dihydrofolate reductase (DHFR)	DHPS; Dihydropteroate pyrophosphorylase	folP	.	Streptococcus pyogenes	1314	Streptococcus pyogenes	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MKIGKFVIDGNAAIMGILNVTPDSFSDGGSYTTVQKVLQQVDQLIAGGAKIIDVGGESTRPGYQFVSAADEIERVVPMIKAIKAKYDVLISIDTYKTETARAALEAGADILNDVRAGLYDGEMLALAAEYDVPIILMHNQKEEVYQDVTQDVCDFLSARAQAAIDAGVPKDNIWIDPGFGFPKSVQHNMELLKGLDHVCQLGYPVLFGISRKGVVDALLGGNTKAKERDGATAALSAYALGKGCQLVRVHDVKANQEIVAVLSQLM	.	"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives."	.	.	DHPS_STRPY	Reviewed	.	.	.	.	.	.
Mol00902	Protein	Dihydrofolate reductase (DHFR)	DHPS; Dihydropteroate pyrophosphorylase; dhpS; b3177; JW3144	folP	66672921	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINAGATIIDVGGESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAEVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVKETVEAMRVVEATLSAKENKRYE	.	"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives."	PDB: 1AJ0; PDB: 1AJ2; PDB: 1AJZ	.	DHPS_ECOLI	Reviewed	.	.	.	.	.	.
Mol00903	Protein	Dihydrofolate reductase (DHFR)	.	dhfr	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MMEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCNSLDMKYFCAVTTYVNESKYEKLKYKRCKYLNKETVDNVNDMPNSKKLQNVVVMGRTSWESIPKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCFIIGGS	.	"Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP."	.	.	D0QXK2_PLAFA	Unreviewed	.	.	.	.	.	.
Mol00904	Protein	Dihydrofolate reductase (DHFR)	dfrA17; BVL39_26665; HmCms169_04568	dfrA27	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKISLMAAKARNGVIGCGSDIPWNAKGEQLLFKAITYNQWLLVGRKTFEAMGALPNRKYAVVSRSGSVATNDDVVVFPSIEAAMRELKTLTNHVVVSGGGEIYKSLIAHADTLHISTIDSEPEGNVFFPEIPKEFNVVFEQEFHSNINYRYQIWQRG	.	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis."	.	.	B2ZNP4_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00905	Protein	Dihydrofolate reductase (DHFR)	.	dhps	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	ESHGPFVIPNPKISERDLVVPVLQLFQKEWNDIKNKIVKCDAKPIISIDTINYNVFKECVDNDLVDILNDISACTNNPEIIKLLKKKNKFYSVVLMHKRGNPHTMDELTNYDNLVYDIKNYLEQRLNFLVLNGIPRYRILFDIGLGFA	.	.	.	.	A0A7S6UBG4_PLAFA	Unreviewed	.	.	.	.	.	.
Mol00906	Protein	Dihydrofolate reductase type 6 (DFRA6)	Dihydrofolate reductase type VI; dfrVI	dhfrVI	.	Proteus mirabilis	1885	Streptomyces actuosus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MKISLMAAVSENGVIGSGLDIPWHVQGEQLLFKAMTYNQWLLVGRKTFDSMGKLPNRKYAVVTRSKIISNDPDVVYFASVESALAYLNNATAHIFVSGGGEIYKALIDQADVIHLSVIHKHISGDVFFPPVPQGFKQTFEQSFSSNIDYTYQIWAKG	.	"Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity)."	.	.	DYR6_PROMI	Reviewed	.	.	.	.	.	.
Mol00907	Protein	Dipeptide and tripeptide permease A (DTPA)	tppB; ydgR; b1634; JW1626	dtpA	58463902	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSTANQKPTESVSLNAFKQPKAFYLIFSIELWERFGYYGLQGIMAVYLVKQLGMSEADSITLFSSFSALVYGLVAIGGWLGDKVLGTKRVIMLGAIVLAIGYALVAWSGHDAGIVYMGMAAIAVGNGLFKANPSSLLSTCYEKNDPRLDGAFTMYYMSVNIGSFFSMIATPWLAAKYGWSVAFALSVVGLLITIVNFAFCQRWVKQYGSKPDFEPINYRNLLLTIIGVVALIAIATWLLHNQEVARMALGVVAFGIVVIFGKEAFAMKGAARRKMIVAFILMLEAIIFFVLYSQMPTSLNFFAIRNVEHSILGLAVEPEQYQALNPFWIIIGSPILAAIYNKMGDTLPMPTKFAIGMVMCSGAFLILPLGAKFASDAGIVSVSWLVASYGLQSIGELMISGLGLAMVAQLVPQRLMGFIMGSWFLTTAGANLIGGYVAGMMAVPDNVTDPLMSLEVYGRVFLQIGVATAVIAVLMLLTAPKLHRMTQDDAADKAAKAAVA	.	"Proton-dependent permease that transports di- and tripeptides as well as structurally related peptidomimetics such as aminocephalosporins into the cell. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate."	PDB: 6GS1; PDB: 6GS4; PDB: 6GS7	.	DTPA_ECOLI	Reviewed	.	.	.	.	.	.
Mol00908	Protein	DNA gyrase subunit A (GYRA)	A7M90_09590; ACX61_04300; APC21_10810; AYR68_13875; B7L45_04805; BAA1790NC_0825; BS065_04290; C5H40_06045; CBE85_02115; CBL15_04175; CTZ19_04410; D8O08_005595; DLI71_16065; DLI72_00820; DVA69_12175; E2532_05700; E2533_17310; E2534_13875; E2535_13035; E2536_17230; E2538_14860; E2539_15885; E2540_18225; E2541_11870; EA720_014895; EGM95_04500; EP550_04305; EP560_13775; EQH48_04245; F4T85_11695; F4T91_03100; FDN00_16230; FE003_04235; FGL68_06165; FJU36_00200; FJU42_06115; G3N53_06980; GSE42_15410; GUK62_11895; H0529_20915; HB367_17765; HBK86_13835; HIN86_04470; IAG11_03370; ITE13_00290; NCTC13421_00917; SAMEA104305281_03293; SI89_04710	gyrA	.	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSVSEIRPIAIEDELKHSYLDYAMSVIVSRALPDVRDGLKPVHRRVLYAMHELGNDYNKAYKKSARVVGDVIGKYHPHGDLAVYETIVRMAQDFSLRYLLVDGQGNFGSIDGDSAAAMRYTEVRMTKLAHELLADLEKDTVDWEDNYDGSERIPEVLPTRVPNLLINGAAGIAVGMATNMAPHNMTEVVNACLAYADNPNISIEGLMEYITGPDFPTGGIIYGKSGIVDAYRTGKGRLHIRGKYHFEEDEKTGRTTIVFTEIPYQVNKARVIERIAELVKEKKLEGISELRDESDKEGMRIAIDLKRGENAEVVVNNLFLNTQLENSFSINMVCLDNGQPKLMNLKDIIAAFIRHRQEVVTRRTMFELRKARERGHILEGLTVALANIDEIIETIKTSANPAEARERLLAGEWAGGGVVALLEKAGAISVRPDEIEGEDPNRPFGLSDSIYRLSPTQVGAILELRLHRLTGLEQDKLHAEYTEILGQIAELTAILNDFNLLMGVIREELAQVLQQYGDARRTEIVESRVDFCREDLIPEEQVVLTVSQTGYAKTQPLSDYQAQRRGGRGKSATSMKDDDFIQHLIVASNHATVLCFTNVGKVYRLKVFEVPQASRGAKGRPIVNLLPLDATETVTAILPLTEFPENHYVFMATASGTVKRVELEQFANIRSNGLRAIELNEEDTLIGVAITDGNQQIMLFSNEGKAIRFAETDVRAMGRTAKGVRGMRVSFASSTLSEEDADVENDDSDDNDDSADSSLVSRIVSLVVVPETGEVLCASANGYGKRTPVNDFPTKKRGGKGVIAIKTSERNGELVGAVSIDETKELLLISDGGTLVRTRAAEVAMTGRNAQGVRLIRLSEEETLVGVVSIEAVEDEEELLEGEVDTTETDSEEAVSNNEDTSEE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	X2L5Z9_ACIBA	Unreviewed	.	.	.	.	.	.
Mol00909	Protein	DNA gyrase subunit A (GYRA)	STY2499; D4Z37_12715; DKA88_12845; EID90_09240; FI137_04115; G9X37_004513; GND71_002474; K3U68_02995	gyrA	.	Salmonella typhi	90370	Salmonella enterica subsp. enterica serovar Typhi	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHGLMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDNEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEADAKTGRETIIVHEIPYQVNKARLIEKIAELVKDKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIISAFVRHRREVVTRRTIFELRKARDRAHILEALAIALANIDPIIELIRRAPTPAEAKAALISRPWDLGNVAAMLERAGDDAARPEWLEPEFGVRDGQYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLEQIAELLHILGSADRLMEVIREEMELIRDQFGDERRTEITANSADINIEDLISQEDVVVTLSHQGYVKYQPLTDYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDTILCFSSRGRLYWMKVYQLPEASRGARGRPIVNLLPLEANERITAILPVREYEEGVNVFMATASGTVKKTALTEFSRPRSAGIIAVNLNDGDELIGVDLTSGSDEVMLFSAAGKVVRFKEDAVRAMGRTATGVRGIKLAGDDKVVSLIIPRGEGAILTVTQNGYGKRTAADEYPTKSRATQGVISIKVTERNGSVVGAVQVDDCDQIMMITDAGTLVRTRVSEISVVGRNTQGVILIRTAEDENVVGLQRVAEPVDDEELDAIDGSVTEGDEDIAPEAESDDDVADDADE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	Q8Z562_SALTI	Unreviewed	.	.	.	.	.	.
Mol00910	Protein	DNA gyrase subunit A (GYRA)	.	gyrA	.	Bartonella bacilliformis	774	Bartonella bacilliformis	Bartonella	773	Bartonellaceae	772	Hyphomicrobiales	356	Alphaproteobacteria	28211	Proteobacteria	1224	.	.	.	MTDLTRLPEHDVSTGIEPVSIIEEMQCSYLDYAMSVIVSRALPDVRDGLKPVHRRILHAMNEMGLLFNKPYRKSAGVVGEVMGKFHPHGDASIYDALVRMAQDFSLRNPLIDGQGNFGSVDGDPPAAMRYTECRLEKVAEELLADIDKDTVDFQDNYDGREHEPIVLPARFPNLLVNGSGGIAVGMATNIPPHNLGEVIDGCVALIDNPNITIDEMLAIIPGPDFPTGGIILGHSGVRSAYETGRGSIIMRAKVEIEEIRNQRQAIIVSEIPYQVNKATMVEKMAELVRDKRIEGISDLRDESDRDGYRVVIELKREAVADVVLNQLYRYTPLQASFGCNMVALNGGKPEQMTLLDMLRAFVSFREEVVSRRTKYLLRKARERAHVLVGLAIAVANIDEIIELIRKAHDPQTARTQLMERRWPASEVAALIKLIDDPRHIIHEDNTYNLSEEQARAILELRLQRLTALGRNEIADELNAIGEDIADYLGILASRSRIMDIVKSELSALRETFATPRRTVFGFGSAEMDCEDLIVPEDMVVTVSHSGYIKRVPLNTYRAQRRGGKGRSGMATKDQDFVTRLFVANTHTPVLFFSSRGIVYKEKVWRLPVGTPQSRGRALINMLPLQQGERITTIMPLPEDEASWGKLDIMFATTRGTVRRNKLSDFIQVNRNGKIAMKLDEEGDEILSVETCTEHDDVVLITANGQCIRFPVTDIRVFSGRNSMGVRGINMVEGDKVISMTILEHVEATSVERSAYIKRAINERRVAGSDDEDILTVDEDGEETEVELTDERYAELSAHEQMLLTVSEFGYGKRSSSYDFRISGRGGKGIRATDLSKAAEIGKLVAAFPVGERDQIMLVSDGGQLIRVPVNCIRIAGRSTKGVTVFNTAKGEKVVSVERISESENDTNQLDIESEEHSGTVSMSEEKKL	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	Q8RT68_BARBA	Unreviewed	.	.	.	.	.	.
Mol00911	Protein	DNA gyrase subunit A (GYRA)	UU082	gyrA	29672273	Ureaplasma parvum	134821	Ureaplasma parvum	Ureaplasma	2129	Mycoplasmataceae	2092	Mycoplasmatales	2085	Mollicutes	31969	Tenericutes	544448	.	.	.	MALKKPKKSRLTTEEIKQQLEGSTIKEQSITKEVETSFLDYSMSVIVARALPDVRDGFKPVHRRALFAAFENGMTHDKPYKKSARWVGDVIGKYHPHGDQAVYQTIVRMAQDFSMRYLLVDGHGNFGSIDGDSAAAMRYTEARLSKISYELLKYIDKETVDFVPNYDASEQEPSVLPSGFPNLLTNGTTGIAVGMATNIPPHNLTEVCQAIKAYAKNHNVTISEIMEYLKGPDFPTGAEIYGDSGIIKYFNTGRGSVTIRSKYEIEDIGQGRVAIVVTEIPYMVNKANLIEKIVELVTNKQIEGISDLRDESSRDGIRIVIEVKRDVIPEVLLNKLFKTTPLQTNFSVNNLALVNGVPMVLNIKEMIKYYFEHQIEILVRRTNFDLKKAKERIHIVEGLVIAVNNIDEVIKIIKASGDDDIASKSLIQRFDLTELQTKAILEMRLRALTGLNIDKLKKEYEDLILVIKDLEDVLNNYNRQVNIICENLDYLIEKFGDERRTEIMYGVSSHIDDEDLIPVEDIVVTMSKRGYFKRLPIDTYKNQRRGGVGVQGLKTYEDDDVEKILVANTHTDLLFFSDLGRVYRLRGHEVPLGSRQSKGIPAINFLPIEKSESILTILPIDNYDQGSLFFTTSKGIIKRANLSDFESIRANGKIAITLKDGDKLFSVMQTLGNDEVFIGASNGNVIRFNENDAREMGRIATGVKGINLENDEYVVGTGLSSHGEYVLAVGSKGLGKLTDINDYRLTKRGAKGVNTLKVNDKTGNLVSIKVVNREEEALIITTSGKVIRLSIKDISVIGRNTSGVKLISLENKEEVKSIAIFKKEEINDEQLLQENDYNLK	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	GYRA_UREPA	Reviewed	.	.	.	.	.	.
Mol00912	Protein	DNA gyrase subunit A (GYRA)	spr1099	gyrA	60233881	Streptococcus pneumoniae	1313	Streptococcus pneumoniae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MQDKNLVNVNLTKEMKASFIDYAMSVIVARALPDVRDGLKPVHRRILYGMNELGVTPDKPHKKSARITGDVMGKYHPHGDSSIYEAMVRMAQWWSYRYMLVDGHGNFGSMDGDSAAAQRYTEARMSKIALEMLRDINKNTVDFVDNYDANEREPLVLPARFPNLLVNGATGIAVGMATNIPPHNLGETIDAVKLVMDNPEVTTKDLMEVLPGPDFPTGALVMGKSGIHKAYETGKGSIVLRSRTEIETTKTGRERIVVTEFPYMVNKTKVHEHIVRLVQEKRIEGITAVRDESNREGVRFVIEVKRDASANVILNNLFKMTQMQTNFGFNMLAIQNGIPKILSLRQILDAYIEHQKEVVVRRTRFDKEKAEARAHILEGLLIALDHIDEVIRIIRASETDAEAQAELMSKFKLSERQSQAILDMRLRRLTGLERDKIQSEYDDLLALIADLADILAKPERVSQIIKDELDEVKRKFSDKRRTELMVGQVLSLEDEDLIEESDVLITLSNRGYIKRLDQDEFTAQKRGGRGVQGTGVKDDDFVRELVSTSTHDHLLFFTNKGRVYRLKGYEIPEYGRTAKGLPVVNLLKLDEDESIQTVINVESDRSDDAYLFFTTRHGIVKRTSVKEFANIRQNGLKALNLKDEDELINVLLAEGDMDIIIGTKFGYAVRFNQSAVRGMSRIATGVKGVNLREGDTVVGASLITDQDEVLIITEKGYGKRTVATEYPTKGRGGKGMQTAKITEKNGLLAGLMTVQGDEDLMIITDTGVMIRTNLANISQTGRATMGVKVMRLDQDAQIVTFTTVAVAEKEEVGTENETEGEA	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	PDB: 4Z2C; PDB: 4Z2D; PDB: 4Z2E; PDB: 6N1P; PDB: 6N1Q; PDB: 6N1R	.	GYRA_STRR6	Reviewed	.	.	.	.	.	.
Mol00913	Protein	DNA gyrase subunit A (GYRA)	.	gyrA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MAELPQSRINERNITSEMRESFLDYAMSVIVARALPDVRDGLKPVHRRILYGLNEQGMTPDKSYKKSARIVGDVMGKYHPHGDSSIYEAMVRMAQDFSYRYPLVDGQGNFGSMDGDGAAAMRYTEARMTKITLELLRDINKDTIDFIDNYDGNEREPSVLPARFPNLLANGASGIAVGMATNIPPHNLTELINGVLSLSKNPDISIAELMEDIEGPDFPTAGLILGKSGIRRAYETGRGSIQMRSRAVIEERGGGRQRIVVTEIPFQVNKARMIEKIAELVRDKKIDGITDLRDETSLRTGVRVVIDVRKDANASVILNNLYKQTPLQTSFGVNMIALVNGRPKLINLKEALVHYLEHQKTVVRRRTQYNLRKAKDRAHILEGLRIALDHIDEIISTIRESDTDKVAMESLQQRFKLSEKQAQAILDMRLRRLTGLERDKIEAEYNELLNYISELEAILADEEVLLQLVRDELTEIRDRFGDDRRTEIQLGGFEDLEDEDLIPEEQIVITLSHNNYIKRLPVSTYRAQNRGGRGVQGMNTLEEDFVSQLVTLSTHDHVLFFTNKGRVYKLKGYEVPELSRQSKGIPVVNAIELENDEVISTMIAVKDLESEDNFLVFATKRGVVKRSALSNFSRINRNGKIAISFREDDELIAVRLTSGQEDILIGTSHASLIRFPESTLRPLGRTATGVKGITLREGDEVVGLDVAHANSVDEVLVVTENGYGKRTPVNDYRLSNRGGKGIKTATITERNGNVVCITTVTGEEDLMIVTNAGVIIRLDVADISQNGRAAQGVRLIRLGDDQFVSTVAKVKEDAEDETNEDEQSTSTVSEDGTEQQREAVVNDETPGNAIHTEVIDSEENDEDGRIEVRQDFMDRVEEDIQQSLDEDEE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	PDB: 4PLB; PDB: 5BS3; PDB: 6Z1A	.	GYRA_STAAU	Reviewed	.	.	.	.	.	.
Mol00914	Protein	DNA gyrase subunit A (GYRA)	SF2311; S2444	gyrA	1027274	Shigella flexneri	623	Shigella flexneri	Shigella	620	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRREVVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRHAPTPAEAKTALVANPWQLGNVAAMLERAGDDAARPEWLEPEFGVRDGLYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLDQIAELLRILGSADRLMEVIREELELVREQFGDKRRTEITANSADINLEDLITQEDVVVTLSHQGYVKYQPLSEYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDHILCFSSRGRVYSMKVYQLPEATRGARGRPIVNLLPLEQDERITAILPVTEFEEGVKVFMATANGTVKKTVLTEFNRLRTAGKVAIKLVDGDELIGVDLTSGEDEVMLFSAEGKVVRFKESSVRAMGCNTTGVRGIRLGEGDKVVSLIVPRGDGAILTATQNGYGKRTAVAEYPTKSRATKGVISIKVTERNGLVVGAVQVDDCDQIMMITDAGTLVRTRVSEISIVGRNTQGVILIRTAEDENVVGLQRVAEPVDEEDLDTIDGSAAEGDDEIAPEVDVDDEPEEE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	PDB: 2Y3P	.	GYRA_SHIFL	Reviewed	.	.	.	.	.	.
Mol00915	Protein	DNA gyrase subunit A (GYRA)	PA3168	gyrA	882800	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MGELAKEILPVNIEDELKQSYLDYAMSVIVGRALPDARDGLKPVHRRVLYAMSELGNDWNKPYKKSARVVGDVIGKYHPHGDTAVYDTIVRMAQPFSLRYMLVDGQGNFGSVDGDNAAAMRYTEVRMAKLAHELLADLEKETVDWVPNYDGTEQIPAVMPTKIPNLLVNGSSGIAVGMATNIPPHNLGEVIDGCLALMDNPDLTVDELMQYIPGPDFPTAGIINGRAGIIEAYRTGRGRIYIRARAVVEEMEKGGGREQIIITELPYQLNKARLIEKIAELVKEKKIEGISELRDESDKDGMRVVIELRRGEVGEVVLNNLYAQTQLQSVFGINVVALVDGQPRTLNLKDMLEVFVRHRREVVTRRTVYELRKARERGHILEGQAVALSNIDPVIELIKSSPTPAEAKERLIATAWESSAVEAMVERAGADACRPEDLDPQYGLRDGKYYLSPEQAQAILELRLHRLTGLEHEKLLSEYQEILNLIGELIRILTNPARLMEVIREELEAVKAEFGDARRTEIVASQVDLTIADLITEEDRVVTISHGGYAKSQPLAAYQAQRRGGKGKSATGMKDEDYIEHLLVANSHATLLLFSSKGKVYWLRTFEIPEASRTARGRPLVNLLPLDEGERITAMLQIDLEALQQNGGADDDLDEAEGAVLEGEVVEAAEVEEVEGETAELVAEPTGAYIFMATAFGTVKKTPLVQFSRPRSSGLIALKLEEGDTLIAAAITDGAKEVMLFSSAGKVIRFAESVVRIMGRNARGVRGMRLGKGQQLISMLIPESGAQILTASERGFGKRTPLSKFPRRGRGGQGVIAMVTNERNGALIAAVQVQEGEEIMLISDQGTLVRTRVDEVSLSGRNTQGVTLIKLASDEVLVGLERVQEPSGGDDEDLPEGEEAAESLGESAESESEPAAEAEGNEE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	GYRA_PSEAE	Reviewed	.	.	.	.	.	.
Mol00916	Protein	DNA gyrase subunit A (GYRA)	.	gyrA	.	Neisseria gonorrhoeae	485	Neisseria gonorrhoeae	Neisseria	482	Neisseriaceae	481	Neisseriales	206351	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MTDATIRHDHKFALETLPVSLEDEMRKSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMHELKNNWNAAYKKSARIVGDVIGKYHPHGDSAVYDTIVRMAQNFAMRYVLIDGQGNFGSVDGLAAAAMRYTEIRMAKISHEMLADIEEETVNFGPNYDGSEHEPLVLPTRFPTLLVNGSSGIAVGMATNIPPHNLTDTINACLRLLDEPKTEIDELIDIIQAPDFPTGATIYGLGGVREGYKTGRGRVVMRGKTHIEPIGKNGERERIVIDEIPYQVNKAKLVEKIGDLVREKTLEGISELRDESDKSGMRVVIELKRNENAEVVLNQLYKLTPLQDSFGINMVVLVDGQPRLLNLKQILSEFLRHRREVVTRRTLFRLKKARHEGHIAERKAVALSNIDEIIKLIKESPNAAEAKEKLLARPWASSLVEEMLTRSGLDLEMMRPEGLVANIGLKKQGYYLSEIQADAILRMSLRNLTGLDQKEIIESYKNLMGKIIDFVDILSKPERITQIIRDELEEIKTNYGDERRSEINPFGGDIADEDLIPQREMVVTLTHGGYIKTQPTTDYQAQRRGGRGKQAAATKDEDFIETLFVANTHDYLMCFTNLGKCHWIKVYKLPEGGRNSRGRPINNVIQLEEGEKVSAILAVREFPEDQYVFFATAQGMVKKVQLSAFKNVRAQGIKAIALKEGDYLVGAAQTGGADDIMLFSNLGKAIRFNEYWEKSGNDEAEDADIETEISDDLEDETADNENTLPSGKNGVRPSGRGSGGLRGMRLPADGKIVSLITFAPETEESGLQVLTATANGYGKRTPIADYSRKNKGGQGSIAINTGERNGDLVAATLVGETDDLMLITSGGVLIRTKVEQIRETGRAAAGVKLINLDEGETLVSLERVAEDESELSGASVISNVTEPEAEN	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	GYRA_NEIGO	Reviewed	.	.	.	.	.	.
Mol00917	Protein	DNA gyrase subunit A (GYRA)	hisW; nalA; parD; b2231; JW2225	gyrA	66673880	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDDEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEVDAKTGRETIIVHEIPYQVNKARLIEKIAELVKEKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIIAAFVRHRREVVTRRTIFELRKARDRAHILEALAVALANIDPIIELIRHAPTPAEAKTALVANPWQLGNVAAMLERAGDDAARPEWLEPEFGVRDGLYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLDQIAELLRILGSADRLMEVIREELELVREQFGDKRRTEITANSADINLEDLITQEDVVVTLSHQGYVKYQPLSEYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDHILCFSSRGRVYSMKVYQLPEATRGARGRPIVNLLPLEQDERITAILPVTEFEEGVKVFMATANGTVKKTVLTEFNRLRTAGKVAIKLVDGDELIGVDLTSGEDEVMLFSAEGKVVRFKESSVRAMGCNTTGVRGIRLGEGDKVVSLIVPRGDGAILTATQNGYGKRTAVAEYPTKSRATKGVISIKVTERNGLVVGAVQVDDCDQIMMITDAGTLVRTRVSEISIVGRNTQGVILIRTAEDENVVGLQRVAEPVDEEDLDTIDGSAAEGDDEIAPEVDVDDEPEEE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase IV (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than many other bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical. The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box."	PDB: 1AB4; PDB: 1X75; PDB: 1ZI0; PDB: 2Y3P; PDB: 3NUH; PDB: 4ELY; PDB: 6RKS; PDB: 6RKU; PDB: 6RKV; PDB: 6RKW	.	GYRA_ECOLI	Reviewed	.	.	.	.	.	.
Mol00918	Protein	DNA gyrase subunit A (GYRA)	UUR2_0088	gyrA	45015642	Ureaplasma urealyticum	2130	Ureaplasma urealyticum	Ureaplasma	2129	Mycoplasmataceae	2092	Mycoplasmatales	2085	Mollicutes	31969	Tenericutes	544448	.	.	.	MALKKPKKSRLTTEEIKQQLEGSTIKEQSITKEVETSFLDYSMSVIVARALPDVRDGFKPVHRRALFAAFENGMTHDKPYKKSARWVGDVIGKYHPHGDQAVYQTIVRMAQEFSMRYLLVDGHGNFGSIDGDSAAAMRYTEARLSKISYELLKYIDKETVDFVPNYDASEQEPSVLPSGFPNLLTNGTTGIAVGMATNIPPHNLTEVCQAIKAYAKNHDISIPEIMEHLKGPDFPTGAEIYGDSGIINYFNTGRGSVTIRSKYEIEDIGQGRVAIVVTEIPYMVNKVNLIEKIVELVTNKQIEGISDLRDESSRDGIRIVIEVKRDVIPEVLLNKLFKTTALQTNFSVNNLALVNGVPMVLNIKEMIKYYFEHQIEVLVRRTKFDLRKAKERIHIVEGLVIAVNNIDEVIKIIKASGDDDIASKALIARFGLTELQTKAILEMRLRALTGLNIDKLKKEYEDLLLIIEDLEDILENYDRQVNIICENLDYLIEKFGDERRTEIMYGVSSHIDDEDLIPVEDIVVTMSKRGYFKRLPIDTYKNQRRGGVGVQGLKTYEDDDVEKILVANTHTDLLFFSDLGRVYRLRGHEVPLGSRQSKGIPAINFLPIEKSESILTILPIDNYEQGSLFFTTSKGIIKRANLSDFESIRANGKIAITLKEGDKLFSVMQTLGNDEVFIGASNGNVIRFNENDAREMGRIATGVKGINLEDDEYVVGTGLSSHGEYVLAVGSKGLGKLTDINDYRLTKRGAKGVNTLKVNDRTGNLVSIKVVNRDEEALIITTSGKVIRLSIQDISVIGRNTSGVKLISLENKEEVKSIAIFKKEEIDDNDDEQKTSHGNEHNLE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	C0AGY7_UREUR	Unreviewed	.	.	.	.	.	.
Mol00919	Protein	DNA gyrase subunit A (GYRA)	A3S27_07540; A3T49_11750; A3T75_10885; A3U47_11000; A3U54_15670; A3U78_08660; A3V15_12060; A3W22_11510; A4J95_17280; A5970_06235; A6267_10695; A6O48_14880; A6T07_14520; A7C55_22090; A7H28_14915; A9591_15930; A9C99_13165; A9D71_07300; A9S47_21950; A9S88_13990; A9X19_20225; AAA56_17725; AAD13_20045; ABA14_15950; ABA47_3410; ABQ42_18810; AC587_15710; AC591_19140; ACM10_17230; ACT92_11880; ADR00_19640; ADS36_14560; AGN17_15580; AGP91_18625; AH461_18300; AIE92_15595; AIU46_12350; AKX49_16640; AL461_15535; ALZ46_05750; AM321_13320; AM525_14495; AN727_15895; AO198_13475; AO799_20620; AOL87_06575; AOL88_12670; APN68_19330; APO02_23745; AQ518_16205; AR267_15550; AS882_15970; ASN84_14535; ASV75_17465; AU775_08200; AU778_18860; AU856_09945; AVB14_13770; B0A21_19780; B0F61_14375; B1868_14195; B4P96_09255; B4W84_09705; B5C64_20755; B6339_09725; B6379_16480; B6M83_13600; B7136_21190; B7900_13705; B7919_13675; B7C82_08095; B7J34_12305; B7M41_21280; B7Q10_07100; B8V98_19290; B8Y98_15240; B8Z45_13310; B9176_14960; B9672_01270; B9673_08825; B9727_19315; B9756_15565; B9H85_12340; B9I48_11615; B9P12_15915; BB088_21340; BBL75_19995; BCA48_07525; BCB01_007530; BCB09_0007530; BCP76_14105; BCP85_17695; BCP91_16805; BH227_16735; BJO06_10880; BJO39_11145; BK099_10820; BK864_05105; BKF55_13590; BKO29_15005; BSD53_17785; BXJ37_15570; BZ670_19565; BZ722_16010; BZ734_16545; BZ777_15885; BZ881_08400; BZ894_10235; BZ895_15690; BZ908_14335; BZ955_13295; BZ980_14995; BZT14_22255; C3C87_16260; CA124_13705; CAD25_20340; CAD70_08740; CAI12_06465; CB062_13840; CB096_15955; CB308_09830; CB345_15145; CB472_11025; CB498_14600; CB501_07250; CB596_15080; CB604_13800; CB666_11280; CB721_10455; CBB04_11275; CBB05_15890; CBN70_21180; CBP97_10150; CBS03_13285; CBS08_14355; CBS55_17015; CBS77_12355; CBU16_15235; CC149_15105; CC297_17535; CC379_14300; CC404_21910; CC421_12430; CC678_09035; CC680_07430; CC754_09230; CC805_13065; CCG98_16750; CCP20_15955; CD530_18440; CDG21_20895; CE949_02915; CEA09_13040; CEI41_18055; CEM11_18765; CEW05_17495; CFC01_17480; CFD56_06630; CRE05_16545; D0175_13640; D0A07_16255; D3E03_21985; D4415_15115; D4F08_17785; D4X57_17780; D4Z56_13575; D5O28_14265; D5O87_14765; D6K13_14215; D6P81_15305; D6R78_19565; D6T13_06365; D8Q93_14750; D8S08_23300; D9O81_16345; DLM07_17770; DMI96_08400; DN254_14125; DO678_13480; DOH87_20005; DOJ41_15475; DOR31_13560; DP790_05145; DP797_16245; DPF44_13415; DPR73_14990; DQ906_13585; DQY42_06765; DQZ81_12490; DRD18_08845; DRM04_12610; DRX23_12505; DRX96_06340; DS187_14885; DS631_20005; DS637_12670; DSH04_14675; DSH32_19740; DSN07_18465; DTD96_21510; DTF75_11885; DU772_07825; DUA99_20215; DUG35_13880; DUG37_10790; DUU06_19460; DW487_12215; DY875_22045; DYT79_22100; E2D06_12360; E3C38_16780; E3C57_22230; E5382_18120; E5B97_16950; EAH10_07070; EBB65_15985; EBB99_15700; EBC54_14810; EBC72_12190; EC480_17775; ED439_14510; EES12_14320; EGL58_08905; EHF05_15940; EI456_08765; EI507_11690; EIL34_15880; EJG81_13470; EKH43_13475; EKP78_16970; EL812_16570; ELS48_10570; ELY67_16120; EU248_02565; EU373_19060; EUZ49_16145; EVI13_19610; EVU69_17725; EZV86_13095; F0E06_17610; F9O65_15615; F9Q56_15005; FEE84_13560; FEO32_13775; FI295_15735; FI296_11990; FII38_14830; FII69_12450; FTS15_16580; G0A24_18725; G0D20_14815; G0F99_21485; G0G01_19245; G0G02_21525; G0G04_17855; G0G05_13095; G0G06_17250; G0G07_16630; G0G14_12685; G0G15_12485; G0G17_20450; G0G22_21355; G0G23_18460; G0G27_15605; G0G31_23500; G0G35_23005; G0G37_18430; G0G38_18870; G0G39_20510; G0G40_21955; G0G41_20565; G0G45_22400; G0G49_18465; G0G50_22245; G0G51_23880; G0G52_22290; G0G53_16555; G0G54_14720; G0G60_21180; G0G61_04410; G0G62_20580; G0G64_13525; G2169_19375; G2170_17195; G2210_14135; G2222_12945; G2233_16065; G2235_14250; G2237_11775; G2242_12875; G2243_17560; G2264_18550; G2266_17700; G2271_11875; G2282_11545; G2286_18700; G2298_09615; G2300_14715; G2301_10905; G2322_09820; G2331_13445; G2345_13945; G2351_18725; G2395_17680; G2410_11070; G2484_17735; G2668_14590; G2672_13180; G2673_16355; G2674_15200; G2681_10225; G2684_14215; G2685_15165; G2686_14765; G2687_12525; G2689_15730; G2693_14670; G2696_16850; G2699_13915; G2700_13360; G2703_16415; G2705_16855; G2706_11650; G2710_12125; G2716_14460; G2717_15430; G2719_13945; G2723_13965; G2726_15440; G2729_14065; G2732_11210; G2737_12750; G2740_11525; G2745_10690; G2747_15195; G2749_09850; G2751_07855; G2757_14470; G2767_08145; G2784_12655; G2847_15095; G2849_16090; G2856_11060; G2858_13195; G2859_11065; G2860_14775; G2861_10195; G2862_13555; G2863_14005; G2866_07605; G2872_08260; G2874_09850; G2879_08935; G2880_13520; G2882_03415; G2888_14445; G2889_12090; G2890_09170; G2894_11065; G2896_09965; G2902_11985; G2905_07605; G2914_15720; G2925_13520; G2934_12965; G2939_19810; G2959_11860; G2964_18110; G2968_16290; G2971_18565; G2973_17800; G2981_17155; G2984_09935; G2989_08715; G2991_18750; G3259_002535; G3346_002951; G3348_001197; G3453_004543; G3972_003205; G3984_003978; G3A07_10275; G3A13_17440; G3A29_08410; G3V00_002672; G3V03_002877; G3W49_002338; G4179_002290; G4B49_001953; G4D14_004342; G4G55_002896; G4G70_003860; G4J27_002774; G4K89_003525; G4L00_000612; G4L11_003364; G4O33_002276; G4O34_002305; G4O38_002138; G4O43_002808; G4P59_002517; G4P65_002663; G4P71_001730; G4Q33_002026; G4Q34_002534; G4Y16_004282; G4Y74_000453; G4Y75_001660; G9273_002228; G9374_001969; G9375_002816; G9C39_002613; G9G26_003746; G9G29_004023; G9G49_004326; G9W24_002722; G9W26_002453; G9W60_003647; GB023_17510; GB033_22345; GB059_08195; GB073_13845; GB084_18505; GB092_13660; GB104_15440; GB108_16345; GB119_15980; GB125_14525; GB136_17565; GB146_18235; GB163_18290; GB172_18250; GB174_18995; GB183_15450; GB184_17060; GB191_16675; GB219_20320; GB220_16170; GB260_16710; GB264_17450; GB268_14720; GB322_18300; GB323_11270; GB340_08990; GB350_17280; GB366_16940; GB384_16670; GB389_15595; GB395_18065; GB398_13795; GB400_13975; GB410_15325; GB411_17275; GB424_16515; GB444_19685; GB453_20920; GB458_09610; GB471_13705; GB474_10090; GB488_17730; GB512_18890; GB517_18815; GB521_12175; GB522_14830; GB528_17810; GB536_18120; GB542_15780; GB545_15435; GB552_02125; GB560_11670; GB608_16765; GB611_15680; GB617_16655; GB628_17875; GB638_14220; GBR90_17935; GBR92_16500; GBR96_17295; GBS02_06615; GBS31_17290; GBS48_15830; GBS51_17290; GBV48_12975; GBV49_12810; GBV51_16215; GBV59_22565; GBW10_12955; GBW37_17285; GBW58_11275; GBW81_18895; GBW93_13845; GBX02_17450; GBX28_16740; GBX44_21710; GBX50_16940; GBX65_10225; GBY10_15435; GBY16_11340; GBY22_09585; GBY26_19970; GBY30_20575; GBY40_15175; GBY51_20145; GBY71_17420; GBY80_19055; GBY98_19680; GBZ02_16765; GBZ07_20110; GBZ09_11710; GBZ19_17225; GBZ20_14725; GBZ21_17355; GBZ57_17775; GBZ88_18260; GBZ96_21045; GCY20_14660; GDA07_15020; GDI37_15195; GDI50_12650; GDN42_21205; GI500_17515; GI569_15380; GI571_14910; GI574_08415; GI576_14025; GI598_14910; GI602_14910; GI603_14920; GI605_09425; GI606_14395; GI607_14885; GI610_14610; GI614_17000; GI616_17645; GI617_14910; GI618_14405; GI619_14840; GI623_15385; GI627_15380; GI628_15085; GI641_15080; GI643_14680; GI648_17000; GI652_13940; GI653_16690; GI656_11640; GI657_08065; GI658_13820; GI661_10075; GI664_15275; GI666_05580; GI667_14900; GI672_08060; GI673_14615; GI678_12200; GI679_12390; GI681_13190; GI682_15130; GI684_13595; GJE23_09590; GJE52_09800; GJE53_09800; GJE57_14600; GJE58_13940; GJE66_14620; GJE68_16405; GJE69_13775; GJE75_14920; GJE76_14910; GJE78_14910; GJE80_14910; GJE81_09805; GJE83_14605; GJE85_15855; GJE87_13850; GJE88_14890; GJE97_15125; GJE99_09080; GJF04_14910; GJF05_13815; GJF06_13550; GJF07_17670; GJF11_04095; GJF12_16735; GJF15_15805; GJF17_12520; GJF18_15375; GJF25_16625; GJF26_14880; GJF28_14640; GJF31_09800; GJF33_16690; GJF41_17345; GJF44_16305; GJF47_14910; GJF49_14605; GJF51_14910; GJF54_13625; GJF59_14015; GJF61_15390; GJF63_13935; GJF64_14910; GJF68_11605; GJF69_15895; GJF75_16615; GJF76_14905; GJF77_15385; GJF78_15385; GJF81_17310; GJF83_16685; GJF85_15385; GJF86_15780; GJF88_14910; GJF90_16605; GJF91_14620; GJF93_14000; GJF95_16385; GJF99_15720; GJG01_15380; GJG02_14820; GJG03_15385; GJG05_15530; GJG07_12735; GJG10_10465; GJG11_06405; GJG13_14605; GJG14_07990; GJG15_15515; GJG16_17850; GJG17_15575; GJG18_07595; GJG24_06955; GJG25_16140; GJG26_06955; GJG29_05280; GJG30_10460; GJG35_17040; GJG37_08930; GJG38_09745; GJG39_14920; GJG40_15630; GJG45_14905; GJG48_18255; GJG49_14410; GJG51_13525; GJG54_14910; GJG57_12590; GJG58_10845; GJG60_14650; GJG62_11355; GJG63_12390; GJG66_12225; GJG70_15725; GJG71_10465; GJG73_16345; GJG76_05810; GJG77_14450; GJG81_17175; GJG84_09800; GNA67_003230; GNA68_002846; GNA90_001497; GNA95_002946; GNB01_001914; GNB24_002728; GNB30_002756; GNB32_002703; GNB39_003014; GNB51_003234; GNB52_002892; GNB53_003303; GNB87_002323; GNB90_003304; GYI57_002061; GYK12_18245; GYK13_15015; OB33_16300; R841_16620; ZQ07_17755; ZR89_15070; ZW25_15880; ZX60_22135	gyrA	.	Salmonellaentericasubsp.entericaserovar Enteritidis	149539	Salmonella enterica subsp. enterica serovar Enteritidis	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDLAREITPVNIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLYAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEIRLAKIAHELMADLEKETVDFVDNYDGTEKIPDVMPTKIPNLLVNGSSGIAVGMATNIPPHNLTEVINGCLAYIDNEDISIEGLMEHIPGPDFPTAAIINGRRGIEEAYRTGRGKVYIRARAEVEADAKTGRETIIVHEIPYQVNKARLIEKIAELVKDKRVEGISALRDESDKDGMRIVIEVKRDAVGEVVLNNLYSQTQLQVSFGINMVALHHGQPKIMNLKDIISAFVRHRREVVTRRTIFELRKARDRAHILEALAIALANIDPIIELIRRAPTPAEAKAALISRPWDLGNVAAMLERAGDDAARPEWLEPEFGVRDGQYYLTEQQAQAILDLRLQKLTGLEHEKLLDEYKELLEQIAELLHILGSADRLMEVIREEMELIRDQFGDERRTEITANSADINIEDLISQEDVVVTLSHQGYVKYQPLTDYEAQRRGGKGKSAARIKEEDFIDRLLVANTHDTILCFSSRGRLYWMKVYQLPEASRGARGRPIVNLLPLEANERITAILPVREYEEGVNVFMATASGTVKKTALTEFSRPRSAGIIAVNLNDGDELIGVDLTSGSDEVMLFSAAGKVVRFKEDAVRAMGRTATGVRGIKLAGDDKVVSLIIPRGEGAILTVTQNGYGKRTAADEYPTKSRATQGVISIKVTERNGSVVGAVQVDDCDQIMMITDAGTLVRTRVSEISVVGRNTQGVILIRTAEDENVVGLQRVAEPVDDEELDAIDGSVAEGDEDIAPEAESDDDVADDADE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	A0A1X8W869_SALEN	Unreviewed	.	.	.	.	.	.
Mol00920	Protein	DNA gyrase subunit A (GYRA)	WS90_23820; WT26_08525	gyrA	.	Burkholderia cepacia	292	Burkholderia cepacia	Burkholderia	32008	Burkholderiaceae	119060	Burkholderiales	80840	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MDQFAKETLPTSLEEEMRRSYLDYAMSVIVGRALPDVRDGLKPVHRRVLFAMHELNNDWNRAYKKSARIVGDVIGKYHPHGDTAVYDTIVRMAQDFSLRYMLIDGQGNFGSIDGDNAAAMRYTEIRMAKIGHELLADIDKETVDFEPNYDGNEMQPSVLPSRIPNLLINGSSGIAVGMATNIPPHNLNEVVDACQHLLGNPEATIDELIEIIPAPDFPTAGIIYGVAGVRDGYRTGRGRVVMRAATHFEEIDRGQRMAIIVDELPYQVNKRSLLERIAELVNEKKLEGISDIRDESDKSGMRVVIELKRGEVPEVVLNNLYKATQLQDTFGMNMVALVDGQPKLLNLKEILQCFLSHRREVLTRRTIYELRKARERGHVLEGLAVALANIDEFIAIIKAAPTPPIAKAELMAKPWDSSLVREMLTRAESENAAAGGRSAYRPEGLNPAFGMQGDGLYRLSDTQAQEILQMRLQRLTGLEQDKIIGEYREVMAQIADLLDILARPERITTMIGEELTSVKAEFGDARRSKIELNATELNTEDLITPQDMVVTMSHAGYVKSQPLSEYRAQKRGGRGKQATQMKEDDWIETLFIANTHDYILCFSNRGRVYWVKVYEVPQGSRNSRGRPIVNMFPLQEGEKINVVLPVKEFSADKFIFMATSLGTVKKTPLEAFSRPMKKGIIAVGLDEGDYLIGASITDGAHDVMLFSDSGKAVRFDENDVRPMGREARGVRGMQLEDGQQVIAMLVAGSEEQTVLTATENGYGKRTPITEYTRHGRGTKGMIAIQTSERNGKVVAATLVDAEDQIMLITTAGVLIRTRVSEIREMGRATQGVTLISLDEGTKLSGLQQIAEAEEGDGEADEASDGEA	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	A0A103ZCJ7_BURCE	Unreviewed	.	.	.	.	.	.
Mol00921	Protein	DNA gyrase subunit B (GYRB)	.	gyrB	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MVTALSDVNNTDNYGAGQIQVLEGLEAVRKRPGMYIGSTSERGLHHLVWEIVDNSIDEALAGYANQIEVVIEKDNWIKVTDNGRGIPVDIQEKMGRPAVEVILTVLHAGGKFGGGGYKVSGGLHGVGSSVVNALSQDLEVYVHRNETIYHQAYKKGVPQFDLKEVGTTDKTGTVIRFKADGEIFTETTVYNYETLQQRIRELAFLNKGIQITLRDERDEENVREDSYHYEGGIKSYVELLNENKEPIHDEPIYIHQSKDDIEVEIAIQYNSGYATNLLTYANNIHTYEGGTHEDGFKRALTRVLNSYGLSSKIMKEEKDRLSGEDTREGMTAIISIKHGDPQFEGQTKTKLGNSEVRQVVDKLFSEHFERFLYENPQVARTVVEKGIMAARARVAAKKAREVTRRKSALDVASLPGKLADCSSKSPEECEIFLVEGDSAGGSTKSGRDSRTQAILPLRGKILNVEKARLDRILNNNEIRQMITAFGTGIGGDFDLAKARYHKIVIMTDADVDGAHIRTLLLTFFYRFMRPLIEAGYVYIAQPPLYKLTQGKQKYYVYNDRELDKLKSELNPTPKWSIARYKGLGEMNADQLWETTMNPEHRALLQVKLEDAIEADQTFEMLMGDVVENRRQFIEDNAVYANLDF	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	PDB: 3G75; PDB: 3G7B; PDB: 3TTZ; PDB: 3U2D; PDB: 3U2K; PDB: 4PLB; PDB: 4URM; PDB: 4URO; PDB: 5BS3; PDB: 5CPH; PDB: 5CTU; PDB: 5CTW; PDB: 5CTX; PDB: 5CTY; PDB: 5D6P; PDB: 5D6Q; PDB: 5D7C; PDB: 5D7D; PDB: 5D7R; PDB: 5IWI; PDB: 5IWM; PDB: 5Z9P; PDB: 6QTK; PDB: 6QTP; PDB: 6QX1; PDB: 6QX2; PDB: 6TCK; PDB: 6TTG; PDB: 6Z1A; PDB: 7MVS	.	GYRB_STAAU	Reviewed	.	.	.	.	.	.
Mol00922	Protein	DNA gyrase subunit B (GYRB)	Rv0005; MTCY10H4.03	gyrB	45423962	Mycobacteriumtuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAAQKKKAQDEYGAASITILEGLEAVRKRPGMYIGSTGERGLHHLIWEVVDNAVDEAMAGYATTVNVVLLEDGGVEVADDGRGIPVATHASGIPTVDVVMTQLHAGGKFDSDAYAISGGLHGVGVSVVNALSTRLEVEIKRDGYEWSQVYEKSEPLGLKQGAPTKKTGSTVRFWADPAVFETTEYDFETVARRLQEMAFLNKGLTINLTDERVTQDEVVDEVVSDVAEAPKSASERAAESTAPHKVKSRTFHYPGGLVDFVKHINRTKNAIHSSIVDFSGKGTGHEVEIAMQWNAGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDRKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQKVCNEQLTHWFEANPTDAKVVVNKAVSSAQARIAARKARELVRRKSATDIGGLPGKLADCRSTDPRKSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDIGKLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIENGHVFLAQPPLYKLKWQRSDPEFAYSDRERDGLLEAGLKAGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state, while in the absence of ATP it relaxes supercoiled dsDNA (15047530. 16876129060136377678426902844099596810805881). Also catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes. Gyrase from M.tuberculosis has higher decatenation than supercoiling activity compared to E.coli; as M.tuberculosis only has 1 type II topoisomerase, gyrase has to fulfill the decatenation function of topoisomerase IV as well. At comparable concentrations M.tuberculosis gyrase cannot introduce as many negative supercoils into DNA as the E.coli enzyme, and its ATPase activity is lower, perhaps because it does not couple DNA wrapping and ATP binding as well as E.coli."	.	.	GYRB_MYCTU	Reviewed	.	.	.	.	.	.
Mol00923	Protein	DNA gyrase subunit B (GYRB)	ML0005	gyrB	.	Mycobacterium leprae	1769	Mycobacterium leprae	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAAQRKAQDEYGAASITILEGLEAVRKRPGMYVGSTGERGLHHLIWEVVDNSVDEAMAGYATQVDVRLFDDGSVEVADNGRGIPVAVHATGVPTVDVVMTQLHAGGKFGGKDSGYNVSGGLHGVGVSVVNALSTRVEVDIKRDGYEWSQFYDKAVPGILKQGEATEATGTTIRFWADPDIFETTKYDFGTVARRIQEVAFLNKGLTINLVDERVKQDEVVDDVVSDTAEAPVAMTVEEKSTESSAPHKVRHRTFHYPGGLVDFVKHINRTKTPIQQSIIDFDGKGAGHEVEVAMQWNGGYSESVHTFANTINTHEGGTHEEGFRSALTSVVNKYAKDKKLLKDKDPNLTGDDIREGLAAVISVKVSEPQFEGQTKTKLGNTEVKSFVQRVCNEQLIHWFEANPVDAKAVVNKAISSAQARIAARKARELVRRKSATDLGGLPGKLADCRSTDPRSSELYVVEGDSAGGSAKSGRDSMFQAILPLRGKIINVEKARIDRVLKNTEVQAIITALGTGIHDEFDISRLRYHKIVLMADADVDGQHISTLLLTLLFRFMRPLIEHGYVFLAQPPLYKLKWQRMDPEFAYSDSERDGLLETGLKLGKKINKEDGIQRYKGLGEMDAKELWETTMDPSVRVLRQVTLDDAAAADELFSILMGEDVDARRSFITRNAKDVRFLDV	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	GYRB_MYCLE	Reviewed	.	.	.	.	.	.
Mol00924	Protein	DNA gyrase subunit B (GYRB)	Type IIA topoisomerase subunit GyrB; acrB; cou; himB; hisU; nalC; parA; pcbA; b3699; JW5625	gyrB	66672403	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI	.	"DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical. The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box."	PDB: 1AJ6; PDB: 1EI1; PDB: 1KZN; PDB: 3G7E; PDB: 3NUH; PDB: 4DUH; PDB: 4HYP; PDB: 4KFG; PDB: 4PRV; PDB: 4PRX; PDB: 4PU9; PDB: 4WUB; PDB: 4WUC; PDB: 4WUD; PDB: 4XTJ; PDB: 4ZVI; PDB: 5L3J; PDB: 5MMN; PDB: 5MMO; PDB: 5MMP; PDB: 5Z4H; PDB: 5Z4O; PDB: 5Z9B; PDB: 5Z9E; PDB: 5Z9F; PDB: 5Z9L; PDB: 5Z9M; PDB: 5Z9N; PDB: 5Z9Q; PDB: 6ENG; PDB: 6F86; PDB: 6F8J; PDB: 6F94; PDB: 6KZV; PDB: 6KZX; PDB: 6KZZ; PDB: 6L01; PDB: 6RKS; PDB: 6RKU; PDB: 6RKV; PDB: 6RKW; PDB: 7C7N; PDB: 7C7O	.	GYRB_ECOLI	Reviewed	.	.	.	.	.	.
Mol00925	Protein	DNA gyrase subunit B (GYRB)	H8R20_15075; NCTC235_00006	gyrB	67496344	Morganella morganii	582	Morganella morganii	Morganella	581	Morganellaceae	1903414	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSNTYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGYCKDIIVTIHNDNSVSVQDDGRGIPTGIHEEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLELVIRRDGKVHEQIYRHGEPQDRLTVVGETDKTGTRVRFWPSMDTFKGETEFQYDILAKRLRELSFLNSGVSIRLIDKRDGKEDHFHYEGGIKAFVEYLSRAKTSIHNNVFYFSTEKDDIGVEISMQWNDSFQENVYCFTNNIPQRDGGAHLAGFRAAMTRTLNSYIEKEGLNKKSKVSTTGDDAREGLVAVISVKVPDPKFSSQTKDKLVSSEVKTAVETLMNEKLSEYLDENPNDTKIIVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPAFSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLASQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIIERGYVYIAQPPLYKVKKGKQEQYIKDDEAMEQYQVSIALDGAALYVNENAAPIQGEHLEKLLHEYNGAHKIIRRLERLYPLALLNSLVYQPKLEESALLNKTEVEAWAQSLTERLTRHEEHGSTYSYRIAENKERQLFEPVLTIRTHGVDTDYNLDFDFVHGSEYARISKLGELIRGLIEEGAYVVRGERRQNVSNFEQALDWLMKESRRGLAVQRYKGLGEMNPEQLWETTMNPETRRMLQVTVKDAIATDQLFTTLMGDDVEPRRAFIEENALKAANIDV	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	A0A3S4CQ88_MORMO	Unreviewed	.	.	.	.	.	.
Mol00926	Protein	DNA topoisomerase (ATP-hydrolyzing) (PARC)	.	parC	.	Mycoplasma hominis	2098	Metamycoplasma hominis	Metamycoplasma	2895509	Metamycoplasmataceae	2895623	Mycoplasmoidales	2790996	.	.	Tenericutes	544448	.	.	.	MKKDRKEEIQEVTENIIEKNMADIMSDRFGRYSKYIIQQRAIPDARDGLKPVQRRILYSMWNLHLKNSEPFKKSARIVGDVIGRYHPHGDSSIYEALVRMAQDWKSNFPLIEMHGNKGSIDDDPAAAMRYTESRLEKISELMLKDLDRKVVKMAPNFDDSEYEPIVLPALFPNLLVNGAKGIAAGFATEIPPHNLGEVIDATIALIKNPTISIEELSEIVKGPDFPTGAIINGINEIKKALSSGQGRITISSKYHYVYDKKDESKIIGIEIIEIPFGVVKSKLVADIDAIAIDKKISGIKEVLDQTDRNGISIFIQLEDGANADAIIAYLMNKTELSISYSYNMVAIDNNRPVILNLYSALIAYLSHLKEVNINGINYDLKKFKLRLEIVEGFIKVAEISDEVIHLIKESDNSKKGVILALMNKFKFSELQATAIAELRLYKLSRMDQIEFQEEKKNLEIQIENCNKLLNDKWEFNQYLIKQLLEIKNQYSKPRLTEISDQKIDKEIDHKLLTKNEDFYLYITKDGYYKKISLKVYTSNELSTFKLKEEDNVFYFDKVNSLSKILFFTNLGNYFIIDCHLFKDCNWKDLGQHISSIVALESSEKIIRVIEITSFNNYANFILMSKLGYAKKVNLRDFENKSSLKTKTCMSFKDDNDELIDAQISNDEKMLFILLNNGMYHLVSENELKVGISLKARGIRLLLNLYKHPQLQVSGFITVSKYNNIIYLTQGGYIKCWDTSKLESTTRNTPKMLFTPLKNNILGLQSLAVTLSNLKMLYTDNNGNLAEYDWKFILKDKTKESKLLKLDYSFTNPGYFITPIKINELIEVDEIEQEKIRQEYQGYIDKNIELTAEHALIKKSYNQDIQHLNNEEQEELFQISTEDIELPNVSNNVNDNQKDKKNIATKESVSQKIQEIEKIDLETIMQKIKQIKKK	.	.	.	.	O52166_MYCHO	Unreviewed	.	.	.	.	.	.
Mol00927	Protein	DNA topoisomerase (ATP-hydrolyzing) (PARC)	UUR10_0524	parC	45016061	Ureaplasma urealyticum	2130	Ureaplasma urealyticum	Ureaplasma	2129	Mycoplasmataceae	2092	Mycoplasmatales	2085	Mollicutes	31969	Tenericutes	544448	.	.	.	MSVNQQKIINTPLDNIVGESYAKYAKYIIQDRALPDIRDGLKPVQRRILYAMSELGIFHDKPYKKSARTVGEVIGKYHPHGDSSIYEAMVRMSQDWKNNLCLLDMHGNKGSIDGDNAAAMRYTETRLSKIASVMLTNLKKDVVKFSPNFDDSEKEPSILPSLFPNLLINGATGIASGYATSIPPHNPNEVFDALIYRIDHPDCSIEKLIKICPAPDFPTGGEIHDLNGCANAHKTGEGKFVIRASIEFKTSEAKINQIIINSIPYETNKALIIKEIEDIIYNKEVAGLIEVRDESDAKGVSIIIDTKKDVNLENVKNYLYKKTSLEISYNTKFIAIVHRTPTLVSLSTYLDAQINHSLDVINKVDLYDLNKVLLRIEIVEGLIKCVDLIDEIIKIIRASDSRQDAKNALIQTFAFTNNQAEAIIMMRLHNLTRTDIFDLRNEWESLQQQAKTLKERIKSLQVRKNYLKQKMIEFKKEFGYQRKTKLFDEFIKAEVNEDQMIEKQSLNLVISRDGYIKTVSKKSFESSKYDELGLKTNDLLFYHNVINSHDRILIITSKAKLINLIAHKISCMRWKDVGEHLNNYAKFDANEKVVAVYVCNEQFKVDEHQLVLGSKLNLIKRIELNELDLNKNSKQISIMKLNENDGLISANLIKKDHNQFVVAISKLGLVLMFLVHEINCLNRLAKGIKIMKLKPNDEISSILIVPNNGYSIQLFLDQGNKCFSISELKLSKRAMTPSPLYLPTKKAQSVLAAFLVGNENVFYLLDEQQKINPYYLPNLKPIKLDSKINKYENDLIITDVVKDSFLSDSVISDFKKISMYANEFDSELLKTNENQEQDDLQLELINEKEEND	.	.	.	.	B5ZBX0_UREU1	Unreviewed	.	.	.	.	.	.
Mol00928	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A; SP_0855	parC	.	Streptococcus pneumoniae	1313	Streptococcus pneumoniae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MSNIQNMSLEDIMGERFGRYSKYIIQDRALPDIRDGLKPVQRRILYSMNKDSNTFDKSYRKSAKSVGNIMGNFHPHGDSSIYDAMVRMSQNWKNREILVEMHGNNGSMDGDPPAAMRYTEARLSEIAGYLLQDIEKKTVPFAWNFDDTEKEPTVLPAAFPNLLVNGSTGISAGYATDIPPHNLAEVIDAAVYMIDHPTAKIDKLMEFLPGPDFPTGAIIQGRDEIKKAYETGKGRVVVRSKTEIEKLKGGKEQIVIIEIPYEINKANLVKKIDDVRVNNKVAGIAEVRDESDRDGLRIAIELKKDANTELVLNYLFKYTDLQINYNFNMVAIDNFTPRQVGIVPILSSYIAHRREVILARSRFDKEKAEKRLHIVEGLIRVISILDEVIALIRASENKADAKENLKVSYDFTEEQAEAIVTLQLYRLTNTDVVVLQEEEAELREKIAMLAAIIGDERTMYNLMKKELREVKKKFATPRLSSLEDTAKAIEIDTASLIAEEDTYVSVTKAGYIKRTSPRSFAASTLEEIGKRDDDRLIFVQSAKTTQHLLMFTSLGNVIYRPIHELADIRWKDIGEHLSQTITNFETNEEILYVEVLDQFDDATTYFAVTRLGQIKRVERKEFTPWRTYRSKSVKYAKLKDDTDQIVAVAPIKLDDVVLVSQNGYALRFNIEEVPVVGAKAAGVKAMNLKEDDVLQSGFICNTSSFYLLTQRGSLKRVSIEEILATSRAKRGLQVLRELKNKPHRVFLAGAVAEQGFVGDFFSTEVDVNDQTLLVQSNKGTIYESRLQDLNLSERTSNGSFISDTISDEEVFDAYLQEVVTEDK	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	PDB: 2NOV; PDB: 3FOE; PDB: 3FOF; PDB: 3K9F; PDB: 3KSA; PDB: 3KSB; PDB: 3LTN; PDB: 3RAD; PDB: 3RAE; PDB: 3RAF; PDB: 4I3H; PDB: 4JUO; PDB: 4KOE; PDB: 4KPE; PDB: 4KPF; PDB: 4Z3O; PDB: 4Z4Q; PDB: 4Z53	.	PARC_STRPN	Reviewed	.	.	.	.	.	.
Mol00929	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A; grlA	parC	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MSEIIQDLSLEDVLGDRFGRYSKYIIQERALPDVRDGLKPVQRRILYAMYSSGNTHDKNFRKSAKTVGDVIGQYHPHGDFSVYKAMVRLSQDWKLRHVLIEMHGNNGSIDNDPPAAMRYTEAKLSLLAEELLRDINKETVSFIPNYDDTTLEPMVLPSRFPNLLVNGSTGISAGYATDIPPHNLAEVIQATLKYIDNPDITVNQLMKYIKGPDFPTGGIIQGIDGIKKAYESGKGRIIVRSKVEEETLRNGRKQLIITEIPYEVNKSSLVKRIDELRADKKVDGIVEVRDETDRTGLRIAIELKKDVNSESIKNYLYKNSDLQISYNFNMVAISDGRPKLMGIRQIIDSYLNHQIEVVANRTKFELDNAEKRMHIVEGLIKALSILDKVIELIRSSKNKRDAKENLIEVFEFTEEQAEAIVMLQLYRLTNTDIVALEGEHKELEALIKQLRHILDNHDALLNVIKEELNEIKKKFKSERLSLIEAEIEEIKIDKEVMVPSEEVILSMTRHGYIKRTSIRSFNASGVEDIGLKDGDSLLKHQEVNTQDTVLVFTNKGRYLFIPVHKLADIRWKELGQHVSQIVPIEEDEVVINVFNEKDFNTDAFYVFATQNGMIKKSTVPLFKTTRFNKPLIATKVKENDDLISVMRFEKDQLITVITNKGMSLTYNTSELSDTGLRAAGVKSINLKAEDFVVMTEGVSENDTILMATQRGSLKRISFKILQVAKRAQRGITLLKELKKNPHRIVAAHVVTGEHSQYTLYSKSNEEHGLINDIHKSEQYTNGSFIVDTDDFGEVIDMYIS	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	PARC_STAAU	Reviewed	.	.	.	.	.	.
Mol00930	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A; SF3063; S3267	parC	1026670	Shigella flexneri	623	Shigella flexneri	Shigella	620	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	PARC_SHIFL	Reviewed	.	.	.	.	.	.
Mol00931	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A; STM3174	parC	1254697	Salmonella typhi	99287	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNATAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYAELLLSELGQGTADWVPNFDGTMQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAKAAITLIEQPKTTLDQLLDIVQGPDYPTEAEIITPRAEIRKIYENGRGSVRMRAVWTKEDGAVVISALPHQVSGAKVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMEQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILTEWLAFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRSEDEPKPALMSRFGISETQAEAILELKLRHLAKLEEMKIRGEQDELEKERDQLQGILASERKMNTLLKKELQADADAYGDDRRSPLREREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFIDTTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVEHMLMEGDDQKLLMASDAGYGFVCTFNDLVARNRAGKTLITLPENAHVMPPLVIEDEHDMLLAITQAGRMLMFPVDSLPQLSKGKGNKIINIPSAEAAKGDDGLAHLYVLPPQSTLTIHVGKRKIKLRPEELQKVVGERGRRGTLMRGLQRIDRIEIDSPHRVSHGDSEE	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	PARC_SALTY	Reviewed	.	.	.	.	.	.
Mol00932	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A	parC	.	Neisseria gonorrhoeae	485	Neisseria gonorrhoeae	Neisseria	482	Neisseriaceae	481	Neisseriales	206351	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MNTQPHASHTDSNTLMLGRYAERAYLEYAMSVVKGRALPEVSDGQKPVQRRILFAMRDMGLTAGAKPVKSARVVGEILGKYHPHGDSSAYEAMVRMAQDFTLRYPLIDGIGNFGSRDGDGAAAMRYTEARLTPIAELLLSEINQGTVDFMPNYDGAFDEPLHLPARLPMVLLNGASGIAVGMATEIPSHNLNEVTQAAIALLKKPTLETADLMQYIPAPDFAGGGQIITPADELRRIYETGKGSVRVRARYEIEKLARGQWRVIVTELPPNANSAKILAEIEEQTNPKPKAGKKQLNQDRLNTKKLMLDLIDRVRDESDGEHPVRLVFEPKSSRIDTDTFINTLMAQTSLEGNVSMNLVMMGLDNRPAQKNLKTILQEWLDFRIVTVTRRLKFRLNQVEKRLHILEGRLKVFLHIDEVIKVIRESDDPKADLMAVFGLTEIQAEDILEIRLRQLARLEGFKLEKELNELREEQGRLNIFLGDENEKRKLIIKEMQADMKQFGDARRTLVEEAGRAVLTQTAADEPITLILSEKGWIRSRAGHNLDLSQTAFKEGDRLKQTLEGPHCFTRRHPRFIRGRTYSIDAAEIPGGRGDGVPVSSLIELQNGAKPVAMLTGLPEQHYLLSSSGGYGFIAKLGDMVGRVKAGKVVMTADSGETVLPPVAVYASSFINPDCKIIAATSQNRALAFPIGELKIMAKGKGLQIIGLNAGESMTHTAVSSEPEILIESEGRRGAAHKDRLPVALIEAKRGKKGRLLPISGSLKQLSSPK	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	PARC_NEIGO	Reviewed	.	.	.	.	.	.
Mol00933	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A; b3019; JW2987	parC	66673087	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDMAERLALHEFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLNASAKFKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYSELLLSELGQGTADWVPNFDGTLQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNLREVAQAAIALIDQPKTTLDQLLDIVQGPDYPTEAEIITSRAEIRKIYENGRGSVRMRAVWKKEDGAVVISALPHQVSGARVLEQIAAQMRNKKLPMVDDLRDESDHENPTRLVIVPRSNRVDMDQVMNHLFATTDLEKSYRINLNMIGLDGRPAVKNLLEILSEWLVFRRDTVRRRLNYRLEKVLKRLHILEGLLVAFLNIDEVIEIIRNEDEPKPALMSRFGLTETQAEAILELKLRHLAKLEEMKIRGEQSELEKERDQLQGILASERKMNNLLKKELQADAQAYGDDRRSPLQEREEAKAMSEHDMLPSEPVTIVLSQMGWVRSAKGHDIDAPGLNYKAGDSFKAAVKGKSNQPVVFVDSTGRSYAIDPITLPSARGQGEPLTGKLTLPPGATVDHMLMESDDQKLLMASDAGYGFVCTFNDLVARNRAGKALITLPENAHVMPPVVIEDASDMLLAITQAGRMLMFPVSDLPQLSKGKGNKIINIPSAEAARGEDGLAQLYVLPPQSTLTIHVGKRKIKLRPEELQKVTGERGRRGTLMRGLQRIDRVEIDSPRRASSGDSEE	.	"Topoisomerase IV is essential for chromosome segregation; it is the principal protein responsible for decatenating newly replicated chromosomes. It relaxes supercoiled DNA (12269820, PuMed:16023671300644). MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation."	PDB: 1ZVT; PDB: 1ZVU; PDB: 4MN4	.	PARC_ECOLI	Reviewed	.	.	.	.	.	.
Mol00934	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A; EJP75_01330	parC	.	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTSLAHHATENRSVAEFTEQAYLNYAMYVIMDRALPHISDGLKPVQRRIVYAMSELGLKSTGKPKKSARTVGDVLGKYHPHGDLACYEAMVLMAQPFSYRYPLIEGQGNWGSPDDPKSFAAMRYTEAKLSAYSELLLSELGQGTSEWQDNFDGSMKEPITLPARIPNILLNGTTGIAVGMATDIPPHNLREVVKGTIALIRNPETTDEKLAEYIPAPDLPTKAEIITAPEELLKIQTTGRGSYRARAVYTVEKNEIVITELPYQVSGSKVVTQIADQMIAKKLPLVADIRDESDHKNPTRLVIVLRSNRVDAETVMSHLFATTDLESSYRVNLNMIGADGRPQVKSIRRILLEWIEIRKQTVTRRLQYHLTKIEKRLHILAGLLIAYLDIDTVIRIIREEDQPKPVLMQHFGIDDIQAEAILELKLRHLAKLEEMEIRREQEELEAKAAIIREQLANPESLKNLIIGELKEDAKKFGDDRRSPIVTRADAVQIKEQDLMPAETVTVVLSEAGWVRAAKGGDVDAANLNFRAGDQYLSHAVGKTNQRVYFLDETGRSYALPISSLPSARGLGEPLSSKLAPASGVSFIQVFVDEDSNELLAVSSNGYGFKTQAAQLDTNAKAGKAFLTVADNATALPLLPIQQATHVAILSSSGRLLIIDLAELPVLNKGKGNKLIQLDEKEQILSMTTLNLDEIIQVAAGQQHLKLKGDDLQKYIGKRATKGQLLPRGYQKANRLLIQR	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	A0A3Q8UHN5_ACIBA	Unreviewed	.	.	.	.	.	.
Mol00935	Protein	DNA topoisomerase 4 subunit A (PARC)	Topoisomerase IV subunit A; SAMN05216301_3029	parC	.	Morganella morganii	582	Morganella morganii	Morganella	581	Morganellaceae	1903414	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSEITHDGVERQALHNFTENAYLNYSMYVIMDRALPFIGDGLKPVQRRIVYAMSELGLSNSAKYKKSARTVGDVLGKYHPHGDSACYEAMVLMAQPFSYRYPLVDGQGNWGAPDDPKSFAAMRYTESRLSKYAEVLLSELGHGTADWVPNFDGTMQEPKMLPARLPNILLNGTTGIAVGMATDIPPHNAREVTGALLALIDKPSLSLEDVMAFIPGPDYPTEAEIITGPEDIRKIYKSGRGSVRMRAVWTIEDGNAVITALPHQVSGAKVLEQIAAQMRAKKLPMVEDLRDESDHENPTRLVVVPRSNRIDLDQVMTHLFATTDLERSYRINLNMIGLDGRPAVKGLVEILNEWLVYRRETVRRRLNHRLEKVLRRLHILDGLLLAYLNIDEVIDIIRSEDEPKPVLMDRFGLSDTQAEAILELKLRHLAKLEEMKIRGEQDELAKERDKLQAILGSERRMNTLLKKELEEDAKQYGDDRRSPLNEREEAKAMSEHDILPSEPLTVVLSQMGWVRSAKGHDIDPAGMNYKAGDSFLGAARGKSNQPVVFLDSTGRSYSLDPLELPGARGQGEPLTGKLTPPPGAVFEQVLMNDENQKYLMASDAGYGFICTFSDLVAKNKAGKVLITLPDNAKVMTPIEVNDEENDLLLAVSQEGRMLLFPVGDLPQLSKGKGNKIISITSAAAAAGEDGLAHLFVIRPDASVTLHFGKRKLMLRPEDLQKFRAERGRRGTALPRGMQKKIERIDISEPEPKA	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	A0A1M7LLM7_MORMO	Unreviewed	.	.	.	.	.	.
Mol00936	Protein	DNA topoisomerase 4 subunit B (PARE)	Topoisomerase IV subunit B; gyrB; BARBAKC583_0899	parE	.	Bartonella bacilliformis	774	Bartonella bacilliformis	Bartonella	773	Bartonellaceae	772	Hyphomicrobiales	356	Alphaproteobacteria	28211	Proteobacteria	1224	.	.	.	MSNDNKDLFSVLNHAQSRIDRKENTQYTSAHSEIVVPAVPLSSPHHHKEDSTYNASSIRILEGLEPVRLRPGMYIGGTDSKALHHLFSEIIDNAMDEAVAGYADLIDITLDSNNYLTVTDNGRGIPIENHPQIPDKSTLEVIMTHLHSGGKFDGKAYQTSGGLHGVGISVVNALSDDMEVEVARERKLYRQRFSRGIPQSGLEELGDVYNRRGTRVCFHPDSQIFGENTAFDPEKIYKIARSKAYLFNGVKIRWNCDPAALKDAKNIPEKDVFYFPDGLKDYLSLSLKNKHLVTAEIFSGKTQQLSGHGSVEWAIAWHNGDAYIQSYCNTIPTEEGGTHETGLRQTLLRGLKAYAELIGNKRASIITSDDVMASTVVMLSVFIKDPQFVGQTKDRLATTEAQRIVENAIRDPFDHWLANSPHEATKLLNWVIERAEERLKRRQDREINRKTAVRKLRLPGKLADCSQNSAAGAELFIVEGDSAGGSAKQARNRTNQAILPLRGKILNVASAAREKMSSSQTIADLILALGCGTRSKYREEDLRYERIIIMTDADVDGAHIASLLITFFFQEIPDLIRAGHLYLAVPPLYRISQGGKVAYARDDSHKDELLKTEFTGKGKIEIGRFKGLGEMRAEQLKETTMNPKKRTLLRVSIDTFEMQETKETVQNLMGTKPEERFRFIQESSTFANNLDI	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	PARE_BARBK	Reviewed	.	.	.	.	.	.
Mol00937	Protein	DNA topoisomerase 4 subunit B (PARE)	Topoisomerase IV subunit B; grlB	parE	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNKQNNYSDDSIQVLEGLEAVRKRPGMYIGSTDKRGLHHLVYEIVDNSVDEVLNGYGNEIDVTINKDGSISIEDNGRGMPTGIHKSGKPTVEVIFTVLHAGGKFGQGGYKTSGGLHGVGASVVNALSEWLEVEIHRDGNIYHQSFKNGGSPSSGLVKKGKTKKTGTKVTFKPDDTIFKASTSFNFDVLSERLQESAFLLKNLKITLNDLRSGKERQEHYHYEEGIKEFVSYVNEGKEVLHDVATFSGEANGIEVDVAFQYNDQYSESILSFVNNVRTKDGGTHEVGFKTAMTRVFNDYARRINELKTKDKNLDGNDIREGLTAVVSVRIPEELLQFEGQTKSKLGTSEARSAVDSVVADKLPFYLEEKGQLSKSLVKKAIKAQQAREAARKAREDARSGKKNKRKDTLLSGKLTPAQSKNTEKNELYLVEGDSAGGSAKLGRDRKFQAILPLRGKVINTEKARLEDIFKNEEINTIIHTIGAGVGTDFKIEDSNYNRVIIMTDADTDGAHIQVLLLTFFFKYMKPLVQAGRVFIALPPLYKLEKGKGKTKRVEYAWTDEELNKLQKELGKGFTLQRYKGLGEMNPEQLWETTMNPETRTLIRVQVEDEVRSSKRVTTLMGDKVQPRREWIEKHVEFGMQEDQSILDNSEVQVLENDQFDEEEI	.	Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule.	.	.	PARE_STAAU	Reviewed	.	.	.	.	.	.
Mol00938	Protein	DNA topoisomerase 4 subunit B (PARE)	Topoisomerase IV subunit B; nfxD; b3030; JW2998	parE	66673071	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTQTYNADAIEVLTGLEPVRRRPGMYTDTTRPNHLGQEVIDNSVDEALAGHAKRVDVILHADQSLEVIDDGRGMPVDIHPEEGVPAVELILCRLHAGGKFSNKNYQFSGGLHGVGISVVNALSKRVEVNVRRDGQVYNIAFENGEKVQDLQVVGTCGKRNTGTSVHFWPDETFFDSPRFSVSRLTHVLKAKAVLCPGVEITFKDEINNTEQRWCYQDGLNDYLAEAVNGLPTLPEKPFIGNFAGDTEAVDWALLWLPEGGELLTESYVNLIPTMQGGTHVNGLRQGLLDAMREFCEYRNILPRGVKLSAEDIWDRCAYVLSVKMQDPQFAGQTKERLSSRQCAAFVSGVVKDAFILWLNQNVQAAELLAEMAISSAQRRMRAAKKVVRKKLTSGPALPGKLADCTAQDLNRTELFLVEGDSAGGSAKQARDREYQAIMPLKGKILNTWEVSSDEVLASQEVHDISVAIGIDPDSDDLSQLRYGKICILADADSDGLHIATLLCALFVKHFRALVKHGHVYVALPPLYRIDLGKEVYYALTEEEKEGVLEQLKRKKGKPNVQRFKGLGEMNPMQLRETTLDPNTRRLVQLTIDDEDDQRTDAMMDMLLAKKRSEDRRNWLQEKGDMAEIEV	.	Topoisomerase IV is essential for chromosome segregation; it is the principal protein responsible for decatenating newly replicated chromosomes. It relaxes supercoiled DNA. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation.	PDB: 1S14; PDB: 1S16; PDB: 3FV5; PDB: 4HZ0	.	PARE_ECOLI	Reviewed	.	.	.	.	.	.
Mol00939	Protein	DNA-directed RNA polymerase subunit beta (RPOB)	RNAP subunit beta; RNA polymerase subunit beta; Transcriptase subunit beta; SAOUHSC_00524	rpoB	3920377	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MAGQVVQYGRHRKRRNYARISEVLELPNLIEIQTKSYEWFLREGLIEMFRDISPIEDFTGNLSLEFVDYRLGEPKYDLEESKNRDATYAAPLRVKVRLIIKETGEVKEQEVFMGDFPLMTDTGTFVINGAERVIVSQLVRSPSVYFNEKIDKNGRENYDATIIPNRGAWLEYETDAKDVVYVRIDRTRKLPLTVLLRALGFSSDQEIVDLLGDNEYLRNTLEKDGTENTEQALLEIYERLRPGEPPTVENAKSLLYSRFFDPKRYDLASVGRYKTNKKLHLKHRLFNQKLAEPIVNTETGEIVVEEGTVLDRRKIDEIMDVLESNANSEVFELHGSVIDEPVEIQSIKVYVPNDDEGRTTTVIGNAFPDSEVKCITPADIIASMSYFFNLLSGIGYTDDIDHLGNRRLRSVGELLQNQFRIGLSRMERVVRERMSIQDTESITPQQLINIRPVIASIKEFFGSSQLSQFMDQANPLAELTHKRRLSALGPGGLTRERAQMEVRDVHYSHYGRMCPIETPEGPNIGLINSLSSYARVNEFGFIETPYRKVDLDTHAITDQIDYLTADEEDSYVVAQANSKLDENGRFMDDEVVCRFRGNNTVMAKEKMDYMDVSPKQVVSAATACIPFLENDDSNRALMGANMQRQAVPLMNPEAPFVGTGMEHVAARDSGAAITAKHRGRVEHVESNEILVRRLVEENGVEHEGELDRYPLAKFKRSNSGTCYNQRPIVAVGDVVEYNEILADGPSMELGEMALGRNVVVGFMTWDGYNYEDAVIMSERLVKDDVYTSIHIEEYESEARDTKLGPEEITRDIPNVSESALKNLDDRGIVYIGAEVKDGDILVGKVTPKGVTELTAEERLLHAIFGEKAREVRDTSLRVPHGAGGIVLDVKVFNREEGDDTLSPGVNQLVRVYIVQKRKIHVGDKMCGRHGNKGVISKIVPEEDMPYLPDGRPIDIMLNPLGVPSRMNIGQVLELHLGMAAKNLGIHVASPVFDGANDDDVWSTIEEAGMARDGKTVLYDGRTGEPFDNRISVGVMYMLKLAHMVDDKLHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEILTYKSDDTVGRVKTYEAIVKGENISRPSVPESFRVLMKELQSLGLDVKVMDEQDNEIEMTDVDDDDVVERKVDLQQNDAPETQKEVTD	.	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	.	.	RPOB_STAA8	Reviewed	.	.	.	.	.	.
Mol00940	Protein	DNA-directed RNA polymerase subunit beta (RPOB)	RNAP subunit beta; RNA polymerase subunit beta; Transcriptase subunit beta; Rv0667; MTCI376.08c	rpoB	888164	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MLEGCILADSRQSKTAASPSPSRPQSSSNNSVPGAPNRVSFAKLREPLEVPGLLDVQTDSFEWLIGSPRWRESAAERGDVNPVGGLEEVLYELSPIEDFSGSMSLSFSDPRFDDVKAPVDECKDKDMTYAAPLFVTAEFINNNTGEIKSQTVFMGDFPMMTEKGTFIINGTERVVVSQLVRSPGVYFDETIDKSTDKTLHSVKVIPSRGAWLEFDVDKRDTVGVRIDRKRRQPVTVLLKALGWTSEQIVERFGFSEIMRSTLEKDNTVGTDEALLDIYRKLRPGEPPTKESAQTLLENLFFKEKRYDLARVGRYKVNKKLGLHVGEPITSSTLTEEDVVATIEYLVRLHEGQTTMTVPGGVEVPVETDDIDHFGNRRLRTVGELIQNQIRVGMSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIKEFFGTSQLSQFMDQNNPLSGLTHKRRLSALGPGGLSRERAGLEVRDVHPSHYGRMCPIETPEGPNIGLIGSLSVYARVNPFGFIETPYRKVVDGVVSDEIVYLTADEEDRHVVAQANSPIDADGRFVEPRVLVRRKAGEVEYVPSSEVDYMDVSPRQMVSVATAMIPFLEHDDANRALMGANMQRQAVPLVRSEAPLVGTGMELRAAIDAGDVVVAEESGVIEEVSADYITVMHDNGTRRTYRMRKFARSNHGTCANQCPIVDAGDRVEAGQVIADGPCTDDGEMALGKNLLVAIMPWEGHNYEDAIILSNRLVEEDVLTSIHIEEHEIDARDTKLGAEEITRDIPNISDEVLADLDERGIVRIGAEVRDGDILVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGESGKVIGIRVFSREDEDELPAGVNELVRVYVAQKRKISDGDKLAGRHGNKGVIGKILPVEDMPFLADGTPVDIILNTHGVPRRMNIGQILETHLGWCAHSGWKVDAAKGVPDWAARLPDELLEAQPNAIVSTPVFDGAQEAELQGLLSCTLPNRDGDVLVDADGKAMLFDGRSGEPFPYPVTVGYMYIMKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMECWAMQAYGAAYTLQELLTIKSDDTVGRVKVYEAIVKGENIPEPGIPESFKVLLKELQSLCLNVEVLSSDGAAIELREGEDEDLERAAANLGINLSRNESASVEDLA	.	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	PDB: 4KBJ; PDB: 4KBM; PDB: 5UH5; PDB: 5UH6; PDB: 5UH8; PDB: 5UH9; PDB: 5UHA; PDB: 5UHB; PDB: 5UHC; PDB: 5UHD; PDB: 5UHE; PDB: 5UHF; PDB: 5UHG; PDB: 5ZX2; PDB: 5ZX3; PDB: 6BZO; PDB: 6C04; PDB: 6C05; PDB: 6C06; PDB: 6DV9; PDB: 6DVB; PDB: 6DVC; PDB: 6DVD; PDB: 6DVE; PDB: 6EDT; PDB: 6EE8; PDB: 6EEC; PDB: 6FBV; PDB: 6JCX; PDB: 6JCY; PDB: 6KON; PDB: 6KOO; PDB: 6KOP; PDB: 6KOQ; PDB: 6M7J; PDB: 6TYE; PDB: 6TYF; PDB: 6TYG; PDB: 6VVX; PDB: 6VVY; PDB: 6VVZ; PDB: 6VW0; PDB: 7KIF; PDB: 7KIM; PDB: 7KIN; PDB: 7KUF; PDB: 7KUG	.	RPOB_MYCTU	Reviewed	.	.	.	.	.	.
Mol00941	Protein	DNA-directed RNA polymerase subunit beta (RPOB)	RNAP subunit beta; RNA polymerase subunit beta; Transcriptase subunit beta; groN; nitB; rif; ron; stl; stv; tabD; b3987; JW3950	rpoB	67415312	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQSYSGNSELQYVSYRLGEPVFDVQECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQEVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVIFEIRDNKLQMELVPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEVPVEYIAGKVVAKDYIDESTGELICAANMELSLDLLAKLSQSGHKRIETLFTNDLDHGPYISETLRVDPTNDRLSALVEIYRMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNRSLLREEIEGSGILSKDDIIDVMKKLIDIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLSLGDLDTLMPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHKRRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYAQTNEYGFLETPYRKVTDGVVTDEIHYLSAIEEGNYVIAQANSNLDEEGHFVEDLVTCRSKGESSLFSRDQVDYMDVSTQQVVSVGASLIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMERAVAVDSGVTAVAKRGGVVQYVDASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQMPCVSLGEPVERGDVLADGPSTDLGELALGQNMRVAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELACVSRDTKLGPEEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLSEELQILEAGLFSRIRAVLVAGGVEAEKLDKLPRDRWLELGLTDEEKQNQLEQLAEQYDELKHEFEKKLEAKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKINPIEDMPYDENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDKINAMLKQQQEVAKLREFIQRAYDLGADVRQKVDLSTFSDEEVMRLAENLRKGMPIATPVFDGAKEAEIKELLKLGDLPTSGQIRLYDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMPESFNVLLKEIRSLGINIELEDE	.	DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	PDB: 3IYD; PDB: 3LTI; PDB: 3LU0; PDB: 3T72; PDB: 3TBI; PDB: 4JK1; PDB: 4JK2; PDB: 4KMU; PDB: 4KN4; PDB: 4KN7; PDB: 4MEX; PDB: 4MEY; PDB: 4S20; PDB: 4XSX; PDB: 4XSY; PDB: 4XSZ; PDB: 4YG2; PDB: 4YLN; PDB: 4YLO; PDB: 4YLP; PDB: 4ZH2; PDB: 4ZH3; PDB: 4ZH4; PDB: 5BYH; PDB: 5EZK; PDB: 5IPL; PDB: 5IPM; PDB: 5IPN; PDB: 5MS0; PDB: 5MY1; PDB: 5NSR; PDB: 5NSS; PDB: 5NWT; PDB: 5UAC; PDB: 5UAG; PDB: 5UAH; PDB: 5UAJ; PDB: 5UAL; PDB: 5UAQ; PDB: 5VSW; PDB: 5VT0; PDB: 5W1S; PDB: 5W1T; PDB: 6ALF; PDB: 6ALG; PDB: 6ALH; PDB: 6ASX; PDB: 6BJS; PDB: 6BYU; PDB: 6C6S; PDB: 6C6T; PDB: 6C6U; PDB: 6C9Y; PDB: 6CA0; PDB: 6CUX; PDB: 6FLP; PDB: 6FLQ; PDB: 6GFW; PDB: 6GH5; PDB: 6GH6; PDB: 6JBQ; PDB: 6JNX; PDB: 6K4Y; PDB: 6KJ6; PDB: 6LDI; PDB: 6N4C; PDB: 6N57; PDB: 6N58; PDB: 6N60; PDB: 6N61; PDB: 6OMF; PDB: 6OUL; PDB: 6P18; PDB: 6P19; PDB: 6P1K; PDB: 6PSQ; PDB: 6PSR; PDB: 6PSS; PDB: 6PST; PDB: 6PSU; PDB: 6PSV; PDB: 6PSW; PDB: 6R9B; PDB: 6R9G; PDB: 6RH3; PDB: 6RI7; PDB: 6RI9; PDB: 6RIN; PDB: 6RIP; PDB: 6TQN; PDB: 6TQO; PDB: 6UTV; PDB: 6VJS; PDB: 6WMU; PDB: 6X26; PDB: 6X2F; PDB: 6X2N; PDB: 6X43; PDB: 6X4W; PDB: 6X4Y; PDB: 6X50; PDB: 6XAS; PDB: 6XAV; PDB: 6XH7; PDB: 6XH8; PDB: 6XL5; PDB: 6XL9; PDB: 6XLJ; PDB: 6XLL; PDB: 6XLM; PDB: 6XLN; PDB: 6Z9P; PDB: 6Z9Q; PDB: 6Z9R; PDB: 6Z9S; PDB: 6Z9T; PDB: 6ZTL; PDB: 7ADB; PDB: 7ADC; PDB: 7ADD; PDB: 7ADE; PDB: 7C17; PDB: 7C97; PDB: 7CHW; PDB: 7KHB; PDB: 7KHC; PDB: 7KHE; PDB: 7KHI; PDB: 7MKN; PDB: 7MKO; PDB: 7MKQ	.	RPOB_ECOLI	Reviewed	.	.	.	.	.	.
Mol00942	Protein	DNA-directed RNA polymerase subunit beta' (RPOC)	RNAP subunit beta'; RNA polymerase subunit beta'; Transcriptase subunit beta'; CD630_00670	rpoC	66352565	Clostridioides difficile	1496	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MFELNNFESIKIALASPEKIRQWSRGEVKKPETINYRTLKPEKDGLFCERIFGPQKDWECHCGKYRRVRYKGVVCDRCGVEVTKSKVRRERMGHIELAAPMSHIWYFKGIPSRMGLLLDMSPRSLEKILYFASYVVVDPGETGLNEKQLLTEKEYRTALEKYGYTFTVGMGAEAVKTLLQNIDLEQQSKDLRAELKDSTGQKKVRTIRRLEVVEAFKKSGNKPEWMILDAIPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLELGAPDIIVRNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKFYQCGLPKKMALELFKPFVMDKLVKEGYAHNIKSAKSIVEKVKPEVWDVLEDVIKSHPVLLNRAPTLHRLGIQAFEPILVEGKAIKLHPLVCTAYNADFDGDQMAVHVPLSVEAQAEARFLMLSVNNILAPKDGSPITTPSQDMVLGCYYLTIEAQDGAKGTGMVFKDFNELLLAYYNKSVHLHALVKLKVTLEDGRSSLVESTVGRFIFNENIPQDLGFVDRKENPFALEVDFLADKKSLGKIIDKCFRKHGNTETAELLDYIKALGFKYSTLGGITVAVDDMSVPEEKKVFIAEAEAKVDKYEKAYRRGLISDEERYEKVIETWTETTDKVTDALMGGLDRLNNIYIMAHSGARGSKNQIRQLAGMRGLMANASGKTVEIPVKSNFREGLSVLEYFTSSHGARKGLADTAIRTAESGYLTRRLVDVSQDVIVREIDCGTEDTTEIYAIKEGNEVIEEIYDRIVGRYTIDPILNPETGEVIVEADSMIQEDEAETIVALGIEKIRIRTVLNCKTNHGVCSKCYGRNLATGKEVNIGEAVGIIAAQSIGEPGTQLTMRTFHTGGVAGADITQGLPRVEELFEARKPKGLAVITEVSGRVEIDETGKRKEVNVIPEEGETQTYVIPYGSRLKVKQGQMLEAGDPLTQGFINPHDIVRVNGVKGVQEYIVKEVQRVYRLQGVDVNDKHIEVIVRQMLSKVKVEDPGDTDLLPGGYEDVLTFNECNKDAIDKGLRPAVAKRVLLGITKASLATDSFLSAASFQETTRVLTEAAIKGKEDHLIGLKENVILGKLIPAGTGMKKYRNIAVEKIED	.	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	.	.	RPOC_CLOD6	Reviewed	.	.	.	.	.	.
Mol00943	Protein	DNA-directed RNA polymerase subunit beta 2 (RPOB2)	RNAP subunit beta 2; RNA polymerase subunit beta 2; Transcriptase subunit beta 2; NFA_50990	rpoB2	61135673	Nocardia farcinica	37329	Nocardia farcinica	Nocardia	1817	Nocardiaceae	85025	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MLEGRILAVSTQTKAVAGIPGAPKRVSFAKIREPLEVPGLLDLQTESFAWLIGSPEWRERAAARGDVGLVGGLEEVLEELSPIEDFSGSMSLSFSDPRFEEVKASIDECKEKDMTYAAPLFVTAEFINNNTGEIKSQTVFMGDFPMMTDKGTFIINGTERVVVSQLVRSPGVYFDHSIDKGTEKDLHSVRVIPSRGAWLEFDVDKRDTVGVRIDRKRRQPVTVLLKALGWTTEEIAERFGFSEIMMSTLEKDNTAGQDEALLDIYRKLRPGEPPTKESAQTLLENLFFKEKRYDLARVGRYKINKKLGIHVGEPVTGSVLTKEDIVTTIEYLVRLHAGDKTMTAPGGVEVPVEVDDIDHFGNRRLRTVGELIQNQIRVGLSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIKEFFGTSQLSQFMDQNNPLSGLTHKRRLSALGPGGLSRERAGLEVRDVHPSHYGRMCPIETPEGPNIGLIGSLSVYARVNPFGFIETPYRKVVDGRVTDEVVYLTADEEDRHVRAQANSPVGPDGRFLEDRVLCRRGNEEMEYVAATEVDFMDVSPRQMVSVATAMIPFLEHDDANRALMGANMQRQAVPLIRSEAPIVGTGMELRAAVDAGDVVVNEKAGVVEEVSADYVTVMADDGTRKSYRMRKFNRSNQGTCSNQRPIVDEGQRVEAGQVLADGPCTENGEMALGKNLLVAIMPWEGHNYEDAIILSQRLVEQDVLTSIHIEEHEIDARDTKLGAEEITRDIPNVSDEVLADLDERGIVRIGAEVRDGDILVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGESGKVIGIRVFSREDDDDLPPGVNELVRVYVAQKRKIQDGDKLAGRHGNKGVIGKILPTEDMPFLPDGTPVDIILNTHGVPRRMNIGQILETHLGWIGKAGWKVEGNPEWAKDLPEEMWEAPADSNIATPVFDGAREEELTGLLGSTLPNRDGERMVDDNGKAVLFDGRSGEPFPYPVAVGYMYILKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMECWAMQAYGAAYTLQELLTIKSDDVVGRVKVYEAIVKGENIPEPGIPESFKVLLKELQSLCLNVEVLSSDGAAIELREGEDEDLERAAANLGINLSRNEAATVDDLAN	.	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.	.	.	RPOB2_NOCFA	Reviewed	.	.	.	.	.	.
Mol00944	Protein	DUF2154 domain-containing protein (LIAF)	GTI81_10090	GTI81_10090	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNNPWRFFIVAEALLFILALWQIVHNPGLAVLLTIGVLLVAYVSRKASKTHFNNFQFVLGVVFIVIGAMNSTAVWFMLIFGVLFIGLKGFEISGVDIAERAPWRKKQMIMVETAAKEPKNGKRFKRRWVANERIGNNIYEWDDINIDLISGDTIIDLGNTLLPKEDNIIIIRKGFGRTRILVPLGVAILLEHSTFYGTVRFEEEKYQLKNESLKIYSNDYDTNLRRLKIMTNTLVGDVEVIRV	.	.	.	.	A0A6I4XRK1_ENTFL	Unreviewed	.	.	.	.	.	.
Mol00945	Protein	Efflux pump membrane transporter (ACRD)	AAB79_19405; AL144_17250; AL168_17425; AL184_18975; BG493_06900; CB646_21645; DPB42_17850; DSF94_20865; DU071_19840; G0J43_21235; G0L29_16840; G0L79_20560; G0O37_22790; G0O42_22770; G2218_17035; G2279_23155; GB055_22220; GB131_17830; GB224_18795; GB331_18005; GB452_09625; GB510_10715; GB567_15985; GBS44_19240; GBV53_21030; GBV54_17380; GBX12_11300; GBX46_22285	acrD	.	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MANFFIDRPIFAWVLAILLCLTGALAIFSLPVEQYPDLAPPNVRITANYPGASAQTLENTVTQVIEQNMTGLDNLMYMSSQSSGTGQATITLSFIAGTDPDEAVQQVQNQLQSAMRKLPQAVQDQGVTVRKTGDTNILTIAFVSTDGSMDKQDIADYVASNIQDPLSRVNGVGDIDAYGSQYSMRIWLDPAKLNSFQMTTKDVTDAIESQNAQIAVGQLGGTPSVDKQALNATINAQSLLQTPQQFRDITLRVNQDGSEVKLGDVATVELGAEKYDYLSRFNGNPASGLGVKLASGANEMATAKLVLDRLNELAQYFPHGLEYKIAYETTSFVKASIIDVVKTLLEAIALVFLVMYLFLQNFRATLIPTIAVPVVLMGTFSVLYAFGYSINTLTMFAMVLAIGLLVDDAIVVVENVERIMSEEGLTPREATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGTTGAIYRQFSITIVSAMVLSVLVAMILTPALCATLLKPLHKGEQHGQRGFFGWFNRTFNRNAERYEKGVAKILHRSLRWILIYVLLLGGMVFLFLRLPTSFLPQEDRGMFTTSIQLPSGSTQQQTLKVVEKVENYYFTHEKDNIMSVFSTVGSGPGGNGQNVARMFVRLKDWDARDPTTGSSFAIIERATKAFNQIKEARVFASSPPAISGLGSSAGFDMELQDHAGAGHDALMAARDQLIELAGKNSSLTRVRHNGLDDSPQLQIDIDQRKAQALGVSIDDINDTLQTAWGSSYVNDFMDRGRVKKVYVQAAAKYRMLPDDINLWYVRNKDGGMVPFSAFATSRWETGSPRLERYNGYSAVEIVGEAAPGVSTGTAMDVMESLVHQLPGGFGLEWTAMSYQERLSGAQAPALYAISLLVVFLCLAALYESWSVPFSVMLVVPLGVIGALLATWMRGLENDVYFQVGLLTVIGLSAKNAILIVEFANEMNQKGHALLDATLYASRQRLRPILMTSLAFIFGVLPMATSTGAGSGSQHAVGTSVMGGMISATVLAIFFVPLFFVLIRRRFPLKPRPK	.	.	.	.	A0A5V9BEU7_SALTM	Unreviewed	.	.	.	.	.	.
Mol00946	Protein	Elongation factor Tu (TUF)	tufB; Fragment	tufB	.	Enterococcus avium	33945	Enterococcus avium	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	GAILVVSATDGPMPQTREHILLSRQVGVKHLIVFLNKVDLVDDEELIDLVEMEVRELLSEYGFPGDDIPVLKGSALKALEGDPEQEQVILDLMDTVDEYIPTPERDTDKPFLLPVEDVFSITGRGTVASGRIDRGEVKVGDEVEIIGIKPEIQKAVVTGLEMFRKTLDYGEAGDNVGVLLRGITRDEIERGQVLAKPGSITPHTKFSAEVYVLTKEEGGRHTPS	.	.	.	.	Q9EZZ1_ENTAV	Unreviewed	.	.	.	.	.	.
Mol00947	Protein	Elongation factor Tu (TUF)	tufB; Fragment	tufB	.	Enterococcus gallinarum	1353	Enterococcus gallinarum	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	GAILVVSATDGPMPQTREHILLSRQVGVKHLIVFLNKIDLVDDEELIDLVEMEVRELLSEYNFPGDDIPVIKGSALKALEGDPDAEAAIMELMDTVDSYIPTPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVGDEVEIVGIKPETQKAVVTGVEMFRKTMDFGEAGDNVGVLLRGITRDEIERGQVLAKPGSITPHTKFQAEVYVLTKEEGGRHTPFFNNYRPQFYFRTTDVTGNITLPEGTE	.	.	.	.	Q9EZY1_ENTGA	Unreviewed	.	.	.	.	.	.
Mol00948	Protein	Elongation factor Tu (TUF)	EF-Tu	tuf	.	Streptomyces cinnamoneus	53446	Streptomyces cinnamoneus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAKAKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLHDAIPDLNPFTPFDEIDKAPEERQRGITISIAHVEYQTESRHYAHVDCPGHADYIKNMITGAAQMDGAILVVAATDGPMPQTKEHVLLARQSGVPYIVVALNKADMVDDEEIMELVELEVRELLSEYEFDGDNCPVVQVSALKALEGDKEWGEKLLGLMKAVDENIPQPERDVDKPFLMPIEDVFTITGRGTVVTGRIERGVLKVNETVDIIGIKTEKTTTTVTGIEMFRKLLDEGQAGENVGLLLRGIKREDVERGQCIIKPGTVTPHTEFEATAYILSKDEGGRHTPFFNNYRPQFYFRTTDVTGVVTLKEGTEMVMPGDNAEMTVNLIQPVAMEEGLRFTIREGGRTVGAGQVVKINK	.	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	.	.	EFTU_STRCJ	Reviewed	.	.	.	.	.	.
Mol00949	Protein	Elongation factor Tu (TUF)	EF-Tu; tufA; CD630_00580; tufB; CD630_00710	tuf1	66352569	Clostridioides difficile	1496	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MAKAKYERTKPHVNIGTIGHVDHGKTTLTAAITKTLYDRYQLGEAVDFANIDKAPEERERGITISTAHVEYETPNRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSATDGPMPQTREHILLSRQVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLTEYDFPGDDTPIVRGSALMALEDPKSEWGDKIVELFEQIDEYIPAPERDTDKPFLMPVEDVFSITGRGTVATGRVERGVLKVQDEVELVGLTEAPRKVVVTGVEMFRKLLDQAQAGDNIGALLRGVQRNEIERGQVLAKTGSVKAHTKFTAEVYVLKKEEGGRHTPFFDGYRPQFYFRTTDVTGACKLPEGIEMVMPGDNVTMEVDLINSIVVEEGLRFSIREGGRTVASGVVATIIE	.	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	.	.	EFTU_CLOD6	Reviewed	.	.	.	.	.	.
Mol00950	Protein	Elongation factor Tu (TUF)	EF-Tu; RV13_GL002741	tuf	67038763	Enterococcus raffinosus	71452	Enterococcus raffinosus	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITTVLAKQGGAQAMDYAQIDGAPEERERGITINTAHVEYETDNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLSRNVGVPYIVVFLNKMDMVDDEELLELVEMEVRDLLTEYDFPGDDTPVIAGSALKALEGDASYEEKILELMAAVDEYIPTPVRDTDKPFMMPVEDVFSITGRGTVATGRVERGQVRVGDEVEIVGIAEETAKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDIQRGQVLAKPASITPHTKFSAEVYVLTKEEGGRHTPFFTNYRPQFYFRTTDVTGVVDLPEGTEMVMPGDNVTMEVELIHPIAIEDGTRFSIREGGRTVGSGVVTTIKA	.	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	.	.	A0A1L8X576_9ENTE	Unreviewed	.	.	.	.	.	.
Mol00951	Protein	Elongation factor Tu (TUF)	EF-Tu; tuf; BH739_11460; BZK37_12225; D8N35_02625; DW084_10410; DW201_05310; EQ871_03935; EZ072_05275; I6H55_06960; I6I78_03065; I6I79_06190; NCTC12362_00252; NCTC4725_00358; NCTC7179_01977; RU99_GL000254; SAMN05216513_103246	tufA	15140833	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITTVLSKKGLAQASAYDQIDGAPEERERGITISTAHVEYETEARHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLSRNVGVPYIVVFLNKMDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVIAGSALKALEGDASYEEKIMELMAAVDEYVPTPERDTDKPFMMPVEDVFSITGRGTVATGRVERGQVRVGDEVEIVGIAEETAKTTVTGVEMFRKLLDYAEAGDNIGALLRGVAREDIQRGQVLAKAGTITPHTKFKAEVYVLTKEEGGRHTPFFTNYRPQFYFRTTDVTGVVELPEGTEMVMPGDNVTIDVELIHPIAIEDGTRFSIREGGRTVGSGVVTSIQA	.	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.	.	.	A0A1L8SLM0_ENTCA	Unreviewed	.	.	.	.	.	.
Mol00952	Protein	Elongation factor Tu 1 (TUFA)	EF-Tu 1; Bacteriophage Q beta RNA-directed RNA polymerase subunit III; P-43; b3339; JW3301	tufA	66672781	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLG	.	This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.; FUNCTION: May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.; FUNCTION: Plays a stimulatory role in trans-translation; binds tmRNA.	PDB: 1D8T; PDB: 1EFC; PDB: 1ETU; PDB: 1MJ1; PDB: 2FX3; PDB: 2HCJ; PDB: 2HDN; PDB: 3EP2; PDB: 3EQ3; PDB: 3EQ4; PDB: 3U2Q; PDB: 3U6B; PDB: 3U6K; PDB: 4G5G; PDB: 4PC3; PDB: 4PC7; PDB: 4Q7J; PDB: 4V69; PDB: 5I4Q; PDB: 5I4R; PDB: 5JBQ; PDB: 5UYK; PDB: 5UYL; PDB: 5UYM; PDB: 5UYN; PDB: 5UYP; PDB: 5UYQ	.	EFTU1_ECOLI	Reviewed	.	.	.	.	.	.
Mol00953	Protein	Elongation factor Tu 2 (TUFB)	EF-Tu 2; Bacteriophage Q beta RNA-directed RNA polymerase subunit III; P-43; b3980; JW3943	tufB	66672109	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS	.	"This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.; FUNCTION: May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.; FUNCTION: Plays a stimulatory role in trans-translation, binds tmRNA."	PDB: 1DG1; PDB: 1EFM; PDB: 1EFU; PDB: 1LS2; PDB: 1OB2; PDB: 1QZD; PDB: 2BVN; PDB: 3AGP; PDB: 3AGQ; PDB: 3AVT; PDB: 3AVU; PDB: 3AVV; PDB: 3AVW; PDB: 3AVX; PDB: 3AVY; PDB: 3MMP; PDB: 3VNU; PDB: 3VNV; PDB: 4FWT; PDB: 4R71; PDB: 4V6K; PDB: 4V6L; PDB: 5AFI; PDB: 5I4R; PDB: 5WDT; PDB: 5WE4; PDB: 5WE6; PDB: 5WFK; PDB: 6EZE; PDB: 7ABZ	.	EFTU2_ECOLI	Reviewed	.	.	.	.	.	.
Mol00954	Protein	Enterococcal surface protein (ESP)	esp; Fragment	esp	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	DSWLSDTNKKLIQNTYGTGYYYLQDIDGDGNPDDKEESGDTNPYIGKPELEEVYDVDTTVKGKVFIHELAGTGHKAQLVDKEGTVLAEKTIAPNEKDGAPISDTVEFEFTGVDSSKLIAKDELKIQIVSPGFDKPEEGSTVIKESPKAVDKQTVVVGFKPDA	.	.	.	.	B7SF46_9ENTE	Unreviewed	.	.	.	.	.	.
Mol00955	Protein	Erm methyltransferase (ERM42)	erm(42); rRNA methylase	erm(42)	.	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNKNTKIKNKNFNIKDSQNFLHNTKLVEDLLFKSNITKEDFVVEIGPGKGIITKALSKICKAVNAIEFDSVLADKLSHEFKSSNVSIIEADFLKYNLPDHNYKVFSNIPFNITASILNKLLDSENPPLDTFLIMQYEPFLKYAGAPSYKESYKSLLYKPFFKTNILHSFSKFDFKPAPNANIILGQFSYKDFTDINLEDRHAWKDFLAFVFLEKGVTFKEKTKRIFSYKQQKIILKESRINDDSNISNWSYEFWLKMFKLYNSNMVSKDKKVLVNNSYKRMLEHESSLEKIHRNRKQNNRK	.	.	.	.	E5BDA4_PASMD	Unreviewed	.	.	.	.	.	.
Mol00956	Protein	ErmR rRNA adenine N6-methyltransferase (ERMR)	ermR; AERYTH_15865; EC 2.1.1.184; Ribosomal RNA methyltransferase	ermR	.	Aeromicrobium erythreum	2041	Aeromicrobium erythreum	Aeromicrobium	2040	Nocardioidaceae	85015	Propionibacteriales	85009	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAGPQDRPRGRGPSSGRPQRPVGGRSQRDRDRRVLGQNFLRDPATIRRIADAADVDPDGLVVEAGPGEGLLTRELARRAGRVRTYELDQRLARRLSTDLAQETSIEVVHADFLTAPHPEEPFQFVGAIPYGITSAIVDWCLTAPTLTSATLVTQQEFARKRTGDYGRWTALTVTTWPTFEWQYVAKVDRTLFTPVPRVHSAIMRLRRRPQPLLRDAAARSRFADMVEIGFVGKGGSLYRSLTREWPRSKVDSAFARADVHHDEIVAFVHPDQWITLFQLLDGSRGGAARGPGDQRGRRGRPGGGPRPDGRAGGGPRRDAGGRRTGDGRGGRPRPPRGGQA	.	.	.	.	Q5Y9H5_9ACTN	Unreviewed	.	.	.	.	.	.
Mol00957	Protein	Erythromycin esterase (EREA2)	ereA2; Erythromycin esterase	ereA2	.	Providencia stuartii	588	Providencia stuartii	Providencia	586	Morganellaceae	1903414	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTWRTTRTLLQPQKLEFNEFEILNPVVEGARIVGIGEGAHFVAEFSLARASLIRYFVERHDFNAIGLECGAIQASRLSEWLNSTAGAHELERFSDTLTFSLYGSVLIWVKSYLRESGRKLQLVGIDLPNTLNPRDDLAQLAEIIQVIDHLMKPHVDALTQLLTSIDGQSAVISSAKWGELETAQQEKAISGVTRLKLRLASLAPVLKNHVNSDFFRKASDRIESIEYTLETLRVMKAFFDGTSLEGDTSVRDSYMAGVVDGMVRANPDVRIILLAHNNHLQKTPVSFSGELTAVPMGQHLAEREEGDYRAIAFTHLGLTVPEMHFPSPDSPLGFSVVTTPADAIREDSVEQYVIDACGKEDSCLTLTDDPMEAKRMRSQSASVETNLSEAFDAIVCVPSAGKDSLVAL	.	.	.	.	Q9ZFJ8_PROST	Unreviewed	.	.	.	.	.	.
Mol00958	Protein	Erythromycin esterase (EREA2)	ereA2; Erythromycin esterase	ereA2	.	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTWRTTRTLLQPQKLEFNEFEILNPVVEGARIVGIGEGAHFVAEFSLARASLIRYFVERHDFNAIGLECGAIQASRLSEWLNSTAGAHELERFSDTLTFSLYGSVLIWVKSYLRESGRKLQLVGIDLPNTLNPRDDLAQLAEIIQVIDHLMKPHVDALTQLLTSIDGQSAVISSAKWGELETAQQEKAISGVTRLKLRLASLAPVLKNHVNSDFFRKASDRIESIEYTLETLRVMKAFFDGTSLEGDTSVRDSYMAGVVDGMVRANPDVRIILLAHNNHLQKTPVSFSGELTAVPMGQHLAEREEGDYRAIAFTHLGLTVPEMHFPSPDSPLGFSVVTTPADAIREDSVEQYVIDACGKEDSCLTLTDDPMEAKRMRSQSASVETNLSEAFDAIVCVPSAGKDSLVAL	.	.	.	.	Q7B6B2_VIBCL	Unreviewed	.	.	.	.	.	.
Mol00959	Protein	Erythromycin resistance protein (ERM33)	Macrolide-lincosamide-streptogramin B resistance protein; rRNA adenine N-6-methyltransferase; erm33	erm(33)	.	Staphylococcus sciuri	1296	Mammaliicoccus sciuri 	Mammaliicoccus	2803850	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNKKNIKDSQNFITSKRNIDKIMTNISLNEHDNIFEIGSGKGHFTLELVQRCNFVTAIEIDHKLCKTTENKLVDHDNFQVLNKDILQFKFPKNQSYNIFGNIPYNISTDIVKRITFESQAKYSYLIVEKGFAKRLQNLQRALGLLLMVEMDIKMLKKVPPLYFHPKPSVDSVLIVLERHQPLISKKDYKKYRSFVYKWVNREYRVLFTKNQFRQALKHANVTNINKLSKEQFLSIFNSYKLFH	.	"This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics."	.	.	Q8KLN5_MAMSC	Unreviewed	.	.	.	.	.	.
Mol00960	Protein	Erythromycin resistance protein (ERM38)	erm(38); 38	erm(38)	.	Mycolicibacterium smegmatis	1772	Mycolicibacterium smegmatis	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSTPHHGRHELGQNFLSDRRVIADIVEIVSRTNGPIIEIGAGDGALTIPLQRLARPLTAVEVDARRARRLAQRTARSAPGPASRPTEVVAADFLRYPLPRSPHVVVGNLPFHLTTAILRRLLHGPGWTTAVLLMQWEVARRRAAVGGATMMTAQWWPWFEFGLARKVSAASFTPRPAVDAGLLTITRRSRPLVDVADRARYQALVHRVFTGRGHGMAQILQRLPTPVPRTWLRANGIAPNSLPRQLSAAQWAALFEQTRLTGAQRVDRPRDVQHGRAHRRRGGEVDRPATHHKQTGPVVGQRQPQRGRDADADPDDQRTAPPVTRHHQGERRDEDQADHQDRPLTGEHLAGEFLWRHASFDSSASTTLVSRKARVNGPTPPGLGDT	.	.	.	.	Q79N53_MYCSM	Unreviewed	.	.	.	.	.	.
Mol00961	Protein	Ethidium resistance protein (EMRE)	qacF; emrE; CAZ10_01525; CGU42_14710; DT376_08255; E4V10_08075; E5D53_06015; ECC04_029850; GNQ48_04330; IPC111_10130; IPC112_11955; IPC113_21010; IPC114_15435; IPC115_21895; IPC116_07445; IPC117_13035; IPC118_14365; IPC119_19225; IPC120_13415; IPC121_04700; IPC122_19705; IPC123_10700; IPC124_11850; IPC125_15685; IPC126_12045; IPC127_24310; IPC128_20585; IPC1295_07910; IPC129_22120; IPC1306_06520; IPC1307_14550; IPC130_21585; IPC1310_15780; IPC1311_13730; IPC1312_14020; IPC1313_14790; IPC1314_17675; IPC1315_15730; IPC1316_01990; IPC1317_20870; IPC1318_01540; IPC1319_01565; IPC131_00995; IPC1320_07235; IPC1321_15480; IPC1322_06185; IPC1323_06805; IPC1324_06810; IPC1325_01560; IPC1326_01560; IPC1327_01560; IPC1328_13205; IPC1329_15165; IPC132_05115; IPC1331_04465; IPC1332_13740; IPC1333_09990; IPC1334_11330; IPC1335_04920; IPC1336_07425; IPC1337_01650; IPC1338_15555; IPC1339_15375; IPC133_01565; IPC1340_13945; IPC1341_14405; IPC1342_01455; IPC1343_01565; IPC1345_09540; IPC1346_10675; IPC1347_04740; IPC1348_15570; IPC1349_00690; IPC134_00990; IPC135_01565; IPC137_20225; IPC139_07480; IPC140_04920; IPC141_01570; IPC143_06390; IPC144_06980; IPC145_01570; IPC146_06075; IPC1474_13830; IPC1476_06705; IPC1477_09170; IPC1478_04470; IPC1479_12565; IPC147_09320; IPC1480_11880; IPC1481_04360; IPC1482_01560; IPC1485_07045; IPC1486_02225; IPC1487_07880; IPC1489_06135; IPC148_11425; IPC1491_01620; IPC1494_11855; IPC1495_07595; IPC1496_05945; IPC1498_15600; IPC1499_06665; IPC149_06070; IPC1500_12105; IPC1501_14840; IPC1502_13785; IPC1503_13850; IPC1504_10570; IPC1505_01855; IPC1506_20965; IPC1507_20265; IPC1508_06345; IPC1509_09460; IPC150_09060; IPC1510_00930; IPC1511_09015; IPC1512_18795; IPC1513_06930; IPC1514_15400; IPC1515_16655; IPC1516_11610; IPC1517_06880; IPC1518_03930; IPC1519_06065; IPC151_09050; IPC1520_02015; IPC1521_06525; IPC1522_06240; IPC152_06975; IPC153_01570; IPC154_20580; IPC155_21475; IPC156_20655; IPC157_24080; IPC1583_06300; IPC1584_09385; IPC1585_01565; IPC1586_10105; IPC1587_05785; IPC1588_02005; IPC1589_11005; IPC158_25780; IPC1591_01565; IPC1592_01565; IPC1593_15130; IPC1594_10140; IPC1595_01840; IPC1596_06255; IPC1597_05910; IPC1598_05700; IPC1599_10710; IPC159_23025; IPC1600_01560; IPC1601_14200; IPC1602_05240; IPC1603_06525; IPC1604_15475; IPC1605_01175; IPC1606_08240; IPC161_06535; IPC162_16675; IPC163_15040; IPC164_15490; IPC165_15045; IPC166_16360; IPC167_14665; IPC168_21810; IPC169_15065; IPC170_15355; IPC171_09885; IPC172_01565; IPC173_01565; IPC174_02320; IPC175_04885; IPC176_01995; IPC177_03335; IPC178_10800; IPC179_01345; IPC180_01560; IPC181_01560; IPC182_13570; IPC183_05820; IPC184_18590; IPC26_05280; IPC27_14305; IPC29_05570; IPC30_06520; IPC31_07745; IPC32_10065; IPC33_14965; IPC34_05855; IPC35_05850; IPC36_10190; IPC37_09220; IPC38_06130; IPC40_05280; IPC41_01565; IPC42_01565; IPC43_13675; IPC44_12655; IPC45_05550; IPC46_05360; IPC47_01590; IPC48_01565; IPC49_01565; IPC50_01565; IPC51_05220; IPC54_16865; IPC55_14250; IPC56_15165; IPC574_07455; IPC575_15630; IPC576_09675; IPC577_11880; IPC578_07460; IPC579_07895; IPC57_05485; IPC580_15420; IPC582_07450; IPC584_16115; IPC586_07465; IPC589_16680; IPC58_01625; IPC596_09650; IPC597_05335; IPC598_07825; IPC599_10385; IPC59_13705; IPC600_07530; IPC601_10040; IPC602_10460; IPC603_01580; IPC604_01560; IPC605_01560; IPC606_23180; IPC607_09455; IPC608_04710; IPC609_12330; IPC60_12915; IPC610_07855; IPC611_01565; IPC612_01560; IPC613_01560; IPC614_08185; IPC615_01570; IPC616_01570; IPC618_01570; IPC620_01590; IPC621_00465; IPC622_11400; IPC623_13455; IPC624_01560; IPC625_12015; IPC627_08180; IPC629_13880; IPC630_06460; IPC632_02000; IPC633_00980; IPC634_02000; IPC64_14630; IPC65_01470; IPC66_07820; IPC67_01570; IPC68_01575; IPC70_15470; IPC71_04780; IPC72_08430; IPC737_05875; IPC73_07640; IPC74_18665; JEV80_16765; NCTC13621_03545; PA52Ts2_0763; PAMH19_2703; Multidrug efflux SMR transporter; Multidrug transporter; SMR multidrug efflux transporter	qacF	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTNYLYLAIAIAAEVVATTSLKAVAGFSKPLPLLLVVGGYVLAFSMLVLVMRTLPVGVVYAIWSGLGIVLVSLVAMFVYGQRLDPAALLGIGLIIAGVLVIQLFSRASGH	.	.	.	.	A0A071KTJ7_PSEAI	Unreviewed	.	.	.	.	.	.
Mol00962	Protein	Fatty acid synthase (FASN)	Type I fatty acid synthase; FAS	FASN	2194	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000306749.4, FASN-201, 8464; ENST00000634990.1, FASN-206, 8407; ENST00000635197.1, FASN-207, 627; ENST00000636628.1, FASN-209, 100; ENST00000637026.1, FASN-211, 100; ENST00000636968.1, FASN-210, 100; ENST00000580382.1, FASN-204, 681; ENST00000637525.1, FASN-212, 141; ENST00000635733.1, FASN-208, 100; ENST00000637693.1, FASN-213, 100; ENST00000578424.2, FASN-202, 951; ENST00000584610.2, FASN-205, 857; ENST00000579410.1, FASN-203, 424"	MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLARALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPGAQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEEPEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG	chr17:82078338-82098294[-]	Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.	PDB: 1XKT; PDB: 2CG5; PDB: 2JFD; PDB: 2JFK; PDB: 2PX6; PDB: 3HHD; PDB: 3TJM; PDB: 4PIV; PDB: 4W82; PDB: 4W9N; PDB: 4Z49; PDB: 5C37; PDB: 6NNA	HGNC:3594	FAS_HUMAN	Reviewed	ENSG00000169710	.	.	.	.	.
Mol00963	Protein	FDH-N subunit gamma (FDHNI)	Anaerobic formate dehydrogenase cytochrome b556 subunit; Formate dehydrogenase-N subunit gamma; FDH-N subunit gamma; b1476; JW1472	fdnI	66674672	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSKSKMIVRTKFIDRACHWTVVICFFLVALSGISFFFPTLQWLTQTFGTPQMGRILHPFFGIAIFVALMFMFVRFVHHNIPDKKDIPWLLNIVEVLKGNEHKVADVGKYNAGQKMMFWSIMSMIFVLLVTGVIIWRPYFAQYFPMQVVRYSLLIHAAAGIILIHAILIHMYMAFWVKGSIKGMIEGKVSRRWAKKHHPRWYREIEKAEAKKESEEGI	.	"Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar)."	PDB: 1KQF; PDB: 1KQG	.	FDNI_ECOLI	Reviewed	.	.	.	.	.	.
Mol00964	Protein	Flavin-dependent monooxygenase (TETX3)	TetX monooxygenase; TetX	tet(X3)	.	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTMRIDTDKQMNLLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHKGSGQEAMKKAGLLQTYYDLALPMGVNIADEKGNILSTKNVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKIRSFVTDTQVEETGTFNIQADILQPEINCPGFFQLCNGNRLMAGHQGILLFANPNNNGALYLGISFKTPDEWKNKIPLDFQDRNSVADFLLKRFSKWSEVYKQLIRSVSTFQCLPTRKFPLNNDWKSNRPLPITMIGDAAHLMSPFAGQGVNTGLLDALILSENLTNGEFTSIENAIENYEQQMFVYAKDTQDESTENETEMFSPNFSFQKLLNL	.	"An FAD-requiring monooxygenase active on some tetracycline antibiotic derivatives, which leads to their inactivation. Hydroxylates carbon 11a of tetracycline and some analogs."	.	.	A0A7D5G3X7_ACISP	Unreviewed	.	.	.	.	.	.
Mol00965	Protein	Flavin-dependent monooxygenase (TETX4)	TetX monooxygenase; TetX; pRF14-1_50k_tetX_00027	tet(X4)	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSNKEKQMNLLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHKGSGQEAMKKAGLLQTYYDLALPMGVNIADEKGNILSTKNVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVIIANGGMSKVRKFVTDTEVEETGTFNIQTDIHHPEVNCPGFFQLCNGNRLMAAHQGNLLFANPNNNGALHFGISFKTPDEWKNQTQVDFQNRNSVVDFLLKEFSDWDERYKELIRVTSSFVGLATRIFPLGKSWKSKRPLPITMIGDAAHLMPPFAGQGVNSGLMDALILSDNLTNGKFNSIEEAIENYEQQMFIYGKEAQEESTQNEIEMFKPDFTFQQLLNV	.	"An FAD-requiring monooxygenase active on some tetracycline antibiotic derivatives, which leads to their inactivation. Hydroxylates carbon 11a of tetracycline and some analogs."	.	.	A0A6H1PXF0_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00966	Protein	Flavohemoprotein (HCP)	Flavohemoglobin; HMP; Hemoglobin-like protein; Nitric oxide dioxygenase; NO oxygenase; NOD; fsrB; hmpA; b2552; JW2536	hmp	66673560	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MLDAQTIATVKATIPLLVETGPKLTAHFYDRMFTHNPELKEIFNMSNQRNGDQREALFNAIAAYASNIENLPALLPAVEKIAQKHTSFQIKPEQYNIVGEHLLATLDEMFSPGQEVLDAWGKAYGVLANVFINREAEIYNENASKAGGWEGTRDFRIVAKTPRSALITSFELEPVDGGAVAEYRPGQYLGVWLKPEGFPHQEIRQYSLTRKPDGKGYRIAVKREEGGQVSNWLHNHANVGDVVKLVAPAGDFFMAVADDTPVTLISAGVGQTPMLAMLDTLAKAGHTAQVNWFHAAENGDVHAFADEVKELGQSLPRFTAHTWYRQPSEADRAKGQFDSEGLMDLSKLEGAFSDPTMQFYLCGPVGFMQFTAKQLVDLGVKQENIHYECFGPHKVL	.	"Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.; FUNCTION: In the presence of oxygen and NADH, HMP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that HMP might act as an amplifier of superoxide stress. Under anaerobic conditions, HMP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.; FUNCTION: Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if these reactions are of any biological significance in vivo."	PDB: 1GVH	.	HMP_ECOLI	Reviewed	.	.	.	.	.	.
Mol00967	Protein	Fluoroquinolone efflux MFS transporter QepA1 (QEPA1)	pef; QepA; qepA; qepA1; BVL39_07900; EHH55_26410; IPF_141; pHN3A11_013; Plasmid efflux fluoroquinolone; QepA protein; Quinolone efflux pump	pef	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSATLHDTAADRRKATRREWIGLAVVALPCLVYAMDLTVLNLALPVLSRELQPSSAQLLWILDIYGFFVAGFLITMGTLGDRIGRRRLLLIGAAFFAFASVLAALADTAALLIAARALLGLAGATIAPSTMALVRNMFHDPRQRQFAIGVWIAAFSLGSAIGPLVGGVLLEFFHWGAVFWLNVPVMLLTLALGPRFLPEYRDPDAGHLDLASVLLSLAAVLLTIYGLKQLAEHGAGLASMAALLAGLAVGALFLRRQGHIAYPLLDLRLFAHAPFRAALAAYALAALAMFGVYIFMTQYLQLVLGLSPLQAGLATLPWSLCFVIGSLLSPQLAARWPAARILVVGLSAAAFGFAVLGLGQGLWWLVPATIVMGLGLAPVFTIGNEIIITSAPSERAGAASALSETVSEFSGALGIALFGSVGLVVYRQALTSAALPGLPADALQAAGASLGGAVHLADTLPAWQGAALLAAARAGFTDALQATAWAGAVLVLVAAGLVARLLRKRPALASG	.	.	.	.	A5H8A5_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00968	Protein	Fur1 uracil phosphoribosyltransferase (FUR1)	QG37_00045	QG37_00045	.	Candida auris	498019	Candida auris	.	.	Metschnikowiaceae	27319	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSTPQNVSKNVILLPQTNQLRGLYSIIRDQLTKRGDFVFYSDRIIRLLVEEGLNQLPVEEAIIECHGGHKYKGAKFLGKICGVSIVRAGESMEMGLRDCCRSVRIGKILIQRDEETALPKLFYEKLPEDISERYVFLLDPMLATGGSAMMAVEVLLSRGVRMDRIFFLNLLAAPEGINAFHEKYPDVRIITGGIDEKLDDDKYIVPGLGDFGDRYYCI	.	.	.	.	A0A0L0P8H5_CANAR	Unreviewed	.	.	.	.	.	.
Mol00969	Protein	HIV1 Reverse transcriptase (HIV1 RT)	Pr160Gag-Pol; MA; CA; SP1; p2; NC; TF; p6*; PR; Retropepsin; Exoribonuclease H; p66 RT; IN	gag-pol	155348	Human immunodeficiency virus type 1	11676	Human immunodeficiency virus 1	Lentivirus	11646	Retroviridae	11632	Ortervirales	2169561	Revtraviricetes	2732514	Artverviricota	2732409	Pararnavirae	2732397	.	PISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNRGRQKVVTLTDTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDQSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKVL	.	"Multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA3-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends."	PDB: 1A30; PDB: 1BV7; PDB: 1BV9; PDB: 1BVE; PDB: 1BVG; PDB: 1BWA; PDB: 1BWB; PDB: 1C0T; PDB: 1C0U; PDB: 1C1B; PDB: 1C1C; PDB: 1DMP; PDB: 1DTQ; PDB: 1DTT; PDB: 1E6J; PDB: 1EP4; PDB: 1ESK; PDB: 1EX4; PDB: 1EXQ; PDB: 1FB7; PDB: 1FK9; PDB: 1FKO; PDB: 1FKP; PDB: 1G6L; PDB: 1HIV; PDB: 1HVH; PDB: 1HVR; PDB: 1HWR; PDB: 1HXB; PDB: 1JKH; PDB: 1JLA; PDB: 1JLB; PDB: 1JLC; PDB: 1JLE; PDB: 1JLF; PDB: 1JLG; PDB: 1JLQ; PDB: 1KLM; PDB: 1LV1; PDB: 1LW0; PDB: 1LW2; PDB: 1LWC; PDB: 1LWE; PDB: 1LWF; PDB: 1NCP; PDB: 1O1W; PDB: 1ODW; PDB: 1ODY; PDB: 1QBR; PDB: 1QBS; PDB: 1QBT; PDB: 1QBU; PDB: 1REV; PDB: 1RT1; PDB: 1RT2; PDB: 1RT3; PDB: 1RT4; PDB: 1RT5; PDB: 1RT6; PDB: 1RT7; PDB: 1RTD; PDB: 1RTH; PDB: 1RTI; PDB: 1RTJ; PDB: 1S1T; PDB: 1S1U; PDB: 1S1V; PDB: 1S1W; PDB: 1S1X; PDB: 1T05; PDB: 1TAM; PDB: 1TKT; PDB: 1TKX; PDB: 1TKZ; PDB: 1TL1; PDB: 1TL3; PDB: 1VRT; PDB: 1VRU; PDB: 2HND; PDB: 2HNY; PDB: 2HNZ; PDB: 2KOD; PDB: 2NPH; PDB: 2OPP; PDB: 2OPQ; PDB: 2OPR; PDB: 2OPS; PDB: 2RF2; PDB: 2RKI; PDB: 2WHH; PDB: 2WOM; PDB: 2WON; PDB: 2YNF; PDB: 2YNG; PDB: 2YNH; PDB: 2YNI; PDB: 3AO2; PDB: 3C6T; PDB: 3C6U; PDB: 3DI6; PDB: 3DLE; PDB: 3DLG; PDB: 3DM2; PDB: 3DMJ; PDB: 3DOK; PDB: 3DOL; PDB: 3DOX; PDB: 3DRP; PDB: 3DRR; PDB: 3DRS; PDB: 3DYA; PDB: 3E01; PDB: 3FFI; PDB: 3I0R; PDB: 3I0S; PDB: 3KJV; PDB: 3KK1; PDB: 3KK2; PDB: 3KK3; PDB: 3KT2; PDB: 3KT5; PDB: 3LAK; PDB: 3LAL; PDB: 3LAM; PDB: 3LAN; PDB: 3LP0; PDB: 3LP1; PDB: 3LP2; PDB: 3M8P; PDB: 3M8Q; PDB: 3MEC; PDB: 3MED; PDB: 3MEE; PDB: 3MEG; PDB: 3N3I; PDB: 3NBP; PDB: 3PHV; PDB: 3QIN; PDB: 3QIO; PDB: 3QIP; PDB: 3T19; PDB: 3T1A; PDB: 3TAM; PDB: 4B3O; PDB: 4B3P; PDB: 4B3Q; PDB: 4I7F; PDB: 4KSE; PDB: 4KV8; PDB: 4NCG; PDB: 4Q1W; PDB: 4Q1X; PDB: 4Q1Y; PDB: 4Q5M; PDB: 4QLH; PDB: 4U1H; PDB: 4U1I; PDB: 4U1J; PDB: 4U7Q; PDB: 4U7V; PDB: 5DGU; PDB: 5DGW; PDB: 5EU7; PDB: 5HRN; PDB: 5HRP; PDB: 5HRR; PDB: 5HRS; PDB: 5IM7; PDB: 5J2M; PDB: 5J2N; PDB: 5J2P; PDB: 5J2Q; PDB: 5K14; PDB: 5KAO; PDB: 5T82; PDB: 5TC2; PDB: 5VZ6; PDB: 5XOS; PDB: 5XOT; PDB: 5YRS; PDB: 6BJ2; PDB: 6BJ3; PDB: 6BSG; PDB: 6BSH; PDB: 6BSI; PDB: 6BSJ; PDB: 6DIF; PDB: 6DIL; PDB: 6DJ1; PDB: 6DJ2; PDB: 6DJ5; PDB: 6DJ7; PDB: 6DV0; PDB: 6DV4; PDB: 6E7J; PDB: 6E9A; PDB: 6EWA; PDB: 6EX9; PDB: 6GL1; PDB: 6J1V; PDB: 6J1W; PDB: 6OR7; PDB: 6OTZ; PDB: 6P1I; PDB: 6P1X; PDB: 6P2G; PDB: 6PYL; PDB: 6SKK; PDB: 6SKM; PDB: 6SKN; PDB: 6SLQ; PDB: 6SLU; PDB: 6SMU; PDB: 6UIR; PDB: 6UIS; PDB: 6UIT; PDB: 6UJX; PDB: 6UJY; PDB: 6UJZ; PDB: 6UK0; PDB: 6VPZ; PDB: 6VQ2; PDB: 6VQD; PDB: 6VQE; PDB: 6VQY; PDB: 6VQZ; PDB: 6WAZ; PDB: 6WB1; PDB: 6WPF; PDB: 6WPH; PDB: 6WPJ	.	POL_HV1H2 (588-1147)	Reviewed	.	.	.	.	.	.
Mol00970	Protein	HIV2 Protease (HIV2 PR)	Pr160Gag-Pol; MA; CA; SP1; p2; NC; TF; p6*; PR; Retropepsin; Exoribonuclease H; p66 RT; IN	gag-pol	1490001	Human immunodeficiency virus type 2	11676	Human immunodeficiency virus 1	Lentivirus	11646	Retroviridae	11632	Ortervirales	2169561	Revtraviricetes	2732514	Artverviricota	2732409	Pararnavirae	2732397	.	PQFSLWRRPVVKACIEGQSVEVLLDTGVDDSIVAGIELGSNYTPKIVGGIGGFINTKEYKDVEIEVVGKRVRATIMTGDTPINIFGRNILNTLGMTLNF	.	"Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins"	PDB: 1A9M; PDB: 1AJV; PDB: 1AJX; PDB: 1AXA; PDB: 1BQM; PDB: 1BQN; PDB: 1D4H; PDB: 1D4I; PDB: 1D4J; PDB: 1DLO; PDB: 1DW6; PDB: 1EBK; PDB: 1EBW; PDB: 1EBY; PDB: 1EBZ; PDB: 1EC0; PDB: 1EC1; PDB: 1EC2; PDB: 1EC3; PDB: 1EET; PDB: 1G35; PDB: 1GNM; PDB: 1GNN; PDB: 1GNO; PDB: 1HAR; PDB: 1HBV; PDB: 1HEF; PDB: 1HEG; PDB: 1HIH; PDB: 1HMV; PDB: 1HNI; PDB: 1HNV; PDB: 1HOS; PDB: 1HPS; PDB: 1HPZ; PDB: 1HQE; PDB: 1HQU; PDB: 1HRH; PDB: 1HTE; PDB: 1HTF; PDB: 1HTG; PDB: 1HVI; PDB: 1HVK; PDB: 1HVU; PDB: 1HYS; PDB: 1IKV; PDB: 1IKW; PDB: 1IKX; PDB: 1IKY; PDB: 1J5O; PDB: 1KJH; PDB: 1MER; PDB: 1MES; PDB: 1MET; PDB: 1MEU; PDB: 1N5Y; PDB: 1N6Q; PDB: 1NPA; PDB: 1NPV; PDB: 1NPW; PDB: 1QE1; PDB: 1QMC; PDB: 1R0A; PDB: 1RDH; PDB: 1RTD; PDB: 1S6P; PDB: 1S6Q; PDB: 1S9E; PDB: 1S9G; PDB: 1SBG; PDB: 1SUQ; PDB: 1SV5; PDB: 1T03; PDB: 1T05; PDB: 1T7K; PDB: 1TV6; PDB: 1TVR; PDB: 1UWB; PDB: 1W5V; PDB: 1W5W; PDB: 1W5X; PDB: 1W5Y; PDB: 1YT9; PDB: 1ZP8; PDB: 1ZPA; PDB: 1ZSF; PDB: 1ZSR; PDB: 2AQU; PDB: 2B5J; PDB: 2B6A; PDB: 2BAN; PDB: 2BBB; PDB: 2BE2; PDB: 2EXF; PDB: 2G69; PDB: 2HB3; PDB: 2HMI; PDB: 2HNZ; PDB: 2HS1; PDB: 2HS2; PDB: 2I4D; PDB: 2I4U; PDB: 2I4V; PDB: 2I4W; PDB: 2I4X; PDB: 2I5J; PDB: 2IAJ; PDB: 2IC3; PDB: 2IDW; PDB: 2IEO; PDB: 2JZW; PDB: 2L45; PDB: 2L46; PDB: 2L4L; PDB: 2UXZ; PDB: 2UY0; PDB: 2VG5; PDB: 2VG6; PDB: 2VG7; PDB: 2X4U; PDB: 2YKM; PDB: 2YKN; PDB: 2ZD1; PDB: 2ZE2; PDB: 3AVI; PDB: 3BGR; PDB: 3DLK; PDB: 3GGA; PDB: 3GGV; PDB: 3GGX; PDB: 3HVT; PDB: 3IG1; PDB: 3IRX; PDB: 3IS9; PDB: 3ISN; PDB: 3ITH; PDB: 3JSM; PDB: 3JYT; PDB: 3K2P; PDB: 3K4V; PDB: 3KLE; PDB: 3KLF; PDB: 3KLG; PDB: 3KLH; PDB: 3KLI; PDB: 3NDT; PDB: 3NU3; PDB: 3NU4; PDB: 3NU5; PDB: 3NU6; PDB: 3NU9; PDB: 3NUJ; PDB: 3NUO; PDB: 3OK9; PDB: 3PSU; PDB: 3QAA; PDB: 3QLH; PDB: 3QO9; PDB: 3TKG; PDB: 3TKW; PDB: 3TL9; PDB: 3TLH; PDB: 3V4I; PDB: 3V6D; PDB: 3V81; PDB: 3ZPS; PDB: 3ZPT; PDB: 3ZPU; PDB: 4COE; PDB: 4CP7; PDB: 4CPQ; PDB: 4CPR; PDB: 4CPS; PDB: 4CPT; PDB: 4CPU; PDB: 4CPW; PDB: 4CPX; PDB: 4DG1; PDB: 4G1Q; PDB: 4G8G; PDB: 4G8I; PDB: 4G9D; PDB: 4G9F; PDB: 4H4M; PDB: 4H4O; PDB: 4I2P; PDB: 4I2Q; PDB: 4ICL; PDB: 4ID5; PDB: 4IDK; PDB: 4IFV; PDB: 4IFY; PDB: 4IG0; PDB: 4IG3; PDB: 4KFB; PDB: 4KKO; PDB: 4KO0; PDB: 4LSL; PDB: 4LSN; PDB: 4MFB; PDB: 4O44; PDB: 4O4G; PDB: 4OJR; PDB: 4PQU; PDB: 4PUO; PDB: 4PWD; PDB: 4Q0B; PDB: 4QAG; PDB: 4R5P; PDB: 4RW4; PDB: 4RW6; PDB: 4RW7; PDB: 4RW8; PDB: 4RW9; PDB: 4U8W; PDB: 4WE1; PDB: 4YE3; PDB: 4YHQ; PDB: 4ZIP; PDB: 4ZLS; PDB: 5AGZ; PDB: 5AH6; PDB: 5AH7; PDB: 5AH8; PDB: 5AH9; PDB: 5AHA; PDB: 5AHB; PDB: 5AHC; PDB: 5BRY; PDB: 5BS4; PDB: 5C24; PDB: 5C25; PDB: 5C42; PDB: 5CYM; PDB: 5CYQ; PDB: 5D3G; PDB: 5FDL; PDB: 5HBM; PDB: 5HLF; PDB: 5HP1; PDB: 5HRO; PDB: 5I3U; PDB: 5I42; PDB: 5J1E; PDB: 5JFP; PDB: 5JFU; PDB: 5JG1; PDB: 5OI2; PDB: 5OI3; PDB: 5OI5; PDB: 5OI8; PDB: 5OIA; PDB: 5T6Z; PDB: 5T70; PDB: 5TER; PDB: 5TUQ; PDB: 5TW3; PDB: 5TXL; PDB: 5TXM; PDB: 5TXN; PDB: 5TXO; PDB: 5TXP; PDB: 5UFZ; PDB: 5ULT; PDB: 5UOV; PDB: 5UPZ; PDB: 5UV5; PDB: 5V5L; PDB: 5V5M; PDB: 5VQQ; PDB: 5VQR; PDB: 5VQS; PDB: 5VQT; PDB: 5VQU; PDB: 5VQV; PDB: 5VQW; PDB: 5VQX; PDB: 5VQY; PDB: 5VQZ; PDB: 5W5W; PDB: 5YOJ; PDB: 6AMO; PDB: 6AN2; PDB: 6AN8; PDB: 6ANQ; PDB: 6AOC; PDB: 6ASW; PDB: 6AVM; PDB: 6AVT; PDB: 6B19; PDB: 6BZ2; PDB: 6C0J; PDB: 6C0K; PDB: 6C0L; PDB: 6C0N; PDB: 6C0O; PDB: 6C0P; PDB: 6C0R; PDB: 6C8X; PDB: 6C8Y; PDB: 6CGF; PDB: 6D0D; PDB: 6D0E; PDB: 6DTW; PDB: 6DTX; PDB: 6DUF; PDB: 6DUG; PDB: 6DUH; PDB: 6ECL; PDB: 6ELI; PDB: 6HAK; PDB: 6KMP; PDB: 6O48; PDB: 6O9E; PDB: 6OE3; PDB: 6OUN; PDB: 6PRF; PDB: 6UL5; PDB: 6VUG; PDB: 6WAZ; PDB: 6WB0; PDB: 6WB1; PDB: 6WB2; PDB: 6X47; PDB: 6X49; PDB: 6X4A; PDB: 6X4B; PDB: 6X4C; PDB: 6X4D; PDB: 6X4E; PDB: 6X4F; PDB: 7AHX; PDB: 7AID; PDB: 7AIF; PDB: 7AIG; PDB: 7AII; PDB: 7AIJ; PDB: 7KJV; PDB: 7KJW; PDB: 7KJX; PDB: 7KRC; PDB: 7KRD; PDB: 7KRE; PDB: 7KRF; PDB: 7KWU; PDB: 7LPW; PDB: 7LPX; PDB: 7LQU; PDB: 7OT6; PDB: 7OTA; PDB: 7OTK; PDB: 7OTN; PDB: 7OTX; PDB: 7OTZ; PDB: 7OUT; PDB: 7OXQ; PDB: 7OZ2; PDB: 7OZ5; PDB: 7OZW; PDB: 7P15	.	POL_HV2D2 (513-611)	Reviewed	.	.	.	.	.	.
Mol00971	Protein	Galactarate dehydratase (L-threo-forming) (GARD)	GalcD; yhaG; b3128; JW3097	garD	947641	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MANIEIRQETPTAFYIKVHDTDNVAIIVNDNGLKAGTRFPDGLELIEHIPQGHKVALLDIPANGEIIRYGEVIGYAVRAIPRGSWIDESMVVLPEAPPLHTLPLATKVPEPLPPLEGYTFEGYRNADGSVGTKNLLGITTSVHCVAGVVDYVVKIIERDLLPKYPNVDGVVGLNHLYGCGVAINAPAAVVPIRTIHNISLNPNFGGEVMVIGLGCEKLQPERLLTGTDDVQAIPVESASIVSLQDEKHVGFQSMVEDILQIAERHLQKLNQRQRETCPASELVVGMQCGGSDAFSGVTANPAVGYASDLLVRCGATVMFSEVTEVRDAIHLLTPRAVNEEVGKRLLEEMEWYDNYLNMGKTDRSANPSPGNKKGGLANVVEKALGSIAKSGKSAIVEVLSPGQRPTKRGLIYAATPASDFVCGTQQVASGITVQVFTTGRGTPYGLMAVPVIKMATRTELANRWFDLMDINAGTIATGEETIEEVGWKLFHFILDVASGKKKTFSDQWGLHNQLAVFNPAPVT	.	Catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate (5-KDG).	PDB: 3LAZ; PDB: 6U7L	.	GARD_ECOLI	Reviewed	.	.	.	.	.	.
Mol00972	Protein	GDH/6PGL endoplasmic bifunctional protein (H6PD)	Glucose 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; 6PGL	H6pd	100198	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000030830.4, H6pd-201, 4745; ENSMUST00000084117.13, H6pd-202, 4571; ENSMUST00000153394.2, H6pd-204, 650; ENSMUST00000152907.2, H6pd-203, 392"	MLLAAMCLALLGCLQAQELKGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGKGHSFSFHGAALTAPQQGQKLMDKVLESLSCPKDLVPSRCDELKGQFLQLSQYRQLKTVEDYQTLNKDIETQVQQDGLWEAGRIFYFSVPPFAYADIARNINSSCRPHPGAWLRVVFEKPFGHDHLSAQQLASELGSFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEIILKETIDAEGRASFYEEYGVIRDTLQNHLTEILTLVAMELPLNISSSAAVLQHKLWAFQALRGLQKSSAILGQYQAYSGQVRRELQKPDGFQSLTPTFAGVLVHIDNLRWEGVPFILMSGKALDERVGYVRIVFKNRAYCTQSERHWVPEQSRCLPQQIIFYIGHGELGHPAILVSRNLFKPSLPTQKWKEVQDQPGLRLFGRPLSDYYAYRPVREQDAYSTLLSHIFHCRKESFITTENLLASWVFWTPLLDSLAFEVPRPYPGGAENGQLLDFEFSGGQLTFSQQQLEVLIPDLGSVPKPSDFQVLGARYRQSPLITAWPEELISKLASDIEAAAVQAVRHFGKFHLALSGGSSPIALFQQLATGHYSFPWAHTHLWLVDERCVPLSDPDSNFQGLQAHLLQHVRVPYYNIHPMPVHLHQRLCAEEDQGAQTYASEISALVANSSFDLVLLGMGTDGHTASLFPQSPTGLDGDQLVVLTESPFRPHQRMSLSLPLINRAKKVAVLVMGRTKREITTLVSRVGHEPKKWPISGVVPLSGQLVWYMDYEAFLG	chr 4: 150063932-150093480[-] 	"Bifunctional enzyme localized in the lumen of the endoplasmic reticulum that catalyzes the first two steps of the oxidative branch of the pentose phosphate pathway/shunt, an alternative to glycolysis and a major source of reducing power and metabolic intermediates for biosynthetic processes. Has a hexose-6-phosphate dehydrogenase activity, with broad substrate specificity compared to glucose-6-phosphate 1-dehydrogenase/G6PD, and catalyzes the first step of the pentose phosphate pathway. In addition, acts as a 6-phosphogluconolactonase and catalyzes the second step of the pentose phosphate pathway. May have a dehydrogenase activity for alternative substrates including glucosamine 6-phosphate and glucose 6-sulfate. The main function of this enzyme is to provide reducing equivalents such as NADPH to maintain the adequate levels of reductive cofactors in the oxidizing environment of the endoplasmic reticulum. By producing NADPH that is needed by reductases of the lumen of the endoplasmic reticulum like corticosteroid 11-beta-dehydrogenase isozyme 1/HSD11B1, indirectly regulates their activity."	.	.	G6PE_MOUSE	Reviewed	ENSMUSG00000028980	.	.	.	.	.
Mol00973	Protein	Glutathione biosynthesis bifunctional protein GshAB (GSHAB )	Gamma-GCS-GS; GCS-GS; Gamma-ECS; GCS; Gamma-glutamylcysteine synthetase; GSH synthetase; GS; GSH-S; GSHase; Glutathione synthase; gshF; EF_3089	gshAB	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNYRELMQKKNVRPYVLMARFGLEKENQRSTREGLLATTEHPTVFGNRSYHPYIQTDFSETQLELITPVANSGTEMLRFLDAIHDVARRSIPEDEMLWPLSMPPQLPTKDEEIKIAKLDQYDAVLYRRYLAKEYGKRKQMVSGIHFNFEYDQALIQQLYDEQSEVTDCKQFKTKVYMKVARNFLRYRWLITYLFGASPVSEDRYFRVYDDQPQEPVRSIRNSTYGYRNHDNVKVSYASLERYLEDIHRMVENGLLSEEKEFYAPVRLRGGKQMSDLPKTGIRYIELRNLDLNPFSRLGIVEDTVDFLHYFMLYLLWTDEKEEADEWVKTGDIFNEQVALGHPHETIKLIAEGDRIFSEMIDMLDALGIRKGKEVVGKYYQQLRNPQDTVSGKMWTIIQENSNSELGNIFGNQYQSMAFERPYQLAGFREMELSTQIFLFDAIQKGLEIEILDEQEQFLKLQHGEHIEYVKNANMTSKDNYVVPLIMENKTVTKKILSAAGFHVPGGEEFSSFIEAQEAHLRYANKAFVVKPKSTNYGLGITIFKEGASLEDFTEALRIAFKEDTAVLIEEFLPGTEYRFFVLDNDVKAIMLRVPANVTGDGKHTVEELVAAKNSDPLRGTNHRAPLELIQLNDLEKLMLKEQGLTIYSVPEKEQIVYLRENSNVSTGGDSIDMTDVIDDSYKQIAIEAVAALGAKICGIDLIIPDKDVKGTRDSLTYGIIEANFNPAMHMHVYPYAGQGRRLTMDVLKLLYPEVVQ	.	Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.	.	.	GSHAB_ENTFA	Reviewed	.	.	.	.	.	.
Mol00974	Protein	Glycerol dehydrogenase (GLDA)	GDH; GLDH; b3945; JW5556	gldA	66672144	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MDRIIQSPGKYIQGADVINRLGEYLKPLAERWLVVGDKFVLGFAQSTVEKSFKDAGLVVEIAPFGGECSQNEIDRLRGIAETAQCGAILGIGGGKTLDTAKALAHFMGVPVAIAPTIASTDAPCSALSVIYTDEGEFDRYLLLPNNPNMVIVDTKIVAGAPARLLAAGIGDALATWFEARACSRSGATTMAGGKCTQAALALAELCYNTLLEEGEKAMLAAEQHVVTPALERVIEANTYLSGVGFESGGLAAAHAVHNGLTAIPDAHHYYHGEKVAFGTLTQLVLENAPVEEIETVAALSHAVGLPITLAQLDIKEDVPAKMRIVAEAACAEGETIHNMPGGATPDQVYAALLVADQYGQRFLQEWE	.	"Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively."	PDB: 5ZXL	.	GLDA_ECOLI	Reviewed	.	.	.	.	.	.
Mol00975	Protein	Heat-shock protein IbpA (IBPA)	ibpA; PA3126; Heat-shock protein IbpA	ibpA	882640	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSNAFSLAPLFRHSVGFDRFNDLFESALRNEAGSTYPPYNVEKHGDDEYRIVIAAAGFQEEDLDLQVERGVLTVSGGKREKSTDNVTYLHQGIAQRAFKLSFRLADHIEVKAASLANGLLNIDLVRLVPEEAKPKRIAINGQRPALDNQ	.	.	.	.	Q9HZ98_PSEAE	Unreviewed	.	.	.	.	.	.
Mol00976	Protein	HTH-type transcriptional regulator MgrA (MGRA)	Regulator of autolytic activity; norR; rat; SAOUHSC_00694	mgrA	3920998	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MSDQHNLKEQLCFSLYNAQRQVNRYYSNKVFKKYNLTYPQFLVLTILWDESPVNVKKVVTELALDTGTVSPLLKRMEQVDLIKRERSEVDQREVFIHLTDKSETIRPELSNASDKVASASSLSQDEVKELNRLLGKVIHAFDETKEK	.	"Regulatory protein involved in autolytic activity, multidrug resistance and virulence. Controls autolysis by inactivating LytM, LytN (autolysins) and SarV (autolysis activator) and activating ArlRS, LrgAB and LytSR (autolysis inhibitors). Acts as a dual regulator for resistance to multiple drugs by inactivating NorB and tet38 and activating NorA. Positively controls the expression of virulence accessory gene regulator (agr) to promote alpha-hemolysin (hla) transcription and down-regulates staphylococcal accessory regulator (sarS), leading to repression of surface protein A (spa). Binds directly to hla promoter to augment its activation. Binds to sarS promoter to down-regulate spa expression."	.	.	MGRA_STAA8	Reviewed	.	.	.	.	.	.
Mol00977	Protein	Hydrolase (HYDE)	ELS01_26210; G0M02_24435; G0M02_24760	ELS01_26210	.	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MPVLFRVKVIPLVLLLAMIFAFLLNWPILLHFYEILSHLEHVKIGFVISIPFVLVAALNVVFMPFSVRFLLKPFFALLFITGSLVSYSTLKYKVMFDQTMIQNIIETNPQEAHSYLNGSIIIWFVFTGILPAILLFSIKIQYPEKWYKGIAYRLLSVLASLSLIAGVAALYYQDYASVGRNNSTLNKEIIPANYAYSTFQYVKDTYFTTKVPFQTLGNDAKRVVAHEKPTLMFLVIGETARSQNFSMNGYSRDTNAFTSKSGGVISFKNMHSCGTATAISVPCMFSNMNRTEYDSKKASNSENFLDIVQKTGVSLLWKENDGGCKGVCSRIPTVEIKPSDNPKLCDGKTCHDEVMLENLDDEIAKMPGDKLVAFHIIGSHGPTYYLRYPAEHRHFMPECARSDIENCTQEQLVNTYDNTLRYTDYVLAEMIEKLKNYSDQYNTVLLYVSDHGESLGESGLYLHGTPYKLAPDQQTHIPMQVWMSPGFIAGKHINMSCLENNAAKKSYSHDNLFSSILGLWDVSTSVYNPDRDLFRECRG	.	.	.	.	A0A1I9W690_SALTM	Unreviewed	.	.	.	.	.	.
Mol00978	Protein	Imipenem-hydrolyzing beta-lactamase (NMCA)	Carbapenemase; NMC-A	nmcA	.	Enterobacter cloacae	550	Enterobacter cloacae	Enterobacter	547	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSLNVKQSRIAILFSSCLISISFFSQANTKGIDEIKNLETDFNGRIGVYALDTGSGKSFSYRANERFPLCSSFKGFLAAAVLKGSQDNRLNLNQIVNYNTRSLEFHSPITTKYKDNGMSLGDMAAAALQYSDNGATNIILERYIGGPEGMTKFMRSIGDEDFRLDRWELDLNTAIPGDERDTSTPAAVAKSLKTLALGNILSEHEKETYQTWLKGNTTGAARIRASVPSDWVVGDKTGSCGAYGTANDYAVVWPKNRAPLIISVYTTKNEKEAKHEDKVIAEASRIAIDNLK	.	"Hydrolyzes carbapenems such as imipenem, which are extended-spectrum beta-lactam antibiotics."	PDB: 1BUE; PDB: 1BUL	.	BLAN_ENTCL	Reviewed	.	.	.	.	.	.
Mol00979	Protein	Isocitrate dehydrogenase NAD 3 alpha (IDH3A)	Isocitric dehydrogenase subunit alpha; NAD(+)-specific ICDH subunit alpha	IDH3A	3419	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000299518.7, IDH3A-201, 4083; ENST00000558554.5, IDH3A-207, 1595; ENST00000559186.5, IDH3A-212, 744; ENST00000559881.5, IDH3A-216, 738; ENST00000557826.5, IDH3A-202, 587; ENST00000560770.5, IDH3A-221, 586; ENST00000561279.5, IDH3A-222, 569; ENST00000559205.1, IDH3A-213, 566; ENST00000561366.1, IDH3A-223, 389; ENST00000629769.2, IDH3A-224, 114; ENST00000560667.5, IDH3A-220, 2110; ENST00000559803.5, IDH3A-214, 1008; ENST00000558933.5, IDH3A-210, 878; ENST00000558509.5, IDH3A-205, 617; ENST00000559865.5, IDH3A-215, 568; ENST00000559106.5, IDH3A-211, 567; ENST00000560396.5, IDH3A-218, 483; ENST00000557960.1, IDH3A-203, 424; ENST00000558535.1, IDH3A-206, 2586; ENST00000558605.1, IDH3A-209, 573; ENST00000559889.5, IDH3A-217, 2461; ENST00000558602.5, IDH3A-208, 2217; ENST00000560414.1, IDH3A-219, 559; ENST00000558016.1, IDH3A-204, 535"	MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICRRVKDLD	chr15:78131498-78171945[+]	"Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers."	PDB: 5GRE; PDB: 5GRF; PDB: 5GRH; PDB: 5GRI; PDB: 5GRL; PDB: 5YVT; PDB: 6KDE; PDB: 6KDF; PDB: 6KDY; PDB: 6KE3; PDB: 6L57; PDB: 6L59; PDB: 7CE3	HGNC:5384	IDH3A_HUMAN	Reviewed	ENSG00000166411	.	.	.	.	.
Mol00980	Protein	Isocitrate lyase 1 (ICL1)	ICL1; Isocitrase; Isocitratase; Methylisocitrate lyase; MICA; MT0483	icl1	45424429	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSVVGTPKSAEQIQQEWDTNPRWKDVTRTYSAEDVVALQGSVVEEHTLARRGAEVLWEQLHDLEWVNALGALTGNMAVQQVRAGLKAIYLSGWQVAGDANLSGHTYPDQSLYPANSVPQVVRRINNALQRADQIAKIEGDTSVENWLAPIVADGEAGFGGALNVYELQKALIAAGVAGSHWEDQLASEKKCGHLGGKVLIPTQQHIRTLTSARLAADVADVPTVVIARTDAEAATLITSDVDERDQPFITGERTREGFYRTKNGIEPCIARAKAYAPFADLIWMETGTPDLEAARQFSEAVKAEYPDQMLAYNCSPSFNWKKHLDDATIAKFQKELAAMGFKFQFITLAGFHALNYSMFDLAYGYAQNQMSAYVELQEREFAAEERGYTATKHQREVGAGYFDRIATTVDPNSSTTALTGSTEEGQFH	.	"Involved in the persistence and virulence of M.tuberculosis. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. It also catalyzes the formation of pyruvate and succinate from 2-methylisocitrate, a key step in the methylcitrate cycle (propionate degradation route)."	.	.	ACEA1_MYCTO	Reviewed	.	.	.	.	.	.
Mol00981	Protein	Isocitrate lyase 2 (ICL2)	ICL2; Isocitrase; Isocitratase; aceA-2; MT1966	icl2	.	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAIAETDTEVHTPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQRGTIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPGQAVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLSQVPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDFRPFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRPGTKKCGHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVARTDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAMVRRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGLVSDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMTYGEAVADVLEFGQSEGEPIGMAPEEWRAFAARASLHAARAKAKELGADPPWDCELAKTPEGYYQIRGGIPYAIAKSLAAAPFADILWMETKTADLADARQFAEAIHAEFPDQMLAYNLSPSFNWDTTGMTDEEMRRFPEELGKMGFVFNFITYGGHQIDGVAAEEFATALRQDGMLALARLQRKMRLVESPYRTPQTLVGGPRSDAALAASSGRTATTKAMGKGSTQHQHLVQTEVPRKLLEEWLAMWSGHYQLKDKLRVQLRPQRAGSEVLELGIHGESDDKLANVIFQPIQDRRGRTILLVRDQNTFGAELRQKRLMTLIHLWLVHRFKAQAVHYVTPTDDNLYQTSKMKSHGIFTEVNQEVGEIIVAEVNHPRIAELLTPDRVALRKLITKEA	.	"Involved in the persistence and virulence of M.tuberculosis. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates."	.	.	ACEA2_MYCTO	Reviewed	.	.	.	.	.	.
Mol00982	Protein	Kasugamycin 2' acetyltransferase (KA2A)	aac(2')-IIb; AK95_15585; 2')-IIb	aac(2')-IIb	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNHRKGNEPTAAALMELHVLAMFTHDGNMQIRTINEPWPGEELAPRFFMGRTIDGSSICRFRHDVPEGIAGQLRALVEDEPIVTEEVLTRPKHFAAYMNLLRAEHYTSGPCYRIPDQTTQAKQTVRITPGNIREYSLTGFEWLTTEIDYDQPCVALIHENRVVSVCRSVRITERAHEAGLETSEEFRGRGYAAAVVAGWAIEVQKMGALALYSTLWGNSSSRRVANKLGLSYYGVNFTIS	.	.	.	.	A0A1I9ZKL2_9BACL	Unreviewed	.	.	.	.	.	.
Mol00983	Protein	Lanosterol 14-alpha demethylase (ERG11)	ERG11; Lanosterol 14 alpha-demethylase	ERG11	.	Cryptococcus neoformans var. grubii	178876	Cryptococcus neoformans var. grubii	Cryptococcus	5206	Cryptococcaceae	1884633	Tremellales	5234	Tremellomycetes	155616	Basidiomycota	5204	Fungi	4751	.	MSAIIPQVQQLLGQVAQFIPPWFAALPTSVKVVIAVIGIPALVICLNVFQQLCLPRRKDLPPVVFHYIPWFGSAAYYGEDPYKFLFECRDKYGDLFTFILMGRRVTVALGPKGNNLSLGGKISQVSAEEAYTHLTTPVFGKGVVYDCPNEMLMQQKKFIKSGLTTESLQSYPPMITSECEDFFTKEVGISPQKPSATLDLLKSMSELIILTASRTLQGKEVRESLNGQFAKYYEDLDGGFTPLNFMFPNLPLPSYKRRDEAQKAMSDFYLKIMENRRKGESDHEHDMIENLQSCKYRNGVPLSDRDIAHIMIALLMAGQHTSSATSSWTLLHLADRPDVVEALYQEQKQKLGNPDGTFRDYKYEDLKELPIMDSIIRETLRMHAPIHSIYRKVLSDIPVPPSLSAPSENGQYIIPKGHYIMAAPGVSQMDPRIWQDAKVWNPARWHDEKGFAAAAMAQYSKAEQVDYGFGSVSKGTESPYQPFSAGRHRCVGEQFAYTQLSTIFTYVVRNFTLKLAVPKFPETNYRTMIVQPNNPLVTFTLRNAEVK	.	.	.	.	A0A0G3F2G2_CRYNV	Unreviewed	.	.	.	.	.	.
Mol00984	Protein	Lanosterol 14-alpha demethylase (ERG11)	CYPLI; Cytochrome P450 51; Cytochrome P450-14DM; Cytochrome P450-LIA1; Sterol 14-alpha demethylase; CYP51	ERG11	.	Candida tropicalis	5482	Candida tropicalis	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MAIVDTAIDGINYFLSLSLTQQITILVVFPFIYNIAWQLLYSLRKDRVPMVFYWIPWFGSAASYGMQPYEFFEKCRLKYGDVFSFMLLGKVMTVYLGPKGHEFIYNAKLSDVSAEEAYTHLTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKTYVPKIREEVLNYFVNDVSFKTKERDHGVASVMKTQPEITIFTASRCLFGDEMRKSFDRSFAQLYADLDKGFTPINFVFPNLPLPHYWRRDAAQRKISAHYMKEIKRRRESGDIDPKRDLIDSLLVNSTYKDGVKMTDQEIANLLIGVLMGGQHTSASTSAWFLLHLAEQPQLQDDLYEELTNLLKEKGGDLNDLTYEDLQKLPLVNNTIKETLRMHMPLHSIFRKVMNPLRVPNTKYVIPKGHYVLVSAGYAHTSDRWFEHPEHFNPRRWESDDTKASAVSFNSEDTVDYGFGKISKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILTTYIYNFKWRLNGDKVPDVDYQSMVTLPLEPAEIVWEKRDTCMV	.	"Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol."	.	.	CP51_CANTR	Reviewed	.	.	.	.	.	.
Mol00985	Protein	Lanosterol 14-alpha demethylase (ERG11)	LDM; Cytochrome P450 51; Cytochrome P450-14DM; Cytochrome P450-LIA1; CYPLI; Ergosterol biosynthesis protein 11; Sterol 14-alpha demethylase; CYP51; ERG16; CAALFM_C500660CA; CaO19.922	ERG11	3641571	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MAIVETVIDGINYFLSLSVTQQISILLGVPFVYNLVWQYLYSLRKDRAPLVFYWIPWFGSAASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVYLGPKGHEFVFNAKLSDVSAEDAYKHLTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKRYVPKIREEILNYFVTDESFKLKEKTHGVANVMKTQPEITIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPLPHYWRRDAAQKKISATYMKEIKSRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQEIANLLIGILMGGQHTSASTSAWFLLHLGEKPHLQDVIYQEVVELLKEKGGDLNDLTYEDLQKLPSVNNTIKETLRMHMPLHSIFRKVTNPLRIPETNYIVPKGHYVLVSPGYAHTSERYFDNPEDFDPTRWDTAAAKANSVSFNSSDEVDYGFGKVSKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILTTFVYNLRWTIDGYKVPDPDYSSMVVLPTEPAEIIWEKRETCMF	.	"Lanosterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway. The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol."	PDB: 5FSA; PDB: 5TZ1; PDB: 5V5Z	.	CP51_CANAL	Reviewed	.	.	.	.	.	.
Mol00986	Protein	Lanosterol 14-alpha demethylase (ERG11)	14-alpha-demethylase; B9J08_001448	ERG11	.	Candida auris	498019	Candida auris	.	.	Metschnikowiaceae	27319	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MALKDCIVDVVDRFSALPVPVKLAVLILVPIVYNLVWQFVYSLRKDRAPLVFHWVPWVGSAVVYGMQPYQFFESCREKYGDVFAFVMLGKVMTVYLGPKGHEFVLNAKLADVSAEAAYSHLTTPVFGKGVIYDCPNSRLMEQKKFAKTALTKEAFQRYVPRIQEEVLDYFKACSQFKMNERNNGVANVMKTQPEMTILTASKSLMGDDMRARFDASFAKLYSDLDKGFTPINFVFPHLPLPAYWKRDAAQQKISATYMSLINERRKTGDIVPDRDLIDSLMTNSTYKDGVKMTDQEVANLLIGVLMGGQHTSASTSAWFLLHLAEQPKLQEELYNEVLSVLAEKGGSLKDLAYDDLQKMPLINQTIKETLRLHMPLHSIFRKVMNPLVVPNTKYVVPKGHYVMVSPGYAQTNEKWFPRANEFDPHRWDEETSSNIDTDAVDYGFGKVTKGVSSPYLPFGGGRHRCIGEQFAYVQLGTILATYVYNIKWRFKKDGSLPPVDYQSMVTLPMEPAEIEWEKRETCVY	.	.	.	.	A0A2H1A309_CANAR	Unreviewed	.	.	.	.	.	.
Mol00987	Protein	Lincomycin resistance efflux pump (LMRS)	lmrS; GZ128_11505; GZ156_01550; HCU70_08510; HUW54_11080; Multidrug efflux MFS transporter LmrS	lmrS	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MAKVELTTRRRNFIVAVMLISAFVAILNQTLLNTALPSIMRELNINESTSQWLVTGFMLVNGVMIPLTAYLMDRIKTRPLYLAAMGTFLLGSIVAALAPNFGVLMLARVIQAMGAGVLMPLMQFTLFTLFSKEHRGFAMGLAGLVIQFAPAIGPTVTGLIIDQASWRVPFIIIVGIALVAFVFGLVSISSYNEVKYTKLDKRSVMYSTIGFGLMLYAFSSAGDLGFTSPIVIGALIISMVIIYLFIRRQFNITNALLNLRVFKNRTFALCTISSMIIMMSMVGPALLIPLYVQNSLSLSALLSGLVIMPGAIINGIMSVFTGKFYDKYGPRPLIYTGFTILTITTIMLCFLHTDTSYTYLIVVYAIRMFSVSLLMMPINTTGINSLRNEEISHGTAIMNFGRVMAGSLGTALMVTLMSFGAKIFLSTSPSHLTATEIKQQSIAIGVDISFAFVAVLVMAAYVIALFIREPKEIESNRRKF	.	.	.	.	F6MF49_STAAU	Unreviewed	.	.	.	.	.	.
Mol00988	Protein	Lincosamide nucleotidyltransferase (LNUG)	lnu(G); lnuG; EY666_09475; G)	lnu(G)	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MLKQKELMARVKELVQSDERISACMMYGSFTKGEGDQYSDIEYYVFLKDDTISTFDSAKWLNEVASYTLLYQNEYGTEVVIFENLIRGEFHFLSENEMNIIPSFKESGYIPDTKAMFIYDETGQLELYLSELEGPGPNRLTEENVNFLLNNFSNLWLMGINVLKRGENARSLELLSQLQKNILQLIRIAEENADNWFNMTKNLEKEISPENYEKFKKTTARLNELELYEAYKNSLLLVMELRNLVEKQYQLTISDDFLGKLFNYMNE	.	.	.	.	A0A1L7HA90_ENTFL	Unreviewed	.	.	.	.	.	.
Mol00989	Protein	L-lactate dehydrogenase B chain (LDHB)	LDH-B; LDH heart subunit; LDH-H; Renal carcinoma antigen NY-REN-46	LDHB	3945	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000350669.5, LDHB-201, 1303; ENST00000396076.5, LDHB-203, 1538; ENST00000673047.2, LDHB-211, 1303; ENST00000396075.5, LDHB-202, 744; ENST00000450584.5, LDHB-204, 732; ENST00000539782.1, LDHB-208, 487; ENST00000535112.1, LDHB-207, 252; ENST00000470280.1, LDHB-205, 710; ENST00000470985.3, LDHB-206, 678; ENST00000542765.4, LDHB-209, 672; ENST00000544151.1, LDHB-210, 544"	MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL	chr12:21635342-21757857[-]	.	PDB: 1I0Z; PDB: 1T2F; PDB: 7DBJ; PDB: 7DBK	HGNC:6541	LDHB_HUMAN	Reviewed	ENSG00000111716	.	.	.	.	.
Mol00990	Protein	Lon protease (LON)	ATP-dependent protease La; PA0779	lon	877837	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSDQDVNPEHISDAQPAGTGLVLPGQTLPTTLYVIPIHNRPFFPAQVLPVIVNEEPWAETLELVAKTDHHSLALFFMDNPPEDPRHFDVNSLPEHGTLVRVHHASREGGKLQFVAQGLSRVRIRGWIKRHRPPFMVEVDYPKTPIDPSDEVKAYGMALINAIKELLPLNPLYSEELKNYLNRFSPNDPSPLTDFAAALTTAPGGELQEVLDTVPILKRMEKVLPLLRKEVEVARLQKELSAEVNRKIGEHQREFFLKEQLKIIQQELGITKDDKSADADEFRARLEGKVLPEQARKRIDEELNKLSILESGSPEYAVTRNYLDWATALPWGVYGKDKLDLKHARKVLDKHHAGLDDIKDRILEFLAVGSFKGEIAGSIVLLVGPPGVGKTSIGKSIAESLGRPFYRFSVGGMRDEAEIKGHRRTYIGALPGKLVQALKEVEVMNPVIMLDEIDKLGASYQGDPASALLETLDPEQNVEFLDHYLDLRLDLSKVLFVCTANTLDSIPGPLLDRMEVIRLSGYISEEKLAIAKRHLWPKQLEKAGVPKGRLSISDAALRAVIEGYAREAGVRQLEKQLGKLVRKSVVKLLEDPESKVKIGPRDLEDYLGMPVFRSEQVLSGIGVITGLAWTSMGGATLPIEATRIHTLNRGFKLTGQLGDVMKESAEIAYSYIGSHLKKYGGDPTFFDQAFVHLHVPEGATPKDGPSAGVTMASALLSLARNQVPKKGVAMTGELTLTGQVLPIGGVREKVIAARRQKIFELILPEANRGHFEELPDYLREGLTVHFAKRYGDVAKVLFPA	.	"ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner."	.	.	Q9I5F9_PSEAE	Unreviewed	.	.	.	.	.	.
Mol00991	Protein	Macrolide 2'-phosphotransferase II (MPHB)	mphB; mph(B); BON70_03915; DAH50_23490; GF147_25890; GF147_27035; HVY77_26855; pO103_99; B) family macrolide 2'-phosphotransferase	mphB	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSKDIKQVIEIAKKHNLFLKEETIQFNESGLDFQAVFAQDNNGIDWVLRLPRREDVMPRTKVEKQALDLVNKYAISFQAPNWIIYTEELIAYKKLDGVPAGTIDHNIGNYIWEIDINNVPELFHKSLGRVLAELHSIPSNKAAALDLVVHTPEEARMSMKQRMDAVRAKFGVGENLWNRWQAWLNDDDMWPKKTGLIHGDVHAGHTMIDKDANVTGLIDWTEAKVTDVSHDFIFNYRAFGEEGLEALILAYKEIGGYYWPKMKEHIIELNAAYPVSIAEFALVSGIEEYEQMAKEALEVQGS	.	.	.	.	O32553_ECOLX	Unreviewed	.	.	.	.	.	.
Mol00992	Protein	Macrolide export ATP-binding/permease protein MacB (MACB)	STM0942	macB	1252461	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTALLELCNVSRSYPSGEEQVAVLKDISLQIHAGEMVAIVGVSGSGKSTLMNILGCLDKPTSGTYRVAGRDVSTLDPDALAQLRREHFGFIFQRYHLLSHLTAAQNVEIPAVYAGIERKKRQARARELLLRLGLSDRVDYPPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILRQLRDRGHTVIIVTHDPLIAAQAERIIEIHDGKIVHNPPAQEKKREQGVDAAVVNTAPGWRQFASSFREALSMAWLAMAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRAMGTNTIDIHPGKDFGDDNPQYRQALKYDDLVAIQKQPWVNSATPSVSKSLRLRYGNIDIAVNANGVSGDYFNVYGMSFREGNTFNAVQQQDRAQVVVLDANTRRQLFPNKANVVGEVVLAGNMPVIVIGVAEEKPSMYGNSNLLQVWLPYSTMSDRIMGQSWLNSITVRVKDGVDSDQAEQQLTRLLTLRHGKKDFFTWNMDSVLKTAEKTTYTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVLQQFLIEAVLVCLVGGALGISLSMFIAFMLQLFLPGWEIGFSLTALASAFLCSTFTGILFGWLPARNAARLDPVDALARE	.	"Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides."	.	.	MACB_SALTY	Reviewed	.	.	.	.	.	.
Mol00993	Protein	Macrolide-lincosamide-streptogramin B resistance protein (ERMA)	rRNA adenine N-6-methyltransferase	erm(A)	.	Streptococcus pyogenes	1314	Streptococcus pyogenes	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MKQKNPKNTQNFITSKKHVKEILKYTNINKQDKIIEIGSGKGHFTKELVEMSQRVNAIEIDEGLFM	.	.	.	.	B1PT65_STRPY	Unreviewed	.	.	.	.	.	.
Mol00994	Protein	Macrolide-lincosamide-streptogramin B resistance protein (ERMQ)	rRNA adenine N-6-methyltransferase	ermQ	.	Clostridium perfringens	1502	Clostridium perfringens	Clostridium	1485	Clostridiaceae	31979	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKAKSNNYRGKVDISVSQNFITSKNTIYKLIKKTNISKNDFVIEIGPGKGHITEALCEKSYWVTAIELDRSLYGNLINKFKSKNNVTLINKDFLNWKLPKKREYKVFSNIPFYITTKIIKKLLLEELNSPTDMWLVMEKGSAKRFMGIPRESKLSLLLKTKFDIKIVHYFNREDFHPMPSVDCVLVYFKRKYKYDISKDEWNEYTSFISKSINNLRDVFTKNQIHAVIKYLGINLNNISEVSYNDWIQLFRYKQKID	.	.	.	.	Q46194_CLOPF	Unreviewed	.	.	.	.	.	.
Mol00995	Protein	Major facilitator superfamily efflux pump (AMVA)	smvA; ABUW_1679; C6N18_11580; EA686_06090; F2P40_10035; NCTC13421_01570	amvA	.	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MQKKWLILTIIVLIYLPVTIDATVMHVATPSLSAALNLTANQLLWIIDIYSLIMAGLILPMGALGDRIGFKKLLFIGTAVFGVGSLAAAFSPTAYALIASRAILGLGAAMLIPATLSGIRNAFTEEKQRNFALGIWSTVGGGGAAFGPLVGGFVLEHFHWGAVFLINIPIILAVLVMIVMIIPKQQEKTDQPINLGQALVLVVAILSLIYSIKSAMYNFSVLTVVMFVVGISTLIHFIRSQKRATTPMIDLELFKHPVISTSIVMAVVSMIALVGFELLLSQELQFVHGFSPLQAAMFIIPFMIAISLGGPLAGICLNKWGLRRVSSLGILVSALSLWGLAQLNFSTDHFLAWTCMVFLGFSIEIALLASTAAIMSSVPPQKASAAGAIEGMAYELGAGLGVAIFGLMLSWFYSRSIILPAELPSNLIEKASISIGETMQLASNLENPLGGQLIVVAQQAFSYAHSWVLTLSAICFFLLTVFVWFSFPKKVN	.	.	.	.	C4PAW9_ACIBA	Unreviewed	.	.	.	.	.	.
Mol00996	Protein	Major facilitator superfamily MFS_1 (TETV)	tetV; NCTC7017_03777; Tetracycline-resistance determinant tetV	tetV	66736503	Mycolicibacterium smegmatis	1772	Mycolicibacterium smegmatis	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MRSPRPVAGWRVLAPFRIREYRLLIAAVTLSIFAEGMWSVVMALQVIAIDNDPASLSLVATCLGVGLVAFVLVGGITADRINQRTIIIAVEVVNFVTVAVISALALLGVLKIWHMAVAAGILGIAAAFFFPAYSAILPRILPPEQLLAANGVEGVVRPVFQRSVGPAVAGMVIGATMPSIGAVVVAVLFALGLALLVATRPPAQPASEHHERPHVLRDLREGFAFVLKTPWLLWTVLFASMFVLVVLGPIEVLLPFIAQDRFADGARAYGFILAFFGIGSAMGALTVSSRRMPRRYLTTMMLMWGLGSIPLVIVGYTSSFPLMAAATFVIGVTDGAGMVIWGTLLQRRVPTEMLGRVSSLDFFVSLAFMPLSFAIVGPLSKVVSMEVIFATAGLVPVAIAAVAFTAARMHRDEVANPLL	.	.	.	.	O31137_MYCSM	Unreviewed	.	.	.	.	.	.
Mol00997	Protein	Major facilitator superfamily multidrug transporter FLU1 (FLU1)	Fluconazole resistance protein 1; CAALFM_C701520WA; orf19.6577	FLU1	3637048	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MNNNTNSNHNDIAPEATITQNTTTSVSNDELQHITNNNNVNVQSYVGPTDSVESSSNTADEENEINSFNAQNVKDYEANVGGELPPDDELSRIESNTELSRRATRSIMNTESLLRTASQSSKPLPPMGGGKEYPPMLGSRDPYVVAFDGPDDPDHPHNYPTWKKILYCASVGLAALSVSMGSAMFSQASADIMQIYHIGWTPATLTTSLFVFGFASGPVIYGPLSELFGRKLVMVPSCLGYVCFSFAVATAKDIQTIMICRFFAGFIGAAPLVVAPAVMADMFNNRYRGTAIAIFSMLLFGGPMLAPILGAFTVKNSALGWRWTSYFCGIIGSLALFMNTFLLQETHHPLILTRRAEELRRRTGNWGIYAPHEELKLSMKEIVENNIARPLKMLFTEPILFLVSLYNAFIYGMLYLFLTAIPLIFLGEYHFVQGVAELPYLAMLIGILIGGGMIMLFEKRYIKAMEDNGGKIIPEKRLEPMMVGGFTFVIGIFWLGWTGNYPQHVHWIVPVIGAAFVGNGLMLIFLPCFNYIIDCYLLYAATALAGNTFIRSAFGAVFPLFARQMFTNLTIKWASTLLGCIGILLLPMPFVFYYYGKSLRHKSKFAFVLE	.	"Major facilitator superfamily transporter that mediates resistance to structurally and functionally unrelated compounds including cycloheximide but also azoles such as fuconazole, ketoconazole and itraconazole. Mediates also efflux of histatin 5, a salivary human antimicrobial peptide, and is responsible for reduction of its toxicity in C.albicans."	.	.	FLU1_CANAL	Reviewed	.	.	.	.	.	.
Mol00998	Protein	Microtubule-associated protein 1 light chain3 (LC3)	LC3	LC3	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol00999	Protein	MATE family efflux transporter (ABEM)	abeM; norM_1; norM_2; A7M90_01030; ABCAM1_0400; ABR2091_0395; APD31_09880; AUO97_09395; AYR68_01385; B7L45_17470; B9X95_14630; BS065_17005; CBE85_05175; CBL15_16565; H0529_14335; IMO23_01850; NCTC13305_02036; SAMEA104305281_01114; SAMEA104305385_01096; Multidrug ABC transporter; Multidrug efflux MATE transporter AbeM; Multidrug resistance protein norM	abeM	66398626	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSNVTSFRSELKQLFHLMLPILITQFAQAGFGLIDTIMAGHLSAADLAAIAVGVGLWIPVMLLFSGIMIATTPLVAEAKGARNTEQIPVIVRQSLWVAVILGVLAMLILQLMPFFLHVFGVPESLQPKASLFLHAIGLGMPAVTMYAALRGYSEALGHPRPVTVISLLALVVLIPLNMIFMYGLGPIPALGSAGCGFATSILQWLMLITLAGYIYKASAYRNTSIFSRFDKINLTWVKRILQLGLPIGLAVFFEVSIFSTGALVLSPLGEVFIAAHQVAISVTSVLFMIPLSLAIALTIRVGTYYGEKNWASMYQVQKIGLSTAVFFALLTMSFIALGREQIVSVYTQDINVVPVAMYLLWFAMAYQLMDALQVSAAGCLRGMQDTQAPMWITLMAYWVIAFPIGLYLARYTDWGVAGVWLGLIIGLSIACVLLLSRLYLNTKRLSQT	.	.	.	.	A0A077GDY5_ACIBA	Unreviewed	.	.	.	.	.	.
Mol01000	Protein	Melanoma antigen A 4 (MAGE4)	MAGEA4; MAGEA4); mRNA	MAGEA4	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MSSEQKSQHCKPEEGVEAQEEALGLVGAQAPTTEEQEAAVSSSSPLVPGTLEEVPAAESAGPPQSPQGASALPTTISFTCWRQPNEGSSSQEEEGPSTSPDAESLFREALSNKVDELAHFLLRKYRAKELVTKAEMLERVIKNYKRCFPVIFGKASESLKMIFGIDVKEVDPTSNTYTLVTCLGLSYDGLLGNNQIFPKTGLLIIVLGTIAMEGDSASEEEIWEELGVMGVYDGREHTVYGEPRKLLTQDWVQENYLEYRQVPGSNPARYEFLWGPRALAETSYVKVLEHVVRVNARVRIAYPSLREAALLEEEEGV	.	.	.	.	Q1RN33_HUMAN	Unreviewed	.	.	.	.	.	.
Mol01001	Protein	Metallo beta lactamase (TMB1)	tmb-1; Metallo beta lactamase	tmb-1	.	Achromobacter xylosoxidans	85698	Achromobacter xylosoxidans	Achromobacter	222	Alcaligenaceae	506	Burkholderiales	80840	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MRPFLFLIIFISHFAFANEEIPGLEVEEIDNGVFLHKSYSRVEGWGLVSSNGLVVISGGKAFIIDTPWSESDTEKLVDWIRSKKYELAGSISTHSHEDKTAGIKWLNGKSITTYASALTNEILKREGKEQARSSFKGNEFSLMDGFLEVYYPGGGHTIDNLVVWIPSSKILYGGCFIRSLESSGLGYTGEAKIDQWPQSARNTISKYPEAKIVVPGHGKIGDFELLKHTKVLAEKASNKANHGDR	.	.	.	.	E7BCS5_9BURK	Unreviewed	.	.	.	.	.	.
Mol01002	Protein	Metallo-beta-lactamase (VIM1)	blaVIM-1; VIM-1 metallo-beta-lactamase	blaVIM-1	.	Achromobacter denitrificans	32002	Achromobacter denitrificans	Achromobacter	222	Alcaligenaceae	506	Burkholderiales	80840	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MLKVISSLLVYMTASVMAVASPLAHSGEPSGEYPTVNEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHSTDNLVVYVPSANVLYGGCAVHELSSTSAGNVADADLAEWPTSVERIQKHYPEAEVVIPGHGLPGGLDLLQHTANVVKAHKNRSVAE	.	.	.	.	Q7AZX3_ACHDE	Unreviewed	.	.	.	.	.	.
Mol01003	Protein	Metallo-beta-lactamase NDM-4 (NDM4)	bla(NDM-4); blaNDM-4; NDM-4; NDM-4; New Delhi metallo-beta-lactamase NDM-4	bla(NDM-4)	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR	.	.	PDB: 4TYF	.	H6WZS9_ECOLX	Unreviewed	.	.	.	.	.	.
Mol01004	Protein	MFS transporter (MDFA)	A3104_18055; A3S30_18005; A3T81_15200; A3U32_21525; A3V03_19205; A3V89_12990; A3W57_19495; A3W75_19840; A3X15_14860; A3X55_19505; A3Y76_20265; A4N07_16795; A4O41_16990; A4R48_16600; AAA76_12510; AAB27_13255; AAB79_11400; AAC35_14255; ADQ28_14875; AF497_07025; AGM99_17835; AHN93_15130; AIT36_15280; AKH62_14175; AL144_13420; AL168_11085; AL184_11925; AU613_18600; AVA38_08035; AVC05_14530; AVL16_18180; AWT30_21215; AXX99_13680; B1265_19495; B1398_12790; B1642_17500; B1P38_13630; B4W90_17455; B6362_15590; B7Q27_19505; B8Z46_18640; BBQ66_21460; BG493_15280; BIC00_19060; BIC13_18810; BK110_19035; BKM50_16760; BMU56_12605; BZZ88_13630; CAC56_14945; CB102_16055; CB119_11535; CB198_19980; CB380_09515; CB535_10655; CB570_06995; CB646_19240; CBM67_15880; CBM76_14270; CBZ90_12605; CC339_15135; CC403_07660; CC652_18825; CC971_19495; CCP17_19640; CDZ72_18660; CED07_20050; CEQ70_21070; CHN22_16875; CIX60_19475; CPS79_09480; D4361_12475; D4387_13435; D4422_18590; D5823_14295; D5N86_12845; D5N95_13625; D5O82_13065; D5P17_11870; D5X47_13530; D5Y28_14105; D6422_14950; D6J79_15275; DD95_12970; DMI89_07745; DMO92_14025; DNM27_20805; DNZ37_19695; DO533_11300; DP680_13465; DPB42_13300; DPD91_11275; DPF68_11140; DPS76_12590; DQD22_14520; DQR44_13050; DRM14_14280; DRT38_19985; DRT61_06145; DRV05_12675; DSF94_11690; DTF68_13430; DU071_21095; DU223_06835; DU879_13460; DUV75_09950; DWU22_16940; DY580_15405; DYM27_19220; E0935_15585; E6W45_16765; EBD14_14485; EEQ30_18310; EHB09_15825; EL822_12005; ELS01_17965; EPB30_14515; EQG93_13725; EVY71_18140; EW905_07325; F0D96_11040; F2P00_17895; F3Q97_15265; F3R12_14645; F9G02_10205; FE758_22575; FEM52_14275; FJM64_10835; FQC24_19635; FQX78_19625; G0038_19525; G0040_15080; G0042_19665; G0045_19465; G0047_18575; G0048_19970; G0051_18980; G0052_18840; G0059_21300; G0061_17855; G0062_19710; G0067_19455; G0069_19560; G0070_18720; G0071_18550; G0072_14580; G0074_19450; G0076_19545; G0077_19485; G0080_19695; G0084_18875; G0086_18955; G0087_19930; G0088_19340; G0089_19335; G0090_16805; G0094_20445; G0100_19990; G0101_21845; G0102_20480; G0111_18345; G0113_21440; G0117_19650; G0123_20275; G0124_19850; G0148_19690; G0157_19350; G0170_19995; G0A05_21160; G0A28_14830; G0A50_17790; G0A52_15940; G0A53_22075; G0A56_11455; G0A58_22385; G0A61_17570; G0A63_16775; G0A66_21645; G0A68_17610; G0A79_15530; G0A85_18435; G0A92_14705; G0A96_15680; G0A99_02660; G0B08_18765; G0B96_23825; G0C03_21465; G0C34_16890; G0E15_22085; G0G84_09920; G0J43_13225; G0J50_13790; G0J53_18235; G0J58_18200; G0J59_15100; G0J65_16620; G0J66_12660; G0J67_17760; G0J69_17575; G0J71_15585; G0J73_15955; G0J76_16065; G0J79_17910; G0J81_16055; G0J85_18410; G0J89_14970; G0J92_13360; G0J94_14525; G0J96_15855; G0K02_16620; G0K04_08125; G0K05_15770; G0K07_17230; G0K10_21205; G0K13_18415; G0K16_16260; G0K18_12245; G0K19_08225; G0K20_09595; G0K25_15765; G0K26_16555; G0K28_17150; G0K30_17535; G0K31_14370; G0K32_06315; G0K33_20090; G0K37_15110; G0K38_16400; G0K39_14575; G0K41_09860; G0K42_16255; G0K44_14770; G0K46_18425; G0K48_14500; G0K49_14320; G0K52_16630; G0K53_16755; G0K56_05505; G0K58_09450; G0K59_16140; G0K61_12700; G0K65_19260; G0K68_15450; G0K70_16455; G0K72_18610; G0K74_05465; G0K75_15355; G0K78_18650; G0K80_12075; G0K83_18540; G0K84_16080; G0K85_13510; G0K88_000554; G0K89_000394; G0K90_000897; G0K94_000101; G0K95_000666; G0L00_001185; G0L02_000828; G0L25_13420; G0L29_11825; G0L35_09835; G0L40_06775; G0L42_04230; G0L51_20070; G0L52_12630; G0L55_16365; G0L59_21645; G0L62_22250; G0L63_21640; G0L65_21880; G0L67_12355; G0L68_14040; G0L70_12965; G0L73_14795; G0L76_18845; G0L77_11720; G0L79_17420; G0L83_12850; G0L86_003265; G0L88_15125; G0L93_15695; G0L96_16670; G0L98_15615; G0M00_16385; G0M02_12285; G0M06_002876; G0M10_07680; G0M13_003370; G0M18_000555; G0M21_11490; G0M22_003030; G0M25_003103; G0M29_003115; G0M30_10700; G0M33_08190; G0M35_14700; G0M36_13795; G0M46_003370; G0M48_002609; G0N45_16630; G0N48_17630; G0N53_16350; G0N55_20295; G0N58_18195; G0N59_18510; G0N60_17215; G0N61_17875; G0N62_18605; G0N64_18495; G0N65_18090; G0N66_17615; G0N67_17535; G0N75_18430; G0N78_19935; G0N82_18380; G0N84_21100; G0N85_18285; G0N86_18225; G0N88_19770; G0N89_19940; G0N90_18635; G0N92_09275; G0N94_10970; G0N95_16845; G0N98_24430; G0N99_17655; G0O00_16250; G0O03_09240; G0O10_18265; G0O14_18955; G0O15_16750; G0O18_10885; G0O19_20965; G0O20_16435; G0O22_20865; G0O25_15015; G0O27_19070; G0O31_18680; G0O32_15565; G0O36_07975; G0O37_16210; G0O39_18230; G0O40_20745; G0O41_18980; G0O42_16455; G0O43_20225; G0O44_12465; G0O47_18550; G0O52_19860; G0O55_17975; G0O57_15685; G0O58_17880; G0O60_17710; G0O66_16125; G0O68_18810; G0O70_19515; G0O71_19285; G0O74_18320; G0O75_18985; G0O77_18890; G0O78_20075; G0O80_17810; G0O81_18905; G0O82_19220; G0O84_18930; G0O85_18405; G0O86_14150; G0O87_18835; G0O88_11655; G0O89_21205; G0O92_18155; G0O93_18110; G0O94_16370; G0O97_12850; G0O99_14605; G0P01_16050; G0P02_15885; G0P05_15920; G0P06_18705; G0P08_16990; G0P13_19565; G0P17_19355; G0P18_18030; G0P24_19875; G0P26_19585; G0P28_20500; G0P30_18795; G0P31_18800; G0P36_10515; G0P37_17770; G0P41_16475; G0P44_17420; G0P45_12305; G0P48_20305; G0P49_13205; G0P52_19840; G0P53_13810; G0P56_19765; G0P57_19485; G0P58_18185; G0P63_19030; G0P67_14070; G0P68_16235; G0P69_19015; G0P75_15740; G0P76_18640; G1O10_18000; G1P03_16185; G1P15_15800; G1P29_16170; G1P37_16115; G1P52_16115; G1P53_16060; G1P61_18590; G1P78_15245; G1P83_15810; G2203_21030; G2218_17735; G2221_06400; G2279_17685; G2290_17340; G2793_12505; G2918_16485; G2951_17910; G3221_002953; G3230_003872; G3231_003911; G3247_003695; G3248_003961; G3263_003501; G3270_003625; G3275_003622; G3336_002927; G3357_003631; G3369_002783; G3433_004500; G3460_004241; G3464_003391; G3593_001586; G3A35_18955; G3V06_003557; G3V17_003295; G3V56_003777; G3V57_002865; G3X03_003407; G4190_003541; G4192_003581; G4198_003656; G4201_003758; G4202_004013; G4A01_004550; G4A73_003648; G4A83_001076; G4A85_004089; G4A87_003555; G4B74_004079; G4C74_002707; G4D32_001776; G4F88_08755; G4F89_15285; G4F91_14945; G4F92_09060; G4G47_004057; G4G62_001078; G4G68_002718; G4G75_002883; G4G79_003463; G4G97_003673; G4H00_003192; G4H04_001312; G4H07_003044; G4H08_002959; G4H18_002805; G4H21_003541; G4H24_002667; G4H63_004104; G4J07_004048; G4J08_003068; G4J12_004288; G4J18_003273; G4J20_002071; G4J37_003605; G4J39_003547; G4J41_004327; G4J45_004641; G4J90_003667; G4K02_003844; G4K03_003166; G4O59_003611; G4O60_004801; G4O67_003016; G4P29_003035; G4P83_003773; G4P85_003371; G4P89_002869; G4P91_003402; G4P93_004069; G4Q12_002276; G4Q28_003621; G4Q31_003490; G4Q59_002860; G4Q60_004330; G4Q63_003846; G4Q67_002729; G4Q94_003049; G4R01_003066; G4R02_003496; G4R15_003171; G4R16_003501; G4W68_001990; G4W73_003175; G4W86_003452; G4W87_003668; G4W88_003505; G4W91_003176; G9269_003953; G9302_002932; G9304_003772; G9309_003443; G9313_002218; G9314_004777; G9367_003434; G9381_003175; G9C24_002336; G9C41_003513; G9C46_003331; G9C47_003502; G9C49_003470; G9C57_001306; G9C64_003531; G9G34_001718; G9G36_002989; G9G45_002025; G9G50_001990; G9G62_004173; G9W19_003835; G9W28_003866; G9W45_002564; G9W63_002288; G9W65_003661; G9W79_002649; G9W95_003825; G9W96_003444; G9X40_003609; GB021_18140; GB055_15860; GB076_10715; GB106_14015; GB114_12650; GB120_20515; GB122_16975; GB131_14390; GB139_20345; GB171_19080; GB209_17400; GB221_14790; GB224_15855; GB280_19480; GB321_19270; GB331_11575; GB342_18155; GB368_16680; GB372_13925; GB452_17335; GB459_17945; GB505_15835; GB510_16440; GB551_20280; GB567_20705; GB645_15765; GBS44_18025; GBS58_20165; GBV53_11210; GBV54_18340; GBW03_15030; GBW52_18910; GBW76_16475; GBX12_18110; GBX46_13480; GBX64_16385; GBY13_16630; GBY73_20275; GBZ51_11030; GBZ55_17145; GEZ01_13955; GJE27_18590; GJE28_18980; GNA59_003731; GNA88_004036; GNA97_003462; GNA99_002977; GNB28_001519; GNB36_002740; GNB86_003523; GNB92_003479; GNC11_003597; GNC95_002547; GND07_002516; GT380_10040; GTH60_17840; GTH62_19930; GTH63_17760; GTH66_16220; GTH67_15595; GTH68_19825; GTH70_21815; GTH72_11435; GTH73_17470; GTH75_19605; GTH77_12175; GTH78_16070; GTH79_15685; GTH81_15200; GTH85_19200; GTH87_18785; GTH91_11590; GTH93_19690; GTH94_19500; GXC51_18545; GXC56_18455; GXG40_18280; GYI58_16855; GYI77_19555; GYJ04_18455; GYJ28_001787; GYJ30_17595; GYJ32_19560; KP44_18395; R035_10810; SE14_00958; SEL4126_29400; Z700_18945; ZV33_11865; ZX03_14395; ZY40_13470	mdfA	.	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MQNRLQSGGRLGRQALLFPLCLVLYEFSTYIGNDMIQPGMLAVVEQYQAGLDWVPTSMTAYLAGGMFLQWLLGPLSDRIGRRPVMLAGVVWFIVTCLATLLAKNIEQFTFLRFLQGISLCFIGAVGYAAIQESFEEAVCIKITALMANVALIAPLLGPLVGAAWVHVLPWEGMFILFAALAAIAFFGLQRAMPETATRRGETLSFKALGRDYRLVIKNRRFVAGALALGFVSLPLLAWIAQSPIIIISGEQLSSYEYGLLQVPVFGALIAGNLVLARLTSRRTVRSLIVMGGWPIVAGLIIAAAATVVSSHAYLWMTAGLSVYAFGIGLANAGLVRLTLFSSDMSKGTVSAAMGMLQMLIFTVGIEVSKHAWLSGGNGLFSLFNLANGILWLLLMLVFLKDKRTGNLQTV	.	.	.	.	A0A0F7DI73_SALTM	Unreviewed	.	.	.	.	.	.
Mol01005	Protein	MipA/OmpV family protein (MIPA)	mipA_1; mipA_2; mipA_3; yeaF; A5U30_001087; A6592_19280; A9819_10670; A9X72_11000; AAG43_000520; ABE90_019965; ACN68_30755; ACN81_10320; ACU57_21615; AM464_26860; APX88_07455; AT845_004658; AW119_12300; AWP93_05925; B6R12_000119; B6R15_000724; B6R31_000233; B6R48_000233; B6R87_000233; BANRA_00248; BANRA_02413; BANRA_02785; BEA19_00875; BF481_000201; BG944_000108; BGZ_01850; BGZ_04388; BHS81_10900; BJI68_17765; BJJ90_14135; BK292_17855; BK383_05390; BMC79_000208; BMT91_18675; BN17_20341; BO068_000018; BOH76_18525; BON63_18125; BON64_22695; BON65_17125; BON66_05905; BON67_18175; BON68_11835; BON70_09730; BON72_27325; BON73_24705; BON74_09895; BON75_13735; BON76_12715; BON77_00925; BON78_12405; BON79_02590; BON80_17505; BON81_01555; BON82_17640; BON83_03860; BON84_24135; BON86_05465; BON87_10815; BON88_03920; BON89_13755; BON90_23850; BON92_13405; BON93_06700; BON94_09770; BON97_12265; BON98_10820; BR158_000390; BTQ06_05315; BvCmsHHP019_05150; BvCmsHHP056_00783; BvCmsKKP036_02059; BvCmsKKP061_04318; BvCmsKSNP073_04520; BvCmsNSP072_02645; BVL39_18970; BXT93_26455; BZL69_19880; C2U48_25900; C3F40_01785; C5N07_01375; C5Y87_05760; C9114_21155; C9160_06050; CA593_19005; CCS08_13955; CCV12_001127; CDC27_09075; CDL36_03065; CDL37_01750; CG692_10065; CG831_002652; CIG67_17150; CO706_05910; CQP61_15935; CR538_11410; CR539_13625; CV83915_04606; CWS33_04795; CXJ73_001049; CY655_11640; D0X26_03230; D1912_31520; D3822_16970; D3C88_29230; D3Y67_22495; D4U49_20170; D9D43_13130; D9D77_22010; D9E34_10800; D9E49_08925; D9J03_05965; DAH17_07560; DAH18_10360; DAH19_08855; DAH20_04095; DAH21_07505; DAH22_12500; DAH27_01220; DAH28_01210; DAH29_00080; DAH30_07025; DAH31_01035; DAH32_01135; DAH33_04575; DAH34_16310; DAH35_04805; DAH36_19115; DAH37_24700; DAH38_17595; DAH40_08950; DAH41_20760; DAH50_23660; DD762_04530; DEN88_11730; DEN89_00890; DEN90_03755; DEN91_17655; DEN92_16575; DEN93_23480; DEN94_04560; DEN95_04520; DEN96_20770; DEN97_21495; DEN98_21765; DEN99_20435; DEO00_21620; DEO01_07425; DEO02_06260; DEO03_18890; DEO12_03005; DEO13_22720; DEO14_17790; DEO15_23745; DEO17_04080; DEO18_07100; DEO19_20950; DEO20_15390; DIV22_02445; DKP82_08850; DM870_14120; DN627_08305; DNQ45_10645; DNX30_01015; DS732_14650; DTL43_17030; DTL90_13380; DTM45_01380; DU321_20785; DXT70_10330; DXT71_10240; DXT73_03825; E0I42_10385; E2112_21315; E2113_12135; E2114_02795; E2115_01280; E2116_00405; E2117_01915; E2118_09800; E2119_18115; E2120_00405; E2121_05085; E2122_02585; E2123_01280; E2124_00405; E2125_00410; E2127_17410; E2128_16240; E2129_01565; E2130_00405; E2131_22975; E2132_17510; E2133_07780; E2134_06170; E2135_23210; E2136_09150; E4K51_20550; E4T14_20665; E5M02_18790; E5P23_21885; E5P24_15030; E5P25_06535; E5P26_00270; E5P27_10215; E5P28_09830; E5P29_01440; E5P30_01535; E5P31_01075; E5P32_07755; E5P33_16540; E5P34_00455; E5P35_16660; E5P36_07830; E5P37_03840; E5P39_04740; E5P40_09010; E5P41_19785; E5P42_10050; E5P43_12600; E5P44_07170; E5P45_06465; E5P46_10550; E5P47_03870; E5P48_14915; E5P49_15255; E5P50_05070; E5P51_13535; E5P52_15985; E5S35_02185; E5S36_01405; E5S38_04890; E5S39_02855; E5S42_05035; E5S43_04650; E5S44_06300; E5S45_12235; E5S46_05700; E5S47_09260; E5S48_20785; E5S51_04835; E5S52_08340; E5S53_18095; E5S55_18050; E5S56_07435; E5S57_03130; E5S58_15820; E5S59_07760; E5S61_03300; E5S62_02555; EA239_04225; EA435_04855; EAI46_10775; EAN77_01895; EAX79_00500; EBP16_08855; EC1094V2_1964; EC3234A_34c00210; EC95NR1_00683; ECs2491; ED648_14425; EHD79_01390; EHH55_08210; EI021_02395; EIZ93_02525; EKI52_27530; EL79_1912; EL80_1940; ELT16_00395; ELT17_11725; ELT20_00680; ELT21_16320; ELT22_01055; ELT24_13955; ELT25_01390; ELT26_11155; ELT27_01960; ELT28_00405; ELT29_01145; ELT30_05295; ELT32_05345; ELT34_05275; ELT35_03060; ELT36_05180; ELT39_02155; ELT40_01420; ELT41_00205; ELT44_08970; ELT45_01865; ELT46_07605; ELT48_10215; ELT49_11110; ELT51_03250; ELT54_02550; ELT55_12615; ELT58_10860; ELT59_05945; ELT60_04415; ELT61_05525; ELT63_13305; ELT72_01705; ELU07_10225; ELU82_08805; ELU83_05645; ELU85_03750; ELU88_03450; ELU89_06625; ELU90_11950; ELU91_07965; ELU94_01225; ELU96_08980; ELU97_03920; ELU98_06740; ELU99_01170; ELV00_06275; ELV01_04475; ELV02_02865; ELV03_03405; ELV04_02295; ELV07_05155; ELV08_22915; ELV09_07175; ELV11_11190; ELV12_04140; ELV13_11495; ELV15_07405; ELV20_21155; ELV21_00265; ELV22_13320; ELV23_06795; ELV24_02430; ELV26_01405; ELV28_00495; ELV29_12935; ELV40_15430; ELX48_02330; ELX56_10545; ELX61_04860; ELX66_00810; ELX68_19715; ELX69_00270; ELX70_00395; ELX76_02960; ELX79_11870; ELX83_09060; ELX85_12885; ELX96_10290; ELY02_04610; ELY05_11780; ELY23_02700; ELY24_09835; ELY31_17470; ELY32_03450; ELY36_02750; ELY39_12015; ELY41_20605; ELY48_20330; ELY50_01015; EPS76_02565; ERS085406_02775; ERS139208_01473; EVY14_10430; ExPECSC038_01753; EXX13_10875; EYV17_15025; EYV18_17220; EYY21_12545; F0L67_07650; F3N40_10230; F9B07_11780; F9S76_09035; F9S83_08110; F9V24_14235; F9X20_18375; FDM60_15565; FFF58_01930; FGG80_00885; FJQ51_02060; FOI11_004140; FOI11_15905; FQ007_03560; FQF29_19030; FV293_05490; FVB16_09965; G3565_11945; G3813_000283; G4A38_01055; G5632_20760; G9448_01750; GAJ26_03765; GF147_00790; GFY34_02530; GIB53_19600; GJ11_12285; GKF86_06995; GKF89_04675; GKG12_15995; GNO40_00255; GNZ05_10870; GP650_05650; GP662_11670; GP711_12185; GP946_06540; GP954_08545; GQA06_15410; GQE64_05925; GQM04_05750; GQM13_04660; GQW07_06150; GQW68_03295; GRC73_09935; GRO95_04335; GRW05_22845; GRW81_12545; GSY44_08620; GUB08_07250; GUB92_03005; GUC01_03955; GUI33_14005; H0O72_06675; H6Y26_000340; HIE29_000876; HJQ60_004801; HJS37_000399; HJU54_003159; HKA49_000193; HL563_01180; HLV18_03785; HLZ50_03035; HmCms169_02729; HMU48_00925; HNC36_15455; HNC59_03960; HNC66_03480; HNC99_00395; HV109_10045; HV209_08430; HVV39_26355; HVW19_04095; HVW43_02080; HVX16_10955; HVY77_11510; HVZ71_10880; HX136_14110; I6H02_02355; IA00_002138; IAI11_20995; IFB95_001680; IH768_04980; IH772_05395; IT029_000050; J0541_000433; J5U05_000369; JE86ST02C_21670; JE86ST05C_22620; JFD_03966; JNP96_15500; NCTC10082_04742; NCTC10429_03374; NCTC10764_01742; NCTC10958_02403; NCTC10974_02532; NCTC11112_06110; NCTC11126_04677; NCTC11181_05270; NCTC11341_05830; NCTC13216_04479; NCTC7922_02489; NCTC7928_06355; NCTC8008_01671; NCTC8179_03916; NCTC8333_02706; NCTC8450_02594; NCTC8500_02483; NCTC8622_04882; NCTC8960_05001; NCTC8985_00802; NCTC9036_02341; NCTC9037_02382; NCTC9044_04949; NCTC9045_02650; NCTC9073_05799; NCTC9111_02336; NCTC9117_02870; NCTC9706_04050; NCTC9775_01021; NCTC9777_04437; ND22_000191; PGD_01451; RG28_13160; SAMEA3472044_01276; SAMEA3472056_01450; SAMEA3472067_01703; SAMEA3472080_04939; SAMEA3472147_03511; SAMEA3751407_03241; SAMEA3752557_04195; SAMEA3753106_04897; TUM18780_19170; WP2S18E08_21310; WP4S18E07_20330; WR15_13500	mipA	58391373	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTKLKLLALGVLIATSAGVAHAEGKFSLGAGVGVVEHPYKDYDTDVYPVPVINYEGDNFWFRGLGGGYYLWNDATDKLSITAYWSPLYFKAKDSGDHQMRHLDDRKSTMMAGLSYAHFTQYGYLRTTLAGDTLDNSNGIVWDMAWLYRYTNGGLTVTPGIGVQWNSENQNEYYYGVSRKESARSGLRGYNPNDSWSPYLELSASYNFLGDWSVYGTARYTRLSDEVTDSPMVDKSWTGLISTGITYKF	.	.	.	.	C3T6U7_ECOLX	Unreviewed	.	.	.	.	.	.
Mol01006	Protein	Mitochondrial protoheme IX farnesyltransferase (COX10)	Heme O synthase; AFUA_4G08340	cox10	3509179	Aspergillus fumigatus	746128	Aspergillus fumigatus	Aspergillus	5052	Aspergillaceae	1131492	Eurotiales	5042	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MIYLRSSLLRSGLARDPARLCSQCFSRLSPSRRPVAVRSFFSSSRLRAGIADHESTPSTVQKTYFSANRTADGLLASLSAVNSSPRSIADNALSQGAASSESITSQSTSQELPHRRRKRLKEEAAKNNAAETELPPDASSQLSTLSSALPATSLRRKLAAFLALTKPRLSFLIVLTTTSAYGMYPISSLLTLDPSMTPLPTLSTSTLTFLYLTTGTFLSSCSANTLNMLLEPKYDALMSRTRNRPLVRGLLSRRAAVLFAIATAAAGLGLLYIGTNPTTTALSASNICLYAFVYTPLKRISVINTWVGAVVGGIPPLMGWTAAAGQTATTGHDSWRDMLFSKDSIGGWLLGGILFAWQFPHFNALSYMIREEYKAAGYRMLAWTNPAANARVALRYSLLMFPFSVGLWWVGVVGNGFLVGSTAANGWLVKEAYKFWRHQGANGSARRLFWASIWQLPILLVGGLVTKKGLWDGVWNNVFGQPVEDEDDYLWEDEDEVAEAERKMIPAKTSSS	.	Converts protoheme IX and farnesyl diphosphate to heme O.	.	.	COX10_ASPFU	Reviewed	.	.	.	.	.	.
Mol01007	Protein	MsrC (MSRC)	msrC; Fragment	msrC	.	Enterococcus faecium	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	FWHQLELSIDSLRVYQQDRIGIIGENGVGKSTLLKLIAGELFPDHGKIQTEITFNYLPQLTYLAEAKDLNLELASHFQLRLEETSERKWSGGEERKIELIRLLSSYEQGMLLDEPTTHLDRKSIDRLIEELRYYYGTLVFVSHDRYFLDELATKIWEVKDGEIREFSGNYSAYLTQKELEKKTQLREAESIMKEKKRLEKSIQEKKKQAEKLEKVSSKKKKQQIRPDRLSSSKQKDSVQKAIQKNAKTLERKLQKIGETTKPQQMKQIRFPVPKSLELHSRYPIMGQNVQLERSGRTLLVNGDFQFSLGKKIAIVGENGSGKTTLLEHIRKQGEGILLSPKVSFQVYQQKDYQMTSEESVIRFVMRQTEFSESLVRSLLNHLGFAQETLAKPLCTLSGGEATRLTIALLFTKPSNVLLLDEPTNFIDMATIEALEKLMQIYPGTILFTSHDSYFVERTADEV	.	.	.	.	A0A0H3XSR7_ENTFC	Unreviewed	.	.	.	.	.	.
Mol01008	Protein	Multidrug efflux pump Tap (TAP)	Tetracycline/aminoglycoside resistance-like efflux pump; Rv1258c; MTCY50.24	tap	887056	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MRNSNRGPAFLILFATLMAAAGDGVSIVAFPWLVLQREGSAGQASIVASATMLPLLFATLVAGTAVDYFGRRRVSMVADALSGAAVAGVPLVAWGYGGDAVNVLVLAVLAALAAAFGPAGMTARDSMLPEAAARAGWSLDRINGAYEAILNLAFIVGPAIGGLMIATVGGITTMWITATAFGLSILAIAALQLEGAGKPHHTSRPQGLVSGIAEGLRFVWNLRVLRTLGMIDLTVTALYLPMESVLFPKYFTDHQQPVQLGWALMAIAGGGLVGALGYAVLAIRVPRRVTMSTAVLTLGLASMVIAFLPPLPVIMVLCAVVGLVYGPIQPIYNYVIQTRAAQHLRGRVVGVMTSLAYAAGPLGLLLAGPLTDAAGLHATFLALALPIVCTGLVAIRLPALRELDLAPQADIDRPVGSAQ	.	"Efflux pump that contributes to intrinsic antibiotic resistance. The pump uses the electrochemical gradient as a source of energy. Confers resistance to rifampicin. Confers low-level resistance to tetracycline and to several aminoglycosides, including streptomycin, gentamicin, 2'-N-ethylnetilmicin and 6'-N-ethylnetilmicin."	.	.	TAP_MYCTU	Reviewed	.	.	.	.	.	.
Mol01009	Protein	Multidrug efflux pump Tap (TAP)	Tetracycline-aminoglycoside resistance protein	tap	.	Mycobacterium fortuitum	1766	Mycolicibacterium fortuitum	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTNTKRGPLLLILFAALTAGAGNGITIVAFPWLVLQHNGSALDASIVAMAGTLPLLVATLIAGAAVDYLGRRRVSMISDLLSALSVAAVPVLALIFGVDAVNVAVLAVLAGLGAFFDPAGMTARETMLPEAAGRAGWTLDHANSVYEAVFNLGYIVGPGIGGLMIATLGGINTMWVTAGAFCCSILAISVLRLEGAGAPDRSVLTEAVLAGIVEGLRFVWYTPVLRTLAIVDLVATGLYMPMESVLFPKYFTDRNEPTELGWVLMALSIGGLLGALGYAVMSRYMSRRATMLTAVITLGVAMTVIAFLPPLPLILVLCAIVGFVYGPIAPIYNYVMQTTAPQHLRGRVVGVMGSLAYAAGPLGLILAGPLADAAGLHATFLALSLPMLLLGVVAVFLPRLRELDLASKP	.	"Efflux pump that contributes to intrinsic antibiotic resistance. The pump uses the electrochemical gradient as a source of energy. Confers low-level resistance to tetracycline and to several aminoglycosides, including streptomycin, gentamicin, 2'-N-ethylnetilmicin and 6'-N-ethylnetilmicin."	.	.	TAP_MYCFO	Reviewed	.	.	.	.	.	.
Mol01010	Protein	Multidrug efflux SMR transporter (ABES)	abeS; emrE_2; A7M90_04670; CBE85_00325; CSB70_2397; FJU36_01990; G3N53_09785; ITE13_14185; NCTC13305_03610; Multidrug efflux SMR transporter AbeS; QacE family quaternary ammonium compound efflux SMR transporter; QacEdelta1 SMR family efflux pump; Small Multidrug Resistance family protein; Transporter	abeS	66396571	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSYLYLAIAIACEVIATSALKASQGFTIPIPSIITVVGYAVAFYLLSLTLKTIPIGIAYAIWSGAGIILISAIGWIFYKQHLDLAACIGLALMIAGIVIINVFSKNTHL	.	.	.	.	A0A090B1X4_ACIBA	Unreviewed	.	.	.	.	.	.
Mol01011	Protein	Multidrug resistance protein 1 (ABCB1)	Benomyl resistance protein 1; BEN; BMR1; CAALFM_C603170CA; CaO19.13047; CaO19.5604	MDR1	3639260	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MHYRFLRDSFVGRVTYHLSKHKYFAHPEEAKDYIVPEKYLADYKPTLADDTSINFEKEEIDNQGEPNSSQSSSSNNTIVDNNNNNDNDVDGDKIVVTWDGDDDPENPQNWPTLQKAFFIFQISFLTTSVYMGSAVYTPGIEELMHDFGIGRVVATLPLTLFVIGYGVGPLVFSPMSENAIFGRTSIYIITLFLFVILQIPTALVNNIAGLCILRFLGGFFASPCLATGGASVADVVKFWNLPVGLAAWSLGAVCGPSFGPFFGSILTVKASWRWTFWFMCIISGFSFVMLCFTLPETFGKTLLYRKAKRLRAITGNDRITSEGEVENSKMTSHELIIDTLWRPLEITVMEPVVLLINIYIAMVYSILYLFFEVFPIYFVGVKHFTLVELGTTYMSIVIGIVIAAFIYIPVIRQKFTKPILRQEQVFPEVFIPIAIVGGILLTSGLFIFGWSANRTTHWVGPLFGAATTASGAFLIFQTLFNFMGASFKPHYIASVFASNDLFRSVIASVFPLFGAPLFDNLATPEYPVAWGSSVLGFITLVMIAIPVLFYLNGPKLRARSKYAN	.	"Plasma membrane multidrug efflux pump that confers resistance to numerous chemicals including azoles such as fluconazole, voriconazole, and benztriazoles, as well as to benomyl, cycloheximide, methotrexate, 4-nitroquinoline-N-oxide, sulfometuron methyl, cerulenin, and brefeldin A."	.	.	MDR1_CANAL	Reviewed	.	.	.	.	.	.
Mol01012	Protein	Multidrug resistance protein 1 (ABCB1)	Chloroquine resistance protein	MDR1	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MGKEQKEKKDGNLSIKEEVEKELNKKSTAELFRKIKNEKISFFLPFKCLPAQHRKLLFISFVCAVLSGGTLPFFISVFGVILKNMNLGDDINPIILSLVSIGLVQFILSMISSYCMDVITSKILKTLKLEYLRSVFYQDGQFHDNNPGSKLRSDLDFYLEQVSSGIGTKFITIFTYASSFLGLYIWSLIKNARLTLCITCVFPLIYVCGVICNKKVKLNKKTSLLYNNNTMSIIEEALMGIRTVASYCGEKTILNKFNLSETFYSKYILKANFVEALHIGLINGLILVSYAFGFWYGTRIIINSATNQYPNNDFNGASVISILLGVLISMFMLTIILPNITEYMKALEATNSLYEIINRKPLVENNDDGETLPNIKKIEFKNVRFHYDTRKDVEIYKDLSFTLKEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIVNDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEAMENYYEENTNDTYENKNFSLISNSMTSNELLEMKKEYQTIKDSDVVDVSKKVLIHDFVSSLPDKYDTLVGSNASKLSGGQKQRISIARAIMRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRERSDNNNNNNNDDNNNNNNNNNNKINNEGSYIIEQGTHDSLMKNKNGIYHLMINNQKISSNKSSNNGNDNGSDNKSSAYKDSDTGNDADNMNSLSIHENENISNNRNCKNTAENEKEEKVPFFKRMFRRKKKAPNNLRIIYKEIFSYKKDVTIIFFSILVAGGLYPVFALLYARYVSTLFDFANLEYNSNKYSIYILLIAIAMFISETLKNYYNNKIGEKVEKTMKRRLFENILYQEMSFFDQDKNTPGVLSAHINRDVHLLKTGLVNNIVIFSHFIMLFLVSMVMSFYFCPIVAAVLTFIYFINMRVFAVRARLTKSKEIEKKENMSSGVFAFSSDDEMFKDPSFLIQEAFYNMHTVINYGLEDYFCNLIEKAIDYKNKGQKRRIIVNAALWGFSQSAQLFINSFAYWFGSFLIKRGTILVDDFMKSLFTFIFTGSYAGKLMSLKGDSENAKLSFEKYYPLMIRKSNIDVRDDGGIRINKNLIKGKVDIKDVNFRYISRPNVPIYKNLSFTCDSKKTTAIVGETGSGKSTFMNLLLRFYDLKNDHIILKNDMTNFQDYQNNNNNSLVLKNVNEFSNQSGSAEDYTVFNNNGEILLDDINICDYNLRDLRNLFSIVSQEPMLFNMSIYENIKFGREDATLEDVKRVSKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRNGTFVQSHGTHDELLSAQDGIYKKYVKLAK	.	Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.	.	.	MDR_PLAFF	Reviewed	.	.	.	.	.	.
Mol01013	Protein	Multidrug resistance protein 1 (ABCB1)	MDR1; Multidrug resistant protein 1; Fragment	MDR1	.	Plasmodium vivax	5855	Plasmodium vivax	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	DEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPSSHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRKNYETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRENGSTVDVDVLGEDPTKDSNEKNEKHDKQEKGGKNSSANQKIGNAGSYIIEQGTHDALMKNKNGIYYTMINNQKVSSKSSSNNDNDKDSDMKSSIYKDSERGYDPDEANGNAKNESASAKKSEKMSDAKASNTNAGGRLAFLRNLFKRKPKAPNNLRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALFYAKYVGTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENILYQEISFFDQDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRARIAANKDVEKKRVNQPGTAFVYNSDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQLFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERYYPLITRKSLIDVRDNGGIKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEQTGESSKEQMQQGDEEQNVGMKNANEFSSSKEGADGQSSTLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSFVQAQ	.	.	.	.	A0A1V0PL80_PLAVI	Unreviewed	.	.	.	.	.	.
Mol01014	Protein	Multidrug resistance protein 1 (ABCB1)	ABCB1; Fragment	ABCB1	.	Sus scrofa	9823	Sus scrofa	Sus	9822	Suidae	9821	Artiodactyla	91561	Mammalia	40674	Chordata	7711	Metazoa	33208	.	GQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSNEYTIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDSKPSIDSYSKNGHKPDNIKGNLEFRNVHFSYPSRNEVKILKGLNLKVESGQTVALVGNSGCGKSTTVQLMQRLYDPTEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMEEIEKAVKEANAYDFIMKLPNKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKAREGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGSHDELMKEKGVYFKLVTMQTKGNEIELENTVGVSKGVVDALDMSPKDLESSLIRRGSTRKSIKGPQGQDRKLSTKEGLDENVPPVSFWRILKLNITEWPYFVVGIFCAIINGGLQPAFSIIFSRIIGVFTKVTDPETKRQDSNIFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEAIENFRTVVSLTREEKFESMYDQSLQVPYSNSLRKAHIFGITFSITQAMMYFSYAACFRFGAYLVQHGHMDFQDVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHVIMIIEKTPQIDSYSTVGLKPNTVEGNLTFNEVMFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLIDGREIKELNVQWLRAHMGIVSQEPILFDCSIAENIAYGDNSRVVSQEEIVQAAKEANIHPFIETLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRRPRILLLDEATSALDTESEKVVQEALDKAR	.	.	.	.	Q5MIZ9_PIG	Unreviewed	.	.	.	.	.	.
Mol01015	Protein	Multidrug resistance protein CDR2 (CDR2)	CAALFM_C304890WA; CaO19.13379; CaO19.5958	CDR2	3635265	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSTANTSLSQQLDEKPWVDASDNSSVQEYQGFDATASHNIQDLARKLTHGSTNGDHHSANDLARYLSHMSDIPGVSPFNGNISHEQLDPDSENFNAKYWVKNLKKLFESDSDYYKPSKLGVAYRNLRAYGIANDSDYQPTVTNALWKFTTEAINKLKKPDDSKYFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSVGDTLEFAARLRTPQNRGEGIDRETYAKHMASVYMATYGLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKTSATILDTTPLIAIYQCSQDAYELFDNVVVLYEGYQIFFGKASKAKEYFENMGWKCPQRQTTADFLTSLTNPAEREPLPGYEDKVPRTAQEFETFWKNSPEYAELTKEIDEYFVECERSNTGETYRESHVAKQSNNTRPSSPYTVSFFMQVRYVIARNFLRMKGDPSIPLISILSQLVMGLILASVFFNLRKSTDTFYFRGGALFFSVLFNAFSSLLEILSLYEARPIVEKHRKYALYRPSADALASIISELPVKLLMTMSFNIVYYFMVNLRRTAGNFFFYWLMCASCTLVMSHMFRSIGAVTTTIATAMSLSTVFLLAMIIYAGFVLPIPYILGWSRWIRYINPVTYIFESLMVNEFHGREFECGQYIPSGPGFENLPVENKVCTTVGSTPGSTVVQGTEYIKLAYQFYSSHKWRNFGITVAFAVFFLGVYVALTEFNKGAMQKGEIVLFLKGSLKKHKRKTAASNKGDIEAGPVAGKLDYQDEAEAVNNEKFTEKGSTGSVDFPENREIFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDKLLFLQKGGRTAYFGELGENCQTMINYFEKYGADPCPKEANPAEWMLQVVGAAPGSHAKQDYFEVWRNSSEYQAVREEINRMEAELSKLPRDNDPEALLKYAAPLWKQYLLVSWRTIVQDWRSPGYIYSKLILVISSSLFIGFSFFKSKNNLQGLQSQMLAVFMFFVPFTTFIDQMLPYFVKHRAVYEVREAPSRTFSWFAFIAGQITSEIPFQIVVGTISYFCWYYPVGLYANAEPTDSVNSRGVLMWMLLTAFYVYTSTMGQLAISLNELIDNAANLATTLFTLCLMFCGVLAGPNVIPGFWIFMYRCNPFTYLIQAILSTGLANAKVTCAPRELVTLKPPMGETCSSFIGPYTEAAGGYFSTNSDGTCSVCRIDSTNQFLESINALFSQRWRNFGIFVAFIGINIILTIFFYWLARVPKGNREKKMKK	.	"Multidrug efflux transporter. Confers resistance to azole antifungal agents, to other antifungals (terbinafine, amorolfine) and to a variety of metabolic inhibitors."	.	.	CDR2_CANAL	Reviewed	.	.	.	.	.	.
Mol01016	Protein	Multidrug resistance protein MdtK (MDTK)	Multidrug-efflux transporter; norM; STM1425	mdtK	1252943	Salmonella enterica serovar Typhimurium	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MQKYTSEARQLLALRIPVILAQVAQTAMGFVDTVMAGGYSATDMAAVAIGTSIWLPAILFGHGLLLALTPVIAQLNGSGRRERIAHQVRQGFWLAGFVSVLVMIVLWNAGYIIRSMHNIDPALADKAVGYLRALLWGAPGYLFFQVARNQCEGLAKTKPGMVMGFLGLLVNIPVNYIFIYGHFGMPELGGIGCGVATAAVYWVMFIAMLSYIKHARSMRDIRNEKGFGKPDSVVMKRLIQLGLPIALALFFEVTLFAVVALLVSPLGIVDVAGHQIALNFSSLMFVLPMSLAAAVTIRVGYRLGQGSTLDAQTAARTGLGVGICMAVVTAIFTVTLRKHIALLYNDNPEVVALAAQLMLLAAVYQISDSIQVIGSGILRGYKDTRSIFFITFTAYWVLGLPSGYILALTDLVVDRMGPAGFWMGFIIGLTSAAVLMMLRMRYLQRQPSAIILQRAAR	.	Multidrug efflux pump that functions probably as a Na(+)/drug antiporter.	.	.	MDTK_SALTY	Reviewed	.	.	.	.	.	.
Mol01017	Protein	Multidrug resistance protein PmpM (PMPM)	H(+)/drug antiporter; Multidrug-efflux transporter; norM; PA1361	pmpM	880959	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNSPALPLSRGLRIRAELKELLTLAAPIMIAQLATTAMGFVDAVMAGRASPHDLAAVALGNSIWIPMFLLMTGTLLATTAKVAQRHGAGDQPGTGPLVRQALWLALLIGPLSGAVLWWLSEPILGLMKVRPELIGPSLLYLKGIALGFPAAALYHVLRCYTNGLGRTRPSMVLGIGGLLLNIPINYALIYGHFGMPKMGGPGCGWATGSVMWFMFLGMLFWVNKASIYRASQLFSRWEWPDRATIGPLVAVGLPIGIAVFAESSIFSVIALLIGGLDENVVAGHQIALNFSALVFMIPYSLGMAVTVRVGHNLGAGLPRDARFAAGVGMAAALGYACVSASLMLLLREQIAAMYSPDPAVIAIAASLIVFSALFQFSDALQVTAAGALRGYQDTRVTMIMTLFAYWGIGLPVGYSLGLTDWFQEPTGPRGLWQGLVVGLTGAAIMLCIRLARSARRFIRQHERLQREDAEAASVLGR	.	"Multidrug efflux pump that functions as an H(+)/drug antiporter. Confers resistance to benzalkonium chloride, fluoroquinolones, ethidium bromide, acriflavine and tetraphenylphosphonium chloride."	.	.	PMPM_PSEAE	Reviewed	.	.	.	.	.	.
Mol01018	Protein	Multidrug transporter MdfA (MDFA)	Chloramphenicol resistance pump Cmr; cmlA; cmr; b0842; JW0826	mdfA	945448	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MQNKLASGARLGRQALLFPLCLVLYEFSTYIGNDMIQPGMLAVVEQYQAGIDWVPTSMTAYLAGGMFLQWLLGPLSDRIGRRPVMLAGVVWFIVTCLAILLAQNIEQFTLLRFLQGISLCFIGAVGYAAIQESFEEAVCIKITALMANVALIAPLLGPLVGAAWIHVLPWEGMFVLFAALAAISFFGLQRAMPETATRIGEKLSLKELGRDYKLVLKNGRFVAGALALGFVSLPLLAWIAQSPIIIITGEQLSSYEYGLLQVPIFGALIAGNLLLARLTSRRTVRSLIIMGGWPIMIGLLVAAAATVISSHAYLWMTAGLSIYAFGIGLANAGLVRLTLFASDMSKGTVSAAMGMLQMLIFTVGIEISKHAWLNGGNGLFNLFNLVNGILWLSLMVIFLKDKQMGNSHEG	.	"Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D-thiogalactopyranoside (IPTG) exclusion and spectinomycin sensitivity. Transport of neutral substrates is electrogenic, whereas transport of cationic substrates is electroneutral. In addition to its role in multidrug resistance, confers extreme alkaline pH resistance, allowing the growth under conditions that are close to those used normally by alkaliphiles. This activity requires Na(+) or K(+)."	PDB: 4ZOW; PDB: 4ZP0; PDB: 4ZP2; PDB: 6EUQ; PDB: 6GV1; PDB: 6OOM; PDB: 6OOP; PDB: 6OOQ; PDB: 6VRZ; PDB: 6VS0; PDB: 6VS1; PDB: 6VS2	.	MDFA_ECOLI	Reviewed	.	.	.	.	.	.
Mol01019	Protein	Multifunctional fusion protein (LPXA)	(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Beta-hydroxyacyl-ACP dehydratase; (3R)-hydroxymyristoyl-ACP dehydrase; UDP-N-acetylglucosamine acyltransferase; fabZ; lpxA; NCTC13305_00288	lpxA_2	.	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MTESTTPKFAIPELPMQIQTIRQYLPHRYPFLLVDRVTEVTDNSIVGYKNVSINEEFLQGHFPEYPIMPGVLIVEALAQVSGVLGFIMNNETPKPGSLFLFAGAERVRFKKQVVAGDQLVLKSELVMQKRGIYKYNCTASVDGIVAATAEIMISHQKNRAGMSNHDLIHSTAIIDPSAVIASDVQIGPYCIIGPQVTIGAGTKLHSHVVVGGFTRIGQNNEIFQFASVGEVCQDLKYKGEETWLEIGNNNLIREHCSLHRGTVQDNALTKIGSHNLLMVNTHIAHDCIVGDHNIFANNVGVAGHVHIGDHVIVGGNSGIHQFCKIDSYSMIGGASLILKDVPAYVMASGNPAHAFGINIEGMRRKGWSKNTIQGLREAYKLIFKSGLTSVQAIEQIKSEILPSVPEAQLLIDSLEQSERGIVR	.	"Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell."	.	.	A0A380UNQ5_ACIBA	Unreviewed	.	.	.	.	.	.
Mol01020	Protein	Na+/H+ exchanger-1 (PFNHE1)	Pfnhe-1; Fragment	Pfnhe-1	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	KKKKISGSNNDNNDNNNDDNNNDNNNNDNHNDDKNNKNDDDNHNDNHNNDDDNNNDNHNDDDNNSSHYNKEKEANFNEYLTYQNLFALQNEDNNIINFFSNDKK	.	.	.	.	C9EIA2_PLAFA	Unreviewed	.	.	.	.	.	.
Mol01021	Protein	NAD-dependent protein deacylase Sir2 (SIR2)	Regulatory protein SIR2 homolog; cobB; npdA; MSMEG_5175; MSMEI_5041	sir2	66736490	Mycolicibacterium smegmatis	1772	Mycolicibacterium smegmatis	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MQVTVLSGAGISAESGVPTFRDAETGLWAQVDPYEISSTDGWQRNPEKVWAWYLWRHYMMARVAPNEAHRTVAAWEDHLDVRVVTQNIDDLHERAGSTNVYHLHGSLFEFRCDACGSAFEGNLPEMPEPVETIDPPVCPCSGLIRPSVVWFGEPLPDAAWNRSVLAVSSADVVIVVGTSSIVYPAAGLPEAALAAGKPVIEVNPERTPLSDSATVSLRETASEALPTLLQRLPELLNRSA	.	NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.	.	.	NDP_MYCS2	Reviewed	.	.	.	.	.	.
Mol01022	Protein	NADH-dependent enoyl-ACP reductase (FABL)	ENR; NADH-dependent enoyl-ACP reductase; envM; b1288; JW1281	fabI	67417387	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK	.	Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.	PDB: 1C14; PDB: 1D8A; PDB: 1DFG; PDB: 1DFH; PDB: 1DFI; PDB: 1I2Z; PDB: 1I30; PDB: 1LX6; PDB: 1LXC; PDB: 1MFP; PDB: 1QG6; PDB: 1QSG; PDB: 2FHS; PDB: 3PJD; PDB: 3PJE; PDB: 3PJF; PDB: 4JQC; PDB: 4JX8; PDB: 5CFZ; PDB: 5CG1; PDB: 5CG2	.	FABI_ECOLI	Reviewed	.	.	.	.	.	.
Mol01023	Protein	Nitrate/nitrite transporter NarU (NARU)	Nitrite extrusion protein 2; Nitrite facilitator 2; yddF; b1469; JW1464	narU	945799	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MALQNEKNSRYLLRDWKPENPAFWENKGKHIARRNLWISVSCLLLAFCVWMLFSAVTVNLNKIGFNFTTDQLFLLTALPSVSGALLRVPYSFMVPIFGGRRWTVFSTAILIIPCVWLGIAVQNPNTPFGIFIVIALLCGFAGANFASSMGNISFFFPKAKQGSALGINGGLGNLGVSVMQLVAPLVIFVPVFAFLGVNGVPQADGSVMSLANAAWIWVPLLAIATIAAWSGMNDIASSRASIADQLPVLQRLHLWLLSLLYLATFGSFIGFSAGFAMLAKTQFPDVNILRLAFFGPFIGAIARSVGGAISDKFGGVRVTLINFIFMAIFSALLFLTLPGTGSGNFIAFYAVFMGLFLTAGLGSGSTFQMIAVIFRQITIYRVKMKGGSDEQAHKEAVTETAAALGFISAIGAVGGFFIPQAFGMSLNMTGSPVGAMKVFLIFYIVCVLLTWLVYGRRKFSQK	.	"Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane. May function as a nitrate/H(+) and nitrite/H(+) channel. Could confer a selective advantage during severe nutrient starvation or slow growth."	PDB: 4IU8; PDB: 4IU9	.	NARU_ECOLI	Reviewed	.	.	.	.	.	.
Mol01024	Protein	Nucleoside diphosphate kinase A (NME1)	NDK A; NDP kinase A; Granzyme A-activated DNase; GAAD; Metastasis inhibition factor nm23; NM23-H1; Tumor metastatic process-associated protein; NDPKA; NM23	NME1	4830	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000393196.8, NME1-203, 890; ENST00000336097.7, NME1-202, 986; ENST00000013034.3, NME1-201, 796; ENST00000511355.5, NME1-209, 1645; ENST00000480143.5, NME1-207, 964; ENST00000456492.1, NME1-204, 510; ENST00000475573.5, NME1-206, 781; ENST00000512768.1, NME1-210, 1056; ENST00000487481.1, NME1-208, 987; ENST00000465188.1, NME1-205, 521"	MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFHPEELVDYTSCAQNWIYE	chr17:51153559-51162428[+]	"Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair."	PDB: 1JXV; PDB: 1UCN; PDB: 2HVD; PDB: 2HVE; PDB: 3L7U; PDB: 4ENO; PDB: 5UI4	HGNC:7849	NDKA_HUMAN	Reviewed	ENSG00000239672	.	.	.	.	.
Mol01025	Protein	Oleandomycin glycosyltransferase oleD (OLED)	UGT102A2	oleD	.	Streptomyces antibioticus	1890	Streptomyces antibioticus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTTQTTPAHIAMFSIAAHGHVNPSLEVIRELVARGHRVTYAIPPVFADKVAATGPRPVLYHSTLPGPDADPEAWGSTLLDNRRTFLNDAIQALPQLADAYADDIPDLVLHDITSYPARVLARRWGVPAVSLSPNLVAWKGYEEEVAEPMWREPRQTERGRAYYARFEAWLKENGITEHPDTFASHPPRSLVLIPKALQPHADRVDEDVYTFVGACQGDRAEEGGWQRPAGAEKVVLVSLGSAFTKQPAFYRECVRAFGNLPGWHLVLQIGRKVTPAELGELPDNVEVHDWVPQLAILRQADLFVTHAGAGGSQEGLATATPMIAVPQAVDQFGNADMLQGLGVARKLATEEATADLLRETALALVDDPEVARRLRRIQAEMAQEGGTRRAADLIEAELPARHERQEPVGDRPNVGDRPAGVRSDRQRSAL	.	Specifically inactivates oleandomycin via 2'-O-glycosylation using UDP-glucose.	PDB: 2IYF; PDB: 4M60; PDB: 4M7P; PDB: 4M83	.	OLED_STRAT	Reviewed	.	.	.	.	.	.
Mol01026	Protein	Oleandomycin glycosyltransferase oleI (OLEL)	oleI; Oleandomycin glycosyltransferase	oleI	.	Streptomyces antibioticus	1890	Streptomyces antibioticus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTSEHRSASVTPRHISFFNIPGHGHVNPSLGIVQELVARGHRVSYAITDEFAAQVKAAGATPVVYDSILPKESNPEESWPEDQESAMGLFLDEAVRVLPQLEDAYADDRPDLIVYDIASWPAPVLGRKWDIPFVQLSPTFVAYEGFEEDVPAVQDPTADRGEEAAAPAGTGDAEEGAEAEDGLVRFFTRLSAFLEEHGVDTPATEFLIAPNRCIVALPRTFQIKGDTVGDNYTFVGPTYGDRSHQGTWEGPGDGRPVLLIALGSAFTDHLDFYRTCLSAVDGLDWHVVLSVGRFVDPADLGEVPPNVEVHQWVPQLDILTKASAFITHAGMGSTMEALSNAVPMVAVPQIAEQTMNAERIVELGLGRHIPRDQVTAEKLREAVLAVASDPGVAERLAAVRQEIREAGGARAAADILEGILAEAG	.	.	PDB: 2IYA	.	Q3HTL7_STRAT	Unreviewed	.	.	.	.	.	.
Mol01027	Protein	OmpK37 (OMPK37)	ompK37; ompN_1; ompN_2; ompS2; A7B01_14055; BANRA_00477; C3F39_02150; DDJ63_15275; FXN67_16010; G5637_10005; NCTC11679_03052; NCTC13465_01341; NCTC13635_00771; SAMEA3499901_03301; SAMEA3649733_02328; SAMEA3727643_03097; SAMEA3729663_03401; SAMEA4873619_03663; Outer membrane pore protein N; non-specific; Outer membrane protein N; Porin; Porin OmpK37; Porin OmpS2	ompK37	.	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	570	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKRKVLALVIPALLAAGAAHAAEIYNKDGNKLDLYGKVDGLHYFSSDSKKDGDQTYLRFGFKGETQINDMLTGYGQWEYNVQANNTETSSDQAWTRLAFAGIKVGDYGSFDYGRNYGVLYDVEGWTDMLPEFGGDSYTYADNFMAGRANGVATYRNSDFFGLVEGLNFALQYQGKNEGQNAQDINVGTNNRSSDSDVRFDNGDGFGLSTSYDFGMGISAAAAYTSSDRTNDQMTQTNARGDKAEAWTAGLKYDANDIYLATMYSETRNMTPYGNDGVANKTQNFEVTAQYQFDFGLRPAISYLQSKGKDLYNNGRYADKDLVKYMDVGATYYFNRNMSTYVDYKINLLDGNDKFYEDNGISTDNIVALGLVYQF	.	.	PDB: 6V78	.	S5UCA2_KLEPN	Unreviewed	.	.	.	.	.	.
Mol01028	Protein	Outer membrane porin (OMP38)	omp38; BURPS1710b_0261; Outer membrane porin	omp38	56594131	Burkholderia pseudomallei	28450	Burkholderia pseudomallei	Burkholderia	32008	Burkholderiaceae	119060	Burkholderiales	80840	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MKKFAVAAAGLAVATGAHASDGSVTLFGLIDAGVSYVSNEGGKRNVYFDDGIAVPNLWGLRGTEDLGGGAKAIFELTSQYALGNGAALPTPGSMFSRTALVGLWSERLGSVTLGQQYDFMTDSLTFGSFDGAFRYGGLYNFRQGPFSKLGIPDNPTGSFDFDRLAGSSRVPNSVKYTSANLNGLVFGLMYGFGNQAGGGLAANSTVSAGLKYETGSFALGAAYVEVKYPQMNNGHDGLRNWGLGARYALSAFDLNLLYTNTRNTLTGAAIDVIQAGVRYVGAPWTIGANYEYMKGNAQLDRNYAHQVTAAAQYALSKRTSAYVETVYQYAGGSAGAHAWINGVMGPDAQSSSRSQFLARIGMLTRF	.	.	.	.	Q3JXM5_BURP1	Unreviewed	.	.	.	.	.	.
Mol01029	Protein	Outer membrane porin C (OMPC)	Outer membrane protein 1B; Outer membrane protein C; Porin OmpC; meoA; par; b2215; JW2203	ompC	946716	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKVKVLSLLVPALLVAGAANAAEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF	.	Forms pores that allow passive diffusion of small molecules across the outer membrane.; FUNCTION: (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF.	PDB: 2J1N; PDB: 2J4U; PDB: 2ZLE; PDB: 4A8D	.	OMPC_ECOLI	Reviewed	.	.	.	.	.	.
Mol01030	Protein	Outer membrane porin F (OMPF)	Outer membrane protein 1A; Outer membrane protein B; Outer membrane protein F; Outer membrane protein IA; Porin OmpF; cmlB; coa; cry; tolF; b0929; JW0912	ompF	66670795	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MMKRNILAVIVPALLVAGTANAAEIYNKDGNKVDLYGKAVGLHYFSKGNGENSYGGNGDMTYARLGFKGETQINSDLTGYGQWEYNFQGNNSEGADAQTGNKTRLAFAGLKYADVGSFDYGRNYGVVYDALGYTDMLPEFGGDTAYSDDFFVGRVGGVATYRNSNFFGLVDGLNFAVQYLGKNERDTARRSNGDGVGGSISYEYEGFGIVGAYGAADRTNLQEAQPLGNGKKAEQWATGLKYDANNIYLAANYGETRNATPITNKFTNTSGFANKTQDVLLVAQYQFDFGLRPSIAYTKSKAKDVEGIGDVDLVNYFEVGATYYFNKNMSTYVDYIINQIDSDNKLGVGSDDTVAVGIVYQF	.	Forms pores that allow passive diffusion of small molecules across the outer membrane.	PDB: 1BT9; PDB: 1GFM; PDB: 1GFN; PDB: 1GFO; PDB: 1GFP; PDB: 1GFQ; PDB: 1HXT; PDB: 1HXU; PDB: 1HXX; PDB: 1MPF; PDB: 1OPF; PDB: 2OMF; PDB: 2ZFG; PDB: 2ZLD; PDB: 3FYX; PDB: 3HW9; PDB: 3HWB; PDB: 3K19; PDB: 3K1B; PDB: 3O0E; PDB: 3POQ; PDB: 3POU; PDB: 3POX; PDB: 4D5U; PDB: 4GCP; PDB: 4GCQ; PDB: 4GCS; PDB: 4JFB; PDB: 4LSE; PDB: 4LSF; PDB: 4LSH; PDB: 4LSI; PDB: 5NUO; PDB: 5NUQ; PDB: 5NUR; PDB: 6WTZ; PDB: 6ZHP; PDB: 6ZHV; PDB: 7NST; PDB: 7NSU	.	OMPF_ECOLI	Reviewed	.	.	.	.	.	.
Mol01031	Protein	Outer membrane protein OprM (OPRM)	oprK; PA0427	oprM	877851	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKRSFLSLAVAAVVLSGCSLIPDYQRPEAPVAAAYPQGQAYGQNTGAAAVPAADIGWREFFRDPQLQQLIGVALENNRDLRVAALNVEAFRAQYRIQRADLFPRIGVDGSGTRQRLPGDLSTTGSPAISSQYGVTLGTTAWELDLFGRLRSLRDQALEQYLATEQAQRSAQTTLVASVATAYLTLKADQAQLQLTKDTLGTYQKSFDLTQRSYDVGVASALDLRQAQTAVEGARATLAQYTRLVAQDQNALVLLLGSGIPANLPQGLGLDQTLLTEVPAGLPSDLLQRRPDILEAEHQLMAANASIGAARAAFFPSISLTANAGTMSRQLSGLFDAGSGSWLFQPSINLPIFTAGSLRASLDYAKIQKDINVAQYEKAIQTAFQEVADGLAARGTFTEQLQAQRDLVKASDEYYQLADKRYRTGVDNYLTLLDAQRSLFTAQQQLITDRLNQLTSEVNLYKALGGGWNQQTVTQQQTAKKEDPQA	.	"The outer membrane component of the MexAB-OprM efflux system that confers multidrug resistance. Also functions as the major efflux pump for n-hexane and p-xylene efflux. Over-expression of the pump increases antibiotic and solvent efflux capacities. Can replace the OprJ outer membrane component of the MexCD-OprJ pump; the antibiotics exported are those exported by the intact MexCD pump, showing that efflux substrate specificity is not conferred by this component. Serves as the outer membrane component for the MexXY efflux system. Implicated in the secretion of the siderophore pyoverdine. OprM is probably involved in the efflux of the siderophore across the outer membrane.; FUNCTION: The ability to export antibiotics and solvents is dramatically decreased in the presence of the proton conductor carbonyl cyanide m-chlorophenylhydrazone (CCCP), showing that an energized inner membrane is required for efflux. It is thought that the MexB subunit is a proton antiporter."	PDB: 1WP1; PDB: 3D5K; PDB: 4Y1K; PDB: 6IOK; PDB: 6IOL; PDB: 6TA5; PDB: 6TA6; PDB: 6ZRE	.	OPRM_PSEAE	Reviewed	.	.	.	.	.	.
Mol01032	Protein	Outer membrane protein U (OMPU)	Porin OmpU; VC_0633	ompU	57739348	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNKTLIALAVSAAAVATGAYADGINQSGDKAGSTVYSAKGTSLEVGGRAEARLSLKDGKAQDNSRVRLNFLGKAEINDSLYGVGFYEGEFTTNDQGKNASNNSLDNRYTYAGIGGTYGEVTYGKNDGALGVITDFTDIMSYHGNTAAEKIAVADRVDNMLAYKGQFGDLGVKASYRFADRNAVDAMGNVVTETNAAKYSDNGEDGYSLSAIYTFGDTGFNVGAGYADQDDQNEYMLAASYRMENLYFAGLFTDGELAKDVDYTGYELAAGYKLGQAAFTATYNNAETAKETSADNFAIDATYYFKPNFRSYISYQFNLLDSDKVGKVASEDELAIGLRYDF	.	Forms pores that allow passive diffusion of small molecules across the outer membrane.	PDB: 5ONU	.	OMPU_VIBCH	Reviewed	.	.	.	.	.	.
Mol01033	Protein	Oxytetracycline resistance efflux MFS transporter OtrB (OTRB)	otr(B); SRIM_038170; Oxytetracycline resistance efflux MFS transporter OtrB	otr(B)	.	Streptomyces rimosus	1927	Streptomyces rimosus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSSANPGPAGTADQAGGAFTHRQILTAMSGLLLAVFLAALDQTVIATAMRTIADDLHGQTEQAWATTGYLIASVLAMPFYGKLSDIYGRKPMYLISIVVFIGGSVLCGTAGSMWELALFRAVQGLGGGGLMSLPTAVVADLAPVRERGRYFAFLQMAWVVASVAGPLAGGFFAEAGQVFGIDGWRWVFLLNVPLGLLALVTVRKALNLPHERREHRMDVLGAAALALFLVPLLIVAEQGRTWGWGSPAALALFALGAAGLAVFIPVELRRGDEAILPLGLFRRGSIALCSAVNFTIGVGIFGTVTTLPLFLQMVQGRTPTQAGLVVIPFMLGTIASQMVSGKLIASSGRFKKLAIVGLGSMAGALLAMATTGATTPMWGIVLIVLWLGVGIGLSQTVITLAMQNSAPKSQLGVANGASGLCRQIGGSTGIAVLFSVMFAVALGRLADLLHTPRYERLLTDPAITGDPANHRFLDMAESGQGAGINLDDTSLLNGIDARLMQPVTDSFAHGFHIMFLAGGVVLLAGFVMTWFLRELQEETAPEEERPAESGAGAKNGPLPASDA	.	.	.	.	L8EYT1_STRR1	Unreviewed	.	.	.	.	.	.
Mol01034	Protein	Parkinson disease protein 7 homolog (PARK7)	Contraception-associated protein 1; Protein CAP1; Fertility protein SP22; Maillard deglycase; Parkinsonism-associated deglycase; Protein DJ-1; DJ-1; Protein/nucleic acid deglycase DJ-1; Cap1	Park7	117287	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSRNOT00000024711.6, Park7-202, 884; ENSRNOT00000091206.2, Park7-201, 1418; ENSRNOT00000087402.2, Park7-203, 963; ENSRNOT00000119817.1, Park7-204, 719"	MASKRALVILAKGAEEMETVIPVDIMRRAGIKVTVAGLAGKDPVQCSRDVVICPDTSLEEAKTQGPYDVVVLPGGNLGAQNLSESALVKEILKEQENRKGLIAAICAGPTALLAHEVGFGCKVTSHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALSGKDMANQVKAPLVLKD	Primary_assembly 5: 161353719-161376970[-] 	"Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (By similarity). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (By similarity). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity)."	.	.	PARK7_RAT	Reviewed	ENSRNOG00000018289	.	.	.	.	.
Mol01035	Protein	Penicillin binding protein PBP 2 (PBP2)	pbp2; ponA; CV021_08520; GO782_04115; NCTC6133_01867; Penicillin-binding protein; Penicillin-binding protein 2	pbp2	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MTENKGSSQPKKNGNNGGKSNSKKNRNVKRTIIKIIGFMIIAFFVVLLLGILLFAYYAWKAPAFTEAKLQDPIPAKIYDKNGELVKTLDNGQRHEHVNLKDVPKSMKDAVLATEDNRFYEHGALDYKRLFGAIGKNLTGGFGSEGASTLTQQVVKDAFLSQHKSIGRKAQEAYLSYRLEQEYSKDDIFQVYLNKIYYSDGVTGIKAAAKYYFNKDLKDLNLAEEAYLAGLPQVPNNYNIYDHPKAAEDRKNTVLYLMHYHKRITDKQWEDAKKIDLKANLVNRTAEERQNIDTNQDSEYNSYVNFVKSELMNNKAFKDENLGNVLQSGIKIYTNMDKDVQKTLQNDVDNGSFYKNKDQQVGATILDSKTGGLVAISGGRDFKDVVNRNQATDPHPTGSSLKPFLAYGPAIENMKWATNHAIQDESSYQVDGSTFRNYDVKSHGTVSIYDALRQSFNIPALKAWQSVKQNAGNDAPKKFAAKLGLNYEGDIGPSEVLGGSASEFSPTQLASAFAAIANGGTYNNAHSIQKVVTRDGETIEYDHTSHKAMSDYTAYMLAEMLKGTFKPYGSAYGHGVSGVNMGAKTGTGTYGAETYSQYNLPDNAAKDVWINGFTPQYTMSVWMGFSKVKQYGENSFVGHSQQEYPQFLYENVMSKISSRDGEDFKRPSSVSGSIPSINVSGSQDNNTTNRSTHGGSDTSANSSGTAQSNNNTRSQQSRNSGGLTGIFN	.	.	.	.	F4NA87_STAAU	Unreviewed	.	.	.	.	.	.
Mol01036	Protein	Penicillin-binding protein 1A (PBP1A)	PBP-1A; Exported protein 2; Peptidoglycan TGase; DD-transpeptidase; exp2; ponA; spr0329	pbpA	60234246	Streptococcus pneumoniae	1313	Streptococcus pneumoniae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNKPTILRLIKYLSISFLSLVIAAIVLGGGVFFYYVSKAPSLSESKLVATTSSKIYDNKNQLIADLGSERRVNAQANDIPTDLVKAIVSIEDHRFFDHRGIDTIRILGAFLRNLQSNSLQGGSALTQQLIKLTYFSTSTSDQTISRKAQEAWLAIQLEQKATKQEILTYYINKVYMSNGNYGMQTAAQNYYGKDLNNLSLPQLALLAGMPQAPNQYDPYSHPEAAQDRRNLVLSEMKNQGYISAEQYEKAVNTPITDGLQSLKSASNYPAYMDNYLKEVINQVEEETGYNLLTTGMDVYTNVDQEAQKHLWDIYNTDEYVAYPDDELQVASTIVDVSNGKVIAQLGARHQSSNVSFGINQAVETNRDWGSTMKPITDYAPALEYGVYESTATIVHDEPYNYPGTNTPVYNWDRGYFGNITLQYALQQSRNVPAVETLNKVGLNRAKTFLNGLGIDYPSIHYSNAISSNTTESDKKYGASSEKMAAAYAAFANGGTYYKPMYIHKVVFSDGSEKEFSNVGTRAMKETTAYMMTDMMKTVLSYGTGRNAYLAWLPQAGKTGTSNYTDEEIENHIKTSQFVAPDELFAGYTRKYSMAVWTGYSNRLTPLVGNGLTVAAKVYRSMMTYLSEGSNPEDWNIPEGLYRNGEFVFKNGARSTWSSPAPQQPPSTESSSSSSDSSTSQSSSTTPSTNNSTTTNPNNNTQQSNTTPDQQNQNPQPAQP	.	Cell wall formation.	PDB: 2C5W; PDB: 2C6W; PDB: 2V2F; PDB: 2ZC5; PDB: 2ZC6	.	PBPA_STRR6	Reviewed	.	.	.	.	.	.
Mol01037	Protein	Penicillin-binding protein 1A (PBP1A)	PBP-1a; PBP1a; Peptidoglycan TGase; DD-transpeptidase; ponA	mrcA	.	Neisseria gonorrhoeae	485	Neisseria gonorrhoeae	Neisseria	482	Neisseriaceae	481	Neisseriales	206351	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MIKKILTTCFGLFFGFCVFGVGLVAIAILVTYPKLPSLDSLQHYQPKMPLTIYSADGEVIGMYGEQRREFTKIGDFPEVLRNAVIAAEDKRFYRHWGVDVWGVARAAVGNVVSGSVQSGASTITQQVAKNFYLSSEKTFTRKFNEVLLAYKIEQSLSKDKILELYFNQIYLGQRAYGFASAAQIYFNKNVRDLTLAEAAMLAGLPKAPSAYNPIVNPERAKLRQKYILNNMLEEKMITVQQRDQALNEELHYERFVRKIDQSALYVAEMVRRELYEKYGEDAYTQGFKVYTTVRTDHQKAATEALRKALRNFDRGSSYRGAENYIDLSKSEDVEETVSQYLSGLYTVDKMVPAVVLDVTKKKNVVIQLPGGRRVALDRRALGFAARAVDNEKMGEDRIRRGAVIRVKNNGGRWAVVQEPLLQGALVSLDAKTGAVRALVGGYDFHSKTFNRAVQAMRQPGSTFKPFVYSAALSKGMTASTVVNDAPISLPGKGPNGSVWTPKNSDGRYSGYITLRQALTASKNMVSIRILMSIGVGYAQQYIRRFGFRPSELPASLSMALGTGETTPLKVAEAYSVFANGGYRVSSHVIDKIYDRDGRLRAQMQPLVAGQNAPQAIDPRNAYIMYKIMQDVVRVGTARGAAALGRTDIAGKTGTTNDNKDAWFVGFNPDVVTAVYIGFDKPKSMGRAGYGGTIAVPVWVDYMRFALKGKQGKGMKMPEGVVSSNGEYYMKERMVTDPGLMLDNSGIAPQPSRRAKEDDEAAVENEQQGRSDETRQDVQETPVLPSNTDSKQQQLDSLF	.	Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). Essential for cell wall synthesis.	.	.	PBPA_NEIGO	Reviewed	.	.	.	.	.	.
Mol01038	Protein	Penicillin-binding protein 2B (PBP2B)	PBP2b; Peptidoglycan transpeptidase; pbp2b; spr1517	penA	.	Streptococcus pneumoniae	1313	Streptococcus pneumoniae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MRKFNSHSIPIRLNLLFSIVILLFMTIIGRLLYMQVLNKDFYEKKLASASQTKITSSSARGEIYDASGKPLVENTLKQVVSFTRSNKMTATDLKETAKKLLTYVSISSPNLTERQLADYYLADPEIYKKIVEALPSEKRLDSDGNRLSESELYNNAVDSVQTSQLNYTEDEKKEIYLFSQLNAVGNFATGTIATDPLNDSQVAVIASISKEMPGISISTSWDRKVLETSLSSIVGSVSSEKAGLPAEEAEAYLKKGYSLNDRVGTSYLEKQYEETLQGKRSVKEIHLDKYGNMESVDTIEEGSKGNNIKLTIDLAFQDSVDALLKSYFNSELENGGAKYSEGVYAVALNPKTGAVLSMSGIKHDLKTGELTPDSLGTVTNVFVPGSVVKAATISSGWENGVLSGNQTLTDQSIVFQGSAPINSWYTQAYGSFPITAVQALEYSSNTYMVQTALGLMGQTYQPNMFVGTSNLESAMEKLRSTFGEYGLGTATGIDLPDESTGFVPKEYSFANYITNAFGQFDNYTPMQLAQYVATIANNGVRVAPRIVEGIYGNNDKGGLGDLIQQLQPTEMNKVNISDSDMSILHQGFYQVAHGTSGLTTGRAFSNGALVSISGKTGTAESYVADGQQATNTNAVAYAPSDNPQIAVAVVFPHNTNLTNGVGPSIARDIINLYQKYHPMN	.	A transpeptidase that forms peptide cross-links between adjacent glycan strands in cell wall peptidoglycan (PG). Part of the elongasome machinery that synthesizes peripheral PG.	PDB: 2WAD; PDB: 2WAE; PDB: 2WAF	.	PBP2_STRR6	Reviewed	.	.	.	.	.	.
Mol01039	Protein	Penicillin-binding protein 2X (PBP2X)	PBP-2X; PBP2X; spr0304	pbpX	60232761	Streptococcus pneumoniae	1313	Streptococcus pneumoniae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MKWTKRVIRYATKNRKSPAENRRRVGKSLSLLSVFVFAIFLVNFAVIIGTGTRFGTDLAKEAKKVHQTTRTVPAKRGTIYDRNGVPIAEDATSYNVYAVIDENYKSATGKILYVEKTQFNKVAEVFHKYLDMEESYVREQLSQPNLKQVSFGAKGNGITYANMMSIKKELEAAEVKGIDFTTSPNRSYPNGQFASSFIGLAQLHENEDGSKSLLGTSGMESSLNSILAGTDGIITYEKDRLGNIVPGTEQVSQRTMDGKDVYTTISSPLQSFMETQMDAFQEKVKGKYMTATLVSAKTGEILATTQRPTFDADTKEGITEDFVWRDILYQSNYEPGSTMKVMMLAAAIDNNTFPGGEVFNSSELKIADATIRDWDVNEGLTGGRMMTFSQGFAHSSNVGMTLLEQKMGDATWLDYLNRFKFGVPTRFGLTDEYAGQLPADNIVNIAQSSFGQGISVTQTQMIRAFTAIANDGVMLEPKFISAIYDPNDQTARKSQKEIVGNPVSKDAASLTRTNMVLVGTDPVYGTMYNHSTGKPTVTVPGQNVALKSGTAQIADEKNGGYLVGLTDYIFSAVSMSPAENPDFILYVTVQQPEHYSGIQLGEFANPILERASAMKDSLNLQTTAKALEQVSQQSPYPMPSVKDISPGDLAEELRRNLVQPIVVGTGTKIKNSSAEEGKNLAPNQQVLILSDKAEEVPDMYGWTKETAETLAKWLNIELEFQGSGSTVQKQDVRANTAIKDIKKITLTLGD	.	A transpeptidase that forms peptide cross-links between adjacent glycan strands in cell wall peptidoglycan (PG). Part of the divisome machinery that synthesizes the septal cross wall. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.	PDB: 1PYY; PDB: 5OAU; PDB: 5OIZ; PDB: 5OJ0; PDB: 5OJ1	.	PBPX_STRR6	Reviewed	.	.	.	.	.	.
Mol01040	Protein	Peptide methionine sulfoxide reductase MsrB (MSRB)	Peptide-methionine (R)-S-oxide reductase; yeaA; b1778; JW1767	msrB	58462326	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MANKPSAEELKKNLSEMQFYVTQNHGTEPPFTGRLLHNKRDGVYHCLICDAPLFHSQTKYDSGCGWPSFYEPVSEESIRYIKDLSHGMQRIEIRCGNCDAHLGHVFPDGPQPTGERYCVNSASLRFTDGENGEEING	.	.	PDB: 6SYM	.	MSRB_ECOLI	Reviewed	.	.	.	.	.	.
Mol01041	Protein	Peroxisome proliferator-activated receptor gamma (PPARG)	PPAR-gamma; Nuclear receptor subfamily 1 group C member 3; Nr1c3	Pparg	25664	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSRNOT00000012137.6, Pparg-202, 1797; ENSRNOT00000082969.2, Pparg-201, 2008"	MGETLGDPPVDPEHGAFADALPMSTSQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNRPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFINLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKVLQKMTDLRQIVTEHVQLLHVIKKTETDMSLHPLLQEIYKDLY	Primary_assembly 4: 148423194-148548468 [+] 	"Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated proinflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of ARNTL/BMAL1 in the blood vessels."	.	.	PPARG_RAT	Reviewed	ENSRNOG00000008839	.	.	.	.	.
Mol01042	Protein	Phosphatidate cytidylyltransferase (CDSA)	B7703_01220; FOB92_07930; GEZ84_01335; RN80_03115; SMNM65_03110	cdsA	.	Streptococcus mitis	28037	Streptococcus mitis	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MTQDLQKRTLFAGIALAIFLPILMIGGLLLQIAIGIIAMLAMHELLKMRGLETMTMEGLLTLFATFALTIPLENYLTFLPVDGNVVAYSVLISIMLGTTVFSKSYTIEDAVFPLAMSFYVGFGFNALLDARVAGLDKALLALCIVWATDSGAYLVGMNYGKRKLAPTVSPNKTFEGALGGILGAILVTIIFMIVDSTVALPYGIYKMSVFAIFFSIAGQFGDLLESSIKRHFGVKDSGKFIPGHGGVLDRFDSMLLVFPIMHLFGLF	.	.	.	.	A0A0M4KGJ3_STRMT	Unreviewed	.	.	.	.	.	.
Mol01043	Protein	Phosphatidylglycerol lysyltransferase (MPREF)	Lysylphosphatidylglycerol synthase; LPG synthase; Multiple peptide resistance factor; fmtC	mprF	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNQEVKNKIFSILKITFATALFIFVAITLYRELSGINFKDTLVEFSKINRMSLVLLFIGGGASLVILSMYDVILSRALKMDISLGKVLRVSYIINALNAIVGFGGFIGAGVRAMVYKNYTHDKKKLVHFISLILISMLTGLSLLSLLIVFHVFDASLILDKITWVRWVLYVVSFFLPLFIIYSMVRPPDKNNRFVGLYCTLVSCVEWLAAAVVLYFCGVIVDAHVSFMSFIAIFIIAALSGLVSFIPGGFGAFDLVVLLGFKTLGVPEEKVLLMLLLYRFAYYFVPVIIALILSSFEFGTSAKKYIEGSKYFIPAKDVTSFLMSYQKDIIAKIPSLSLAILVFFTSMIFFVNNLTIVYDALYDGNHLTYYILLAIHTSACLLLLLNVVGIYKQSRRAIIFAMISILLITVATFFTYASYILITWLAIIFVLLIVAFRRARRLKRPVRMRNIVAMLLFSLFILYVNHIFIAGTLYALDIYTIEMHTSVLRYYFWLTILIIAIIIGMIAWLFDYQFSKVRISSKIEDCEEIINQYGGNYLSHLIYSGDKQFFTNENKTAFLMYRYKASSLVVLGDPLGDENAFDELLEAFYNYAEYLGYDVIFYQVTDQHMPLYHNFGNQFFKLGEEAIIDLTQFSTSGKKRRGFRATLNKFDELNISFEIIEPPFSTEFINELQHVSDLWLDNRQEMHFSVGEFNEEYLSKAPIGVMRNEENEVIAFCSLMPTYFNDAISVDLIRWLPELDLPLMDGLYLHMLLWSKEQGYTKFNMGMATLSNVGQLHYSYLRERLAGRVFEHFNGLYRFQGLRRYKSKYNPNWEPRFLVYRKDNSLWESLSKVMRVIRHK	.	"Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides. Consequently, MprF is shown to affect resistance and susceptibility to moenomycin and vancomycin, resistance to human defensins (HNP1-3) and evasion of oxygen-independent neutrophil killing and susceptibility to methicillin, oxacillin, bacitracin, gentamicin, beta-lactams and synthetic peptides (hBD3, CAP18) and other cationic antimicrobial peptides."	.	.	MPRF_STAAU	Reviewed	.	.	.	.	.	.
Mol01044	Protein	Phosphatidylglycerophosphate synthase (PGSA)	Phosphatidylglycerophosphate synthase; PGP synthase; SAV1283	pgsA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNIPNQITVFRVVLIPVFILFALVDFGFGNVSFLGGYEIRIELLISGFIFILASLSDFVDGYLARKWNLVTNMGKFLDPLADKLLVASALIVLVQLGLTNSVVAIIIIAREFAVTGLRLLQIEQGFVSAAGQLGKIKTAVTMVAITWLLLGDPLATLIGLSLGQILLYIGVIFTILSGIEYFYKGRDVFKQK	.	This protein catalyzes the committed step to the synthesis of the acidic phospholipids.	.	.	PGSA_STAAM	Reviewed	.	.	.	.	.	.
Mol01045	Protein	Phosphofructo-1-kinase isozyme B (PFKB)	ATP-PFK; PFK-L; 6-phosphofructokinase type B; Phosphofructo-1-kinase isozyme B; PFK-B; Phosphohexokinase	PFKL	5211	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000349048.9, PFKL-201, 2907; ENST00000628044.1, PFKL-212, 129; ENST00000397961.6, PFKL-202, 3390; ENST00000496824.5, PFKL-210, 1063; ENST00000491298.1, PFKL-208, 819; ENST00000474114.5, PFKL-207, 6007; ENST00000466134.5, PFKL-205, 5986; ENST00000498841.5, PFKL-211, 3122; ENST00000460521.5, PFKL-204, 2818; ENST00000467315.5, PFKL-206, 1947; ENST00000495274.1, PFKL-209, 951; ENST00000460020.5, PFKL-203, 890"	MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDGSLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQKAMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRSAVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESIVENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLGSDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFNIHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGHLQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFSPVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF	chr21:44300051-44327376[+]	"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway."	.	HGNC:8876	PFKAL_HUMAN	Reviewed	ENSG00000141959	.	.	.	.	.
Mol01046	Protein	Phospholipid-translocating ATPase (RTA2)	RTA2; orf19.24; CAALFM_C206470WA; Phospholipid-translocating ATPase	RTA2	3646567	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSEILNYLSSWTPTSTPTSTTLSSIATSHVSKLSQTVASVISQATTETDWYNLRSLSQAYRGAQASLTIISAEKVLATATDSQVQSRATQAIFEATLNLKDLSMEQNIYGYELNRAANIIYLVVYAIIFGYTLLMCIKSKYWWYNVTFVCGYGLEFVGFLGRVLSFNDTSNMSHYIMQSVALTIAPAFIMAGVYFLFGQLVVIHGRQYSVLKPMWYSYFFITADVVSLLIQAAGGGIASVASSNHKDSSVGTNIMIAGIAAQVVAMTIFLVFWFEFLNRLYFKNSRSDLIVDCPYGRRSISNYFKLLLNVKSVRGHRHTHLEKYYNEKFASIRQIPLFDYMVLAMTIAVIVVYIRCVYRVAELAEGWGGYLFTHEPYLMILDAAMIAIAGLIFIPFHPVWVFGKNNIVKLATIKKNLDENEKNQDVEYNDDVESQERSSSVVANDIHCLNSKL	.	.	.	.	Q59Q40_CANAL	Unreviewed	.	.	.	.	.	.
Mol01047	Protein	Plasmepsin II (PMII)	PLM II; Aspartic hemoglobinase II; PfAPD; PfPM1; Plasmepsin 2	PMII	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MDITVREHDFKHGFIKSNSTFDGLNIDNSKNKKKIQKGFQILYVLLFCSVMCGLFYYVYENVWLQRDNEMNEILKNSEHLTIGFKVENAHDRILKTIKTHKLKNYIKESVNFLNSGLTKTNYLGSSNDNIELVDFQNIMFYGDAEVGDNQQPFTFILDTGSANLWVPSVKCTTAGCLTKHLYDSSKSRTYEKDGTKVEMNYVSGTVSGFFSKDLVTVGNLSLPYKFIEVIDTNGFEPTYTASTFDGILGLGWKDLSIGSVDPIVVELKNQNKIENALFTFYLPVHDKHTGFLTIGGIEERFYEGPLTYEKLNHDLYWQITLDAHVGNIMLEKANCIVDSGTSAITVPTDFLNKMLQNLDVIKVPFLPFYVTLCNNSKLPTFEFTSENGKYTLEPEYYLQHIEDVGPGLCMLNIIGLDFPVPTFILGDPFMRKYFTVFDYDNHSVGIALAKKNL	.	"During the asexual blood stage, participates in initial cleavage of native host hemoglobin (Hb) resulting in Hb denaturation. May cleave preferentially denatured hemoglobin that has been cleaved by PMI. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable)."	PDB: 1LEE; PDB: 1LF2; PDB: 1LF3; PDB: 1LF4; PDB: 1M43; PDB: 1ME6; PDB: 1PFZ; PDB: 1SME; PDB: 1W6H; PDB: 1W6I; PDB: 1XDH; PDB: 1XE5; PDB: 1XE6; PDB: 2BJU; PDB: 2IGX; PDB: 2IGY; PDB: 2R9B; PDB: 3F9Q; PDB: 4CKU; PDB: 4Y6M; PDB: 4YA8; PDB: 4Z22; PDB: 5BWY	.	PLM2_PLAFX	Reviewed	.	.	.	.	.	.
Mol01048	Protein	Pleiotropic ABC efflux transporter of multiple drugs (PDR5)	Pleiotropic drug resistance protein 5; Suppressor of toxicity of sporidesmin; LEM1; STS1; YDR1; YOR153W	PDR5	854324	Saccharomyces cerevisiae	4932	Saccharomyces cerevisiae	Saccharomyces	4930	Saccharomycetaceae	4893	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MPEAKLNNNVNDVTSYSSASSSTENAADLHNYNGFDEHTEARIQKLARTLTAQSMQNSTQSAPNKSDAQSIFSSGVEGVNPIFSDPEAPGYDPKLDPNSENFSSAAWVKNMAHLSAADPDFYKPYSLGCAWKNLSASGASADVAYQSTVVNIPYKILKSGLRKFQRSKETNTFQILKPMDGCLNPGELLVVLGRPGSGCTTLLKSISSNTHGFDLGADTKISYSGYSGDDIKKHFRGEVVYNAEADVHLPHLTVFETLVTVARLKTPQNRIKGVDRESYANHLAEVAMATYGLSHTRNTKVGNDIVRGVSGGERKRVSIAEVSICGSKFQCWDNATRGLDSATALEFIRALKTQADISNTSATVAIYQCSQDAYDLFNKVCVLDDGYQIYYGPADKAKKYFEDMGYVCPSRQTTADFLTSVTSPSERTLNKDMLKKGIHIPQTPKEMNDYWVKSPNYKELMKEVDQRLLNDDEASREAIKEAHIAKQSKRARPSSPYTVSYMMQVKYLLIRNMWRLRNNIGFTLFMILGNCSMALILGSMFFKIMKKGDTSTFYFRGSAMFFAILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVLSEIPSKLIIAVCFNIIFYFLVDFRRNGGVFFFYLLINIVAVFSMSHLFRCVGSLTKTLSEAMVPASMLLLALSMYTGFAIPKKKILRWSKWIWYINPLAYLFESLLINEFHGIKFPCAEYVPRGPAYANISSTESVCTVVGAVPGQDYVLGDDFIRGTYQYYHKDKWRGFGIGMAYVVFFFFVYLFLCEYNEGAKQKGEILVFPRSIVKRMKKRGVLTEKNANDPENVGERSDLSSDRKMLQESSEEESDTYGEIGLSKSEAIFHWRNLCYEVQIKAETRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERVTMGVITGDILVNGIPRDKSFPRSIGYCQQQDLHLKTATVRESLRFSAYLRQPAEVSIEEKNRYVEEVIKILEMEKYADAVVGVAGEGLNVEQRKRLTIGVELTAKPKLLVFLDEPTSGLDSQTAWSICQLMKKLANHGQAILCTIHQPSAILMQEFDRLLFMQRGGKTVYFGDLGEGCKTMIDYFESHGAHKCPADANPAEWMLEVVGAAPGSHANQDYYEVWRNSEEYRAVQSELDWMERELPKKGSITAAEDKHEFSQSIIYQTKLVSIRLFQQYWRSPDYLWSKFILTIFNQLFIGFTFFKAGTSLQGLQNQMLAVFMFTVIFNPILQQYLPSFVQQRDLYEARERPSRTFSWISFIFAQIFVEVPWNILAGTIAYFIYYYPIGFYSNASAAGQLHERGALFWLFSCAFYVYVGSMGLLVISFNQVAESAANLASLLFTMSLSFCGVMTTPSAMPRFWIFMYRVSPLTYFIQALLAVGVANVDVKCADYELLEFTPPSGMTCGQYMEPYLQLAKTGYLTDENATDTCSFCQISTTNDYLANVNSFYSERWRNYGIFICYIAFNYIAGVFFYWLARVPKKNGKLSKK	.	"Active efflux of weakly charged organic compounds of 90 cubic Angstroms to 300 cubic Angstroms surface volume. Confers resistance to numerous chemicals including cycloheximide, sulfomethuron methyl, steroids, antiseptics, antibiotics, anticancer, herbicides, mycotoxins, insecticides, ionophores, alkaloids, flavonoids, phenothiazines, organotin compounds, carbazoles, lysosomotropic aminoesters, detergents, rhodamines and other fluorophores, azoles and other antifungals. Exhibits nucleoside triphosphatase activity."	.	.	PDR5_YEAST	Reviewed	.	.	.	.	.	.
Mol01049	Protein	Pleiotropic ABC efflux transporter of multiple drugs CDR1 (CDR1)	Pleiotropic drug resistance protein CDR1; CAALFM_C305220WA; CaO19.13421; CaO19.6000	CDR1	3635237	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSDSKMSSQDESKLEKAISQDSSSENHSINEYHGFDAHTSENIQNLARTFTHDSFKDDSSAGLLKYLTHMSEVPGVNPYEHEEINNDQLNPDSENFNAKFWVKNLRKLFESDPEYYKPSKLGIGYRNLRAYGVANDSDYQPTVTNALWKLATEGFRHFQKDDDSRYFDILKSMDAIMRPGELTVVLGRPGAGCSTLLKTIAVNTYGFHIGKESQITYDGLSPHDIERHYRGDVIYSAETDVHFPHLSVGDTLEFAARLRTPQNRGEGIDRETYAKHMASVYMATYGLSHTRNTNVGNDFVRGVSGGERKRVSIAEASLSGANIQCWDNATRGLDSATALEFIRALKTSAVILDTTPLIAIYQCSQDAYDLFDKVVVLYEGYQIFFGKATKAKEYFEKMGWKCPQRQTTADFLTSLTNPAEREPLPGYEDKVPRTAQEFETYWKNSPEYAELTKEIDEYFVECERSNTRETYRESHVAKQSNNTRPASPYTVSFFMQVRYGVARNFLRMKGDPSIPIFSVFGQLVMGLILSSVFYNLSQTTGSFYYRGAAMFFAVLFNAFSSLLEIMSLFEARPIVEKHKKYALYRPSADALASIISELPVKLAMSMSFNFVFYFMVNFRRNPGRFFFYWLMCIWCTFVMSHLFRSIGAVSTSISGAMTPATVLLLAMVIYTGFVIPTPSMLGWSRWINYINPVGYVFESLMVNEFHGREFQCAQYVPSGPGYENISRSNQVCTAVGSVPGNEMVSGTNYLAGAYQYYNSHKWRNLGITIGFAVFFLAIYIALTEFNKGAMQKGEIVLFLKGSLKKHKRKTAASNKGDIEAGPVAGKLDYQDEAEAVNNEKFTEKGSTGSVDFPENREIFFWRDLTYQVKIKKEDRVILDHVDGWVKPGQITALMGASGAGKTTLLNCLSERVTTGIITDGERLVNGHALDSSFQRSIGYVQQQDVHLETTTVREALQFSAYLRQSNKISKKEKDDYVDYVIDLLEMTDYADALVGVAGEGLNVEQRKRLTIGVELVAKPKLLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSALIMAEFDRLLFLQKGGRTAYFGELGENCQTMINYFEKYGADPCPKEANPAEWMLQVVGAAPGSHAKQDYFEVWRNSSEYQAVREEINRMEAELSKLPRDNDPEALLKYAAPLWKQYLLVSWRTIVQDWRSPGYIYSKIFLVVSAALFNGFSFFKAKNNMQGLQNQMFSVFMFFIPFNTLVQQMLPYFVKQRDVYEVREAPSRTFSWFAFIAGQITSEIPYQVAVGTIAFFCWYYPLGLYNNATPTDSVNPRGVLMWMLVTAFYVYTATMGQLCMSFSELADNAANLATLLFTMCLNFCGVLAGPDVLPGFWIFMYRCNPFTYLVQAMLSTGLANTFVKCAEREYVSVKPPNGESCSTYLDPYIKFAGGYFETRNDGSCAFCQMSSTNTFLKSVNSLYSERWRNFGIFIAFIAINIILTVIFYWLARVPKGNREKKNKK	.	"Pleiotropic ABC efflux transporter that confers resistance to numerous chemicals including anisomycin, cycloheximide, fluconazole, miconazole, ketoconazole, itriconazole, nystatin, terbinafine, amorolfine, brefeldin A, amphotericin B, fluphenazine, as well as estrogen. Plays a role in farnesol-induced apoptotic process through glutathione efflux activity. Mediates in-to-out translocation of membrane phospholipids including aminophospholipids and thus regulates asymmetric distribution of phosphatidylethanolamine. Exhibits nucleoside triphosphatase activity."	.	.	CDR1_CANAL	Reviewed	.	.	.	.	.	.
Mol01050	Protein	Polyamine transporter 1 (TPO1)	YLL028W; L0939	TPO1	850631	Saccharomyces cerevisiae	4932	Saccharomyces cerevisiae	Saccharomyces	4930	Saccharomycetaceae	4893	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSDHSPISNKENHLLPSDSSRSSSSDMHSTGTTGTTGVEPVDFTGEGAKYTTATEGNGGADLAIQRTTTMNSAAESEVNITRRLTKILTGSVNEPDRVEVDYTNCAPMGGDRPYPPSLPSRDLYEVTFDGPNDPLHPFNWPMKKKVLLCLVLCLDSIAIAMCSSIFASAVPQICEIYHVIEVVAILGITLFVLGFAASPVIYAPLSELYGRKGVLVLSAFGFALFQFAVATAENLQTIFICRFFGGFIGAAPMAVVPAAFADMFDTNVRGKAIALFSLGVFVGPILSPVMGSYIAQRTTWRWLEYVVGCFASAVFVAIVLFFEETHHPTILVNKAKQMRKQSNNWGIHAAHEDVELSIKDIVQKTVTRPIIMLFVEPLLLFVTIYNSFVYGILYLLLEAYPLVFVEGYGFTENGELPYIALIIGMMVCAAFIWYMDNDYLKRCRAKGKLVPEARLYAMVIAGTVFPIGILWFCWTGYYPHKIHWMVPTVGGAFIGFGLMGIFLPCLNYIIESYLLLAASAVAANTFMRSAFGACFPLFAGYMFRGMGIGWAGLLLGLFAAAMIPVPLLFLKYGESIRKKSKYAYAA	.	"Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Catalyzes polyamine uptake at alkaline pH and excretion at acidic pH. Recognizes spermidine, spermine and putrescine, the polyamine analogs methylglyoxal bis(guanylhydrazone) (MGBG) and paraquat, the antimalarial drug quinidine, and cycloheximide. Confers resistance to the non-steroidal anti-inflammatory drug indomethacin."	.	.	TPO1_YEAST	Reviewed	.	.	.	.	.	.
Mol01051	Protein	Porin D (OPRD)	Imipenem/basic amino acid-specific outer membrane pore; Outer membrane protein D2; PA0958	oprD	881970	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKVMKWSAIALAVSAGSTQFAVADAFVSDQAEAKGFIEDSSLDLLLRNYYFNRDGKSGSGDRVDWTQGFLTTYESGFTQGTVGFGVDAFGYLGLKLDGTSDKTGTGNLPVMNDGKPRDDYSRAGGAVKVRISKTMLKWGEMQPTAPVFAAGGSRLFPQTATGFQLQSSEFEGLDLEAGHFTEGKEPTTVKSRGELYATYAGETAKSADFIGGRYAITDNLSASLYGAELEDIYRQYYLNSNYTIPLASDQSLGFDFNIYRTNDEGKAKAGDISNTTWSLAAAYTLDAHTFTLAYQKVHGDQPFDYIGFGRNGSGAGGDSIFLANSVQYSDFNGPGEKSWQARYDLNLASYGVPGLTFMVRYINGKDIDGTKMSDNNVGYKNYGYGEDGKHHETNLEAKYVVQSGPAKDLSFRIRQAWHRANADQGEGDQNEFRLIVDYPLSIL	.	Porin with a specificity for basic amino acids. Also possesses serine protease activity.	PDB: 2ODJ; PDB: 3SY7; PDB: 4FOZ	.	PORD_PSEAE	Reviewed	.	.	.	.	.	.
Mol01052	Protein	Probable arabinosyltransferase B (EMBB)	Rv3795; MTCY13D12.29	embB	886126	Mycobacteriumtuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTQCASRRKSTPNRAILGAFASARGTRWVATIAGLIGFVLSVATPLLPVVQTTAMLDWPQRGQLGSVTAPLISLTPVDFTATVPCDVVRAMPPAGGVVLGTAPKQGKDANLQALFVVVSAQRVDVTDRNVVILSVPREQVTSPQCQRIEVTSTHAGTFANFVGLKDPSGAPLRSGFPDPNLRPQIVGVFTDLTGPAPPGLAVSATIDTRFSTRPTTLKLLAIIGAIVATVVALIALWRLDQLDGRGSIAQLLLRPFRPASSPGGMRRLIPASWRTFTLTDAVVIFGFLLWHVIGANSSDDGYILGMARVADHAGYMSNYFRWFGSPEDPFGWYYNLLALMTHVSDASLWMRLPDLAAGLVCWLLLSREVLPRLGPAVEASKPAYWAAAMVLLTAWMPFNNGLRPEGIIALGSLVTYVLIERSMRYSRLTPAALAVVTAAFTLGVQPTGLIAVAALVAGGRPMLRILVRRHRLVGTLPLVSPMLAAGTVILTVVFADQTLSTVLEATRVRAKIGPSQAWYTENLRYYYLILPTVDGSLSRRFGFLITALCLFTAVFIMLRRKRIPSVARGPAWRLMGVIFGTMFFLMFTPTKWVHHFGLFAAVGAAMAALTTVLVSPSVLRWSRNRMAFLAALFFLLALCWATTNGWWYVSSYGVPFNSAMPKIDGITVSTIFFALFAIAAGYAAWLHFAPRGAGEGRLIRALTTAPVPIVAGFMAAVFVASMVAGIVRQYPTYSNGWSNVRAFVGGCGLADDVLVEPDTNAGFMKPLDGDSGSWGPLGPLGGVNPVGFTPNGVPEHTVAEAIVMKPNQPGTDYDWDAPTKLTSPGINGSTVPLPYGLDPARVPLAGTYTTGAQQQSTLVSAWYLLPKPDDGHPLVVVTAAGKIAGNSVLHGYTPGQTVVLEYAMPGPGALVPAGRMVPDDLYGEQPKAWRNLRFARAKMPADAVAVRVVAEDLSLTPEDWIAVTPPRVPDLRSLQEYVGSTQPVLLDWAVGLAFPCQQPMLHANGIAEIPKFRITPDYSAKKLDTDTWEDGTNGGLLGITDLLLRAHVMATYLSRDWARDWGSLRKFDTLVDAPPAQLELGTATRSGLWSPGKIRIGP	.	Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.	PDB: 7BVF	.	EMBB_MYCTU	Reviewed	.	.	.	.	.	.
Mol01053	Protein	Probable dual-specificity RNA methyltransferase RlmN (RLMN )	23S rRNA (adenine(2503)-C(2))-methyltransferase; 23S rRNA m2A2503 methyltransferase; Ribosomal RNA large subunit methyltransferase N; tRNA (adenine(37)-C(2))-methyltransferase; tRNA m2A37 methyltransferase; AK95_17035	rlmN	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKPFIYDYSLEELQAWAQENGEPAFRGTQIYDWLYVKRVNDFAEMTNLSKEFRTKLEQEFSFVTLTEITKLESKDGTVKFLFGLHDDHAIETVIMRHNYGNSICVTTQVGCRIGCTFCASTLGGLKRNLTSGEIVAQVVQAQKILDKTGERVSSIVIMGSGEPFENYEATMKFLRTMIHEKGLNIGQRHITVSTSGIVPNIYKFTEEDTQINLAISIHAPNDKLRSKLMPVNRRFPFDDVIESLRYYQAKTGRRITFEYALIGGVNDQVEHAEELADVIKDMNCFVNLIPVNHVPERKYVRTSRNDIFKFQRALADKGVNVTIRREQGHDIAAACGQLRAKHMELR	.	Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.	.	.	A0A1S2EVL7_9BACL	Unreviewed	.	.	.	.	.	.
Mol01054	Protein	"Probable peptidoglycan D,D-transpeptidase PenA (PENA)"	Penicillin-binding protein 2; PBP-2	penA	.	Neisseria gonorrhoeae	485	Neisseria gonorrhoeae	Neisseria	482	Neisseriaceae	481	Neisseriales	206351	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MLIKSEYKPRMLPKEEQVKKPMTSNGRISFVLMAMAVLFACLIARGLYLQTVTYNFLKEQGDNRIVRTQALPATRGTVSDRNGAVLALSAPTESLFAVPKDMKEMPSAAQLERLSELVDVPVDVLRNKLEQKGKSFIWIKRQLDPKVAEEVKALGLENFVFEKELKRHYPMGNLFAHVIGFTDIDGKGQEGLELSLEDSLYGEDGAEVVLRDRQGNIVDSLDSPRNKAPQNGKDIILSLDQRIQTLAYEELNKAVEYHQAKAGTVVVLDARTGEILALANTPAYDPNRPGRADSEQRRNRAVTDMIEPGSAIKPFVIAKALDAGKTDLNERLNTQPYKIGPSPVRDTHVYPSLDVRGIMQKSSNVGTSKLSARFGAEEMYDFYHELGIGVRMHSGFPGETAGLLRNWRRWRPIEQATMSFGYGLQLSLLQLARAYTALTHDGVLLPLSFEKQAVAPQGKRIFKESTAREVRNLMVSVTEPGGTGTAGAVDGFDVGAKTGTARKFVNGRYADNKHVATFIGFAPAKNPRVIVAVTIDEPTAHGYYGGVVAGPPFKKIMGGSLNILGISPTKPLTAAAVKTPS	.	Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.	PDB: 3EQU; PDB: 3EQV; PDB: 4U3T; PDB: 5KSH; PDB: 6HZJ; PDB: 6P52; PDB: 6P53; PDB: 6P54; PDB: 6P55; PDB: 6P56; PDB: 6VBM; PDB: 6XQV; PDB: 6XQX; PDB: 6XQY; PDB: 6XQZ	.	PBP2_NEIGO	Reviewed	.	.	.	.	.	.
Mol01055	Protein	HBV Polymerase/reverse transcriptase domain (HBV RT)	HBV RT	.	1403460	Hepatitis B virus genotype C	2764122	Hepatitis B virus genotype C	Orthohepadnavirus	10405	Hepadnaviridae	10404	Blubervirales	2732515	Revtraviricetes	2732514	Artverviricota	2732409	Pararnavirae	2732397	.	MPLSYQHFRKLLLLDDEAGPLEEELPRLADEGLNRRVAEDLNLGNLNVSIPWTHKVGNFTGLYSSTVPVFNPDWKTPSFPHIHLQEDIINRCQQYVGPLTVNEKRRLKLIMPARFYPNLTKYLPLDKGIKPYYPEYAVNHYFKTRHYLHTLWKAGILYKRETTRSASFCGSPYSWEQELQHGRLVFQTSTRHGDESFCSQSSGILSRSPVGPCVRSQLKQSRLGLQPQQGSLARGKSGRSGSIWSRVHPTTRRPFGVEPSGSGHIDNTASSTSSCLHQSAVRKTAYSHLSTSKRQSSSGHAVELHNIPPSSARSQSEGPIFSCWWLQFRNSKPCSDYCLTHIVNLLEDWGPCTEHGEHNIRIPRTPARVTGGVFLVDKNPHNTTESRLVVDFSQFSRGSTHVSWPKFAVPNLQSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLVGSSGLPRYVARLSSTSRNINYQHGTMQNLHDSCSRNLYVSLLLLYKTFGRKLHLYSHPIILGFRKIPMGVGLSPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGAKSVQHLESLFTSITNFLLSLGIHLNPNKTKRWGYSLNFMGYVIGSWGTLPQEHIVQKLKQCFRKLPVNRPIDWKVCQRIVGLLGFAAPFTQCGYPALMPLYACIQSKQAFTFSPTYKAFLCKQYLNLYPVARQRSGLCQVFADATPTGWGLAIGHRRMRGTFVAPLPIHTAELLAACFARSRSGAKLIGTDNSVVLSRKYTSFPWLLGCAANWILRGTSFVYVPSALNPADDPSRGRLGLYRPLLHLPFRPTTGRTSLYAVSPSVPSHLPDRVHFASPLHVAWRPP	.	.	PDB: 2LZP; PDB: 2LZQ; PDB: 2MKB	.	DPOL_HBVCJ (357-600)	Reviewed	.	.	.	.	.	.
Mol01056	Protein	Protein SNQ2 (SNQ2)	YDR011W; YD8119.16	SNQ2	851574	Saccharomyces cerevisiae	4932	Saccharomyces cerevisiae	Saccharomyces	4930	Saccharomycetaceae	4893	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSNIKSTQDSSHNAVARSSSASFAASEESFTGITHDKDEQSDTPADKLTKMLTGPARDTASQISATVSEMAPDVVSKVESFADALSRHTTRSGAFNMDSDSDDGFDAHAIFESFVRDADEQGIHIRKAGVTIEDVSAKGVDASALEGATFGNILCLPLTIFKGIKAKRHQKMRQIISNVNALAEAGEMILVLGRPGAGCSSFLKVTAGEIDQFAGGVSGEVAYDGIPQEEMMKRYKADVIYNGELDVHFPYLTVKQTLDFAIACKTPALRVNNVSKKEYIASRRDLYATIFGLRHTYNTKVGNDFVRGVSGGERKRVSIAEALAAKGSIYCWDNATRGLDASTALEYAKAIRIMTNLLKSTAFVTIYQASENIYETFDKVTVLYSGKQIYFGLIHEAKPYFAKMGYLCPPRQATAEFLTALTDPNGFHLIKPGYENKVPRTAEEFETYWLNSPEFAQMKKDIAAYKEKVNTEKTKEVYDESMAQEKSKYTRKKSYYTVSYWEQVKLCTQRGFQRIYGNKSYTVINVCSAIIQSFITGSLFYNTPSSTSGAFSRGGVLYFALLYYSLMGLANISFEHRPILQKHKGYSLYHPSAEAIGSTLASFPFRMIGLTCFFIILFFLSGLHRTAGSFFTIYLFLTMCSEAINGLFEMVSSVCDTLSQANSISGILMMSISMYSTYMIQLPSMHPWFKWISYVLPIRYAFESMLNAEFHGRHMDCANTLVPSGGDYDNLSDDYKVCAFVGSKPGQSYVLGDDYLKNQFQYVYKHTWRNFGILWCFLLGYVVLKVIFTEYKRPVKGGGDALIFKKGSKRFIAHADEESPDNVNDIDAKEQFSSESSGANDEVFDDLEAKGVFIWKDVCFTIPYEGGKRMLLDNVSGYCIPGTMTALMGESGAGKTTLLNTLAQRNVGIITGDMLVNGRPIDASFERRTGYVQQQDIHIAELTVRESLQFSARMRRPQHLPDSEKMDYVEKIIRVLGMEEYAEALVGEVGCGLNVEQRKKLSIGVELVAKPDLLLFLDEPTSGLDSQSSWAIIQLLRKLSKAGQSILCTIHQPSATLFEEFDRLLLLRKGGQTVYFGDIGKNSATILNYFERNGARKCDSSENPAEYILEAIGAGATASVKEDWHEKWLNSVEFEQTKEKVQDLINDLSKQETKSEVGDKPSKYATSYAYQFRYVLIRTSTSFWRSLNYIMSKMMLMLVGGLYIGFTFFNVGKSYVGLQNAMFAAFISIILSAPAMNQIQGRAIASRELFEVRESQSNMFHWSLVLITQYLSELPYHLFFSTIFFVSSYFPLRIFFEASRSAVYFLNYCIMFQLYYVGLGLMILYMSPNLPSANVILGLCLSFMLSFCGVTQPVSLMPGFWTFMWKASPYTYFVQNLVGIMLHKKPVVCKKKELNYFNPPNGSTCGEYMKPFLEKATGYIENPDATSDCAYCIYEVGDNYLTHISSKYSYLWRNFGIFWIYIFFNIIAMVCVYYLFHVRQSSFLSPVSILNKIKNIRKKKQ	.	"Could be an ATP-dependent permease. Confers hyper-resistance to the mutagens 4-nitroquinoline-N-oxide (4-NQO) and triaziquone, as well as to the chemicals sulphomethuron methyl phenanthroline when present in multiple copies. Exhibits nucleoside triphosphatase activity."	.	.	SNQ2_YEAST	Reviewed	.	.	.	.	.	.
Mol01057	Protein	Protein TetT (TETT)	tetT; TetT	tetT	.	Streptococcus pyogenes	1314	Streptococcus pyogenes	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTVTEGLLYKSGAINKIGRVDNATTTTDSMELERDRGITIRASTVSFNYNDTKVNIIDTPGHMDFIAEVERTLKVLDGAILVISAKEGIQVQTKVIFNTLVKLNIPTLIFVNKIDRKGVCLDEIYTQIQEKLTSNLAIMQSVKIKDKGDFELTNVRDDKVIQSQIIEKLLDINDYLAEKYINGDVIAEKEYNDVFLDEINNCNLYPVFHGSALKNIGIDELLFAITKYLPTKSYNTEDLLSAYVYKIDRDEKSRKMTFLRVFSGNIRTRQDVYINGTEETFKIKSLESIMNGEIVKVGQVNSGDIAIISNANSLKIGDYIGKKYDGILDIKIAQPALRASIKPCDLSKRSKLIEALFELTEEDPFLDCEINGDTGEIILRLFGNIQMEVIESLLKSRYKIDARFGELKTIYKERPKRNSKAVIHIEVPPNPYWASIGLSIEPLPIGSGLLYKTEVSYGYLNNSFQNAVKDAVEKACKEGLYGWEVTDLKVTFDYGLYYSPVSTPSDFRNLTPYVFWEALRKAGTEILEPYLKYTVQVPNDFCGRVMSDLRKMRASIEDIIAKGEETTLSGKIPVDTSKSYQSELLSYSNGKGIFITEPYGYDIYNDKPIINDIGNDNNDSNKEGLRYLFQKQDEN	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	Q9RLW0_STRPY	Unreviewed	.	.	.	.	.	.
Mol01058	Protein	Putative ABC transporter ATP-binding component (OTRC)	otrC; Putative ABC transporter ATP-binding component	otrC	.	Streptomyces rimosus	1927	Streptomyces rimosus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGPXGAAXXRGALPAHVXGPDAGRRPWRFXTWCANRRALRRTIGXHRPVRXGRRESFSGRENLYMIGRXLDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIAQAGLDGIAGATADHEDGVVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQLXEVFLAITGQKTSEAADGGPQDGPQDQQGVQDKQYEEVPA	.	.	.	.	Q6R7P5_STRRM	Unreviewed	.	.	.	.	.	.
Mol01059	Protein	Putative chloroquine resistance transporter (PVCRT)	Probable transporter cg10; pvcg10; pfcrt ortholog; pvcrt-o; CRT-O; PVX_087980	CG10	5472721	Plasmodium vivax	5855	Plasmodium vivax	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MTILKKKKKGSPQITPDERYRELDSHAQNESEIQEDVPISRKIANFLKLAYNEIRENISIYLLIIVYLCVCVMNKLLAKRTLKKIGNYSFVTSETHNCICMVVFFALYFMFGRRVMSAKERHRNFGVQFLLISLLDACSVIIAFIGLTRTTGNIQSFVMQLSIPINMFFCFLILRYRYHLFNYVGAFIIVVTIAVVEFMLSFETQEENSIVFNLVLIASLIPLSFSNMTREIVFKKYKINILRLNAVVSFFQIFTSCLMLPMYTLPFLKQINLPFSEIGTNIKNGFRCLFLGQNTIVENCGLGMSKMCDDCEGAWKTFIAYSFFNICDNLITSFIIEKFSTMTYTIVSCIQGPAIAIAYYFKFLAGDAVMQPRMLDFVTLFGYLFGSIIYRIGNIILEKKRMMEAGNDDDSEGELTNADSIITH	.	May regulate endogenous transporter.	.	.	CRT_PLAVS	Reviewed	.	.	.	.	.	.
Mol01060	Protein	Fur1 uracil phosphoribosyltransferase (FUR1)	fur1; EC 2.4.2.9	fur1	.	Candida albicans	5476	Candida albicans	Candida	1535326	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSVAKAVSKNVILLPQTNQLIGLYSIIRDQRTKRGDFVFYSDRIIRLLVEEGLNQLPVEEAIIKCHGGYEYKGAKFLGKICGVSIVRAGESMEMGLRDCCRSVRIGKILIQRDEETALPKLFYEKLPEDISERYVFLLDPMLATGGSAMMAVEVLLARGVKMDRILFLNLLAAPEGIKAFQDKYPDVKIITGGIDEKLDENKYIVPGLGDFGDRYYCI	.	.	.	.	G1UA34_CANAX	Unreviewed	.	.	.	.	.	.
Mol01061	Protein	Pyruvate dehydrogenase E1 component subunit alpha (PDHA1)	PDHE1-A type I; Pdha-1	Pdha1	18597	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000033662.9, Pdha1-201, 2848; ENSMUST00000127535.2, Pdha1-203, 457; ENSMUST00000156531.2, Pdha1-204, 729; ENSMUST00000126440.2, Pdha1-202, 629"	MRKMLAAVSRVLAGSAQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLPVRAILAELTGRRGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATKFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS	chr X: 158905205-158921409[-] 	"The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle."	.	.	ODPA_MOUSE	Reviewed	ENSMUSG00000031299	.	.	.	.	.
Mol01062	Protein	Quinolone efflux pump (QEPA2)	qepA2; Quinolone efflux pump	qepA2	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSATLHDTAADRRKATRREWIGLAVVALPCLVYAMDLTVLNLALPVLSRELQPSSAQLLWILDIYGFFVAGFLITMGTLGDRIGRRRLLLIGAAFFAFGSVLAALADTAALLIAARALLGLAGATIAPSTMALIRNMFHDPRQRQFAIGVWIAAFSLGSAIGPLVGGVLLEFFHWGAVFWLNVPVMLLTLALGPRFLPEYRDPDAGHLDLASVLLSLAAVLLTIYGLKQLAEHGAGLASMAALLAGLAVGALFLRRQGHIAYPLLDLRLFAHAPFRAALAAYALAALAMFGVYIFMTQYLQLVLGLSPLQAGLATLPWSLCFVIGSLLSPQLAARWPAARILVVGLSAAAFGFAVLGLGQGLWWLVPATIVMGLGLAPVFTIGNEIIITSAPSERAGAASALSETVSEFSGALGIALFGSVGLVVYRQALTSAALPGLPADALQAAGASLGGAVHLADTLPAWQGAALLAAARAGFTDALQATAWAGAVLVLVAAGLVARLLRKRPALASG	.	.	.	.	B5AG18_ECOLX	Unreviewed	.	.	.	.	.	.
Mol01063	Protein	Quinolone resistance protein NorA (NORA)	.	norA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNKQIFVLYFNIFLIFLGIGLVIPVLPVYLKDLGLTGSDLGLLVAAFALSQMIISPFGGTLADKLGKKLIICIGLILFSVSEFMFAVGHNFSVLMLSRVIGGMSAGMVMPGVTGLIADISPSHQKAKNFGYMSAIINSGFILGPGIGGFMAEVSHRMPFYFAGALGILAFIMSIVLIHDPKKSTTSGFQKLEPQLLTKINWKVFITPVILTLVLSFGLSAFETLYSLYTADKVNYSPKDISIAITGGGIFGALFQIYFFDKFMKYFSELTFIAWSLLYSVVVLILLVFANGYWSIMLISFVVFIGFDMIRPAITNYFSNIAGERQGFAGGLNSTFTSMGNFIGPLIAGALFDVHIEAPIYMAIGVSLAGVVIVLIEKQHRAKLKEQNM	.	Involved in quinolone resistance. May constitute a membrane-associated active efflux pump of hydrophilic quinolones.	.	.	NORA_STAAU	Reviewed	.	.	.	.	.	.
Mol01064	Protein	Quinolone resistance protein NorB (NORB)	SAOUHSC_01448	norB	3920226	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MEKPSREAFEGNNKLLIGIVLSVITFWLFAQSLVNVVPILEDSFNTDIGTVNIAVSITALFSGMFVVGAGGLADKYGRIKLTNIGIILNILGSLLIIISNIPLLLIIGRLIQGLSAACIMPATLSIIKSYYIGKDRQRALSYWSIGSWGGSGVCSFFGGAVATLLGWRWIFILSIIISLIALFLIKGTPETKSKSISLNKFDIKGLVLLVIMLLSLNILITKGSELGVTSLLFITLLAIAIGSFSLFIVLEKRATNPLIDFKLFKNKAYTGATASNFLLNGVAGTLIVANTFVQRGLGYSSLQAGSLSITYLVMVLIMIRVGEKLLQTLGCKKPMLIGTGVLIVGECLISLTFLPEIFYVICCIIGYLFFGLGLGIYATPSTDTAIANAPLEKVGVAAGIYKMASALGGAFGVALSGAVYAIVSNMTNIYTGAMIALWLNAGMGILSFVIILLLVPKQNDTQL	.	"Multidrug efflux pump that acts independently of NorA and is one of the factors that confers resistance against diverse quinolones and chemical compounds. Extrudes norfloxacin, ciprofloxacin, cetrimide, tetraphenylphosphonium ion (TPP), sparfloxacin, moxifloxacin and ethidium bromide. Contributes also to the efflux of tetracycline."	.	.	NORB_STAA8	Reviewed	.	.	.	.	.	.
Mol01065	Protein	Ras association domain-containing protein 8 (RASSF8)	RASSF8; Fragment	RASSF8	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MELKVWVDGVQRIVCGVTEVTTCQEVVIALAQAIGRTGRYTLIEKWRDTERHLAPHENPIISLNKWGQYASDVQLILRRTGPSLSERPTSDSVARIPERTLYRQSLPPLAKLRPQIDKSIKRREPKRKSLTFTGGAKGLMDIFGKGKETEFKQKVLNNCKTTADELKKLIRLQTEKLQSIEKQLESNEIEIRFWEQKYNSNLEEEIVR	.	.	.	HGNC:13232	F5H0S5_HUMAN	Unreviewed	.	.	.	.	.	.
Mol01067	Protein	Renal carcinoma antigen NY-REN-56 (PFKFB3)	6PF-2-K/Fru-2;6-P2ase 3; PFK/FBPase 3; 6PF-2-K/Fru-2;6-P2ase brain/placenta-type isozyme; Renal carcinoma antigen NY-REN-56; iPFK-2	PFKFB3	5209	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000379775.9, PFKFB3-203, 4482; ENST00000360521.7, PFKFB3-202, 4524; ENST00000379789.8, PFKFB3-205, 4157; ENST00000640683.1, PFKFB3-219, 2311; ENST00000536985.6, PFKFB3-215, 2094; ENST00000379785.5, PFKFB3-204, 2181; ENST00000317350.8, PFKFB3-201, 1999; ENST00000626882.2, PFKFB3-217, 1965; ENST00000625260.2, PFKFB3-216, 1752; ENST00000450232.1, PFKFB3-208, 595; ENST00000639949.1, PFKFB3-218, 587; ENST00000414237.5, PFKFB3-206, 513; ENST00000441697.1, PFKFB3-207, 244; ENST00000467491.5, PFKFB3-210, 2131; ENST00000461744.5, PFKFB3-209, 2098; ENST00000490474.5, PFKFB3-214, 2086; ENST00000477914.5, PFKFB3-212, 2063; ENST00000475881.5, PFKFB3-211, 536; ENST00000487989.1, PFKFB3-213, 661"	MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH	chr10:6144934-6254644[+]	"Synthesis and degradation of fructose 2,6-bisphosphate."	PDB: 2AXN; PDB: 2DWO; PDB: 2DWP; PDB: 2I1V; PDB: 3QPU; PDB: 3QPV; PDB: 3QPW; PDB: 4D4J; PDB: 4D4K; PDB: 4D4L; PDB: 4D4M; PDB: 4MA4; PDB: 5AJV; PDB: 5AJW; PDB: 5AJX; PDB: 5AJY; PDB: 5AJZ; PDB: 5AK0; PDB: 6ETJ; PDB: 6HVH; PDB: 6HVI; PDB: 6HVJ; PDB: 6IBX; PDB: 6IBY; PDB: 6IBZ; PDB: 6IC0	HGNC:8874	F263_HUMAN	Reviewed	ENSG00000170525	.	.	.	.	.
Mol01068	Protein	Ribonuclease PH (RPH)	RNase PH; tRNA nucleotidyltransferase; LMOf2365_1247	rph	.	Listeria monocytogenes	1639	Listeria monocytogenes	Listeria	1637	Listeriaceae	186820	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MRVDGRESNALRNIEVTPDYLMHPEGSVLIASGNTKVICSASVETKVPPFMRGEGRGWISAEYSMLPRATNTRNIRESSKGKVTGRTMEIQRLIGRALRAVVDLDALGERTIWLDCDVIQADGGTRTASITGAFIAMVMAIAKLDEAVPFAKFPVKDFLAATSVGVLEEGGTVLDLNYVEDSAAQVDMNIIMTGSGAFVELQGTGEEATFSETELAELIALGKKGISELIEIQKETLGDKVTARIKGE	.	"Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation."	.	.	RNPH_LISMF	Reviewed	.	.	.	.	.	.
Mol01069	Protein	Ribosomal RNA large subunit methyltransferase Cfr (CFRB)	23S rRNA (adenine(2503)-C(8))-methyltransferase; 23S rRNA m8A2503 methyltransferase; cfr	cfr(B)	.	Enterococcus faecium	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MQQKNKYIRIQEFLKQNKFPNYRMKQITNAIFPGRINNFNEITVLPKSLRDMLIEEFGESILNIVPLKAQQSTQVSKVLFGISGDEKIETVNMKYKAGWESFCISSQCGCNFGCKFCATGDIGLKRNLTSDEITDQILYFHLQGHSIDSISFMGMGEALANVQVFDALNVLTDPALFALSPRRLSISTIGIIPNIKKLTQNYPQVNLTFSLHSPFNEQRSELMPINERYPLSDVMDTLDEHIRVTSRKVYIAYIMLHGVNDSIEHAKEVVNLLRGRYRSGNLYHVNIIRYNPTVSSRMRFEEANEKCLVNFYKKLKSAGIKVTIRSQFGIDIDAACGQLYGNYQKTNSQ	.	Specifically methylates position 8 of adenine 2503 in 23S rRNA. Confers resistance to some classes of antibiotics.	.	.	A0A0K1TBR6_ENTFC	Unreviewed	.	.	.	.	.	.
Mol01070	Protein	Ribosomal RNA large subunit methyltransferase N (CFRC)	cfrC; Ribosomal RNA large subunit methyltransferase N	cfrC	.	Clostridioides difficile	1496	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MSKYKKMKQLIADMRLPEYRYKQLLDAVFLQGIMRFEDMKLLPKTLREKLVEQFGETVVEIKAIHHEKSMQTDKVLFELSDGNRVETVGLFYKEGWNSFCISSQSGCGFGCKFCATGTLGLRRNLTVDEITDQILYFMQQGCSINSISFMGMGEPFANPQVFEALHDLTAPELFGLSRRRITISTIGIVPGIQKLTREYPQVNLAYSLHAPTDRLRETLMPITKTYPLGQVLDTLDQHIRQTNRKVFLAYIMLKDVNDSDRHAEQLTKLLFKHKKYLPLYHLDLIPYNQTTVTETMVPSSHTRIKAFCRIIHNAGISVNIRTQFGSDINAACGQLAGAYRDDQKQGERTMSARDVKSFGEEVCEYGFYNQGAMRSTNSS	.	.	.	.	A0A2R4QH65_CAMCO	Unreviewed	.	.	.	.	.	.
Mol01071	Protein	Ribosomal tetracycline resistance protein tet(44) (TET44)	aacC1; RCS36_PI-II0023; 3)-I); EC 2.3.1.60	tet(44)	.	Campylobacter fetus subsp. fetus	32019	Campylobacter fetus subsp. fetus	Campylobacter	194	Campylobacteraceae	72294	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MKIINIGILAHVDAGKTTLTESLLYTSGAILELGSVDKGTTRTDTMFLERQRGITIQAAVTSFNWNDYKINIVDTPGHTDFITEVYRSLSVLDGAILVISAKDGVQAQTRILFHALQKMNIPTIIFINKIDQDGINLNNIYQNIKEKLSNDIIVMQNVTLTPEISIKNIIDLDDWDPVISKNDKLLEKYIVGEKLTIQELMYEEYRCVKKGSLFPIYHGSARNNIGTQQLIEAISNLFCSEMNENDSELCGRVFKIEYTDHKQRLVYLRLYSGTLHLRDTIILPEKKKVKLTEIYIPSNGEMIQTKTVCSGDIFIIPNNTLRLNDIIGNEKLLPCNVWNDKTVPILRTRIEPIKIEEREKLLDALTEIADTDPLLRYYVDTITHEIIISFLGTVQLEVICSLLIEKYHINIRIEDPTVIYLEKPLQKADYTIHIEVPPNPFWASIGLSITPLPIGSGIQYESKVSLGYLNQSFQNAVREGINYGLEQGLYGWEVTDCKICFEYGVYYSPVSTPSDFRFLAPIVLEQTLKKAGTQLLEPYLSFILFTPQGYFSRAYKDAQKHCAIIETSQSKNDEVIFTGHIPVRCINEYRNTLTLYTNGQAVFLTELKDYQIATCEPVIQSRRPNNRIDKVRHMFNKKEN	.	.	.	.	D8L9Y9_CAMFE	Unreviewed	.	.	.	.	.	.
Mol01072	Protein	Rifampin monooxygenase (IRI)	iri; Rifampin monooxygenase	iri	.	Rhodococcus equi	43767	Rhodococcus equi	Rhodococcus	1827	Nocardiaceae	85025	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSDVIIVGAGPTGLMLAGELRLQGVDVVVVDKDEEPTQFVRALGIHVRSIEIMEQRGLLDKFLAHGRKYPLGGFFAGISKPAPAHLDTAHGYVLGIPQPEIDRILAEHATEVGADIQRGKRVVAIRQDTDNVAAELSDGTTLHARYLVGCDGGRSTVRKLRSTSVFPASRTSADTLIGEMDVTMPADELAAVVAEIRETHKRFGVGPAGNGAFRVVVPAAEVADGRATPTTLDDIKQQLLAIAGTDFGVHSPRWLSRFGDATRLADDYRRDRVFLAGDAAHIHPPMGGQGLNLGVQDAFNLGWKLAAEINGWAPVGLLDTYESERRPVAADVLDNTRAQAELISTAAGPQAVRRLISELMEFEDVKRYLTEKITAISIRYDFGEGDDLLGRRLRNIALTRGNLYDLMRSGRGLLLDQGGQLSVDGWSDRADHIVDTSTELEAPAVLLRPDGHVAWIGDAQAELDTQLSTWFGRSARDRA	.	.	.	.	P95598_RHOHA	Unreviewed	.	.	.	.	.	.
Mol01073	Protein	Rifampin phosphotransferase (RPHB)	rphB; AK95_09435; RphB	rphB	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MRSLVLDFQEMDKKQLGLVGGKGLHLGELSKIEGIRVPEGFCVTTIGYQRAIEQNETYQAMLNRLTMLSAEDRDQMVEISRKIRQTIMEVEIPSDVVTAVTRYLSRFGEEQAYAVRSSATAEDLPHASFAGQQDTYLNIIGVDAILQHISKCWASLFTDRAVIYRMQNGFDHRQVYLSVVVQRMVFPEASGILFTADPMTSNRKLLSIDAGFGLGEALVSGLVSADGYKVREGEIIEKRIAAKTLAIYGRKEGGTETKQIDPDQQKSQTLTDEQILQLARIGRQIEAHFGQPQDIEWCLAQDTFYIVQSRPITTLYPIPEANDQENHVYVSVGHQQMMTDPMKPLGLSFFLLTTPAPMRTAGGRLFVDTTAMLASPVSRENVLNTLGQSDPLIKDALMTILERGDFIKSLPIAENEQTPGKNNISSAGYQTPIDHDPTIVSDLMERTQSSIEVLKQNIQTKSGSDLFDFILEDIQELKKNLFDPQSSAVIMAAMNASTWINEKMNEWLGEKNAADTLSQSVPGNVTSEMGLALLDVADVIRPYPEIIDYLEQAKDDHFLDKLLTFDGGQQAQDAILDFLDKYGMRCAGEIDLTRTRWSEKPIALVPLILGNIKNFEPNASHRKFEQGRQEALKKEQELLDRLKQLPDGEGKAQETKRMIDLIRNFMGYREYPKYGMVNRYFIYKQALLKEAERLVQAGVIHHKEDIYYLTFEELDEVVRTNKLDNPGSMVEQQAKLAIRQMISKRKEEYNVFEKLTPPRVITSDGEIIAGEYKRENIPAEAIVGLPVSSGTVEGRARVILNMKDADLEEGDILVTAFTDPSWTPLFVSIKGLVTEVGGLMTHGAVIAREYGLPAVVGVENATKRIKDGQRIRVHGSEGYIEILS	.	.	.	.	A0A1I9ZL18_9BACL	Unreviewed	.	.	.	.	.	.
Mol01074	Protein	rRNA adenine N-6-methyltransferase ermC' (ERMC)	Erythromycin resistance protein; Macrolide-lincosamide-streptogramin B resistance protein	ermC'	.	Bacillus subtilis	1423	Bacillus subtilis	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNEKNIKHSQNFITSKHNIDKIMTNIRLNEHDNIFEIGSGKGHFTLELVQRCNFVTAIEIDHKLCKTTENKLVDHDNFQVLNKDILQFKFPKNQSYKIFGNIPYNISTDIIRKIVFDSIADEIYLIVEYGFAKRLLNTKRSLALFLMAEVDISILSMVPREYFHPKPKVNSSLIRLNRKKSRISHKDKQKYNYFVMKWVNKEYKKIFTKNQFNNSLKHAGIDDLNNISFEQFLSLFNSYKLFNK	.	"This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics."	PDB: 1QAM; PDB: 1QAN; PDB: 1QAO; PDB: 1QAQ; PDB: 2ERC	.	ERM_BACIU	Reviewed	.	.	.	.	.	.
Mol01075	Protein	rRNA adenine N-6-methyltransferase ermE (ERME)	NMT; Erythromycin resistance protein; Macrolide-lincosamide-streptogramin B resistance protein; SACE_0733	ermE	.	Saccharopolyspora erythraea	1836	Saccharopolyspora erythraea	Saccharopolyspora	1835	Pseudonocardiaceae	2070	Pseudonocardiales	85010	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSSSDEQPRPRRRNQDRQHPNQNRPVLGRTERDRNRRQFGQNFLRDRKTIARIAETAELRPDLPVLEAGPGEGLLTRELADRARQVTSYEIDPRLAKSLREKLSGHPNIEVVNADFLTAEPPPEPFAFVGAIPYGITSAIVDWCLEAPTIETATMVTQLEFARKRTGDYGRWSRLTVMTWPLFEWEFVEKVDRRLFKPVPKVDSAIMRLRRRAEPLLEGAALERYESMVELCFTGVGGNIQASLLRKYPRRRVEAALDHAGVGGGAVVAYVRPEQWLRLFERLDQKNEPRGGQPQRGRRTGGRDHGDRRTGGQDRGDRRTGGRDHRDRQASGHGDRRSSGRNRDDGRTGEREQGDQGGRRGPSGGGRTGGRPGRRGGPGQR	.	"This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics."	PDB: 6NVM	.	ERME_SACEN	Reviewed	.	.	.	.	.	.
Mol01076	Protein	rRNA adenine N-6-methyltransferase ermF (ERMF)	Erythromycin resistance protein; Macrolide-lincosamide-streptogramin B resistance protein	ermF	.	Bacteroides fragilis	817	Bacteroides fragilis	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MTKKKLPVRFTGQHFTIDKVLIKDAIRQANISNQDTVLDIGAGKGFLTVHLLKIANNVVAIENDTALVEHLRKLFSDARNVQVVGCDFRNFAVPKFPFKVVSNIPYGITSDIFKILMFESLGNFLGGSIVLQLEPTQKLFSRKLYNPYTVFYHTFFDLKLVYEVGPESFLPPPTVKSALLNIKRKHLFFDFKFKAKYLAFISYLLEKPDLSVKTALKSIFRKSQVRSISEKFGLNLNAQIVCLSPSQWLNCFLEMLEVVPEKFHPS	.	Involved in erythromycin resistance.	.	.	ERMF_BACFG	Reviewed	.	.	.	.	.	.
Mol01077	Protein	rRNA adenine N-6-methyltransferase ermG (ERMG)	Erythromycin resistance protein; Macrolide-lincosamide-streptogramin B resistance protein	ermG	60292698	Bacillus sphaericus	1421	Lysinibacillus sphaericus	Lysinibacillus	400634	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNKVNIKDSQNFITSKYHIEKIMNCISLDEKDNIFEIGAGKGHFTAELVKRCNFVTAIEIDSKLCEVTRNKLLNYPNYQIVNDDILKFTFPSHNPYKIFGSIPYNISTNIIRKIVFESSATISYLIVEYGFAKRLLDTNRSLALLLMAEVDISILAKIPRYYFHPKPKVDSALIVLKRKPAKMAFKERKKYETFVMKWVNKEYEKLFTKNQFNKALKHARIYDINNISFEQFVSLFNSYKIFNG	.	Involved in erythromycin resistance.	.	.	ERMG_LYSSH	Reviewed	.	.	.	.	.	.
Mol01078	Protein	rRNA methyltransferase PikR1 (PIKR1)	pikR1; rRNA methyltransferase PikR1	pikR1	.	Streptomyces venezuelae	54571	Streptomyces venezuelae	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAMRDSIPRRADRDTLRRELGQNFLQDDRAVRNLVTHVEGDGRNVLEIGPGKGAITEELVRSFDTVTVVEMDPHWAAHVRRKFEGERVTVFQGDFLDFRIPRDIDTVVGNVPFGITTQILRSLLESTNWQSAALIVQWEVARKRAGRSGGSLLTTSWAPWYEFAVHDRVRASSFRPMPRVDGGVLTIRRRPQPLLPESASRAFQNFAEAVFTGPGRGLAEILRRHIPKRTYRSLADRHGIPDGGLPKDLTLTQWIALFQASQPSYAPGAPGTRMPGQGGGAGGRDYDSETSRAAVPGSRRYGPTRGGEPCAPRAQVRQTKGRQGARGSSYGRRTGR	.	.	.	.	Q9ZGI6_STRVZ	Unreviewed	.	.	.	.	.	.
Mol01079	Protein	rRNA methyltransferase PikR2 (PIKR2)	pikR2; rRNA methyltransferase PikR2	pikR2	.	Streptomyces venezuelae	54571	Streptomyces venezuelae	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAFSPQGGRHELGQNFLVDRSVIDEIDGLVARTKGPILEIGPGDGALTLPLSRHGRPITAVELDGRRAQRLGARTPGHVTVVHHDFLQYPLPRNPHVVVGNVPFHLTTAIMRRLLDAQHWHTAVLLVQWEVARRRAGVGGSTLLTAGWAPWYEFDLHSRVPARAFRPMPGVDGGVLAIRRRSAPLVGQVKTYQDFVRQVFTGKGNGLKEILRRTGRISQRDLATWLRRNEISPHALPKDLKPGQWASLWELTGGTADGSFDGTAGGGAAGSHGAARVGAGHPGGRVSASRRGVPQARRGRGHAVRSSTGTEPRWGRGRAESA	.	.	.	.	Q9ZGI7_STRVZ	Unreviewed	.	.	.	.	.	.
Mol01080	Protein	Sensor protein kinase WalK (WALK)	vicK; yycG	walK	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	CTVILGFFIARTITKPITDMRNQTVEMSRGNYTQRVKIYGNDEIGELALAFNNLSKRVQEAQANTESEKRRLDSVITHMSDGIIATDRRGRIRIVNDMALKMLGMAKEDIIGYYMLSVLSLEDEFKLEEIQENNDSFLLDLNEEEGLIARVNFSTIVQETGFVTGYIAVLHDVTEQQQVERERREFVANVSHELRTPLTSMNSYIEALEEGAWKDEELAPQFLSVTREETERMIRLVNDLLQLSKMDNESDQINKEIIDFNMFINKIINRHEMSAKDTTFIRDIPKKTIFTEFDPDKMTQVFDNVITNAMKYSRGDKRVEFHVKQNPLYNRMTIRIKDNGIGIPINKVDKIFDRFYRVDKARTRKMGGTGLGLAISKEIVEAHNGRIWANSVEGQGTSIFITLPCEVIEDGDWDE	.	"Member of the two-component regulatory system WalK/WalR that regulates genes involved in cell wall metabolism, virulence regulation, biofilm production, oxidative stress resistance and antibiotic resistance via direct or indirect regulation of autolysins. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue in the dimerization domain and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of WalR. In turn, WalR binds to the upstream promoter regions of the target genes to positively and negatively regulate their expression."	PDB: 4MN5; PDB: 4MN6; PDB: 4YWZ	.	WALK_STAAU	Reviewed	.	.	.	.	.	.
Mol01081	Protein	Signal peptidase I (LEPB)	SPase I; Leader peptidase I; spi; SP_0402	lepB	.	Streptococcus pneumoniae	1313	Streptococcus pneumoniae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNSFKNFLKEWGLFLLILSLLALSRIFFWSNVRVEGHSMDPTLADGEILFVVKHLPIDRFDIVVAHEEDGNKDIVKRVIGMPGDTIRYENDKLYINDKETDEPYLADYIKRFKDDKLQSTYSGKGFEGNKGTFFRSIAQKAQAFTVDVNYNTNFSFTVPEGEYLLLGDDRLVSSDSRHVGTFKAKDITGEAKFRLWPITRIGTF	.	.	.	.	LEP_STRPN	Reviewed	.	.	.	.	.	.
Mol01082	Protein	Solute carrier family 16 member 1 (SLC16A1)	MCT 1; Solute carrier family 16 member 1; MCT1	SLC16A1	6566	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000369626.8, SLC16A1-201, 3753; ENST00000538576.5, SLC16A1-207, 4374; ENST00000458229.6, SLC16A1-204, 3849; ENST00000443580.6, SLC16A1-203, 3764; ENST00000429288.2, SLC16A1-202, 3757; ENST00000679803.1, SLC16A1-208, 3647; ENST00000478835.1, SLC16A1-205, 452; ENST00000481750.1, SLC16A1-206, 430; ENST00000679846.1, SLC16A1-209, 3117"	MPPAVGGPVGYTPPDGGWGWAVVIGAFISIGFSYAFPKSITVFFKEIEGIFHATTSEVSWISSIMLAVMYGGGPISSILVNKYGSRIVMIVGGCLSGCGLIAASFCNTVQQLYVCIGVIGGLGLAFNLNPALTMIGKYFYKRRPLANGLAMAGSPVFLCTLAPLNQVFFGIFGWRGSFLILGGLLLNCCVAGALMRPIGPKPTKAGKDKSKASLEKAGKSGVKKDLHDANTDLIGRHPKQEKRSVFQTINQFLDLTLFTHRGFLLYLSGNVIMFFGLFAPLVFLSSYGKSQHYSSEKSAFLLSILAFVDMVARPSMGLVANTKPIRPRIQYFFAASVVANGVCHMLAPLSTTYVGFCVYAGFFGFAFGWLSSVLFETLMDLVGPQRFSSAVGLVTIVECCPVLLGPPLLGRLNDMYGDYKYTYWACGVVLIISGIYLFIGMGINYRLLAKEQKANEQKKESKEEETSIDVAGKPNEVTKAAESPDQKDTDGGPKEEESPV	chr1:112911847-112957593[-]	"Proton-coupled monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate. Depending on the tissue and on cicumstances, mediates the import or export of lactic acid and ketone bodies. Required for normal nutrient assimilation, increase of white adipose tissue and body weight gain when on a high-fat diet. Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate, small molecules that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis."	PDB: 6LYY; PDB: 6LZ0; PDB: 7CKO; PDB: 7CKR; PDB: 7DA5	HGNC:10922	MOT1_HUMAN	Reviewed	ENSG00000155380	.	.	.	.	.
Mol01083	Protein	Solute carrier family 2 member 4 (SLC2A4)	Glucose transporter type 4; insulin-responsive; GLUT-4; Glut4	Slc2a4	25139	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSRNOT00000023256.6, Slc2a4-202, 2543; ENSRNOT00000113573.1, Slc2a4-201, 2321; ENSRNOT00000095666.1, Slc2a4-203, 1613"	MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLAITVLPALLQLLLLPFCPESPRYLYIIRNLEGPARKSLKRLTGWADVSDALAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFELAGVEQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPSMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLRVPETRGRTFDQISATFRRTPSLLEQEVKPSTELEYLGPDEND	Primary_assembly 10: 54666015-54671565[-] 	"Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell."	.	.	GLUT4_RAT	Reviewed	ENSRNOG00000017226	.	.	.	.	.
Mol01084	Protein	Solute carrier family 29 member 1 (SLC29A1)	Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter; Equilibrative NBMPR-sensitive nucleoside transporter; Nucleoside transporter; es-type; Solute carrier family 29 member 1; ENT1	SLC29A1	2030	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371755.9, SLC29A1-206, 2083; ENST00000651428.1, SLC29A1-222, 2358; ENST00000371724.6, SLC29A1-203, 2301; ENST00000371713.6, SLC29A1-202, 2283; ENST00000393844.7, SLC29A1-208, 2204; ENST00000371708.1, SLC29A1-201, 2159; ENST00000652453.1, SLC29A1-223, 2030; ENST00000652680.1, SLC29A1-224, 1998; ENST00000647460.1, SLC29A1-221, 975; ENST00000371740.10, SLC29A1-205, 928; ENST00000371731.6, SLC29A1-204, 906; ENST00000646582.1, SLC29A1-219, 829; ENST00000643028.2, SLC29A1-212, 811; ENST00000393841.6, SLC29A1-207, 745; ENST00000645692.1, SLC29A1-217, 624; ENST00000643869.1, SLC29A1-214, 571; ENST00000645259.1, SLC29A1-215, 537; ENST00000642777.1, SLC29A1-211, 438; ENST00000646251.1, SLC29A1-218, 746; ENST00000472176.2, SLC29A1-209, 1434; ENST00000645607.1, SLC29A1-216, 1042; ENST00000642613.1, SLC29A1-210, 935; ENST00000646878.1, SLC29A1-220, 890; ENST00000643152.1, SLC29A1-213, 570"	MTTSHQPQDRYKAVWLIFFMLGLGTLLPWNFFMTATQYFTNRLDMSQNVSLVTAELSKDAQASAAPAAPLPERNSLSAIFNNVMTLCAMLPLLLFTYLNSFLHQRIPQSVRILGSLVAILLVFLITAILVKVQLDALPFFVITMIKIVLINSFGAILQGSLFGLAGLLPASYTAPIMSGQGLAGFFASVAMICAIASGSELSESAFGYFITACAVIILTIICYLGLPRLEFYRYYQQLKLEGPGEQETKLDLISKGEEPRAGKEESGVSVSNSQPTNESHSIKAILKNISVLAFSVCFIFTITIGMFPAVTVEVKSSIAGSSTWERYFIPVSCFLTFNIFDWLGRSLTAVFMWPGKDSRWLPSLVLARLVFVPLLLLCNIKPRRYLTVVFEHDAWFIFFMAAFAFSNGYLASLCMCFGPKKVKPAEAETAGAIMAFFLCLGLALGAVFSFLFRAIV	chr6:44219553-44234142[+]	Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). It is sensitive (ES) to low concentrations of the inhibitor nitrobenzylmercaptopurine riboside (NBMPR) and is sodium-independent. It has a higher affinity for adenosine. Inhibited by dipyridamole and dilazep (anticancer chemotherapeutics drugs).	PDB: 6OB6; PDB: 6OB7	HGNC:11003	S29A1_HUMAN	Reviewed	ENSG00000112759	.	.	.	.	.
Mol01085	Protein	Spectinomycin 9-adenylyltransferase (ANT)	AAD(9); spc	ant	42043718	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MSNLINGKIPNQAIQTLKIVKDLFGSSIVGVYLFGSAVNGGLRINSDVDVLVVVNHSLPQLTRKKLTERLMTISGKIGNTDSVRPLEVTVINRSEVVPWQYPPKREFIYGEWLRGEFENGQIQEPSYDPDLAIVLAQARKNSISLFGPDSSSILVSVPLTDIRRAIKDSLPELIEGIKGDERNVILTLARMWQTVTTGEITSKDVAAEWAIPLLPKEHVTLLDIARKGYRGECDDKWEGLYSKVKALVKYMKNSIETSLN	.	Mediates bacterial resistance to the antibiotic spectinomycin but not streptomycin.	.	.	S9AD_STAAU	Reviewed	.	.	.	.	.	.
Mol01086	Protein	Spectinomycin 9-O-adenylyltransferase (ANT9)	ant9; spd; SAMEA70245418_02659; EC 2.7.7.47; Spectinomycin adenyltransferase	ant9	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MEEPNKQIDNVLIELKRLFSKDLLGVYLYGSYVKGGLKKDSDVDFLVIINRDMTKEEKRILISKIMPISKEIGEDTSLKYIELTVLNYHENENWSYPPIEEFIYGEWLREDYLNYFIPEKNNNIDLTILLYQAKLSSISIYGENNINNLIPDVPFIDLQKAIKESSKELIKDFYGDETNVILTLCRMIVTYETGKFYSKDLAGSMIIENLSENLSIEENNLISLAISSYKNGNSVDWELFPVKSVIKKLYAYLNYKL	.	.	.	.	W1JB67_STAAU	Unreviewed	.	.	.	.	.	.
Mol01087	Protein	Sterol 14-alpha demethylase (CYP51C)	Cytochrome P450 monooxygenase 51C; Ergosterol biosynthesis protein cyp51C; AFLA_100590	cyp51c	.	Aspergillus flavus	5059	Aspergillus flavus	Aspergillus	5052	Aspergillaceae	1131492	Eurotiales	5042	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MSWPRIGAYALLAFVAIMALNVTYQFLFRMLNKTRPPLVFHWIPFIGSTIHYGMDPYGFFFSCREKYGDIFTFILLGRPTTVYLGTQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNSKLIEQKKFIKFGLSQAALEAHVPLIEKEVEDYLAMSPNFHGTSGEVDIPAAMAEITIFTAGSALQGEEVRSKLTTEFAVLYHDLDKGFTPINFMLPWAPLPHNKKRDAAHARMRSIYIDIINKRRNAGDNVPEKLDMIGNLMQCTYKNGQPLPDKEIAHIMITLLMAGQHSSSSISSWIMLRLASQPAVVEELYQEQLANLERTGPNGSLAPLQYKDFDNLPLHQNVIRETLRLHSSIHSLLRKVKNPLPVPGTPYVIPTSHVLLAAPGVTALSDEYFPNAMAWDPHRWETQAPQENNKDDIVDYGYGAMSKGTSSPYLPFGAGRHRCIGEKFAYLNLAVIVATMVRHLRFSNLDGQTGVPDTDYSSLFSGPMKPARIRWERRAAKSG	.	"Cytochrome P450 monooxygenase involved in the biosynthesis of ergosterol. The existence of several duplicated sterol 14-alpha demethylase genes could be a good strategy to modulate the composition and fluidity of the cell membrane. Catalyzes C14-demethylation of erburicol to produce 4,4,24-trimethyl cholesta-8,24(28)-dien-3-beta-ol. As a target of azole drugs, plays a crucial role in azole drug susceptibility."	.	.	CP51C_ASPFN	Reviewed	.	.	.	.	.	.
Mol01088	Protein	Sterol 14-alpha demethylase cyp51A (CYP51A)	Cytochrome P450 monooxygenase 51A; Ergosterol biosynthesis protein 11A; erg11A; AFUA_4G06890	cyp51A	3509526	Aspergillus fumigatus	746128	Aspergillus fumigatus	Aspergillus	5052	Aspergillaceae	1131492	Eurotiales	5042	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MVPMLWLTAYMAVAVLTAILLNVVYQLFFRLWNRTEPPMVFHWVPYLGSTISYGIDPYKFFFACREKYGDIFTFILLGQKTTVYLGVQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNSKLMEQKKFIKYGLTQSALESHVPLIEKEVLDYLRDSPNFQGSSGRVDISAAMAEITIFTAARALQGQEVRSKLTAEFADLYHDLDKGFTPINFMLPWAPLPHNKKRDAAHARMRSIYVDIITQRRLDGEKDSQKSDMIWNLMNCTYKNGQQVPDKEIAHMMITLLMAGQHSSSSISAWIMLRLASQPKVLEELYQEQLANLGPAGPDGSLPPLQYKDLDKLPFHQHVIRETLRIHSSIHSIMRKVKSPLPVPGTPYMIPPGRVLLASPGVTALSDEHFPNAGCWDPHRWENQATKEQENDKVVDYGYGAVSKGTSSPYLPFGAGRHRCIGEKFAYVNLGVILATIVRHLRLFNVDGKKGVPETDYSSLFSGPMKPSIIGWEKRSKNTSK	.	"Sterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Probable). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms."	.	.	CP51A_ASPFU	Reviewed	.	.	.	.	.	.
Mol01089	Protein	Sterol 14-alpha demethylase cyp51A (CYP51A)	ATEIFO6365_0007029700; ATETN484_0009029700	ATEIFO6365_0007029700	.	Aspergillus terreus	33178	Aspergillus terreus	Aspergillus	5052	Aspergillaceae	1131492	Eurotiales	5042	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MIMSLLTITSYSAVGILALIAWNVIRQLLFQNKSEPPVVFHWIPFLGSTISYGIDPYAFFASCRQKYGDIFTFILLGQKTTVYLGVQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNAKLMEQKKFIKYGLTQAALESHVQLIEREVLDYLRTSPNFHGASGVVDISAAMAELTIFTAGRALQGEEVRRKLTAEFADLYHDLDKGFTPINFMLPWAPLPHNRKRDAAHARMRAIYMDIIRERRAHKNPDQGEAGSDSDMIWNLMRCTYKDGRPVPDKEIAHMMITLLMAGQHSSSSISAWIFLRLASEPRVLEELYQEQVASLGKPDADGAFPPLQFRDLDRLPLHQNVVKETLRLHSSIHSIMRKVKNPLPVPGTPYVVPTSHVLLASPGVTATSDEYFPNASRWDPHRWENHAEPDDDDGEMVDYGYGRVSKGTASPYLPFGGGRHRCIGEKFAYINLGVIVATVVRHLKLFNVDGRKGVPPTDYSSLFSGPLKPAIIGWERRFPTA	.	.	.	.	A0A5M3Z4K7_ASPTE	Unreviewed	.	.	.	.	.	.
Mol01090	Protein	Sterol 14-alpha demethylase cyp51A (CYP51A)	ABL_04779	ABL_04779	.	Aspergillus niger	5061	Aspergillus niger	Aspergillus	5052	Aspergillaceae	1131492	Eurotiales	5042	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MAAIAPNPLNAPDTAVSGQSDCQHHWSLAWFDTLSKGSPSGLIRLRNHREQCLLPLLTVFANHCSGWTDVAQCQGHEPTTTYSFDVLLLTFSFTNTFPINWSFFLPTVASRMAYLAVAGAYAFAALLVAIVLNVARQLLVRNEKEPPVVFHWIPFLGSTISYGMDPYAFFFSCRKKYGDIFTFVLLGKKTTVYLGVQGNDFILNGKLKDVSAEEVYSPLTTPVFGSDVVYDCPNSKLMEQKKFIKFGLTQAALESHVQLIEKETLDYLRDSPRFNGASGVIDIPAAMAEITIYTAARALQGEEVRKKLTAEFAELYHDLDKGFSPINFMLPWAPLPHNRKRDAAHARMREIYTDIINERRKNPDEEKSDMIWNLMHCTYKNGQPVPDKEIAHMMITLLMAGQHSSSSISSWIMLRLASEPQVLEELYQEQLTSLSNRNGVFEPLQYQDLDKLPLLQSVIKETLRIHSSIHSIMRKVKNPLPVPGTSYVIPEDRVLLASPGVTALSDEYFPNATRWDPHRWENQPDKEEEGEMVDYGYGSVSKGTASPYLPFGAGRHRCIGEKFAYVNLGVIIATIVRHLKLFNVDGRKGVPGTDYSTLFSGPLKPAIVGWERRIQDNSKGSLN	.	.	.	.	A0A100IIZ2_ASPNG	Unreviewed	.	.	.	.	.	.
Mol01091	Protein	Streptomycin 3''-adenylyltransferase (AADA27)	aadA27; Streptomycin 3''-adenylyltransferase	aadA27	.	Acinetobacter lwoffii	28090	Acinetobacter lwoffii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSETLQLEQLTESLQQLLGESLFAIYLYGSAVDGGLGPESDLDVLVVVNQALTLHQRQQLAETLLKISYPIGAAQRALEVTIVLKEQILSGSYPLSYELQFGEWLREELNQGALLRAHTDPDLSILLKKAQMHHRSLLGPSLTQWSTAIPEQHLWQAMADTYPSIVAHWDEDADERNQILALCRIYFSLITNEIVPKDQAAHWVIAQLPSLHQPILQRMIQEYKGEIRKQNWQQQHQALGPVVDFLSSKIDEQFNKKSSLIK	.	.	.	.	A0A1C7ZQH8_ACILW	Unreviewed	.	.	.	.	.	.
Mol01092	Protein	Streptomycin 3''-kinase (APHE)	Streptomycin 3''-phosphotransferase; Streptomycin 6-kinase; Streptomycin 6-phosphotransferase	aphE	.	Streptomyces griseus	1911	Streptomyces griseus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSDHPGPGAVTPELFGVGGDWLAVTAGESGASVFRAADATRYAKCVPAADAAGLEAERDRIAWLSGQGVPGPRVLDWYAGDAGACLVTRAVPGVPADRVGADDLRTAWGAVADAVRRLHEVPVASCPFRRGLDSVVDAARDVVARGAVHPEFLPVEQRLVPPAELLARLTGELARRRDQEAADTVVCHGDLCLPNIVLHPETLEVSGFIDLGRLGAADRHADLALLLANARETWVDEERARFADAAFAERYGIAPDPERLRFYLHLDPLTWG	.	The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation.	.	.	APHE_STRGR	Reviewed	.	.	.	.	.	.
Mol01093	Protein	Streptomycin aminoglycoside adenylyltransferase ant(6)-Ib (SA6IB)	ant(6)-Ib; 6)-Ib	ant(6)-Ib	.	Campylobacter fetus subsp. Fetus	32019	Campylobacter fetus subsp. fetus	Campylobacter	194	Campylobacteraceae	72294	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MKMRTEKQIYDTILNFAKADDRIRVVTLEGSRTNINIIPDDFQDYDITFFVTDMQSFINSDEWLNVFGERLIMQKPEDMELFPKEEKGYSYLMLFWDGVKIDLTLLPLEVLDEYFTWDKLVKLLLDKDNRVTNIPVPTDEDYYIEHPTARSFDDCCNEFWNTVTYVVKGLCRKEILFAIDHLNNIVRMELLRMISWKVGIEQGYSFSLGKNYKFLERYISPELWKKILATYNMGSYTEMWKSLELCMGIFRMVSKEVAQCLNYLYPDYDKNISNYVIRQKEKYQR	.	.	.	.	D8L9Z0_CAMFE	Unreviewed	.	.	.	.	.	.
Mol01094	Protein	Streptomycin phosphotransferase (STRB)	strB; Streptomycin phosphotransferase	strB		Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MFMPPVFPAHWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIADELRGADYLVWRNGRGAVRLLGRENNLMLLEYAGERMLSHIVAEHGDYQATEIAAELMAKLYAASEEPLPSALLPIRDRFAALFQRARDDQNAGCQTDYVHAAIIADQMMSNASELRGLHGDLHHENIMFSSRGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVDPRRLLDQAYAYGCLSAAWNADGEEEQRDLAIAAAIKQVRQTSY	.	.	.	.	Q70WT3_PASMD	Unreviewed	.	.	.	.	.	.
Mol01095	Protein	Streptomycin phosphotransferase (STRB)	strB; Streptomycin phosphotransferase	strB		Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MFMPPVFPAHWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIADELRGADYLVWRNGRGAVRLLGRENNLMLLEYAGERMLSHIVAEHGDYQATEIAAELMAKLYAASEEPLPSALLPIRDRFAALFQRARDDQNAGCQTDYVHAAIIADQMMSNASELRGLHGDLHHENIMFSSRGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVDPRRLLDQAYAYGCLSAAWNADGEEEQRDLAIAAAIKQVRQTSY	.	.	.	.	A0A1Y0F581_VIBCL	Unreviewed	.	.	.	.	.	.
Mol01096	Protein	Streptothricin acetyltransferase (STA)	STAT	sta	.	Streptomyces lavendulae	1914	Streptomyces lavendulae	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTTTHGSTYEFRSARPGDAEAIEGLDGSFTTSTVFEVDVTGDGFALREVPADPPLVKVFPDDGGSDGEDGAEGEDADSRTFVAVGADGDLAGFAAVSYSAWNQRLTIEDIEVAPGHRGKGIGRVLMRHAADFARERGAGHLWLEVTNVNAPAIHAYRRMGFAFCGLDSALYQGTASEGEHALYMSMPCP	.	"Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes. Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin."	.	.	STA_STRLA	Reviewed	.	.	.	.	.	.
Mol01097	Protein	Streptothricin N-acetyltransferase Sat4 (SAT4)	dhps; EC 2.5.1.15; Fragment	sat4	.	Campylobacter coli	195	Campylobacter coli	Campylobacter	194	Campylobacteraceae	72294	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MITEMKAGHLKDIDKPSEPFEVIGKIIPRYENENWTFTELLYEAPYLKSYQDEEDEEDEEADCLEYIDNTDKIIYLYYQDDKCVGKVKLRKNWNRYAYIEDIAVCKDFRGQGIGSALINISIEWAKHKNLHGLMLETQDNNLIACKFYHNCGFKIGSVDTMLYANFENNFEKAVFWYLRFFVIISFLGYL	.	.	.	.	A0A7H0XIR7_CAMCO	Unreviewed	.	.	.	.	.	.
Mol01098	Protein	Tartronate semialdehyde reductase (TSAR)	Tartronate semialdehyde reductase; TSAR; yhaE; b3125; JW5526	garR	947631	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENGIIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEVTR	.	Catalyzes the reduction of tatronate semialdehyde to D-glycerate.	.	.	GARR_ECOLI	Reviewed	.	.	.	.	.	.
Mol01099	Protein	Tethering factor for nuclear proteasome STS1 (STS1)	Dumbbell former protein 8; SEC23 suppressor 1; DBF8; SSM5; YIR011C; YIB11C	STS1	854828	Saccharomyces cerevisiae	4932	Saccharomyces cerevisiae	Saccharomyces	4930	Saccharomycetaceae	4893	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MMGFEWGFKPSSKITQSTVSSQGTGNVMIPTAGVKQKRRYANEEQEEEELPRNKNVMKYGGVSKRRPQPGSLIRGQPLPLQRGMELMNKNQLQQLLVDLMTKHPEIQQSVHTRVIGLDFSIQKCLDMLKQKSEAVYQSIPYNRSYESNKLDDYAFVRMKPQILEFLNCLVDFILDNIPPRLENLHASLKFLDICTELVIKLPRFELASNNYYYDKCIEQLSHVWCTLIEHVARDRIILLADNSSVWKSHMTRLQVYNEHSNGLLERPLQLFKSLDMGSPSAASSSTLSLQESIIYHHDTMTANENNNNSGSAATDSPFN	.	Involved in ubiquitin-mediated protein degradation. Regulatory factor in the ubiquitin/proteasome pathway that controls the turnover of proteasome substrates. Targets proteasomes to the nucleus and facilitates the degradation of nuclear proteins. Required for efficient chromosome segregation. Restores protein transport and ribosomal RNA stability.	.	.	STS1_YEAST	Reviewed	.	.	.	.	.	.
Mol01100	Protein	Tetracycline efflux MFS transporter Tet(38) (TET38)	tet38; tet(38); DQV20_03865; G6X35_03865; G6Y24_14280; HK402_00520; 38; Tetracycline resistant protein Tet38	tet38	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNVEYSKIKKAVPILLFLFVFSLVIDNSFKLISVAIADDLNISVTTVSWQATLAGLVIGIGAVVYASLSDAISIRTLFIYGVILIIIGSIIGYIFQHQFPLLLVGRIIQTAGLAAAETLYVIYVAKYLSKEDQKTYLGLSTSSYSLSLVIGTLSGGFISTYLHWTNMFLIALIVVFTLPFLFKLLPKENNTNKAHLDFVGLILVATIATTVMLFITNFNWLYMIGALIAIIVFALYIKNAQRPLVNKSFFQNKRYASFLFIVFVMYAIQLGYIFTFPFIMEQIYHLQLDTTSLLLVPGYIVAVIVGALSGKIGEYLNSKQAIITAIILIALSLILPAFAVGNHISIFVISMIFFAGSFALMYAPLLNEAIKTIDLNMTGVAIGFYNLIINVAVSVGIAIAAALIDFKALNFPGNDALSSHFGIILIILGLMSIVGLVLFVILNRWTQSEK	.	.	.	.	Q5PU79_STAAU	Unreviewed	.	.	.	.	.	.
Mol01101	Protein	Tetracycline efflux Na+/H+ antiporter family transporter Tet(35) (TEE35)	AL538_15790	tet(35)	.	Vibrio harveyi	676	Vibrio fluvialis	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNLIDFAHSPVSLLPPIVALTLAILTRRVLVSLGVGIVLGAVLLNDWSIGNTVGYVSSQVSSVFIEDGGINTWNMSIVGFLILLGMTTALLTLSGGTRAFAEWAQTRVKSKRGSKLLAAFLGVFIFVDDYFNSLAVGAISRPVTDRFYVSRAKLAYILDSTAAPMCVIMPASSWGAYIITIIGGILVSHGITEYSALGAYVRLIPMNFYAVFALLMVFAVAWFGLDIGKMRDHEIAASQGRGFDKDKENDTQEAHELNEELDIRESEKGKVSDLVLPIVTLIVATIASMLYTGGQALAADGKEFALLGAFENTDVGTSLIYGSLLGLAVALFTVLKQGLPMVEIARTLWIGAKSMFGAILILVFAWTIGSVIGDMKTGSYLSTMAQGNINPHWLPVILFLLSGLMAFSTGTSWGTFGIMLPIAGDMAGATDVALMLPMLSAVLAGAVFGDHCSPISDTTILSSTGARCNHIDHVSTQLPYALSVALVSCVGFIALGMTASIAFSFIAASITFVIVCAILSWLSKSKMASCQNA	.	.	.	.	A0A454BA96_VIBHA	Unreviewed	.	.	.	.	.	.
Mol01102	Protein	Tetracycline efflux protein (TET41)	TET41	TET41	.	Serratia marcescens	1823	Nocardia otitidiscaviarum	Nocardia	1817	Nocardiaceae	85025	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MKKPMLVILLTVLLDAVGIGLIMPILPALLRSLGGLDAGSLHYGALLAAYALMQFLFSPILGALSDRFGRRPVLLISLAGAAADYLLMAFAPTLAWLYLGRLLAGITGANMAVATAYVTDITPAGQRARRFGLVGAVFGVGFIVGPLLGGSLGEWHLHAPFLAASAMNAVNLAMAFFLLPESRKPRARAAEKIRLNPFSSLRRLHGKPGLLPLAGIYLIMALVSQAPATLWILYGQDRFGWSMMVAGLSLAGYGACHALSQAFAIGPLVARLGERKALLIGLAADAMGLALLSIATRGWAPFALLPFFAAGGMALPALQALMAQKVDDDHQGELQGTLASMGSLIGVAGPLVATALYAATRDVWPGLVWALAAALYLLVPLLLARSRERDAA	.	Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.	.	.	A0A7S6YKU5_SERMA	Unreviewed	.	.	.	.	.	.
Mol01103	Protein	Tetracycline efflux protein tet(L) (TETL)	tetL; tet; tet(L); CUM81_09970; EU507_16770; EY666_08885; L); Tetracycline resistant protein	tetL	66465484	Streptococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNTSYSQSNLRHNQILIWLCILSFFSVLNEMVLNVSLPDIANDFNKPPASTNWVNTAFMLTFSIGTAVYGKLSDQLGIKRLLLFGIIINCFGSVIGFVGHSFFSLLIMARFIQGAGAAAFPALVMVVVARYIPKENRGKAFGLIGSIVAMGEGVGPAIGGMIAHYIHWSYLLLIPMITIITVPFLMKLLKKEVRIKGHFDIKGIILMSVGIVFFMLFTTSYSISFLIVSVLSFLIFVKHIRKVTDPFVDPGLGKNIPFMIGVLCGGIIFGTVAGFVSMVPYMMKDVHQLSTAEIGSVIIFPGTMSVIIFGYIGGILVDRRGPLYVLNIGVTFLSVSFLTASFLLETTSWFMTIIIVFVLGGLSFTKTVISTIVSSSLKQQEAGAGMSLLNFTSFLSEGTGIAIVGGLLSIPLLDQRLLPMEVDQSTYLYSNLLLLFSGIIVISWLVTLNVYKHSQRDF	.	.	.	.	Q7B6N8_ENTFL	Unreviewed	.	.	.	.	.	.
Mol01104	Protein	Tetracycline efflux protein TetA (TETA)	tetA(33); TetA protein	tetA(33)	.	Corynebacterium glutamicum	1718	Corynebacterium glutamicum	Corynebacterium	1716	Corynebacteriaceae	1653	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSSLTSARGSLATVLITASLDAAGMGLVMPILPALLHEAGVTADAVPLNVGVLIALYAVMQFIFAPVLGTLSDRFGRRRVLLVSLAGATVDYLVLATTSALSVFYIARAVAGITGATNAVTATVIADITPPHQRAKRFGLLSACYGGGMIAGPAMGGLFGAISPHLPFLLAALLSASNLALTFILLRETRPDSPARSASLAQHRGRPGLSAVPGITFLLIAFGLVQFIGQAPGATWVLFTEHRLDWSPVEVGISLSVFGIVQVLVQALLTGRIVEWIGEAKTVIIGCITDALGLVGLAIVTDAFSMAPILAALGIGGIGLPALQTLLSQRVDEQHQGRLQGVLASINSVTSIFGPVAFTTIFALTYINADGFLWLCAAALYVPCVILIMRGTAASPKFGSWASGDSM	.	.	.	.	Q8VVJ1_CORGT	Unreviewed	.	.	.	.	.	.
Mol01105	Protein	Tetracycline efflux proteintet(39) (TET39)	tet39; Tet39	tet39	.	Acinetobacterspp.(Acinetobacter baumannii)	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MPILPELLRSLAGAEAGGVHYGALLAVYALMQFIFAPILGALSDRFGRRPVLIISIAGATADYLLMAAAPSLLWLYIGRIFAGITGANMAVATAYVSDITPAHERAKRFGLLGAVFGIGFIAGPVIGGVLGEWNLHAPFFAAAFMNGINLIMTAVLLKESKHSNKMTEKVQEQSILKKLSYLITQPNMAPLLGIFLIITLVSQVPATLWVIYGQDRYGWSIFIAGVSLASYGICHSIAQAFAIAPMVKRFGEKNTLLCGIACDAIGLLLLSIAVEEWVPFALLPLFALGGVAVPALQAMMSRGISDERQGELQGLLSSFNSLGAIIGPVLVTSLYFMTQASAPGMVWALAAILYVITLPLLLKYRLNKYSGVP	.	Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.	.	.	A0A0M4FLY1_ACIBA	Unreviewed	.	.	.	.	.	.
Mol01106	Protein	Tetracycline repressor protein class H (TETR)	.	tetR	.	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MAKLDKEQVIDDALILLNEVGIEGLTTRNVAQKIGVEQPTLYWHVKNKRALLDALAETILQKHHHHVLPLPNETWQDFLRNNAKSFRQALLMYRDGGKIHAGTRPSESQFETSEQQLQFLCDAGFSLSQAVYALSSIAHFTLGSVLETQEHQESQKEREKVETDTVAYPPLLTQAVAIMDSDNGDAAFLFVLDVMISGLETVLKSAK	.	TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.	PDB: 2VPR	.	TETR8_PASMD	Reviewed	.	.	.	.	.	.
Mol01107	Protein	Tetracycline resistance protein class A (TETA)	TetA(A)	tetA	58463759	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKPNRPLIVILSTVALDAVGIGLIMPVLPGLLRDLVHSNDVTAHYGILLALYALMQFACAPVLGALSDRFGRRPVLLVSLAGAAVDYAIMATAPFLWVLYIGRIVAGITGATGAVAGAYIADITDGDERARHFGFMSACFGFGMVAGPVLGGLMGGFSPHAPFFAAAALNGLNFLTGCFLLPESHKGERRPLRREALNPLASFRWARGMTVVAALMAVFFIMQLVGQVPAALWVIFGEDRFHWDATTIGISLAAFGILHSLAQAMITGPVAARLGERRALMLGMIADGTGYILLAFATRGWMAFPIMVLLASGGIGMPALQAMLSRQVDEERQGQLQGSLAALTSLTSIVGPLLFTAIYAASITTWNGWAWIAGAALYLLCLPALRRGLWSGAGQRADR	.	Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.	.	.	TCR1_ECOLX	Reviewed	.	.	.	.	.	.
Mol01108	Protein	Tetracycline resistance protein Tet (TETW/N/W)	tet(W; N; W); W/N/W	tet(W N W)	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKIINIGILAHVDAGKTTLTESLLYASGAISEPGSVEKGTTRTDTMFLERQRGITIQAAVTSFQWHRCKVNIVDTPGHMDFLAEVYRSLAVLDGAILVISAKDGVQAQTRILFHALRKMNIPTVIFINKIDQAGVDLQSVYQSVRDKLSADIIIKQTVSLSPEIVLEENTDIEAWDAVIENNDELLEKYIAGEPISREKLAREEQQRVQDASLFPVYHGSAKNGLGIQPLMDAVTGLFQPIGEQGGAALCGSVFKVEYTDCGQRLVYLRLYSGTLRLRDTVALAGREKLKITEMRIPSKGEIVRTDTAHKGEIVILPSDSLRLNDILGDKTQLPREMWSDVPFPMLRTTITPKTAEQRDRLLDALTQIADTDPLLHYEVDSITHEIILSFLGRVQLEVVSALLSEKYKLETVVKEPTVIYMERPLKAASHTIHIEVPPNPFWASIGLSVTPLPLGSGVQYESRVSLGYLNQSFQNAVRDGIRYGLEQGLFGWNVTDCKICFEYGLYYSPVSTPADFRSLAPIVLEQALKESGTQLLEPYLSFTLYAPREYLSRAYHDAPKYCATIETVQVKKDEVVFTGEIPARCIQAYRTDLAFYTNGRSVCLTELKGYQATVGEPIIQPRRPNSRLDKVRHMFSKIP	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	A0A142BVK9_9BACT	Unreviewed	.	.	.	.	.	.
Mol01109	Protein	Tetracycline resistance protein tet(59) (TET59)	tet(59); 59	tet(59)	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNKFAITALTITALDAMGIGLIMPVLPTLLREYVSAENLANHYGILLALYAIMQVFFAPLLGKWSDKFGRRPILLLSLAGAAVDYTLLALSSSLWMLYVGRLISGVTGATGAVAASVIADNTASQERTKWFGRLGAAFGIGLIAGPAIGGFTGQFSAHLPFIIAAILNALSFLVIMLIFKDNKIKNTEKNTTETAENSRPFLQVIKPVILLLFIFFMTQMIGQIPATTWVLFTEHRFQWGSMEVGLSLAGLGIMHALFQAFVAGAIAKKFNEKVTIIVGFVVDGAAFIILSLLTKGWMIYPTLILLAGGSIALPALQGLMSAQVNQTNQGKLQGVLVSLTNTTGVIGPLLFSFIFGQTLASWDGWIWMIGAIMYVLLIVFILSFYRSTKKIVKIAKLPAS	.	.	.	.	A0A142BWF2_9BACT	Unreviewed	.	.	.	.	.	.
Mol01110	Protein	Tetracycline resistance protein TetM (TETM)	TetM(1545); tet(M)	tetM	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MKIINIGVLAHVDAGKTTLTESLLYNSGAITELGSVDRGTTKTDNTLLERQRGITIQTAITSFQWKNTKVNIIDTPGHMDFLAEVYRSLSVLDGAILLISAKDGVQAQTRILFHALRKIGIPTIFFINKIDQNGIDLSTVYQDIKEKLSAEIVIKQKVELHPNMRVMNFTESEQWDMVIEGNDYLLEKYTSGKLLEALELEQEESIRFHNCSLFPVYHGSAKNNIGIDNLIEVITNKFYSSTHRGQSELCGKVFKIEYSEKRQRLAYIRLYSGVLHLRDPVRISEKEKIKITEMYTSINGELCKIDKAYSGEIVILQNEFLKLNSVLGDTKLLPQRERIENPLPLLQTTVEPSKPQQREMLLDALLEISDSDPLLRYYVDSATHEIILSFLGKVQMEVTCALLQEKYHVEIEIKEPTVIYMERPLKKAEYTIHIEVPPNPFWASIGLSVAPLPLGSGVQYESSVSLGYLNQSFQNAVMEGIRYGCEQGLYGWNVTDCKICFKYGLYYSPVSTPADFRMLAPIVLEQVLKKAGTELLEPYLSFKIYAPQEYLSRAYNDAPKYCANIVDTQLKNNEVILSGEIPARCIQEYRSDLTFFTNGRSVCLTELKGYHVTTGEPVCQPRRPNSRIDKVRYMFNKIT	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	TET5_ENTFL	Reviewed	.	.	.	.	.	.
Mol01111	Protein	Tetracycline resistance protein TetQ (TETQ)	TetA(Q)1; tet(Q)	tetQ	45365338	Bacteroides thetaiotaomicron	818	Bacteroides thetaiotaomicron	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MNIINLGILAHIDAGKTSVTENLLFASGATEKCGCVDNGDTITDSMDIEKRRGITVRASTTSIIWNGVKCNIIDTPGHMDFIAEVERTFKMLDGAVLILSAKEGIQAQTKLLFNTLQKLQIPTIIFINKIDRAGVNLERLYLDIKANLSQDVLFMQNVVDGSVYPVCSQTYIKEEYKEFVCNHDDNILERYLADSEISPADYWNTIIALVAKAKVYPVLHGSAMFNIGINELLDAITSFILPPASVSNRLSSYLYKIEHDPKGHKRSFLKIIDGSLRLRDVVRINDSEKFIKIKNLKTINQGREINVDEVGANDIAIVEDMDDFRIGNYLGAEPCLIQGLSHQHPALKSSVRPDRPEERSKVISALNTLWIEDPSLSFSINSYSDELEISLYGLTQKEIIQTLLEERFSVKVHFDEIKTIYKERPVKKVNKIIQIEVPPNPYWATIGLTLEPLPLGTGLQIESDISYGYLNHSFQNAVFEGIRMSCQSGLHGWEVTDLKVTFTQAEYYSPVSTPADFRQLTPYVFRLALQQSGVDILEPMLYFELQIPQAASSKAITDLQKMMSEIEDISCNNEWCHIKGKVPLNTSKDYASEVSSYTKGLGIFMVKPCGYQITKGGYSDNIRMNEKDKLLFMFQKSMSSK	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	TETQ_BACT4	Reviewed	.	.	.	.	.	.
Mol01112	Protein	Tetracycline resistance protein TetQ (TETQ)	TetA(Q)2; tet(Q)	tetQ		Bacteroides fragilis	817	Bacteroides fragilis	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MNIINLGILAHIDAGKTSVTENLLFASGATEKCGRVDNGDTITDSMDIEKRRGITVRASTTSIIWNGVKCNIIDTPGHMDFIAEVERTFKMLDGAVLILSAKEGIQAQTKLLFNTLQKLQIPTIIFINKIDRDGVNLERLYLDIKTNLSQDVLFMQTVVDGLVYPICSQTYIKEEYKEFVCNHDDNILERYLADSEISPADYWNTIIDLVAKAKVYPVLHGSAMFNIGINELLDAISSFILPPESVSNRLSAYLYKIEHDPKGHKRSFLKIIDGSLRLRDIVRINDSEKFIKIKNLKTIYQGREINVDEVGANDIAIVEDMEDFRIGDYLGTKPCLIQGLSHQHPALKSSVRPDRSEERSKVISALNTLWIEDPSLSFSINSYSDELEISLYGLTQKEIIQTLLEERFSVKVHFDEIKTIYKERPVKKVNKIIQIEVPPNPYWATIGLTLEPLPLGTGLQIESDISYGYLNHSFQNAVFEGIRMSCQSGLHGWEVTDLKVTFTQAEYYSPVSTPADFRQLTPYVFRLALQQSGVDILEPMLYFELQIPQAASSKAITDLQKMMSEIEDISCNNEWCHIKGKVPLNTSKDYASEVSSYTKGLGVFMVKPCGYQITKGDYSDNIRMNEKDKLLFMFQKSMSSK	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	TETQ_BACFG	Reviewed	.	.	.	.	.	.
Mol01113	Protein	Tetracycline resistance protein TetQ (TETQ)	.	tet(36)	.	Bacteroides sp.(Bacteroides coprosuis)	151276	Bacteroides coprosuis	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MRTINIGILAHIDAGKTSITENLLFASGATIVRGSVDKGNTTTDSMDIEKRRGITVRASTTSIQWNDTKINIIDTPGHMDFLAEVERTFRMLDGAILVVSAKEGIQAQTRLLFNVLQQLEIPTILFVNKIDREGVNLNQLYLEIQNSLSKDIIFMQSVEGKELTSSCTIHYISEKNRETILEKDDLLLEKYLSDTQLSNLDYWNSMVRLVQAAKLHPIYHGSAMYGIGIEDLLNSITTFIETSLPQENALSAYVYKIEHNKKEQKRAYLKIIGGTLKSRKLYSLNGSDENLKIRGLKTFYSGDEIDVDEVFTNDIAIADHADNLMVGDYLGIMPNLFDKLNIPSPALKSSIHPAKVENRSKLISAMNVLSVEDPSLAFSINADNNELEVSLYGATQREVILTLLEERFSVDAYFEEVKTIYKERLKTKSEYTIHIEVPPNPYWASIGLIIEPLPIGAGLVMESEISLGYLNRSFQNAVFDGVKKACESGLYGWEVTDLKVTFSHGIYYSPVSTPADFRSLAPYVFRLALQQADVELLEPILDFKLQIPLAVNARAITDINKMQGEISTITSDGDWTTILGNIPLDTSKEYSAEVSSYTQGLGVFVTRFSGYRPTNKKVSRSVELNEKDKLMYMFEKESIK	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	Q7WT01_9BACE	Unreviewed	.	.	.	.	.	.
Mol01114	Protein	Tetracycline resistance protein TetQ (TETQ)	F3B90_25055; F3F51_14975	tet(Q)		Bacteroides ovatus	28116	Bacteroides ovatus	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MNIINLGILAHIDAGKTSVTENLLFASGATEKCGRVDNGDTITDSMDIEKRRGITVRASTTSIIWNGVKCNIIDTPGHMDFIAEVERTFKMLDGAVLILSAKEGIQAQTKLLFNTLQKLQIPTIIFINKIDRDGVNLERLYLDIKTNLSQDVLFMQTVVDGLVYPICSQTYIKEEYKEFVCNHDDNILERYLADSEISPADYWNTIIDLVAKAKVYPVLHGSAMFNIGINELLDAISSFILPPESVSNRLSAYLYKIEHDPKGHKRSFLKIIDGSLRLRDIVRINDSEKFIKIKNLKTIYQGREINVDEVGANDIAIVEDMEDFRIGDYLGTKPCLIQGLSHQHPALKSSVRPDRSEERSKVISALNTLWIEDPSLSFSINSYSDELEISLYGLTQKEIIQTLLEERFSVKVHFDEIKTIYKERPVKKVNKIIQIEVPPNPYWATIGLTLEPLPLGTGLQIESDISYGYLNHSFQNAVFEGIRMSCQSGLHGWEVTDLKVTFTQAEYYSPVSTPADFRQLTPYVFRLALQQSGVDILEPMLYFELQIPQAASSKAITDLQKMMSEIEDISCNNEWCHIKGKVPLNTSKDYASEVSSYTKGLGVFMVKPCGYQITKGDYSDNIRMNEKDKLLFMFQKSMSSK	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	A0A414E7F7_BACOV	Unreviewed	.	.	.	.	.	.
Mol01115	Protein	Tetracycline resistance protein TetQ (TETQ)	tetM; DW831_19585; DW873_18575; DWW14_02360; DWW83_14920; DWX87_03315; DXB37_20400; DXC07_01500; DXC80_18025; DXD40_14425; ERS852510_00445; ERS852554_00456; GAP41_13825; GAP47_05320; GAP55_14175; GAQ44_06250; GAQ59_16410; GAQ70_12255; GAQ75_13645; HMPREF2141_02710; HUU98_20000; HUV07_17965	tet(Q)	64352988	Bacteroides uniformis	820	Bacteroides uniformis	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MNIINLGILAHIDAGKTSVTENLLFASGATEKCGRVDNGDTITDSMDIEKRRGITVRASTTSIIWNGVKCNIIDTPGHMDFIAEVERTFKMLDGAVLILSAKEGIQAQTKLLFSTLQKLQIPTIIFINKIDRAGVNLERLYMDIKTNLSQDVLFMQTVVDGSVYPVCSQTYIKEEYKEFVCNHDDDILERYLADSEISPADYWNTIIALVAKAKVYPVLHGSAMFNIGINELLDAISSFILPPASVSNRLSAYLYKIEHDPKGHKRSFLKIIDGSLRLRDVVRINDSEKFIKIKNLKTIYQGREINVDEVGANDIAIVEDIEDFRIGDYLGAKPCLIQGLSHQHPALKSSVRPNKPEERSKVISALNTLWIEDPSLSFSINSYSDELEISLYGLTQKEIIQTLLEERFSVKVHFDEIKTIYKERPIKKVNKIIQIEVPPNPYWATIGLTLEPLPLGAGLQIESDISYGYLNHSFQNAVFEGIRMSCQSGLHGWEVTDLKVTFTQAEYYSPVSTPADFRQLTPYVFRLALQQSGVDILEPMLCFELQIPQVASSKAITDLQKLMSEIEDISCNNEWCHIKGKVPLNTSKDYASEVSSYTKGLGIFMVKPCGYQITKDGYSDNIRMNEKDKLLFMFQKSMSLK	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	A0A139K3N9_BACUN	Unreviewed	.	.	.	.	.	.
Mol01116	Protein	Tetracycline resistance protein TetS (TETS)	Tet(S); tet(S)	tetS	66817191	Listeria monocytogenes	1639	Listeria monocytogenes	Listeria	1637	Listeriaceae	186820	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTLTESLLYSSGAIKELGSVDSGTTKTDTMFLERQRGITIQTAITSFQRENVKVNIVDTPGHMDFLADVYRSLSVLDGAILLISAKDGVQSQTRILFHALRKMNIPIIFFINKIDQNGINLPDVYQDIKDKLSDDIIIKQTVNLNLKPYVIDYTEPEQWETVIVGNDYLLEKYTIGKTLNIAELEKEENERIQSCSLYPVYHGSAKNNIGIKQLIEVITSKLFSPTQLNSDKLCGNVFKVEYSDDGQRLVYVRLYSGTLHLRDSVNISEKEKIKVTEMYTSINGELRQIDKAEPGEIIILKNELLKLNNVLGDKKRLPHREILENPLPMLQTTIEPCKSVQREKLLDALFEISDSDPLLQYYVDTVTHEIVLSFLGEVQMEVTCTLIQEKYHIEIETRKPTVIYMERPLKKSEFTIDIEVPPNPFWASIGLSVTPLPLGSGIQYESLVSLGYLNQSFQNAVMEGIRYGCEQGLYGWKLTDCKICFKYGLYYSPVSTPADFRMLAPIVLEQAFRKSGTELLEPYLSFEIYVPQEYLSRAYNDASKYCANILNTKLKGNEVILIGEIPARCIQEYRNSLTFFTNGRSVCLTELKGYQVTNIKSAFQPRRPNNRIDKVRHMFNKINLH	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	TETS_LISMN	Reviewed	.	.	.	.	.	.
Mol01117	Protein	Tetracycline resistance protein TetW (TETW)	Tet(W); tet(W)	tetW	64114426	Butyrivibrio fibrisolvens	831	Butyrivibrio fibrisolvens	Butyrivibrio	830	Lachnospiraceae	186803	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTLTESLLYASGAISEPGSVEKGTTRTDTMFLERQRGITIQAAVTSFQWHRCKVNIVDTPGHMDFLAEVYRSLAVLDGAILVISAKDGVQAQTRILFHALRKMNIPTVIFINKIDQAGVDLQSVVQSVRDKLSADIIIKQTVSLSPEIVLEENTDIEAWDAVIENNDELLEKYIAGEPISREKLAREEQQRVQDASLFPVYHGSAKNGLGIQPLMDAVTGLFQPIGEQGGAALCGSVFKVEYTDCGQRRVYLRLYSGTLRLRDTVALAGREKLKITEMRIPSKGEIVRTDTAYQGEIVILPSDSVRLNDVLGDQTRLPRKRWREDPLPMLRTTIAPKTAAQRERLLDALTQLADTDPLLRCEVDSITHEIILSFLGRVQLEVVSALLSEKYKLETVVKEPSVIYMERPLKAASHTIHIEVPPNPFWASIGLSVTPLSLGSGVQYESRVSLGYLNQSFQNAVRDGIRYGLEQGLFGWNVTDCKICFEYGLYYSPVSTPADFRSLAPIVLEQALKESGTQLLEPYLSFILYAPQEYLSRAYHDAPKYCATIETAQVKKDEVVFTGEIPARCIQAYRTDLAFYTNGRSVCLTELKGYQAAVGQPVIQPRRPNSRLDKVRHMFQKVM	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	TETW_BUTFI	Reviewed	.	.	.	.	.	.
Mol01118	Protein	Tetracycline resistance protein TetW (TETW)	tetW; Tetracycline resistance protein	tetW	.	Mitsuokella multiacidus	52226	Mitsuokella multacida	Mitsuokella	52225	Selenomonadaceae	1843491	Selenomonadales	909929	Negativicutes	909932	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTLTESLLYASGAISEPGSVEKGTTRTDTMFLERQRGITIQAAVTSFQWHRCKVNIVDTPGHMDFLAEVYRSLAVLDGAILVISAKDGVQAQTRILFHALRKMNIPTVIFINKIDQAGVDLQSVVQSVRDKLSADIIIKQTVSLSPEIVLEENTDIEAWDAVIENNDELLEKYIAGEPISREKLAREEQQRVQDASLFPVYHGSAKNGLGIQPLMDAVTGLFQPIGEQGGAALCGSVFKVEYTDCGQRRVYLRLYSGTLRLRDTVALAGREKLKITEMRIPSKGEIVRTDTAYQGEIVILPSDSVRLNDVLGDQTRLPRKRWREDPLPMLRTTIAPKTAAQRERLLDALTQLADTDPLLRCEVDSITHEIILSFLGRVQLEVVSALLSEKYKLETVVKEPSVIYMERPLKAASHTIHIEVPPNPFWASIGLSVTPLSLGSGVQYESRVSLGYLNQSFQNAVRDGIRYGLEQGLFGWNVTDCKICFEYGLYYSPVSTPADFRSLAPIVLEQALKESGTQLLEPYLSFILYAPQEYLSRAYHDAPKYCATIETAQVKKDEVVFTGEIPARCIQAYRTDLAFYTNGRSVCLTELKGYQAAVGQPVIQPRRPNSRLDKVRHMFQKVM	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	Q710C6_9FIRM	Unreviewed	.	.	.	.	.	.
Mol01119	Protein	Tetracycline resistance protein TetW (TETW)	tet(W); TetW	tet(W)	.	Selenomonas ruminantium	971	Selenomonas ruminantium	Selenomonas	970	Selenomonadaceae	1843491	Selenomonadales	909929	Negativicutes	909932	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTLTESLLYASGAISEPGSVEKGTTRTDTMFLERQRGITIQAAVTSFQWHRCKVNIVDTPGHMDFLAEVYRSLAVLDGAILVISAKDGVQAQTRILFHALRKMNIPTVIFINKIDQAGVDLQSVVQSVRDKLSADIIIKQTVSLSPEIVLEENTDIEAWDAVIENNDKLLEKYIAGEPISREKLVREEQRRVQDASLFPVYYGSAKKGLGIQPLMDAVTGLFQPIGEQGSAALCGSVFKVEYTDCGQRRVYLRLYSGTLRLRDTVALAGREKLKITEMRIPSKGEIVRTDTAYPGEIVILPSDSVRLNDVLGDPTRLPRKRWREDPLPMLRTSIAPKTAAQRERLLDALTQLADTDPLLRCEVDSITHEIILSFLGRVQLEVVSALLSEKYKLETVVKEPTVIYMERPLKAASHTIHIEVPPNPFWASIGLSVTPLSLGSGVQYESRVSLGYLNQSFQNAVRDGIRYGLEQGLFGWNVTDCKICFEYGLYYSPVSTPADFRSLAPIVLEQALKESGTQLLEPYLSFTLYAPREYLSRAYHDAPKYCATIETVQVKKDEVVFTGEIPARCIQAYRTDLAFYTNGQSVCLTELKGYQAAVGKPVIQPRRPNSRLDKVRHMFQKVM	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	Q2PYV5_SELRU	Unreviewed	.	.	.	.	.	.
Mol01120	Protein	Tetracycline resistance protein TetW (TETW)	DWZ89_13100	tet	.	Fusobacterium prausnitzii	853	Faecalibacterium prausnitzii	Faecalibacterium	216851	Oscillospiraceae	216572	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTLTESLLYASGAISEPGSVEKGTTRTDTMFLERQRGITIQAAVTSFQWHRCKVNIVDTPGHMDFLAEVYRSLAVLDGAILVISAKDGVQAQTRILFHALRKMNIPTVIFINKIDQAGVDLQSVVQSVRDKLSADIIIKQTVSLSPEIVLEENTDIEAWDAVIENNDELLEKYIAGEPISREKLAREEQQRVQDASLFPVYHGSAKNGLGIQPLMDAVTGLFQPIGEQGGAALCGSVFKVEYTDCGQRRVYLRLYSGTLRLRDTVALAGREKLKITEMRIPSKGEIVRTDTAYQGEIVILPSDSVRLNDVLGDQTRLPRKRWREDPLPMLRTTIAPKTAAQRERLLDALTQLADTDPLLRCEVDSITHEIILSFLGRVQLEVVSALLSEKYKLETVVKEPSVIYMERPLKAASHTIHIEVPPNPFWASIGLSVTPLSLGSGVQYESRVSLGYLNQSFQNAVRDGIRYGLEQGLFGWNVTDCKICFEYGLYYSPVSTPADFRSLAPIVLEQALKESGTQLLEPYLSFILYAPQEYLSRAYHDAPKYCATIETAQVKKDEVVITGEIPARCIQAYRTDLAFYTNGRSVCLTELKGYQAAVGQPVIQPRRPNSRLDKVRHMFQKVM	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	A0A3E2T0Y8_9FIRM	Unreviewed	.	.	.	.	.	.
Mol01121	Protein	TMB-2 metallo-beta-lactamase (BTMB2)	blaTMB-2; TMB-2 metallo-beta-lactamase	blaTMB-2	.	Acinetobacter pittii	48296	Acinetobacter pittii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRPFLFLIIFISHFAFANEEIPGLEVEEIDNGVFLHKSYSRVEGWGLVSSNGLVVISGGKAFIIDTPWSESDTEKLVDWIRSKKYELAGSISTHSHEDKTAGIKWLNGKSITTYASALTNEILKREGKEQARSSFKGNEFSLMDGFLEVYYPGGGHTIDNLVVWIPSSKILYGGCFIRSLEPSGLGYTGEAKIDQWPQSARNTISKYPEAKIVVPGHGKIGDFELLKHTKVLAEKASNKANHGDR	.	.	.	.	L0N611_ACIPI	Unreviewed	.	.	.	.	.	.
Mol01122	Protein	TolC family outer membrane protein (TOLC)	tolC; CSB70_4010; NCTC13305_02171; Type I secretion outer membrane; TolC family protein	tolC	.	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKIKLMLVAGLWSFTSSSFALDLVETYERAKLNDPTWQANQQQFEADQLNLGLATGALLPTVTLSGNITRNRQTVKRSNFPGVDQEGLSDALVSNTSTTKQATLSARQPLFRMDAWEGYKQVKTSVALSEITLRLQKQDHVLNVAEAYFNVLRQQALTAAYLQEEKALLEQLNMMNAKLKEGLVARSDVSEANAQYQNARANRIATNVQLLLAQEQLSEYIGPYQDKLAVLRSDFIFQKPYPAQLDEWLGLAQQQNLKIQQARLQKRYAEDQRRVEKAALYPQIDAVASYGYTKQTPETLISTDGKFDQVGVEMNWNLFNGGRTRTSIKKASVELNKAQAQLDAAIRRANVDVKSAFMQVDTDRAKLEARKAAMDSSALVSQASKASYNEGLKSMVDVLLAQRNAFSAKQDYLNAQYDYLLNVLRLKAAVGQLGEKDLVELNSWLTYQ	.	.	.	.	A0A1V3DAN9_ACIBA	Unreviewed	.	.	.	.	.	.
Mol01123	Protein	Transketolase (TKT)	TK; P68	Tkt	21881	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000022529.8, Tkt-201, 3223; ENSMUST00000223717.2, Tkt-207, 1619; ENSMUST00000162356.2, Tkt-205, 465; ENSMUST00000225857.2, Tkt-209, 1962; ENSMUST00000160274.2, Tkt-203, 391; ENSMUST00000160189.2, Tkt-202, 3159; ENSMUST00000223633.2, Tkt-206, 2438; ENSMUST00000225039.2, Tkt-208, 1401; ENSMUST00000160406.2, Tkt-204, 597"	MEGYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDIYQKRCEAFGWHTIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQIIQEIYSQVQSKKKILATPPQEDAPSVDIANIRMPTPPSYKVGDKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSAAVVGEPGVTVTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVKGLVTKG	chr 14: 30270316-30296677 [+] 	"Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate."	.	.	TKT_MOUSE	Reviewed	ENSMUSG00000021957	.	.	.	.	.
Mol01124	Protein	Transport protein (ALL3255)	all3255; Transport protein	all3255	.	Nostoc punctiforme PCC 73102	63737	Nostoc punctiforme PCC 73102	Nostoc	1177	Nostocaceae	1162	Nostocales	1161	.	.	Cyanobacteria	1117	.	.	.	MNQLLTAFTESLVAFAATNIDDIIILLLLFSQVDVNFRRSHIWVGHFLGFLIIILASLPGFFGGLFVQREFIGLLGILPIIIGIKKLVKKDQENTQIQAVTTDLKGSSPANPILAFISSILHPQVYKVGAVTVANGGDNISIYIPLFAGQNLVTLGVIIGVFFFMVGILCVTADLLSRQAPIAYVLSLHSKTFIPFILIALGLFIMYERGTFSLLMSIKI	.	.	.	.	Q8YS36_NOSS1	Unreviewed	.	.	.	.	.	.
Mol01125	Protein	Tunicamycin resistance protein (TMRB)	BSU03140	tmrB	938346	Bacillus subtilis	1423	Bacillus subtilis	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MIIWINGAFGSGKTQTAFELHRRLNPSYVYDPEKMGFALRSMVPQEIAKDDFQSYPLWRAFNYSLLASLTDTYRGILIVPMTIVHPEYFNEIIGRLRQEGRIVHHFTLMASKETLLKRLRTRAEGKNSWAAKQIDRCVEGLSSPIFEDHIQTDNLSIQDVAENIAARAELPLDPDTRGSLRRFADRLMVKLNHIRIK	.	Involved in the resistance to tunicamycin. Binds ATP.	.	.	TMRB_BACSU	Reviewed	.	.	.	.	.	.
Mol01126	Protein	Tylosin resistance ATP-binding protein TlrC (TLRC)	.	tlrC	.	Streptomyces fradiae	1906	Streptomyces fradiae	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MRTSPSSQLSLHGVTKRYDDRVVLSQVSLAISPGEKAGIIGDNGAGKSTLLRLLAGEERPDAGEVTVIAPGGVGYLPQTLGLPPRATVQDAIDLAMTELRVLEAELRRTEAALAEAATDEALQDALTAYARLTEQYEVRDGYGADARVDAALHGLGLPGLPRDRRLGTLSGGERSRLALAATLASQPELLLLDEPTNDLDDRAVHWLEEHLSGHRGTVVTVTHDRVFLDRLTATVLEVDGRGVSRHGDGYAGYLAAKAAERRRRQQQYDEWRAELDRNRRLAEANVARLDGIPRKMGKAAFGHGAFRARGRDHGAMSRVRNAKERVERLTANPVAPPADRLSLTARIATADGPGEAPAAELDGVVVGSRLRVPKLRLGAAERLLITGPNGAGKSTLLSVLAGELSPDAGAVSVPGRVGHLRQEETPWPAKLTVLEAFAHNRPGDRDEQADRRLSLGLFEPEALRLRVGELSYGQRRRIELARLVSEPVGLLLLDEPTNHLSPALVEELEEALTGYGGALVLVTHDRRMRSRFTGSHLELREGVVSGAR	.	"Responsible for tylosin resistance, and is proposed to be a subunit of a multicomponent export system for the energy-dependent efflux of tylosin."	.	.	TLRC_STRFR	Reviewed	.	.	.	.	.	.
Mol01127	Protein	Type IV pilus biogenesis and competence protein PilQ (PILQ)	Outer membrane protein Omc; omc	pilQ	.	Neisseria gonorrhoeae	485	Neisseria gonorrhoeae	Neisseria	482	Neisseriaceae	481	Neisseriales	206351	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MNTKLTKIISGLFVATAAFQTASAGNITDIKVSSLPNKQKIVKVSFDKEIVNPTGFVTSSPARIALDFEQTGISMDQQVLEYADPLLSKISAAQNSSRARLVLNLNKPGQYNTEVRGNKVWIFINESDDTVSAPARPAVKAAPAAPAKQQAAAPFTESVVSVSAPFSPAKQQAAASAKQQAATPAKQTNIDFRKDGKNAGIIELAALGFAGQPDISQQHDHIIVTLKNHTLPTALQRSLDVADFKTPVQKVTLKRLNNDTQLIITTTGNWELVNKSAAPGYFTFQVLPKKQNLESGGVNNAPKTFTGRKISLDFQDVEIRTILQILAKESGMNIVASDSVSGKMTLSLKDVPWDQALDLVMQARNLDMRQQGNIVNMAPRRAACQRQSLLTSGKRHCRSGRAVFPKLPIEIQKCGRIPQHPALDNADTTGNRNTLVSGRGSVLIDPATNTLIVTDTRSVIEKFRKLIDELDVPAQQVMIEARIVEAADGFSRDLGVKFGATGRKKLKNETSAFGWGVNSGFGGGDKWEAKPKSTCRLPCRKQHFAGARDFSGALNLELSASESLSKTKTLANPRVLTQNRKEAKIESGYEIPFTVTTRSGGGNSTNTELKKAVLGLTVTANITPDGQIIMTVKINKDSPRQCASGNNTILCISTKSLNTQAMVENGGTLIVGGIYEENNGNTLTKVPLLATSPLSATSLKHSGKNRPPRTADFQLPPREL	.	Required for type IV pilus biogenesis and competence. Could function as a pore for exit of the pilus but also as a channel for entry of heme and antimicrobial agents and uptake of transforming DNA.	.	.	PILQ_NEIGO	Reviewed	.	.	.	.	.	.
Mol01128	Protein	UMP-CMP kinase (CMPK1)	Deoxycytidylate kinase; CK; dCMP kinase; Nucleoside-diphosphate kinase; Uridine monophosphate/cytidine monophosphate kinase; UMP/CMP kinase; UMP/CMPK; CMK; CMPK; UCK; UMK; UMPK	CMPK1	51727	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371873.10, CMPK1-203, 2937; ENST00000450808.2, CMPK1-204, 950; ENST00000471289.2, CMPK1-205, 816; ENST00000371871.8, CMPK1-202, 1212; ENST00000371870.3, CMPK1-201, 812"	MKPLVVFVLGGPGAGKGTQCARIVEKYGYTHLSAGELLRDERKNPDSQYGELIEKYIKEGKIVPVEITISLLKREMDQTMAANAQKNKFLIDGFPRNQDNLQGWNKTMDGKADVSFVLFFDCNNEICIERCLERGKSSGRSDDNRESLEKRIQTYLQSTKPIIDLYEEMGKVKKIDASKSVDEVFDEVVQIFDKEG	chr1:47333790-47378839[+]	Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity.	PDB: 1TEV; PDB: 7E9V	HGNC:18170	KCY_HUMAN	Reviewed	ENSG00000162368	.	.	.	.	.
Mol01129	Protein	Uncharacterized MFS-type transporter EfpA (EFPA)	Efflux protein A; Rv2846c	efpA	888575	Mycobacteriumtuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	1763	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTALNDTERAVRNWTAGRPHRPAPMRPPRSEETASERPSRYYPTWLPSRSFIAAVIAIGGMQLLATMDSTVAIVALPKIQNELSLSDAGRSWVITAYVLTFGGLMLLGGRLGDTIGRKRTFIVGVALFTISSVLCAVAWDEATLVIARLSQGVGSAIASPTGLALVATTFPKGPARNAATAVFAAMTAIGSVMGLVVGGALTEVSWRWAFLVNVPIGLVMIYLARTALRETNKERMKLDATGAILATLACTAAVFAFSIGPEKGWMSGITIGSGLVALAAAVAFVIVERTAENPVVPFHLFRDRNRLVTFSAILLAGGVMFSLTVCIGLYVQDILGYSALRAGVGFIPFVIAMGIGLGVSSQLVSRFSPRVLTIGGGYLLFGAMLYGSFFMHRGVPYFPNLVMPIVVGGIGIGMAVVPLTLSAIAGVGFDQIGPVSAIALMLQSLGGPLVLAVIQAVITSRTLYLGGTTGPVKFMNDVQLAALDHAYTYGLLWVAGAAIIVGGMALFIGYTPQQVAHAQEVKEAIDAGEL	.	.	.	.	EFPA_MYCTU	Reviewed	.	.	.	.	.	.
Mol01130	Protein	Uncharacterized oxidoreductase YeiQ (YEIQ)	b2172; JW2160	yeiQ	946688	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNTIASVTLPHHVHAPRYDRQQLQSRIVHFGFGAFHRAHQALLTDRVLNAQGGDWGICEISLFSGDQLMSQLRAQNHLYTVLEKGADGNQVIIVGAVHECLNAKLDSLAAIIEKFCEPQVAIVSLTITEKGYCIDPATGALDTSNPRIIHDLQTPEEPHSAPGILVEALKRRRERGLTPFTVLSCDNIPDNGHVVKNAVLGMAEKRSPELAGWIKEHVSFPGTMVDRIVPAATDESLVEISQHLGVNDPCAISCEPFIQWVVEDNFVAGRPAWEVAGVQMVNDVLPWEEMKLRMLNGSHSFLAYLGYLSGFAHISDCMQDRAFRHAARTLMLDEQAPTLQIKDVDLTQYADKLIARFANPALKHKTWQIAMDGSQKLPQRMLAGIRIHQGRETDWSLLALGVAGWMRYVSGVDDAGNAIDVRDPLSDKIRELVAGSSSEQRVTALLSLREVFGDDLPDNPHFVQAIEQAWQQIVQFGAHQALLNTLKI	.	.	.	.	YEIQ_ECOLI	Reviewed	.	.	.	.	.	.
Mol01131	Protein	Uncharacterized protein YkgG (YKGG)	b0308; JW5042	ykgG	945906	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MDNRGEFLNNVAQALGRPLRLEPQAEDAPLNNYANERLTQLNQQQRCDAFIQFASDVMLTRCELTSEAKAAEAAIRLCKELGDQSVVISGDTRLEELGISERLQQECNAVVWDPAKGAENISQAEQAKVGVVYAEYGLTESGGVVLFSAAERGRSLSLLPEYSLFILRKSTILPRVAQLAEKLHQKAQAGERMPSCINIISGPSSTADIELIKVVGVHGPVKAVYLIIEDC	.	.	.	.	YKGG_ECOLI	Reviewed	.	.	.	.	.	.
Mol01132	Protein	Undecaprenyl-diphosphatase (UPPP)	Bacitracin resistance protein; Undecaprenyl pyrophosphate phosphatase; bacA; upk; EF_2439	uppP	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MLFANLWKAIILGIIEGITEWLPISSTGHLILVDEFIKLDLSKDFMEMFNVVIQLGAIMAVVILYFHKLNPFSPKKNGEEKKDTWILWSKVLVACLPAAVIGLKFDDYLDAHFYNFLTVSIMLIVYGIAFIIIEKRNKNVAPKCTNLKDFTYKAALIVGAFQVLALIPGTSRSGATILGAILIGASRFVATEFSFFLGIPVMFGASFLKIFKFLAKGNTFGSEEIIILITGSIVAFVVSIIAIKFLLNYLKKNDFTVFGWYRVILGAILIGYWLFS	.	Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin (By similarity).	.	.	UPPP1_ENTFA	Reviewed	.	.	.	.	.	.
Mol01133	Protein	Undecaprenyl-diphosphatase BcrC (BCRC)	Undecaprenyl pyrophosphate phosphatase; ywoA; BSU36530	bcrC	936946	Bacillus subtilis	1423	Bacillus subtilis	Bacillus	1386	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNYEIFKAIHGLSHHNSVLDSIMVFITEYAIVAYALILLAIWLFGNTQSRKHVLYAGITGIAGLVINYLITLVYFEPRPFVAHTVHTLIPHAADASFPSDHTTGALAISIAMLFRNRKIGWPLVIFGLLTGFSRIWVGHHYPVDVLGSLVVAIIIGFLFFRFSDLLRPFVDLVVRIYEAIINKLTKKPTDQNF	.	Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.	.	.	BCRC_BACSU	Reviewed	.	.	.	.	.	.
Mol01134	Protein	Viomycin phosphotransferase (VPH)	Viomycin kinase	vph	63984161	Streptomyces vinaceus	1960	Streptomyces vinaceus	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MRIIETHRDLLSRLLPGDTVGGLAVHEGQFHHVVIGSHRVVCFARTRAAADRLPGRADVLRALAGIDLGFRTPQPLSEGGAQGTDEPPYLVLSRIPGAPLEDDVLTSPEVAEAVARQYATLLSGLAAAGDEEKVRAALPEAPANEWQEFATGVRTELFPLMSDGGRERAERELAALDALPHLTSAVVHGDLGGENVLWETVDGVPRMSGVVDWDEVGIGDPAEDLAAIGASYGEELLGRVLALGGWADNGTAERISAIRGTFALQQALYAQRDGDEEELADGLSGYR	.	The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation.	.	.	VPH_STRVI	Reviewed	.	.	.	.	.	.
Mol01135	Protein	Virginiamycin B lyase (VGBB)	Streptogramin B lyase	vgbB	.	Staphylococcus cohnii	29382	Staphylococcus cohnii	Staphylococcus	1279	Staphylococcaceae	90964	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNFYLEEFNLSIPDSGPYGITSSEDGKVWFTQHKANKISSLDQSGRIKEFEVPTPDAKVMCLIVSSLGDIWFTENGANKIGKLSKKGGFTEYPLPQPDSGPYGITEGLNGDIWFTQLNGDRIGKLTADGTIYEYDLPNKGSYPAFITLGSDNALWFTENQNNSIGRITNTGKLEEYPLPTNAAAPVGITSGNDGALWFVEIMGNKIGRITTTGEISEYDIPTPNARPHAITAGKNSEIWFTEWGANQIGRITNDKTIQEYQLQTENAEPHGITFGKDGSVWFALKCKIGKLNLNE	.	"Inactivates the type B streptogramin antibiotics by linearizing the lactone ring at the ester linkage, generating a free phenylglycine carboxylate and converting the threonyl moiety into 2-amino-butenoic acid."	PDB: 2QC5	.	O87275_9STAP	Unreviewed	.	.	.	.	.	.
Mol01136	Protein	Virginiamycin B lyase (VGBC)	Streptogramin B lyase; vgb; AK95_08365	vgbC	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MQIAAQEYKTANRESGPYGITARQDRTIWFTEQKGNRIGRLTKDGDMRTFEVPTPDAGVMSILSAHTGDLWFTEYKANKIGRMTMEGTFAEFELPEANSSPYGLAEGPDGAIWFTELSGNRIGRITPAGIITEYDLPCEGSYPSYITAGPDGALWFTENQNNCIGRITVDGEITEYRIPTEQSGPVGITTGADGALWFVQINGNQIGRITTAGEITEFKLPSGNARPHAITAGVSGDLWFTEWGANQIGRITCTGDITEYPIPTPSAEPHGITVDSGGEVWFAEECDQIGRFTIQY	.	"Inactivates the type B streptogramin antibiotics by linearizing the lactone ring at the ester linkage, generating a free phenylglycine carboxylate and converting the threonyl moiety into 2-amino-butenoic acid."	.	.	A0A1I9ZKK6_9BACL	Unreviewed	.	.	.	.	.	.
Mol01137	Protein	ZBTB16-RARA fusion protein (ZBTB16-RARA)	.	ZBTB16-RARA	7704; 5914	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	ZBT16_HUMAN / RARA_HUMAN	.	.	.	.	.	.	.
Mol01138	Protein	STAT5B-RARA fusion protein (STAT5B-RARA)	.	STAT5B-RARA	6777; 5914	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	STA5B_HUMAN/ RARA_HUMAN	.	.	.	.	.	.	.
Mol01139	Protein	Neurogenic locus notch homolog protein (NOTCH)	.	NOTCH	4853	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256646.7, NOTCH2-201, 11425; ENST00000652302.1, NOTCH2-210, 1847; ENST00000652264.1, NOTCH2-209, 593; ENST00000652737.1, NOTCH2-211, 367; ENST00000640021.1, NOTCH2-206, 2058; ENST00000651371.1, NOTCH2-208, 492; ENST00000650638.1, NOTCH2-207, 2917; ENST00000493703.1, NOTCH2-205, 553; ENST00000478864.1, NOTCH2-202, 520; ENST00000489731.1, NOTCH2-204, 414; ENST00000479412.2, NOTCH2-203, 3221"	MPALRPALLWALLALWLCCAAPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCPQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPGFEGSTCERNIDDCPNHRCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCANRNGGYGCVCVNGWSGDDCSENIDDCAFASCTPGSTCIDRVASFSCMCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEINECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGVLCEENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGVNCEINFDDCASNPCIHGICMDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINGVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGINCEVDKNECLSNPCQNGGTCDNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDISGYTCHCVLPYTGKNCQTVLAPCSPNPCENAAVCKESPNFESYTCLCAPGWQGQRCTIDIDECISKPCMNHGLCHNTQGSYMCECPPGFSGMDCEEDIDDCLANPCQNGGSCMDGVNTFSCLCLPGFTGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCKCQAGFDGVHCENNINECTESSCFNGGTCVDGINSFSCLCPVGFTGSFCLHEINECSSHPCLNEGTCVDGLGTYRCSCPLGYTGKNCQTLVNLCSRSPCKNKGTCVQKKAESQCLCPSGWAGAYCDVPNVSCDIAASRRGVLVEHLCQHSGVCINAGNTHYCQCPLGYTGSYCEEQLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDDCARGPHCLNGGQCMDRIGGYSCRCLPGFAGERCEGDINECLSNPCSSEGSLDCIQLTNDYLCVCRSAFTGRHCETFVDVCPQMPCLNGGTCAVASNMPDGFICRCPPGFSGARCQSSCGQVKCRKGEQCVHTASGPRCFCPSPRDCESGCASSPCQHGGSCHPQRQPPYYSCQCAPPFSGSRCELYTAPPSTPPATCLSQYCADKARDGVCDEACNSHACQWDGGDCSLTMENPWANCSSPLPCWDYINNQCDELCNTVECLFDNFECQGNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCAADQPENLAEGTLVIVVLMPPEQLLQDARSFLRALGTLLHTNLRIKRDSQGELMVYPYYGEKSAAMKKQRMTRRSLPGEQEQEVAGSKVFLEIDNRQCVQDSDHCFKNTDAAAALLASHAIQGTLSYPLVSVVSESLTPERTQLLYLLAVAVVIILFIILLGVIMAKRKRKHGSLWLPEGFTLRRDASNHKRREPVGQDAVGLKNLSVQVSEANLIGTGTSEHWVDDEGPQPKKVKAEDEALLSEEDDPIDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVICGPNRSFLSLKHTPMGKKSRRPSAKSTMPTSLPNLAKEAKDAKGSRRKKSLSEKVQLSESSVTLSPVDSLESPHTYVSDTTSSPMITSPGILQASPNPMLATAAPPAPVHAQHALSFSNLHEMQPLAHGASTVLPSVSQLLSHHHIVSPGSGSAGSLSRLHPVPVPADWMNRMEVNETQYNEMFGMVLAPAEGTHPGIAPQSRPPEGKHITTPREPLPPIVTFQLIPKGSIAQPAGAPQPQSTCPPAVAGPLPTMYQIPEMARLPSVAFPTAMMPQQDGQVAQTILPAYHPFPASVGKYPTPPSQHSYASSNAAERTPSHSGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGAGGGQRGPGTHMSEPPHNNMQVYA	chr1:119911553-120100779[-]	"Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus."	PDB: 2OO4; PDB: 5MWB	HGNC:7882	NOTC2_HUMAN	Reviewed	ENSG00000134250	.	.	.	.	.
Mol01140	Protein	Lipoprotein receptor-related protein (LRP)	A2MR; APR	LRP	4035	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000243077.8, LRP1-201, 14923; ENST00000554174.1, LRP1-207, 2175; ENST00000338962.8, LRP1-202, 2169; ENST00000553277.5, LRP1-204, 1693; ENST00000555124.1, LRP1-208, 550; ENST00000554118.1, LRP1-206, 418; ENST00000553446.1, LRP1-205, 292; ENST00000556356.1, LRP1-211, 5114; ENST00000556830.1, LRP1-212, 1847; ENST00000451724.6, LRP1-203, 1284; ENST00000556247.1, LRP1-210, 611; ENST00000555941.1, LRP1-209, 499"	MLTPPLLLLLPLLSALVAAAIDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMDGSDEGPHCRELQGNCSRLGCQHHCVPTLDGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFICGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANAQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVGGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGVTCLANPSYVPPPQCQPGEFACANSRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHTDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPSVKFGCKDSARCISKAWVCDGDNDCEDNSDEENCESLACRPPSHPCANNTSVCLPPDKLCDGNDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTVHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGQGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNRTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSGLEVIDAMRSQLGKATALAIMGDKLWWADQVSEKMGTCSKADGSGSVVLRNSTTLVMHMKVYDESIQLDHKGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGQYPRIERSRLDGTERVVLVNVSISWPNGISVDYQDGKLYWCDARTDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGSKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGRGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSRRITIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNEQHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKHVGSNMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQDDLTCRAVNSSCRAQDEFECANGECINFSLTCDGVPHCKDKSDEKPSYCNSRRCKKTFRQCSNGRCVSNMLWCNGADDCGDGSDEIPCNKTACGVGEFRCRDGTCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCEHGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESIAAGCLYNSTCDDREFMCQNRQCIPKHFVCDHDRDCADGSDESPECEYPTCGPSEFRCANGRCLSSRQWECDGENDCHDQSDEAPKNPHCTSQEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDSSDERGCHINECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQRCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSSRSVIVDTKITWPNGLTLDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGTNKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTDNCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLVNLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCNLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEHCRNGGTCAASPSGMPTCRCPTGFTGPKCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGYCENFGTCQMAADGSRQCRCTAYFEGSRCEVNKCSRCLEGACVVNKQSGDVTCNCTDGRVAPSCLTCVGHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEHVFSQQQPGHIASILIPLLLLLLLVLVAGVVFWYKRRVQGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA	chr12:57128483-57213361[+]	Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells	PDB: 1CR8; PDB: 1D2L; PDB: 1J8E; PDB: 2FYJ; PDB: 2FYL; PDB: 2KNX; PDB: 2KNY	HGNC:6692	LRP1_HUMAN	Reviewed	ENSG00000123384	.	.	.	.	.
Mol01141	Protein	Protein lin-28 homolog A (CSDD1)	CSDD1; LIN28; ZCCHC1	LIN28A	389421	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000345080.5, LIN28B-201, 5446; ENST00000637759.1, LIN28B-203, 2635; ENST00000635857.1, LIN28B-202, 912"	MGSVSNQQFAGGCAKAAEEAPEEAPEDAARAADEPQLLHGAGICKWFNVRMGFGFLSMTARAGVALDPPVDVFVHQSKLHMEGFRSLKEGEAVEFTFKKSAKGLESIRVTGPGGVFCIGSERRPKGKSMQKRRSKGDRCYNCGGLDHHAKECKLPPQPKKCHFCQSISHMVASCPLKAQQGPSAQGKPTYFREEEEEIHSPTLLPEAQN	chr6:104936616-105083332[+]	"RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism."	PDB: 2CQF; PDB: 2LI8; PDB: 5UDZ	HGNC:32207	LN28A_HUMAN	Reviewed	ENSG00000187772	.	.	.	.	.
Mol01142	Protein	Protein lin-28 homolog B (CSDD2)	CSDD2	LIN28B	79727	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000326279.11, LIN28A-202, 3975; ENST00000254231.4, LIN28A-201, 3458"	MAEGGASKGGGEEPGKLPEPAEEESQVLRGTGHCKWFNVRMGFGFISMINREGSPLDIPVDVFVHQSKLFMEGFRSLKEGEPVEFTFKKSSKGLESIRVTGPGGSPCLGSERRPKGKTLQKRKPKGDRCYNCGGLDHHAKECSLPPQPKKCHYCQSIMHMVANCPHKNVAQPPASSQGRQEAESQPCTSTLPREVGGGHGCTSPPFPQEARAEISERSGRSPQEASSTKSSIAPEEQSKKGPSVQKRKKT	chr1:26410817-26429728[+]	"Suppressor of microRNA (miRNA) biogenesis, including that of let-7 and possibly of miR107, miR-143 and miR-200c. Binds primary let-7 transcripts (pri-let-7), including pri-let-7g and pri-let-7a-1, and sequester them in the nucleolus, away from the microprocessor complex, hence preventing their processing into mature miRNA."	.	HGNC:15986	LN28B_HUMAN	Reviewed	ENSG00000131914	.	.	.	.	.
Mol01143	Protein	Adenylate cyclase-stimulating G alpha protein (GNAS)	GNAS; GNAS1; GSP; Adenylate cyclase-stimulating G alpha protein; Guanine nucleotide-binding protein G(s) subunit alpha isoforms short	GNAS	2778	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371085.8, GNAS-210, 1854; ENST00000371100.9, GNAS-214, 4027; ENST00000313949.11, GNAS-204, 2578; ENST00000371075.7, GNAS-208, 2551; ENST00000419558.7, GNAS-216, 2503; ENST00000453292.7, GNAS-218, 2147; ENST00000371095.7, GNAS-211, 1931; ENST00000265620.11, GNAS-201, 1866; ENST00000354359.12, GNAS-207, 1857; ENST00000371098.6, GNAS-212, 1719; ENST00000371081.5, GNAS-209, 730; ENST00000676826.2, GNAS-261, 4032; ENST00000371102.8, GNAS-215, 3438; ENST00000349036.9, GNAS-206, 3432; ENST00000423897.7, GNAS-217, 2648; ENST00000683015.1, GNAS-271, 2313; ENST00000306120.4, GNAS-203, 2073; ENST00000472183.6, GNAS-229, 1800; ENST00000485673.6, GNAS-243, 1793; ENST00000682803.1, GNAS-267, 1692; ENST00000663479.2, GNAS-259, 1666; ENST00000469431.6, GNAS-227, 1665; ENST00000477931.5, GNAS-233, 1663; ENST00000488652.6, GNAS-247, 1638; ENST00000462499.6, GNAS-220, 1625; ENST00000482112.6, GNAS-240, 1622; ENST00000470512.6, GNAS-228, 1622; ENST00000603546.2, GNAS-255, 1583; ENST00000604005.6, GNAS-256, 1582; ENST00000657090.1, GNAS-258, 1567; ENST00000467321.6, GNAS-225, 1563; ENST00000480232.6, GNAS-236, 1554; ENST00000478585.6, GNAS-234, 1548; ENST00000476935.6, GNAS-232, 1537; ENST00000480975.5, GNAS-237, 1534; ENST00000468895.6, GNAS-226, 1533; ENST00000492907.6, GNAS-250, 1499; ENST00000467227.6, GNAS-224, 1489; ENST00000464788.6, GNAS-222, 1476; ENST00000667293.2, GNAS-260, 1465; ENST00000481039.6, GNAS-238, 1417; ENST00000488546.6, GNAS-246, 1407; ENST00000306090.12, GNAS-202, 1089; ENST00000491348.5, GNAS-249, 1068; ENST00000461152.6, GNAS-219, 1040; ENST00000464960.5, GNAS-223, 986; ENST00000656419.1, GNAS-257, 919; ENST00000493744.5, GNAS-251, 812; ENST00000338783.7, GNAS-205, 674; ENST00000484504.5, GNAS-242, 662; ENST00000464624.7, GNAS-221, 3571; ENST00000481768.6, GNAS-239, 3358; ENST00000494081.5, GNAS-253, 557; ENST00000682134.1, GNAS-263, 3469; ENST00000490374.6, GNAS-248, 750; ENST00000683932.1, GNAS-273, 7318; ENST00000682986.1, GNAS-270, 6600; ENST00000683632.1, GNAS-272, 6319; ENST00000684644.1, GNAS-276, 5862; ENST00000682092.1, GNAS-262, 5826; ENST00000682680.1, GNAS-266, 5743; ENST00000682590.1, GNAS-265, 5729; ENST00000684284.1, GNAS-274, 3921; ENST00000682829.1, GNAS-268, 3870; ENST00000371099.6, GNAS-213, 3709; ENST00000682411.1, GNAS-264, 3637; ENST00000496934.5, GNAS-254, 2837; ENST00000684466.1, GNAS-275, 2181; ENST00000682917.1, GNAS-269, 2070; ENST00000684761.1, GNAS-277, 2035; ENST00000475610.2, GNAS-230, 1895; ENST00000476196.5, GNAS-231, 1839; ENST00000487862.5, GNAS-244, 1782; ENST00000483387.2, GNAS-241, 1170; ENST00000487981.5, GNAS-245, 581; ENST00000493958.5, GNAS-252, 534; ENST00000479025.1, GNAS-235, 466"	MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL	chr20:58839718-58911192[+]	Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs)	PDB: 5G53; PDB: 5UZ7; PDB: 5VAI; PDB: 6AU6; PDB: 6B3J; PDB: 6E3Y; PDB: 6E67; PDB: 6EG8; PDB: 6GDG; PDB: 6LI3; PDB: 6LMK; PDB: 6LPB; PDB: 6M1H; PDB: 6M1I; PDB: 6NI3; PDB: 6NIY; PDB: 6ORV; PDB: 6P9X; PDB: 6P9Y; PDB: 6PB0; PDB: 6PB1; PDB: 6UUN; PDB: 6UUS; PDB: 6UVA; PDB: 6VCB; PDB: 6VN7; PDB: 6WHC; PDB: 6WI9; PDB: 6WPW; PDB: 6WZG; PDB: 6X18; PDB: 6X19; PDB: 6X1A; PDB: 6XOX; PDB: 7BB6; PDB: 7BB7; PDB: 7BPH; PDB: 7BW0; PDB: 7BZ2; PDB: 7C2E; PDB: 7CFM; PDB: 7CFN; PDB: 7CKW; PDB: 7CKX; PDB: 7CKY; PDB: 7CKZ; PDB: 7CRH; PDB: 7CX2; PDB: 7CX3; PDB: 7CX4; PDB: 7CZ5; PDB: 7D3S; PDB: 7D7M; PDB: 7DH5; PDB: 7DHI; PDB: 7DHR; PDB: 7DUQ; PDB: 7DUR; PDB: 7EVM; PDB: 7F16; PDB: 7JOZ; PDB: 7JV5; PDB: 7JVP; PDB: 7JVQ; PDB: 7KH0; PDB: 7KI0; PDB: 7KI1; PDB: 7LCI; PDB: 7LJC; PDB: 7LJD; PDB: 7MBX; PDB: 7RTB; PDB: 7V9M	HGNC:4392	GNAS2_HUMAN	Reviewed	ENSG00000087460	.	.	.	.	.
Mol01144	Protein	Gamma-glutamylcysteine synthetase (GGCS)	Gamma-ECS	ggcs	.	Plasmodium berghei	5821	Plasmodium berghei	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MPALRPALLWALLALWLCCAAPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCPQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPGFEGSTCERNIDDCPNHRCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCANRNGGYGCVCVNGWSGDDCSENIDDCAFASCTPGSTCIDRVASFSCMCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEINECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGVLCEENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGVNCEINFDDCASNPCIHGICMDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINGVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGINCEVDKNECLSNPCQNGGTCDNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDISGYTCHCVLPYTGKNCQTVLAPCSPNPCENAAVCKESPNFESYTCLCAPGWQGQRCTIDIDECISKPCMNHGLCHNTQGSYMCECPPGFSGMDCEEDIDDCLANPCQNGGSCMDGVNTFSCLCLPGFTGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCKCQAGFDGVHCENNINECTESSCFNGGTCVDGINSFSCLCPVGFTGSFCLHEINECSSHPCLNEGTCVDGLGTYRCSCPLGYTGKNCQTLVNLCSRSPCKNKGTCVQKKAESQCLCPSGWAGAYCDVPNVSCDIAASRRGVLVEHLCQHSGVCINAGNTHYCQCPLGYTGSYCEEQLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDDCARGPHCLNGGQCMDRIGGYSCRCLPGFAGERCEGDINECLSNPCSSEGSLDCIQLTNDYLCVCRSAFTGRHCETFVDVCPQMPCLNGGTCAVASNMPDGFICRCPPGFSGARCQSSCGQVKCRKGEQCVHTASGPRCFCPSPRDCESGCASSPCQHGGSCHPQRQPPYYSCQCAPPFSGSRCELYTAPPSTPPATCLSQYCADKARDGVCDEACNSHACQWDGGDCSLTMENPWANCSSPLPCWDYINNQCDELCNTVECLFDNFECQGNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCAADQPENLAEGTLVIVVLMPPEQLLQDARSFLRALGTLLHTNLRIKRDSQGELMVYPYYGEKSAAMKKQRMTRRSLPGEQEQEVAGSKVFLEIDNRQCVQDSDHCFKNTDAAAALLASHAIQGTLSYPLVSVVSESLTPERTQLLYLLAVAVVIILFIILLGVIMAKRKRKHGSLWLPEGFTLRRDASNHKRREPVGQDAVGLKNLSVQVSEANLIGTGTSEHWVDDEGPQPKKVKAEDEALLSEEDDPIDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVICGPNRSFLSLKHTPMGKKSRRPSAKSTMPTSLPNLAKEAKDAKGSRRKKSLSEKVQLSESSVTLSPVDSLESPHTYVSDTTSSPMITSPGILQASPNPMLATAAPPAPVHAQHALSFSNLHEMQPLAHGASTVLPSVSQLLSHHHIVSPGSGSAGSLSRLHPVPVPADWMNRMEVNETQYNEMFGMVLAPAEGTHPGIAPQSRPPEGKHITTPREPLPPMGFLKIGTPLSWEDVQNVKSLIRLYGILQFVHSYKCNKDRKDEHIMFGDEIEYIIIRNDDKLKEASALLCATDLIDEMMNLESGNDCQYGSHWTPEYSSFTIEGTPSVPFKFELNSSYFIEHCMKIRRNKLNNVLSGLRGVQAITLPCYPNVLLNNSLIMAKKINLEKKKKKINKQEIVETSPINYNCIQINKTIHDSESCDENEPRKHISQKNENKNTSNDIISEDVEENKSTHFVSSDFTQQKYDDLLVPDISMDEVDINNRNDPKNDECVEKEDECQCDVANETLGIEEEDNIFISTIKENSIFKCELFKPDITSEYSNSCLVTDMVISPHSRYVTLTKNIRKRRGTKVISFNEIYKDVNTENMDIWKLSLDKNDKRLFKKKLKKTTLDGHLIWNKSMTNEKKKSEKKNKIKNDETELLDKVIKHSLFSNIDDDEDYIYSYNREFIEEYSKKCKNPIKNYVYLDAMFFGMSMCCQQITMSFQTINDAKYVYDQLAVIAPLFLAITACTPYLGGFLTETDARWRVISNSVDCRTEDELSYISKPRYSGISLYISDELPLKKNYYFYNDIDIILNKNVYDKLIKENVDEYLSRHISSLFVRDPIVVFEGSFSEKDITTIQNIMHEKNENINNSKMWSEEEMNKIYLSDDFEFLEDYKEKVLSSHQHFENFQSTNWNSVRFKPPPILDNNYLNGPSSIGWRVEFRTPDIQITDFENASVVALIMTLSKFILKKKLNLYIPMSKLEENLFRSSKRDAILKEKFYFRNDINYDTCNNEIEEKSIYDIFFNKNNGILYLCSLYIEEQFEQGLISLSAKNKINEYIQFIKLRCKGEICTGASFLRKFILNHSAYEQNSYINNQINYDLCKLISDIGKGEIAPHELLGGFVDPHKERIKNNLRQISKRQYLKSLAYKFISGEDYTQYLLLNEDLKHDKDFFIQNKHTNYEESDEYIDNNMLEFGKKLYQFSATFQLIPKGSIAQPAGAPQPQSTCPPAVAGPLPTMYQIPEMARLPSVAFPTAMMPQQDGQVAQTILPAYHPFPASVGKYPTPPSQHSYASSNAAERTPSHSGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGAGGGQRGPGTHMSEPPHNNMQVYA	.	.	.	.	Q8WP96_PLABE	Unreviewed	.	.	.	.	.	.
Mol01145	Protein	Cardiolipin synthase (CLS)	cls; CGZ46_07295; DAI13_08110; EU507_02395; H9Q64_02915	cls	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MKIFVWILLFLLVINVIAALITVFRKPRSISSVLAWMMTLIFLPGIGFIIYLFCGRGIDGQEVFKLSDDEKQMVQRIKEKVDVDNKKAGRDKRYDLLYDAKVLNRYFRNMDASPLAKRNSLQLFTDGQEKFQALFEDIRAAKETVHVEYYAFFNDTIGNQFLDVLIEKLHEGVEVYLIYDPWGSPGANKKFFARYVDAGGKVAPFITSRDMIRKTRLNYHLHRKIVVIDGKIGWTGGFNVGDQYLNVTEKFGYWRDTHIRLVGTAVFSLQEIFIMDWNASVKYPEERMTYHEKYFKLPEDHEVEHLSLQVVSDGPDSEEEILKSGFVRMIFSAEKSVWIQTPYLIPDDSMINALLVAVRSGVDVRIMIPCMPDHPFIYRATQYYANYLHKRGIKIYIYDSGFIHAKTMVIDDELAMVGTTNQDIRSYSLNFEVSTFIYNPDIAWMLAQVFEEDIEKSVLLTDEIIKKQGYWLRFKQNFSRLLSPVL	.	Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.	.	.	A0A246M4D0_ENTFL	Unreviewed	.	.	.	.	.	.
Mol01146	Protein	Colibactin polyketide synthase ClbC (CLBC)	Putative polyketide synthase	clbC	45135052	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MEYASEMNGMEIAIIGMAVRFPQSRTLHEFWHNIVQGKECVTFFSEEELLAEGVEQSTLDNPAYVRAKPYIEGICDFDAAFFGYSHKEAQTLDPKSRVLHEVAYHALEDAGYAQRTSDLITGVFVGASEDVDWLRRSLSQIGGDALNRFESGIYGHKDLLAHLIAYSLNLNGPVYSLYTSCSTSLSATHIACRSLLFGECDLALAGGITIDLPQKSGYFCQQGMIHSTDGHCRPFDSQASGTLFGDGAGVVVLRRLEDALAAGDRIYAVIRGSAVNNDGKQKIGFVAPGHEGQKAVICAACHLAEVSPESIGYVETHGTGTRIGDPIEFAALTEAFDTSHRQYCALGAVKANIGHTHAAAGVAGLIKTALVLHHRTIPPLANYQMPNSKLDLAHSPFYIPIQPQEWPASRMPPRAGVSSFGIGGTNVHMILEGLNPAVRDDHDQVRAPVFIPLSAPSFEQLDELTQQLTPLLATLDASTLAYTQQVARPVFDCRRVIQVENDGTQAMLASLDNLMPDAPWGLHCPDLRTTNDCTYAQWLAHSAHYQREATALTALLDGMNIPPAYCHAETWAAQANSSLLIRGCQTIAALKTWMNLLPTLTLLSGAGTGLLPAAAASGMIATQDVLHLLWEMEQKALHLWLPERHEPIPGYVLAWQGNPITDAQRNDRGFWSEALLADTRELGEGVHSINWVRLPPEIREDVDVLRYVAQLWCAGINVDWAVWYGTPLPQRGSASAYPFAHNHYPLPGRVMGSVETQPEAGPETHHPYQARPVLSVPFVAAHSRGMQYITGLMELLLEISPVGVDDDFFELGGHSLLVTQLTSRLERDFNVHIDLLTLMENPNPRNIYAHIAAQLGGEDNLEIACQ	.	.	.	.	Q0P7J3_ECOLX	Unreviewed	.	.	.	.	.	.
Mol01147	Protein	Tetracycline resistance protein TetW (TETW)	.	tetW	.	Butyrivibrio fibrisolvens	831	Butyrivibrio fibrisolvens	Butyrivibrio	830	Lachnospiraceae	186803	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTLTESLLYASGAISEPGSVEKGTTRTDTMFLERQRGITIQAAVTSFQWHRCKVNIVDTPGHMDFLAEVYRSLAVLDGAILVISAKDGVQAQTRILFHALRKMNIPTVIFINKIDQAGVDLQSVVQSVRDKLSADIIIKQTVSLSPEIVLEENTDIEAWDAVIENNDELLEKYIAGEPISREKLAREEQQRVQDASLFPVYHGSAKNGLGIQPLMDAVTGLFQPIGEQGGAALCGSVFKVEYTDCGQRRVYLRLYSGTLRLRDTVALAGREKLKITEMRIPSKGEIVRTDTAYQGEIVILPSDSVRLNDVLGDQTRLPRKRWREDPLPMLRTTIAPKTAAQRERLLDALTQLADTDPLLRCEVDSITHEIILSFLGRVQLEVVSALLSEKYKLETVVKEPSVIYMERPLKAASHTIHIEVPPNPFWASIGLSVTPLSLGSGVQYESRVSLGYLNQSFQNAVRDGIRYGLEQGLFGWNVTDCKICFEYGLYYSPVSTPADFRSLAPIVLEQALKESGTQLLEPYLSFILYAPQEYLSRAYHDAPKYCATIETAQVKKDEVVFTGEIPARCIQAYRTDLAFYTNGRSVCLTELKGYQAAVGQPVIQPRRPNSRLDKVRHMFQKVM	.	.	.	.	.	.	.	.	.	.	.	.
Mol01148	Protein	Zeste homolog 2 (ZH2)	.	ZH2	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01149	Protein	Unclear drug transporter ykgEF (DT-unclear)	.	ykgEF	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01150	Protein	Unclear drug transporter ydjXYZ (DT-unclear)	.	ydjXYZ	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01151	Protein	Vascular endothelial growth factor (VEGFR)	.	VEGFR	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01152	Protein	Chloramphenicol resistance protein (Tn5561-Unclear)	.	Tn5561	.	Rhodococcus erythropolis	1833	Rhodococcus erythropolis	Rhodococcus	1827	Nocardiaceae	85025	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01153	Protein	Tetracycline resistance protein TetU (TETU)	.	tetU	.	Enterococcus faecium	1352	Enterococcus faecium	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MQLRRGKATDWHAMVQESLDSFASPHFLPIDIKPIDKIVIEGLIAEPSNWSIIARHTKYKYRNLLKQESQNDELTNHLRETFKESADELKKELDTWLLGLDVTEK	.	.	.	.	.	.	.	.	.	.	.	.
Mol01154	Protein	Tetracycline resistance protein TetQ (TETQ)	.	tetQ	.	Bacteroides thetaiotaomicron	818	Bacteroides thetaiotaomicron	Bacteroides	816	Bacteroidaceae	815	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MRFDNASIVVYYCLIQMNIINLGILAHIDAGKTSVTENLLFASGATEKCGRVDNGDTITDSMDIEKRRGITVRASTTSIIWNGVKCNIIDTPGHMDFIAEVERTFKMLDGAVLILSAKEGIQAQTKLLFNTLQKLQIPTIIFINKIDRDGVNLERLYLDIKTNLSQDVLFMQTVVDGLVYPICSQTYIKEEYKEFVCNHDDNILERYLADSEISPADYWNTIIDLVAKAKVYPVLHGSAMFNIGINELLDAISSFILPPESVSNRLSAYLYKIEHDPKGHKRSFLKIIDGSLRLRDIVRINDSEKFIKIKNLKTIYQGREINVDEVGANDIAIVEDMEDFRIGDYLGTKPCLIQGLSHQHPALKSSVRPDRSEERSKVISALNTLWIEDPSLSFSINSYSDELEISLYGLTQKEIIQTLLEERFSVKVHFDEIKTIYKERPVKKVNKIIQIEVPPNPYWATIGLTLEPLPLGTGLQIESDISYGYLNHSFQNAVFEGIRMSCQSGLHGWEVTDLKVTFTQAEYYSPVSTPADFRQLTPYVFRLALQQSGVDILEPMLYFELQIPQAASSKAITDLQKMMSEIEDISCNNEWCHIKGKVPLNTSKDYASEVSSYTKGLGVFMVKPCGYQITKGDYSDNIRMNEKDKLLFMFQKSMSSK	.	.	.	.	.	.	.	.	.	.	.	.
Mol01155	Protein	Tetracycline resistance protein class A48 (TETA48)	.	TetAB(48)	.	Paenibacillus	44249	Paenibacillus	.	.	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01156	Protein	t(17;17)(q21;q21) (Unclear)	.	t(17;17)(q21;q21)	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01157	Protein	t(11;17)(q23;q21) (Unclear)	.	t(11;17)(q23;q21)	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01158	Protein	Sulfate permease 2 (SUL2)	.	sul2	.	Yersinia pestis	632	Yersinia pestis	Yersinia	629	Yersiniaceae	1903411	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNKSLIIFGIVNITSDSFSDGGRYLAPDAAIAQARKLMAEGADVIDLGPASSNPDAAPVSSDTEIARIAPVLDALKADGIPVSLDSYQPATQAYALSRGVAYLNDIRGFPDAAFYPQLAKSSAKLVVMHSVQDGQADRREAPAGDIMDHIAAFFDARIAALTGAGIKRNRLVLDPGMGFFLGAAPETSLSVLARFDELRLRFDLPVLLSVSRKSFLRALTGRGPGDVGAATLAAELAAAAGGADFIRTHEPRPLRDGLAVLAALKETARIR	.	.	.	.	.	.	.	.	.	.	.	.
Mol01159	Protein	Multidrug transporter MdfA (MDFA)	.	cmr	.	Rhodococcus fascians	1828	Rhodococcus fascians	Rhodococcus	1827	Nocardiaceae	85025	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MPFAIYVLGIAVFAQGTSEFMLSGLIPDMAQDLQVSVPTAGLLTSAFAIGMIIGAPLMAIVSMRWQRRRALLTFLITFMVVHVIGALTDSFGVLLVTRIVGALANAGFLAVALGAAMSMVPADMKGRATSVLLGGVTIACVVGVPGGALLGELWGWRASFWEVVLISAPAVAAIMASTPADSPTDSVPNATRELSSLRQRKLQLILVLGALINGATFCSFTYLAPTLTDVAGFDSRWIPLLLGLFGLGSFIGVSVGGRLADTRPFQLLVAGSAALLVGWIVFAITASHPVVTLVMLFVQGTLSFAVGSTLISRVLYVADGAPTLGGSFATAAFNVGAALGPALGGVAIGIGMGYRAPLWTSAALVALAIVIGAATWTRWREPRPALDTVPP	.	.	.	.	.	.	.	.	.	.	.	.
Mol01160	Protein	rgt1438 (Unclear)	.	rgt1438	.	Streptomyces speibonae	195801	Streptomyces speibonae	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MRMLLTTYGSRGDVEPLAGLAAGLRKLGVEARVCAPPDEEFAALPARAGVPLIPLGPPVRPVVAGERPPTPQDAFRLAAELVTARFDTLTEAAEGCQAVLATGLMPAGVRDVAEKLGIPYVFACFHIYGLPSRHFPPGARPGTPPAPDGTDHRELWEQDARSVNALYGDALNRHRTGIGLPPVRNVRDHVLTDRPWLAADPVLCPAEGMTEFDLVQTGPWFLPDERPLPAGLEEFLGAGAPPVYVGFGSMGAYAPEGIARVAVEACRAQGRRVVLARGWAGLTPDDGGADCFAVGEVNQQALFRRVAAVVHHGGAGTTTTAARAGAPQVVVPRIADQPYWAERVRDLGIGSAHPDPVVTFDSLSAALTTALAPEVRARARTVAGTIRTDGASVAARLLVETADRAGRPVSP	.	.	.	.	.	.	.	.	.	.	.	.
Mol01161	Protein	Phosphatidylinositol 3-kinase (PI3K)	.	PI3K	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01162	Protein	ATP-binding cassette sub-family B5 (ABCB5)	.	P-gp	.	Pichia pastoris	4922	Komagataella pastoris	Komagataella	460517	Phaffomycetaceae	115784	Saccharomycetales	4892	Saccharomycetes	4751	Ascomycota	4830	Fungi	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01163	Protein	ATP-binding cassette sub-family B5 (ABCB5)	.	P-gp	.	Salmonella nanoparticle	90371	Salmonella enterica subsp. enterica serovar Typhimurium	Salmonella	590	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01165	Protein	Protein PecM (PeECM)	.	pecM	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01166	Protein	Pyruvate decarboxylase 5 (PDC5)	.	PDC5	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRQVTPETLFEIGSVSKTFTATLAGYALAQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR	.	.	.	.	.	.	.	.	.	.	.	.
Mol01167	Protein	Pyruvate decarboxylase 3 (PDC3)	.	PDC3	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MRDTRFPCLCGIAASTLLFATTPAIAGEAPADRLKALVDAAVQPVMKANDIPGLAVAISLKGEPHYFSYGLASKEDGRRVTPETLFEIGSVSKTFTATLAGYALAQDKMRLDDRASQHWPALQGSRFDGISLLDLATYTAGGLPLQFPDSVQKDQAQIRDYYRQWQPTYAPGSQRLYSNPSIGLFGYLAARSLGQPFERLMEQQVFPALGLEQTHLDVPEAALAQYAQGYGKDDRPLRVGPGPLDAEGYGVKTSAADLLRFVDANLHPERLDRPWAQALDATHRGYYKVGDMTQGLGWEAYDWPISLKRLQAGNSTPMALQPHRIARLPAPQALEGQRLLNKTGSTNGFGAYVAFVPGRDLGLVILANRNYPNAERVKIAYAILSGLEQQGKVPLKR	.	.	.	.	.	.	.	.	.	.	.	.
Mol01168	Protein	Beta-lactamase (BLA)	.	OXA-31	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01169	Protein	Nitrate reductase 1 (narGHJI)	.	narGHJI	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01170	Protein	Major facilitator superfamily (MFS)	.	MFS	.	Vibrio cholerae	666	Vibrio cholerae	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01171	Protein	Multidrug resistance protein (MDR)	.	MDR	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01172	Protein	Colistin resistance protein (MCR-3.3-Unclear)	.	MCR-3.3	.	Aeromonas veronii	654	Aeromonas veronii	Aeromonas	642	Aeromonadaceae	84642	Aeromonadales	135624	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MPSLIKIKIVPLMFFLALYFAFMLNWRGVLHFYEILYKLEDFKFGFAISLPILLVAALNFVFVPFSIRYLIKPFFALLIALSAIVSYTMMKYRVLFDQNMIQNIFETNQNEALAYLSLPIIGWVTIAGFIPAILLFFVEIEYEEKWFKGILTRALSMFASLIVIAVIAALYYQDYVSVGRNNSNLQREIVPANFVNSTVKYVYNRYLAEPIPFTTLGDDAKRDTNQSKPTLMFLVVGETARGKNFSMNGYEKDTNPFTSKSGGVISFNDVRSCGTATAVSVPCMFSNMGRKEFDDNLARNSEGLLDVLQKTGVSIFWKENDGGCKGVCDRVPNIEIKPKDYPKFCDKNTCYDEVVLQELDSEIAQMKGDKLVGFHLIGSHGPTYYKRYPDAHRQFTPDCPRSDIENCTDEELTNTYDNTIRYTDFVIAEMIAKLKTYEDKYNTALLYVSDHGESLGALGLYLHGTPYKFAPDDQTRVPMQVWMSPGFIKEKGMNMECLQKNAAANRYSHDNIFSSVLGIWDVKTAIYEQELDIFKQCRNN	.	.	.	.	.	.	.	.	.	.	.	.
Mol01173	Protein	ABC protein lsaC (lsaC-Unclear)	.	lsaC	.	Streptococcus agalactiae	1311	Streptococcus agalactiae	Streptococcus	1301	Streptococcaceae	1300	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MSTIKIENLTFSYYGYVKPVFENVSFSFDTNWKTGLIGRNGIGKSTLFKLLLNQEVYKGKISKSVDFIKFPPNLSDTSKLGIELYRELISDEEEWKLFRELHLLKVDESLIYRKFETLSKGEQTKILLAILFTREDGFLLIDEPTNHLDMDGRKIVSEYLKNKKGFLLISHDRDFLDGCINHIISINRNSIDVQSGNFTSWYENKLMKDQFEISQNEKLRKDIKRLKEAARQSQIWSDKVENTKNGVKVSGVKPDKGHIGHQSAKMMKKSKNLENRQNKAIEEKQNLLKDIETKESLLLHPLHHHKNPLISVCDLSSYYGKKQILSNISFDIKQGDIVAIYGGNGSGKSTLIKILLGLNHEYSGDVKLASNLKISYVPQDTSNLTGSLNEYIHKQGVDETLCKTILRKLDFARELFEIDMKNYSDGQKKKVLIAVSLSKSAHIFIWDEPLNYLDVISRIQIEEIIKEANPTLIFVEHDKSFVEDIANKIIRL	.	.	.	.	.	.	.	.	.	.	.	.
Mol01174	Protein	Transcriptional regulatory protein LiaR (LIAR)	.	liaR	.	Enterococcus faecalis	1351	Enterococcus faecalis	Enterococcus	1350	Enterococcaceae	81852	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MIKVLLVDDHEMVRLGVSSYLSIQEDIEVIGEAENGRQGYEKAMTLRPDVILMDLVMEEMDGIESTKAILKDWPEAKIIIVTSFIDDEKVYPAIEAGAAGYLLKTSTAHEIADAIRATQRGERVLEPEVTTKMMEKMSRRNEPVLHEELTNRENEILMLISEGKSNQEIADELFITLKTVKTHVSNILAKLEVEDRTQAAIYAFKHGLVK	.	liaR is a response regulator found in the liaFSR signal transduction pathway. Mutations confer daptomycin resistance.	.	.	.	.	.	.	.	.	.	.
Mol01175	Protein	LAMTM4B (Unclear)	.	LAMTM4B	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01176	Protein	kanamycin resistance protein Kmr (KMR)	.	Kmr	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01177	Protein	Colistin resistance PEtN transferase (ICRMc )	.	ICR-Mc	.	Moraxella catarrhalis	480	Moraxella catarrhalis	Moraxella	475	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MSLKHNQTHNTTFTKFLKSNSFWSKGFWSNRHHRTKDLKGLDAYLFMAIVAIFLTTTANVTFFQQVMSVYPLANYAPFIASLAVVLTGVLLLLLVLLGYRHTLKTVAICFILIAAFAGHFTDTYGTVYDTTMLQNALQTDTAETKDLLSMKLLIRVVLLAGLPICWIIGQPLSFGTLKASLMKRLVTYLVALALVGLPILAFSSQYASFFREHKPLRFFTNPVTVMYSAGKLANMSYKNATKPTETIMHANDAIQKTTASTRKPRLVVMVVGETARADHASFNGYQRATFPHMDKLIGLGQVHNFGNVTSCGTSTAYSVPCMFSYLGAEKYDVDTADYHENVIDTLDRLGVAILWRDNNSDSKGVMNRLPAKQYQDYKNSPLQGGNNTICHTNPYDECRDVGMLVDLDDHVKAHANQDILIVLHQMGNHGPAYYKRYDDEFAQFLPVCTSSELAECERQTVINAYDNALLATDDFLKQTIDWLAAQTHADTAMLYLSDHGESLGEKGVYLHGMPKAFAPKEQLSIPALLWLGADTPFAVANSPTAGFSHDAITPTLLNLFDVSTQATADKTAFVNPLD	.	.	.	.	.	.	.	.	.	.	.	.
Mol01178	Protein	Heat shock protein HSP 90 (HSP90 )	.	Hsp90	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01179	Protein	H3 lysine 27 trimethylation (H3K27)	.	H3K27	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01180	Protein	Glutathione S-transferase  (GST)	.	GST	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01181	Protein	srmA open reading frame gimA (GIMA)	.	gimA	.	Streptomyces ambofaciens	1889	Streptomyces ambofaciens	Streptomyces	1883	Streptomycetaceae	2062	Streptomycetales	85011	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MRRGDLHETYRLDYAPHMHDPAHIAMFSIAAHGHVNPSLEVIRELVARGHRVTYAIPPLFAEKVAETGAEPKLWNSTLPGPDADPDAWGTTPLDNVEPFLDDAIQALPQLIAAYEGDEPDLVLHDITSYPARVLAHRWGVPAVSLSPNLVAWEGYEEEVGRPTWEEPLKTERGRAYDARFRGWLKENGITEDPDPFVGRPDRSLVLIPKALQPHADRVDEKTHTFVGACQGDRAAEGDWRRPEGAEKVVLVSLGSSFTKRPAFYRACVEAFGALPGWHVVLQVGRHVDPAELGDVPENVEVRSWVPQLAILKQADLFVTHAGAGGSQEGLATATPIVAVPQAVDQFGNADMLQGLGVGRHLPTEEATAEALRAAGLALVEDPEVARRLKEIQAGMAREGGTRRAADLIEAELAAART	.	.	.	.	.	.	.	.	.	.	.	.
Mol01183	Protein	Fibroblast growth factor receptor (FGFR)	.	FGFR	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01184	Protein	erm(X)cj (Unclear)	.	erm(X)cj	.	Corynebacterium jeikeium	38289	Corynebacterium jeikeium	Corynebacterium	1716	Corynebacteriaceae	1653	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSAYGQGRHEHGQNFLTNHKIINSIIDLVKQTSGPIIEIGPGSGALTHPMAHLGRAITAVEVDAKLAAKITQETSSAAVEVVHDDFLNFRLPATPCVIVGNIPFHLTTAILRKLLHAPAWTDAVLLMQWEVARRRAGVGATTMMTAQWSPWFTFHLGSRVPRSAFRPQPNVDGGILVIRRVGDPKIPIEQRKAFQAMVHTVFTARGRGIGEILRRQGCFHHVQKHNHGCAREESTPRPYLPDCYTNDWIDLFQVTGSSLPHHRPISPSGSSQRPPQRKNRSRRR	.	.	.	.	.	.	.	.	.	.	.	.
Mol01185	Protein	23S ribosomal RNA methyltransferase Erm34 (ERM34)	.	Erm(34)	.	Bacillus clausii	66692	Alkalihalobacillus clausii KSM-K16	Alkalihalobacillus	2675234	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MTKKMNKYNGKKLSRGEPPNFSGQHFMHNKRLLKEIVDKADVSVRDTVLELGAGKGALTTILSERADRVLAVEYDQKCIEALQWKLVGSKNVSILHQDIMKVALPTEPFVVVSNIPYSITTAIMKMLLNNPKNKLQRGAIVMEKGAAKRFTSVSPKDAYVMAWHMWFDIHYERGISRSSFSPPPKVDSALVRIVRKQHPLFPYKEAKAMHDFLSYALNNPRAPLDQVLRGIFTAPQAKKVRQAIGVKPETPVAMLHARQWAMVCDAMVRHVPKVYWPRRKR	.	.	.	.	.	.	.	.	.	.	.	.
Mol01186	Protein	Mitogen-activated protein kinase (MAPK)	.	ERK	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01187	Protein	Defensin resistance ABC transporter DerAB (DERAB)	.	DerAB	.	Lactobacillus casei	1582	Lacticaseibacillus casei	Lacticaseibacillus	2759736	Lactobacillaceae	33958	Lactobacillales	186826	Bacilli	91061	Firmicutes	1239	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01188	Protein	Cytochrome P450 family 3 subfamily A (CYP3A)	.	CYP3A	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01189	Protein	Beta-lactamase (BLA)	.	CTX-M-55	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MVKKSLRQFTLMATATVTLLLGSVPLYAQTADVQQKLAELERQSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAVAAVLKKSESEPNLLNQRVEIKKSDLVNYNPIAEKHVNGTMSLAELSAAALQYSDNVAMNKLIAHVGGPASVTAFARQLGDETFRLDRTEPTLNTAIPGDPRDTTSPRAMAQTLRNLTLGKALGDSQRAQLVTWMKGNTTGAASIQAGLPASWVVGDKTGSGGYGTTNDIAVIWPKDRAPLILVTYFTQPQPKAESRRDVLASAAKIVTDGL	.	.	.	.	.	.	.	.	.	.	.	.
Mol01190	Protein	Cytidine monophosphate deaminase (CMPD)	.	CMPD	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01191	Protein	Ribosomal RNA large subunit methyltransferase (CFR )	.	cfr	.	Paenibacillus sp.	58172	Paenibacillus sp.	Paenibacillus	44249	Paenibacillaceae	186822	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01192	Protein	Beta-lactamase (BLA)	.	blaS1	.	Mycobacterium smegmatis	1772	Mycolicibacterium smegmatis	Mycolicibacterium	1866885	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTNLSRRSVLIGSLAVMAAAGVRMPTASAAPVDDRIADLERRNNASIGIYAVDLDSNRTVAHRADDSFAMCSTFKAYLAARILRGAERGELSLDDRVFVDPAALLSNSPITETHAGGEMTLAELCQAALQRSDNAAANLLLKQIGGPAEITAFARSIGDQRTRLDRWETELNSAVPGDPRDTSTPAALAGGFRAVLTGDVLAPPQRQLLDEWMRANETSSLRAGLPDGWTSADKTGSGDYGSTNDVGIAYGPQGQRILLALMVRTRGDDPNADGFRPLIGELTALVLPELGVH	.	.	.	.	.	.	.	.	.	.	.	.
Mol01193	Protein	Ubiquitin-like modifier-activating enzyme Atg 4 (ATG4)	.	Atg 4	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01194	Protein	Acetylpolyamine amidohydrolase (APAH)	.	aphA15	.	Achromobacter xylosoxydanssubsp.denitrificans	32002	Achromobacter denitrificans	Achromobacter	222	Alcaligenaceae	506	Burkholderiales	80840	Betaproteobacteria	28216	Proteobacteria	1224	.	.	.	MTVALDEVSELKNLLSPLLDECTFEEVEYGQSDARVIRVLFPDRNTAYLKYASGSSAQEILQEHQRTRWLRTRALVPEVISYVSTSTVTILLTKALIGHNAADAADADPVIVVAEMARALRDLHSISPDDCPFDERLHLRLKLASGRLEAGLVDEEDFDHARQGMLARDVYEQLFIQMPGAEQLVVTHGDACPENFIFQGNAFVGFIDCGRVGLADKYQDLALASRNIDAVFGPELTNQFFIEYGEPNPNIAKIEYYRILDEFF	.	.	.	.	.	.	.	.	.	.	.	.
Mol01195	Protein	Acetylpolyamine amidohydrolase (APAH)	.	aphA1	.	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01196	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	.	APH(4)-Ia	.	Escherichia coli	562	Escherichia coli	Escherichia	561	Enterobacteriaceae	543	Enterobacterales	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKKPELTATSVEKFLIEKFDSVSDLMQLSEGEESRAFSFDVGGRGYVLRVNSCADGFYKDRYVYRHFASAALPIPEVLDIGEFSESLTYCISRRAQGVTLQDLPETELPAVLQPVAEAMDAIAAADLSQTSGFGPFGPQGIGQYTTWRDFICAIADPHVYHWQTVMDDTVSASVAQALDELMLWAEDCPEVRHLVHADFGSNNVLTDNGRITAVIDWSEAMFGDSQYEVANIFFWRPWLACMEQQTRYFERRHPELAGSPRLRAYMLRIGLDQLYQSLVDGNFDDAAWAQGRCDAIVRSGAGTVGRTQIARRSAAVWTDGCVEVLADSGNRRPSTRPRAKE	.	.	.	.	.	.	.	.	.	.	.	.
Mol01197	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	.	APH(3')-Iva	.	Bacillus circulans	1397	Niallia circulans	Niallia	2837506	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNESTRNWPEELLELLGQTELTVNKIGYSGDHVYHVKEYRGTPAFLKIAPSVWWRTLRPEIEALAWLDGKLPVPKILYTAEHGGMDYLLMEALGGKDGSHETIQAKRKLFVKLYAEGLRSVHGLDIRECPLSNGLEKKLRDAKRIVDESLVDPADIKEEYDCTPEELYGLLLESKPVTEDLVFAHGDYCAPNLIIDGEKLSGFIDLGRAGVADRYQDISLAIRSLRHDYGDDRYKALFLELYGLDGLDEDKVRYYIRLDEFF	.	.	.	.	.	.	.	.	.	.	.	.
Mol01198	Protein	Aminoglycoside 3'-phosphotransferase (A3AP)	.	APH(3')-Iva	.	Bacillus circulans	1397	Niallia circulans	Niallia	2837506	Bacillaceae	186817	Bacillales	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MNESTRNWPEELLELLGQTELTVNKIGYSGDHVYHVKEYRGTPAFLKIAPSVWWRTLRPEIEALAWLDGKLPVPKILYTAEHGGMDYLLMEALGGKDGSHETIQAKRKLFVKLYAEGLRSVHGLDIRECPLSNGLEKKLRDAKRIVDESLVDPADIKEEYDCTPEELYGLLLESKPVTEDLVFAHGDYCAPNLIIDGEKLSGFIDLGRAGVADRYQDISLAIRSLRHDYGDDRYKALFLELYGLDGLDEDKVRYYIRLDEFF	.	.	.	.	.	.	.	.	.	.	.	.
Mol01199	Protein	RAC serine/threonine-protein kinase (AKT)	.	Akt	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01200	Protein	acrB-acrA (Unclear)	.	acrB-acrA	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01201	Protein	Aminoglycoside (3'') (9) adenylyltransferase (AADA)	.	aadA25	.	Pasteurella multocida	747	Pasteurella multocida	Pasteurella	745	Pasteurellaceae	712	Pasteurellales	135625	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MREAVTIEISNQLSEVLSVIERHLESTLLAVHLYGSAVDGGLKPYSDIDLLVTVAVKLDETTRRALLNDLMEASAFPGESETLRAIEVTLVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPAMIDIDLAILLTKAREHSVALVGPAAEELFDPVPEQDLFEALNETLTLWNSPPDWAGDERNVVLTLSRIWYSAITGKIAPKDVAADWAIKRLPAQYQPVLLEARQAYLGQEEDRLASRADQLEEFVHYVKGEITKVVGK	.	.	.	.	.	.	.	.	.	.	.	.
Mol01202	Protein	Aminoglycoside N(3)-acetyltransferase (AACC2)	.	AAC(3)-IIc	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MHTRKAITEALQKLGVQTGDLLMVHASLKAIGPVEGGAETVVAALRSAVGPTGTVMGYASWDRSPYEETRNGARLDDKTRRTWPPFDPATAGTYRGFGLLNQFLVQAPGARRSAHPDASMVAVGPLAETLTEPHKLGHALGEGSPVERFVRLGGKALLLGAPLNSVTALHYAEAVADIPNKRRVTYEMPMLGSNGEVAWKTASDYDSNGILDCFAIEGKPDAVETIANAYVKLGRHREGVVGFAQCYLFDAQDIVTFGVTYLEKHFGTTPIVPAHEVAECSCEPSG	.	.	.	.	.	.	.	.	.	.	.	.
Mol01203	Protein	Aminoglycoside N(3)-acetyltransferase (AACC2)	.	AAC(3)-IIa	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	286	Pseudomonadaceae	135621	Pseudomonadales	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MHTQKAITEALQKLGVQSGDLLMVHASLKSIGPVEGGAETVVAALRSAVGPTGTVMGYASWDRSPYEETLNGARLDDNARRTWPPFDPATAGTYRGFGLLNQFLVQAPGARRSAHPDASMVAVGPLAETLTEPHELGHALGEGSPNERFVRLGGKALLLGAPLNSVTALHYAEAVADIPNKRWVTYEMPMPGRDGEVAWKTASDYDSNGILDCFAIEGKQDAVETIANAYVKLGRHREGVVGFAQCYLFDAQDIVTFGVTYLEKHFGTTPIVPAHEAIERSCEPSG	.	.	.	.	.	.	.	.	.	.	.	.
Mol01204	Protein	17p13 (Unclear)	.	17p13	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01205	LncRNA	WD repeat domain 7 (WDR7)	WDR7	WDR7	23335	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000254442.8, WDR7-201, 7295; ENST00000357574.7, WDR7-202, 7213; ENST00000593058.1, WDR7-212, 650; ENST00000585669.1, WDR7-203, 572; ENST00000589935.1, WDR7-208, 544; ENST00000591449.1, WDR7-210, 522; ENST00000585824.1, WDR7-205, 1151; ENST00000590557.5, WDR7-209, 590; ENST00000586124.2, WDR7-206, 569; ENST00000587403.5, WDR7-207, 551; ENST00000591524.1, WDR7-211, 872; ENST00000585754.1, WDR7-204, 617"	.	chr18:56651343-57029811[+]	.	.	HGNC:13490	.	.	ENSG00000091157	.	.	.	.	.
Mol01206	LncRNA	TPTE pseudogene 1 (TPTEP1)	TPTEP1	"KIAA0541, TRAG"	387590	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000426585.5, TPTEP1-204, 5725; ENST00000558085.6, TPTEP1-205, 1738; ENST00000588424.1, TPTEP1-207, 1602; ENST00000400593.6, TPTEP1-202, 1430; ENST00000415121.1, TPTEP1-203, 1067; ENST00000383140.7, TPTEP1-201, 971; ENST00000585784.1, TPTEP1-206, 473; ENST00000636884.1, TPTEP1-208, 213"	.	chr22:16601887-16698742[+]	.	.	HGNC:43648	.	.	ENSG00000100181	.	.	.	.	.
Mol01207	LncRNA	"H19, imprinted maternally expressed transcript (H19)"	H19	psiTPTE22	283120	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000411861.5, H19-201, 1771; ENST00000431095.7, H19-207, 944; ENST00000436715.5, H19-208, 861; ENST00000428066.7, H19-206, 1243; ENST00000414790.7, H19-203, 2353; ENST00000412788.6, H19-202, 2309; ENST00000691195.1, H19-213, 2305; ENST00000442037.6, H19-210, 2252; ENST00000439725.5, H19-209, 1929; ENST00000417089.6, H19-204, 1090; ENST00000447298.2, H19-211, 592; ENST00000422826.2, H19-205, 554; ENST00000643292.1, H19-212, 475"	.	chr11:1995171-2001470[-]	.	.	HGNC:4713	.	.	ENSG00000130600	.	.	.	.	.
Mol01208	LncRNA	Cyclin D binding myb like transcription factor 1 (DMTF1)	DMTF1	"ASM, ASM1, D11S813E, LINC00008, MIR675HG, NCRNA00008"	9988	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331242.12, DMTF1-201, 3702; ENST00000394703.9, DMTF1-202, 4038; ENST00000432937.6, DMTF1-213, 2411; ENST00000413276.6, DMTF1-204, 3548; ENST00000454008.6, DMTF1-220, 1158; ENST00000425705.2, DMTF1-209, 980; ENST00000449088.7, DMTF1-218, 783; ENST00000582925.5, DMTF1-234, 770; ENST00000430405.7, DMTF1-211, 637; ENST00000414630.6, DMTF1-205, 627; ENST00000446796.6, DMTF1-215, 610; ENST00000582204.1, DMTF1-232, 587; ENST00000453049.5, DMTF1-219, 585; ENST00000434534.5, DMTF1-214, 581; ENST00000579592.5, DMTF1-226, 579; ENST00000448598.5, DMTF1-217, 572; ENST00000420131.5, DMTF1-206, 568; ENST00000432366.6, DMTF1-212, 557; ENST00000423590.6, DMTF1-207, 545; ENST00000428819.5, DMTF1-210, 533; ENST00000412139.6, DMTF1-203, 4460; ENST00000447863.5, DMTF1-216, 3954; ENST00000579677.5, DMTF1-227, 3915; ENST00000425406.5, DMTF1-208, 3868; ENST00000547146.6, DMTF1-224, 3657; ENST00000579850.5, DMTF1-228, 3483; ENST00000584619.5, DMTF1-238, 1645; ENST00000580710.5, DMTF1-230, 635; ENST00000584457.5, DMTF1-237, 569; ENST00000583751.1, DMTF1-235, 177; ENST00000583833.1, DMTF1-236, 171; ENST00000488352.2, DMTF1-223, 2509; ENST00000480982.5, DMTF1-222, 2493; ENST00000580010.1, DMTF1-229, 2370; ENST00000473521.5, DMTF1-221, 590; ENST00000580803.1, DMTF1-231, 588; ENST00000582887.1, DMTF1-233, 562; ENST00000578926.1, DMTF1-225, 438"	.	chr7:87152409-87196337[+]	.	.	HGNC:14603	.	.	ENSG00000135164	.	.	.	.	.
Mol01209	LncRNA	TatD DNase domain containing 1 (TATDN1)	TATDN1	"DMP1, DMTF, MRUL, hDMP1"	83940	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000276692.11, TATDN1-201, 1029; ENST00000630259.1, TATDN1-221, 915; ENST00000519548.5, TATDN1-206, 889; ENST00000522810.5, TATDN1-214, 990; ENST00000517678.5, TATDN1-202, 815; ENST00000605953.5, TATDN1-220, 726; ENST00000523152.3, TATDN1-216, 692; ENST00000519232.5, TATDN1-205, 604; ENST00000523888.5, TATDN1-219, 591; ENST00000523214.5, TATDN1-217, 1134; ENST00000522927.5, TATDN1-215, 782; ENST00000520938.3, TATDN1-209, 690; ENST00000519776.5, TATDN1-207, 677; ENST00000522310.5, TATDN1-213, 667; ENST00000520321.5, TATDN1-208, 629; ENST00000521546.5, TATDN1-210, 731; ENST00000521973.5, TATDN1-211, 639; ENST00000518133.5, TATDN1-203, 636; ENST00000523631.5, TATDN1-218, 2016; ENST00000522280.1, TATDN1-212, 684; ENST00000518485.5, TATDN1-204, 656"	.	chr8:124488485-124539458[-]	.	.	HGNC:24220	.	.	ENSG00000147687	.	.	.	.	.
Mol01210	LncRNA	Very low density lipoprotein receptor (VLDLR)	VLDLR	CDA11	7436	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000382100.8, VLDLR-203, 9213; ENST00000681306.1, VLDLR-224, 5723; ENST00000680746.1, VLDLR-219, 5185; ENST00000681618.1, VLDLR-227, 4666; ENST00000382099.3, VLDLR-202, 2746; ENST00000680219.1, VLDLR-213, 1818; ENST00000680296.1, VLDLR-215, 1677; ENST00000382096.6, VLDLR-201, 517; ENST00000681518.1, VLDLR-226, 5642; ENST00000681644.1, VLDLR-228, 5087; ENST00000680891.1, VLDLR-221, 4386; ENST00000680043.1, VLDLR-211, 3519; ENST00000681806.1, VLDLR-230, 3239; ENST00000680243.1, VLDLR-214, 3068; ENST00000681942.1, VLDLR-232, 2618; ENST00000681876.1, VLDLR-231, 2298; ENST00000680332.1, VLDLR-216, 5594; ENST00000680745.1, VLDLR-218, 4439; ENST00000679750.1, VLDLR-207, 4079; ENST00000679851.1, VLDLR-209, 3951; ENST00000680751.1, VLDLR-220, 3532; ENST00000679488.1, VLDLR-205, 3257; ENST00000679718.1, VLDLR-206, 3021; ENST00000680021.1, VLDLR-210, 2875; ENST00000680975.1, VLDLR-222, 2421; ENST00000681770.1, VLDLR-229, 2282; ENST00000680440.1, VLDLR-217, 1932; ENST00000478776.2, VLDLR-204, 1911; ENST00000679780.1, VLDLR-208, 1736; ENST00000681087.1, VLDLR-223, 1666; ENST00000681486.1, VLDLR-225, 1338; ENST00000680150.1, VLDLR-212, 475"	.	chr9:2621182-2660056[+]	.	.	HGNC:12698	.	.	ENSG00000147852	.	.	.	.	.
Mol01211	LncRNA	Transmembrane protein 25 (TMEM25)	TMEM25	"CARMQ1, CHRMQ1, VLDLRCH"	84866	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000313236.10, TMEM25-201, 2420; ENST00000524725.5, TMEM25-208, 2630; ENST00000411589.6, TMEM25-205, 2442; ENST00000359862.8, TMEM25-204, 2395; ENST00000442938.6, TMEM25-206, 2228; ENST00000354064.11, TMEM25-202, 1965; ENST00000354284.8, TMEM25-203, 1456; ENST00000533102.5, TMEM25-225, 1410; ENST00000526853.1, TMEM25-212, 747; ENST00000526973.5, TMEM25-214, 583; ENST00000528373.5, TMEM25-217, 573; ENST00000533137.5, TMEM25-226, 570; ENST00000532762.5, TMEM25-224, 565; ENST00000527267.1, TMEM25-215, 565; ENST00000533689.1, TMEM25-229, 548; ENST00000525118.5, TMEM25-209, 596; ENST00000534181.5, TMEM25-230, 586; ENST00000529001.5, TMEM25-219, 936; ENST00000532749.1, TMEM25-223, 582; ENST00000533587.5, TMEM25-227, 558; ENST00000528934.5, TMEM25-218, 554; ENST00000530423.5, TMEM25-221, 546; ENST00000525129.1, TMEM25-210, 287; ENST00000533627.5, TMEM25-228, 3241; ENST00000524522.5, TMEM25-207, 3098; ENST00000531494.1, TMEM25-222, 1280; ENST00000527785.1, TMEM25-216, 841; ENST00000525298.5, TMEM25-211, 839; ENST00000526941.1, TMEM25-213, 656; ENST00000529176.5, TMEM25-220, 555"	.	chr11:118531041-118547280[+]	.	.	HGNC:25890	.	.	ENSG00000149582	.	.	.	.	.
Mol01212	LncRNA	Prostate androgen-regulated transcript 1 (PART1)	PART1	FLJ14399	25859	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000506884.2, PART1-202, 3240; ENST00000661844.1, PART1-204, 6029; ENST00000504876.2, PART1-201, 5616; ENST00000673825.1, PART1-209, 3923; ENST00000674024.1, PART1-211, 3882; ENST00000667192.1, PART1-207, 2831; ENST00000674053.1, PART1-212, 2572; ENST00000515734.2, PART1-203, 2569; ENST00000673670.1, PART1-208, 2567; ENST00000674007.1, PART1-210, 2188; ENST00000663388.1, PART1-205, 908; ENST00000664492.1, PART1-206, 573"	.	chr5:60487713-60548813[+]	.	.	HGNC:17263	.	.	ENSG00000152931	.	.	.	.	.
Mol01213	LncRNA	"Phosphate cytidylyltransferase 1A, choline (PCYT1A)"	PCYT1A	"DKFZP586D0823, NCRNA00206"	5130	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000431016.6, PCYT1A-206, 5546; ENST00000292823.6, PCYT1A-201, 5597; ENST00000419333.5, PCYT1A-204, 1325; ENST00000411591.5, PCYT1A-202, 1084; ENST00000430755.5, PCYT1A-205, 798; ENST00000441879.5, PCYT1A-209, 724; ENST00000443555.1, PCYT1A-210, 549; ENST00000412869.5, PCYT1A-203, 499; ENST00000433733.5, PCYT1A-207, 411; ENST00000444822.5, PCYT1A-211, 724; ENST00000438634.5, PCYT1A-208, 555; ENST00000491544.1, PCYT1A-216, 589; ENST00000473978.5, PCYT1A-214, 1430; ENST00000460677.5, PCYT1A-212, 1393; ENST00000460827.1, PCYT1A-213, 562; ENST00000488235.1, PCYT1A-215, 466"	.	chr3:196214222-196287957[-]	.	.	HGNC:8754	.	.	ENSG00000161217	.	.	.	.	.
Mol01214	LncRNA	Long non-protein coding RNA 1116 (LINC01116)	LINC01116	"CCTalpha, CT, CTPCT, PCYT1"	375295	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000695928.1, LINC01116-205, 3008; ENST00000339037.4, LINC01116-202, 1502; ENST00000295549.9, LINC01116-201, 1424; ENST00000658669.1, LINC01116-204, 1392; ENST00000655532.1, LINC01116-203, 878"	.	chr2:176611464-176637931[-]	.	.	HGNC:49259	.	.	ENSG00000163364	.	.	.	.	.
Mol01215	LncRNA	Long noncoding RNA lnc-IL7R (Lnc-IL7R)	Lnc-IL7R	Lnc-IL7R	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01216	LncRNA	Long non-protein coding RNA SARCC(SARCC)	LncRNA-SARCC	LncRNA-SARCC	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305097.6, P2RY1-201, 6309"	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01217	LncRNA	MIR31 host gene (MIR31HG)	MIR31HG	"P2Y1, SARCC"	554202	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000654736.1, MIR31HG-202, 2557; ENST00000304425.4, MIR31HG-201, 2702; ENST00000670459.1, MIR31HG-204, 2119; ENST00000663833.2, MIR31HG-203, 1914"	.	chr9:21453802-21559900[-]	.	.	HGNC:37187	.	.	ENSG00000171889	.	.	.	.	.
Mol01218	LncRNA	MIR4435-2 host gene (MIR4435-2HG)	MIR4435-2HG	"LOC554202, LncHIFCAR, hsa-lnc-31"	541471	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000605570.1, MIR4435-2HG-219, 1103; ENST00000645030.2, MIR4435-2HG-226, 858; ENST00000673654.1, MIR4435-2HG-275, 6654; ENST00000667670.1, MIR4435-2HG-264, 3647; ENST00000643013.1, MIR4435-2HG-224, 3565; ENST00000661945.1, MIR4435-2HG-246, 3533; ENST00000666144.1, MIR4435-2HG-257, 3455; ENST00000622940.1, MIR4435-2HG-222, 3380; ENST00000659933.1, MIR4435-2HG-241, 3345; ENST00000653568.1, MIR4435-2HG-228, 3214; ENST00000664422.1, MIR4435-2HG-252, 3199; ENST00000673653.1, MIR4435-2HG-274, 2803; ENST00000669515.1, MIR4435-2HG-266, 2746; ENST00000656416.1, MIR4435-2HG-234, 2486; ENST00000431385.6, MIR4435-2HG-205, 2382; ENST00000661559.1, MIR4435-2HG-243, 2104; ENST00000673964.1, MIR4435-2HG-299, 2065; ENST00000371162.4, MIR4435-2HG-202, 2044; ENST00000673960.1, MIR4435-2HG-296, 1946; ENST00000642191.1, MIR4435-2HG-223, 1945; ENST00000669658.1, MIR4435-2HG-267, 1872; ENST00000645051.2, MIR4435-2HG-227, 1831; ENST00000673775.1, MIR4435-2HG-281, 1826; ENST00000660442.1, MIR4435-2HG-242, 1761; ENST00000662384.1, MIR4435-2HG-248, 1758; ENST00000653687.1, MIR4435-2HG-229, 1754; ENST00000673770.1, MIR4435-2HG-280, 1749; ENST00000658936.1, MIR4435-2HG-236, 1729; ENST00000669917.1, MIR4435-2HG-269, 1724; ENST00000674070.1, MIR4435-2HG-305, 1703; ENST00000666390.1, MIR4435-2HG-260, 1695; ENST00000656067.1, MIR4435-2HG-232, 1684; ENST00000659791.1, MIR4435-2HG-239, 1634; ENST00000673961.1, MIR4435-2HG-297, 1628; ENST00000670295.1, MIR4435-2HG-270, 1612; ENST00000666367.1, MIR4435-2HG-259, 1612; ENST00000674132.1, MIR4435-2HG-308, 1609; ENST00000603827.1, MIR4435-2HG-217, 1587; ENST00000673728.1, MIR4435-2HG-278, 1570; ENST00000654473.1, MIR4435-2HG-230, 1557; ENST00000666683.1, MIR4435-2HG-262, 1549; ENST00000670715.1, MIR4435-2HG-271, 1546; ENST00000439362.6, MIR4435-2HG-208, 1542; ENST00000443467.6, MIR4435-2HG-212, 1520; ENST00000661655.1, MIR4435-2HG-244, 1518; ENST00000662635.1, MIR4435-2HG-249, 1516; ENST00000655573.1, MIR4435-2HG-231, 1511; ENST00000656303.1, MIR4435-2HG-233, 1490; ENST00000667218.1, MIR4435-2HG-263, 1481; ENST00000662335.1, MIR4435-2HG-247, 1480; ENST00000609902.6, MIR4435-2HG-221, 1465; ENST00000659079.1, MIR4435-2HG-237, 1459; ENST00000669050.1, MIR4435-2HG-265, 1458; ENST00000666652.1, MIR4435-2HG-261, 1455; ENST00000664009.1, MIR4435-2HG-251, 1435; ENST00000656760.1, MIR4435-2HG-235, 1433; ENST00000609220.2, MIR4435-2HG-220, 1417; ENST00000664443.1, MIR4435-2HG-253, 1413; ENST00000665096.1, MIR4435-2HG-256, 1408; ENST00000674092.1, MIR4435-2HG-307, 1408; ENST00000673668.1, MIR4435-2HG-276, 1401; ENST00000673804.1, MIR4435-2HG-283, 1389; ENST00000662889.1, MIR4435-2HG-250, 1384; ENST00000664999.1, MIR4435-2HG-255, 1358; ENST00000666204.1, MIR4435-2HG-258, 1344; ENST00000659458.1, MIR4435-2HG-238, 1342; ENST00000664498.1, MIR4435-2HG-254, 1340; ENST00000673700.1, MIR4435-2HG-277, 1332; ENST00000451884.6, MIR4435-2HG-214, 1326; ENST00000673798.1, MIR4435-2HG-282, 1299; ENST00000661707.1, MIR4435-2HG-245, 1289; ENST00000673809.1, MIR4435-2HG-284, 1256; ENST00000673962.1, MIR4435-2HG-298, 1255; ENST00000673632.1, MIR4435-2HG-272, 1227; ENST00000673845.1, MIR4435-2HG-289, 1197; ENST00000673649.1, MIR4435-2HG-273, 1138; ENST00000659806.1, MIR4435-2HG-240, 1120; ENST00000673937.1, MIR4435-2HG-293, 1030; ENST00000673866.1, MIR4435-2HG-290, 1027; ENST00000673878.1, MIR4435-2HG-291, 991; ENST00000674013.1, MIR4435-2HG-301, 986; ENST00000453478.2, MIR4435-2HG-215, 969; ENST00000673988.1, MIR4435-2HG-300, 968; ENST00000643766.1, MIR4435-2HG-225, 963; ENST00000673814.1, MIR4435-2HG-285, 908; ENST00000673958.1, MIR4435-2HG-294, 903; ENST00000432268.1, MIR4435-2HG-206, 881; ENST00000674037.1, MIR4435-2HG-303, 871; ENST00000673959.1, MIR4435-2HG-295, 864; ENST00000674087.1, MIR4435-2HG-306, 832; ENST00000419736.5, MIR4435-2HG-204, 777; ENST00000604981.5, MIR4435-2HG-218, 759; ENST00000673843.1, MIR4435-2HG-288, 708; ENST00000439494.1, MIR4435-2HG-209, 707; ENST00000441075.1, MIR4435-2HG-210, 704; ENST00000673756.1, MIR4435-2HG-279, 680; ENST00000444301.5, MIR4435-2HG-213, 666; ENST00000673840.1, MIR4435-2HG-287, 660; ENST00000669875.1, MIR4435-2HG-268, 645; ENST00000673894.1, MIR4435-2HG-292, 628; ENST00000674045.1, MIR4435-2HG-304, 598; ENST00000432818.5, MIR4435-2HG-207, 572; ENST00000308604.5, MIR4435-2HG-201, 552; ENST00000442293.5, MIR4435-2HG-211, 546; ENST00000409569.2, MIR4435-2HG-203, 514; ENST00000674026.1, MIR4435-2HG-302, 419; ENST00000603310.5, MIR4435-2HG-216, 413; ENST00000673821.1, MIR4435-2HG-286, 392"	.	chr2:111006015-111523376[-]	.	.	HGNC:35163	.	.	ENSG00000172965	.	.	.	.	.
Mol01219	LncRNA	ZNFX1 antisense RNA 1 (ZFAS1)	ZFAS1	"AGD2, AK001796, LINC00978, MIR4435-1HG, MORRBID, lncRNA-AWPPH"	441951	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000663883.1, ZFAS1-213, 640; ENST00000620594.2, ZFAS1-209, 4526; ENST00000652916.1, ZFAS1-211, 2880; ENST00000371743.8, ZFAS1-202, 2608; ENST00000450535.5, ZFAS1-206, 1075; ENST00000441722.5, ZFAS1-205, 946; ENST00000417721.5, ZFAS1-203, 860; ENST00000623640.1, ZFAS1-210, 732; ENST00000667889.1, ZFAS1-214, 627; ENST00000618800.1, ZFAS1-208, 597; ENST00000458653.5, ZFAS1-207, 596; ENST00000428008.6, ZFAS1-204, 568; ENST00000659056.1, ZFAS1-212, 527; ENST00000326677.9, ZFAS1-201, 504"	.	chr20:49278178-49299600[+]	.	.	HGNC:33101	.	.	ENSG00000177410	.	.	.	.	.
Mol01220	LncRNA	Cancer susceptibility 2 (CASC2)	C20orf199; HSUP1; HSUP2; NCRNA00275; ZNFX1-AS1; C10orf5	CASC2	255082	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000435944.5, CASC2-203, 3270; ENST00000454781.6, CASC2-205, 5817; ENST00000454857.6, CASC2-206, 3931; ENST00000426021.5, CASC2-202, 3232; ENST00000665675.1, CASC2-210, 2965; ENST00000657543.1, CASC2-209, 976; ENST00000439517.2, CASC2-204, 957; ENST00000622752.1, CASC2-208, 762; ENST00000414722.5, CASC2-201, 679; ENST00000614455.4, CASC2-207, 489"	.	chr10:118046279-118210158[+]	.	.	HGNC:22933	.	.	ENSG00000177640	.	.	.	.	.
Mol01222	LncRNA	Protein disulfide isomerase family A member 3 pseudogene 1 (PDIA3P1)	PDIA3P1	C10orf5	171423	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000649713.1, PDIA3P1-203, 2212; ENST00000440377.2, PDIA3P1-201, 1571; ENST00000471856.1, PDIA3P1-202, 1510"	.	chr1:147172744-147179622[+]	.	.	HGNC:4607	.	.	ENSG00000180867	.	.	.	.	.
Mol01223	LncRNA	TP53 target 1 (TP53TG1)	TP53TG1	"GRP58P, PDIA3P"	11257	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000661943.2, TP53TG1-210, 3168; ENST00000654969.1, TP53TG1-209, 2982; ENST00000416560.7, TP53TG1-202, 1447; ENST00000421293.3, TP53TG1-203, 1265; ENST00000359941.11, TP53TG1-201, 1144; ENST00000653182.1, TP53TG1-208, 949; ENST00000610086.1, TP53TG1-206, 849; ENST00000690980.1, TP53TG1-221, 818; ENST00000687819.1, TP53TG1-217, 814; ENST00000685707.1, TP53TG1-213, 733; ENST00000689725.1, TP53TG1-220, 729; ENST00000542586.2, TP53TG1-205, 685; ENST00000686297.1, TP53TG1-215, 628; ENST00000689667.1, TP53TG1-219, 604; ENST00000685722.1, TP53TG1-214, 565; ENST00000432193.7, TP53TG1-204, 561; ENST00000685527.1, TP53TG1-211, 489; ENST00000616845.1, TP53TG1-207, 468; ENST00000685636.1, TP53TG1-212, 349; ENST00000688353.1, TP53TG1-218, 320; ENST00000686728.1, TP53TG1-216, 305"	.	chr7:87322943-87345552[-]	.	.	HGNC:17026	.	.	ENSG00000182165	.	.	.	.	.
Mol01224	LncRNA	WT1 antisense RNA (WT1-AS)	WT1-AS	"H_RG012D21.9, LINC00096, TP53AP1"	51352	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000690579.1, WT1-AS-211, 931; ENST00000395900.1, WT1-AS-201, 3828; ENST00000494911.5, WT1-AS-205, 1320; ENST00000525436.1, WT1-AS-206, 1254; ENST00000689448.1, WT1-AS-210, 1254; ENST00000686872.1, WT1-AS-207, 1254; ENST00000687495.1, WT1-AS-208, 618; ENST00000478367.5, WT1-AS-204, 561; ENST00000691801.1, WT1-AS-212, 542; ENST00000442957.1, WT1-AS-202, 482; ENST00000687964.1, WT1-AS-209, 460; ENST00000459866.1, WT1-AS-203, 328"	.	chr11:32435518-32500632[+]	.	.	HGNC:18135	.	.	ENSG00000183242	.	.	.	.	.
Mol01225	LncRNA	Long non-protein coding RNA 518 (LINC00518)	LINC00518	"WIT-1, WIT1, WT1-AS1, WT1AS"	221718	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000655125.1, LINC00518-206, 1433; ENST00000496285.6, LINC00518-205, 1729; ENST00000662081.1, LINC00518-208, 1709; ENST00000479822.2, LINC00518-202, 1362; ENST00000656574.1, LINC00518-207, 1287; ENST00000491317.1, LINC00518-204, 1228; ENST00000487130.1, LINC00518-203, 999; ENST00000472178.1, LINC00518-201, 853"	.	chr6:10429255-10435015[-]	.	.	HGNC:28626	.	.	ENSG00000183674	.	.	.	.	.
Mol01226	LncRNA	Solute carrier family 6 member 9 (SLC6A9)	SLC6A9	"C6orf218, MGC40222"	6536	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000372310.8, SLC6A9-205, 3206; ENST00000673836.1, SLC6A9-212, 3119; ENST00000360584.6, SLC6A9-202, 2330; ENST00000357730.6, SLC6A9-201, 2168; ENST00000475075.6, SLC6A9-207, 1881; ENST00000372307.7, SLC6A9-204, 2162; ENST00000372306.7, SLC6A9-203, 1926; ENST00000466926.1, SLC6A9-206, 591; ENST00000528803.1, SLC6A9-210, 524; ENST00000492434.6, SLC6A9-209, 592; ENST00000533007.1, SLC6A9-211, 508; ENST00000489764.1, SLC6A9-208, 930"	.	chr1:43991500-44031467[-]	.	.	HGNC:11056	.	.	ENSG00000196517	.	.	.	.	.
Mol01227	LncRNA	Small nucleolar RNA host gene 12 (SNHG12)	SNHG12	GLYT1	85028	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000648327.1, SNHG12-215, 1998; ENST00000474814.1, SNHG12-206, 1903; ENST00000481368.6, SNHG12-209, 1800; ENST00000461448.6, SNHG12-201, 1644; ENST00000470977.6, SNHG12-205, 1104; ENST00000648251.1, SNHG12-214, 1090; ENST00000461832.2, SNHG12-202, 1082; ENST00000464612.5, SNHG12-204, 719; ENST00000464115.1, SNHG12-203, 712; ENST00000650259.1, SNHG12-217, 389; ENST00000648127.1, SNHG12-213, 1871; ENST00000488745.5, SNHG12-211, 1365; ENST00000650239.1, SNHG12-216, 1149; ENST00000481220.6, SNHG12-208, 754; ENST00000531126.7, SNHG12-212, 728; ENST00000483436.5, SNHG12-210, 682; ENST00000692541.1, SNHG12-218, 639; ENST00000475441.6, SNHG12-207, 524; ENST00000693199.1, SNHG12-219, 480"	.	chr1:28578538-28583132[-]	.	.	HGNC:30062	.	.	ENSG00000197989	.	.	.	.	.
Mol01228	LncRNA	Small nucleolar RNA host gene 5 (SNHG5)	SNHG5	"ASLNC04080, C1orf79, LINC00100, PNAS-123"	387066	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000656092.1, SNHG5-230, 5764; ENST00000431043.2, SNHG5-207, 1504; ENST00000662914.1, SNHG5-253, 1208; ENST00000420199.6, SNHG5-203, 1105; ENST00000655847.1, SNHG5-228, 1316; ENST00000658077.1, SNHG5-235, 5169; ENST00000673634.1, SNHG5-284, 4192; ENST00000655116.1, SNHG5-226, 3657; ENST00000673729.1, SNHG5-287, 2956; ENST00000670094.1, SNHG5-279, 2704; ENST00000673640.1, SNHG5-285, 2459; ENST00000673769.1, SNHG5-288, 2358; ENST00000663073.1, SNHG5-254, 2112; ENST00000661011.1, SNHG5-249, 2052; ENST00000666667.1, SNHG5-264, 2012; ENST00000658742.1, SNHG5-238, 1969; ENST00000658584.1, SNHG5-237, 1914; ENST00000671327.1, SNHG5-282, 1897; ENST00000658919.1, SNHG5-241, 1831; ENST00000665113.1, SNHG5-261, 1743; ENST00000667693.1, SNHG5-271, 1741; ENST00000668505.1, SNHG5-273, 1640; ENST00000659484.1, SNHG5-243, 1489; ENST00000654795.1, SNHG5-225, 1450; ENST00000664449.1, SNHG5-259, 1440; ENST00000659276.1, SNHG5-242, 1425; ENST00000623650.4, SNHG5-217, 1425; ENST00000661487.1, SNHG5-251, 1394; ENST00000623163.4, SNHG5-215, 1364; ENST00000670410.1, SNHG5-281, 1345; ENST00000656441.1, SNHG5-231, 1323; ENST00000624128.2, SNHG5-220, 1293; ENST00000655881.1, SNHG5-229, 1278; ENST00000660580.1, SNHG5-247, 1265; ENST00000657398.1, SNHG5-234, 1258; ENST00000657203.1, SNHG5-232, 1236; ENST00000652832.1, SNHG5-224, 1232; ENST00000623901.4, SNHG5-218, 1231; ENST00000661360.1, SNHG5-250, 1187; ENST00000655834.1, SNHG5-227, 1176; ENST00000667289.1, SNHG5-266, 1167; ENST00000658383.1, SNHG5-236, 1163; ENST00000666607.1, SNHG5-263, 1162; ENST00000666912.1, SNHG5-265, 1154; ENST00000658836.1, SNHG5-239, 1129; ENST00000660318.1, SNHG5-246, 1095; ENST00000668100.1, SNHG5-272, 1065; ENST00000659725.1, SNHG5-244, 1058; ENST00000669413.1, SNHG5-276, 1022; ENST00000670327.1, SNHG5-280, 1008; ENST00000587692.6, SNHG5-211, 1000; ENST00000662245.1, SNHG5-252, 977; ENST00000658871.1, SNHG5-240, 967; ENST00000623910.4, SNHG5-219, 961; ENST00000657339.1, SNHG5-233, 947; ENST00000369605.9, SNHG5-201, 934; ENST00000665270.1, SNHG5-262, 902; ENST00000674091.1, SNHG5-289, 871; ENST00000663448.1, SNHG5-256, 871; ENST00000428833.6, SNHG5-206, 866; ENST00000427501.6, SNHG5-205, 823; ENST00000650155.1, SNHG5-223, 818; ENST00000665041.1, SNHG5-260, 804; ENST00000435947.6, SNHG5-209, 790; ENST00000671650.1, SNHG5-283, 772; ENST00000622963.4, SNHG5-213, 765; ENST00000668512.1, SNHG5-274, 750; ENST00000669824.1, SNHG5-278, 738; ENST00000669160.1, SNHG5-275, 703; ENST00000659811.1, SNHG5-245, 703; ENST00000663133.1, SNHG5-255, 680; ENST00000667622.1, SNHG5-269, 638; ENST00000624295.3, SNHG5-221, 632; ENST00000425170.2, SNHG5-204, 623; ENST00000667637.1, SNHG5-270, 612; ENST00000664198.1, SNHG5-257, 600; ENST00000673721.1, SNHG5-286, 593; ENST00000589187.5, SNHG5-212, 568; ENST00000667545.1, SNHG5-268, 553; ENST00000669678.1, SNHG5-277, 518; ENST00000664396.1, SNHG5-258, 467; ENST00000623001.4, SNHG5-214, 456; ENST00000414002.6, SNHG5-202, 451; ENST00000433843.2, SNHG5-208, 438; ENST00000453754.5, SNHG5-210, 401; ENST00000623267.3, SNHG5-216, 374; ENST00000667421.1, SNHG5-267, 365; ENST00000660949.1, SNHG5-248, 279; ENST00000625175.3, SNHG5-222, 257"	.	chr6:85650491-85678932[-]	.	.	HGNC:21026	.	.	ENSG00000203875	.	.	.	.	.
Mol01229	LncRNA	Ewing sarcoma associated transcript 1 (EWSAT1)	EWSAT1	"C6orf160, LINC00044, MGC16362, NCRNA00044, U50HG, bA33E24.2"	283673	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000415504.5, EWSAT1-201, 2214; ENST00000440444.1, EWSAT1-203, 2498; ENST00000558922.2, EWSAT1-206, 1725; ENST00000435479.1, EWSAT1-202, 872; ENST00000558147.1, EWSAT1-204, 661; ENST00000558369.5, EWSAT1-205, 561; ENST00000559914.1, EWSAT1-207, 536; ENST00000559964.5, EWSAT1-208, 359"	.	chr15:69072926-69095820[+]	.	.	HGNC:26596	.	.	ENSG00000212766	.	.	.	.	.
Mol01230	LncRNA	Urothelial cancer associated 1 (UCA1)	UCA1	"FLJ33768, LINC00277, NCRNA00277, TMEM84"	652995	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000645805.1, UCA1-229, 2365; ENST00000644174.2, UCA1-213, 2688; ENST00000644567.2, UCA1-216, 2627; ENST00000397381.6, UCA1-201, 2057; ENST00000655708.1, UCA1-238, 1916; ENST00000655191.1, UCA1-237, 1892; ENST00000666830.1, UCA1-243, 1789; ENST00000645156.1, UCA1-222, 1731; ENST00000642256.2, UCA1-204, 1725; ENST00000645764.1, UCA1-228, 1659; ENST00000644400.1, UCA1-214, 1572; ENST00000644103.1, UCA1-212, 1337; ENST00000643552.1, UCA1-208, 1319; ENST00000671188.1, UCA1-245, 1287; ENST00000644962.1, UCA1-221, 1284; ENST00000644796.2, UCA1-219, 1279; ENST00000645177.1, UCA1-223, 1267; ENST00000659568.1, UCA1-240, 1263; ENST00000645708.2, UCA1-227, 1245; ENST00000646397.1, UCA1-233, 1215; ENST00000644845.2, UCA1-220, 1208; ENST00000647185.1, UCA1-235, 1199; ENST00000670862.1, UCA1-244, 1193; ENST00000645221.1, UCA1-224, 1191; ENST00000646128.1, UCA1-232, 1174; ENST00000646494.1, UCA1-234, 1172; ENST00000642894.1, UCA1-207, 1159; ENST00000645251.1, UCA1-225, 1155; ENST00000644730.1, UCA1-218, 1122; ENST00000642269.1, UCA1-205, 1111; ENST00000643846.1, UCA1-211, 1084; ENST00000643818.1, UCA1-210, 1055; ENST00000600160.3, UCA1-203, 998; ENST00000647292.1, UCA1-236, 994; ENST00000642440.2, UCA1-206, 984; ENST00000589333.3, UCA1-202, 957; ENST00000665604.1, UCA1-242, 926; ENST00000645389.2, UCA1-226, 878; ENST00000644590.1, UCA1-217, 864; ENST00000644502.1, UCA1-215, 855; ENST00000645877.1, UCA1-231, 720; ENST00000645821.2, UCA1-230, 594; ENST00000664784.1, UCA1-241, 591; ENST00000643567.1, UCA1-209, 581; ENST00000658824.1, UCA1-239, 548"	.	chr19:15828206-15836328[+]	.	.	HGNC:37126	.	.	ENSG00000214049	.	.	.	.	.
Mol01231	LncRNA	Maternally expressed 3 (MEG3)	MEG3	"CUDR, LINC00178, UCAT1, onco-lncRNA-36"	55384	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000556407.5, MEG3-226, 632; ENST00000522771.9, MEG3-220, 12998; ENST00000455531.1, MEG3-213, 4867; ENST00000452120.7, MEG3-210, 4504; ENST00000424076.9, MEG3-207, 4471; ENST00000398461.5, MEG3-202, 3452; ENST00000398460.3, MEG3-201, 3382; ENST00000524035.5, MEG3-222, 2853; ENST00000523671.7, MEG3-221, 2346; ENST00000662362.1, MEG3-250, 2072; ENST00000649261.1, MEG3-242, 1949; ENST00000648609.1, MEG3-234, 1949; ENST00000423456.6, MEG3-206, 1835; ENST00000519709.6, MEG3-214, 1760; ENST00000650041.1, MEG3-244, 1729; ENST00000398474.7, MEG3-203, 1721; ENST00000554639.5, MEG3-224, 1712; ENST00000650023.1, MEG3-243, 1701; ENST00000412736.7, MEG3-205, 1694; ENST00000556736.5, MEG3-227, 1689; ENST00000398518.6, MEG3-204, 1674; ENST00000650549.1, MEG3-247, 1662; ENST00000648802.1, MEG3-235, 1650; ENST00000648456.1, MEG3-231, 1643; ENST00000647780.1, MEG3-228, 1637; ENST00000650513.1, MEG3-246, 1635; ENST00000429159.6, MEG3-208, 1608; ENST00000451743.6, MEG3-209, 1582; ENST00000521404.5, MEG3-217, 1426; ENST00000520714.5, MEG3-215, 1351; ENST00000650556.1, MEG3-248, 1283; ENST00000654077.1, MEG3-249, 1206; ENST00000649086.1, MEG3-239, 1181; ENST00000648138.1, MEG3-230, 1178; ENST00000648820.1, MEG3-236, 1113; ENST00000649036.1, MEG3-238, 1046; ENST00000650077.1, MEG3-245, 1042; ENST00000522618.1, MEG3-219, 954; ENST00000648950.1, MEG3-237, 846; ENST00000648547.1, MEG3-233, 750; ENST00000524131.5, MEG3-223, 721; ENST00000555928.5, MEG3-225, 720; ENST00000649174.1, MEG3-241, 698; ENST00000649161.1, MEG3-240, 644; ENST00000648123.1, MEG3-229, 644; ENST00000521812.1, MEG3-218, 635; ENST00000648512.1, MEG3-232, 515; ENST00000521256.1, MEG3-216, 505; ENST00000455286.1, MEG3-212, 499; ENST00000452514.6, MEG3-211, 461"	.	chr14:100779410-100861031[+]	.	.	HGNC:14575	.	.	ENSG00000214548	.	.	.	.	.
Mol01232	LncRNA	Long non-protein coding RNA 1118 (LINC01118)	LINC01118	"GTL2, LINC00023, NCRNA00023, onco-lncRNA-83"	388948	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650611.1, LINC01118-204, 1947; ENST00000479311.1, LINC01118-203, 1588; ENST00000409912.5, LINC01118-202, 1023; ENST00000409518.1, LINC01118-201, 834"	.	chr2:46698940-46822804[+]	.	.	HGNC:49261	.	.	ENSG00000222005	.	.	.	.	.
Mol01233	LncRNA	Cytoskeleton regulator RNA (CYTOR)	CYTOR	CYTOR	112597	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000646636.1, CYTOR-237, 1020; ENST00000642451.1, CYTOR-216, 7512"	.	chr2:87454781-87636740[+]	.	.	HGNC:28717	.	.	ENSG00000222041	.	.	.	.	.
Mol01234	LncRNA	Long non-protein coding RNA (LINC00473)	ENSG00000223414	"C2orf59, LINC00152, MGC4677, NCRNA00152"	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	ENSG00000223414	.	.	.	.	.
Mol01235	LncRNA	TINCR ubiquitin domain containing (TINCR)	TINCR	TINCR	257000	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000646160.1, TINCR-204, 603; ENST00000448587.5, TINCR-201, 3733; ENST00000587632.1, TINCR-202, 402; ENST00000646675.1, TINCR-205, 946; ENST00000590789.1, TINCR-203, 583"	.	chr19:5558167-5578349[-]	.	.	HGNC:14607	.	.	ENSG00000223573	.	.	.	.	.
Mol01236	LncRNA	LncRNA in non-homologous end joining pathway 1 (LINP1)	LINP1	"FLJ90734, LINC00036, NCRNA00036, PLAC2, onco-lncRNA-16"	108570035	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000417112.2, LINP1-201, 1243; ENST00000650334.1, LINP1-204, 2529; ENST00000649087.1, LINP1-202, 2096; ENST00000649511.1, LINP1-203, 1290"	.	chr10:6709530-6740532[+]	.	.	HGNC:53170	.	.	ENSG00000223784	.	.	.	.	.
Mol01237	LncRNA	ROR1 antisense RNA 1 (ROR1-AS1)	ROR1-AS1	.	101927034	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000424995.2, ROR1-AS1-202, 3040; ENST00000412349.7, ROR1-AS1-201, 1576; ENST00000676235.1, ROR1-AS1-207, 1281; ENST00000657702.1, ROR1-AS1-203, 655; ENST00000674987.1, ROR1-AS1-204, 601; ENST00000675261.1, ROR1-AS1-205, 501; ENST00000675824.1, ROR1-AS1-206, 500"	.	chr1:64094379-64171342[-]	.	.	HGNC:40508	.	.	ENSG00000223949	.	.	.	.	.
Mol01238	LncRNA	EGFR antisense RNA 1 (EGFR-AS1)	EGFR-AS1	EGFR-AS1	100507500	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000442411.1, EGFR-AS1-201, 2806"	.	chr7:55179750-55188934[-]	.	.	HGNC:40207	.	.	ENSG00000224057	.	.	.	.	.
Mol01239	LncRNA	Small nucleolar RNA host gene 14 (SNHG14)	SNHG14	SNHG14	104472715	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000563205.1, -, 1965"	.	chr15:24978583-25420336[+]	.	.	HGNC:37462	.	.	ENSG00000224078	.	.	.	.	.
Mol01240	LncRNA	HOXD antisense growth-associated long non-coding RNA (HAGLR)	HAGLR	"NCRNA00214, UBE3A-AS, UBE3A-AS1, UBE3A-ATS"	401022	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000452365.2, HAGLR-207, 4183; ENST00000416928.8, HAGLR-202, 4095; ENST00000669485.1, HAGLR-217, 4042; ENST00000642267.2, HAGLR-213, 3826; ENST00000643050.2, HAGLR-214, 3804; ENST00000644334.1, HAGLR-215, 3327; ENST00000645228.1, HAGLR-216, 2847; ENST00000417086.6, HAGLR-203, 1322; ENST00000436126.5, HAGLR-205, 945; ENST00000456876.1, HAGLR-208, 636; ENST00000425005.5, HAGLR-204, 623; ENST00000549329.5, HAGLR-211, 609; ENST00000546798.5, HAGLR-209, 581; ENST00000552156.5, HAGLR-212, 576; ENST00000447538.6, HAGLR-206, 558; ENST00000413969.6, HAGLR-201, 465; ENST00000547207.2, HAGLR-210, 454"	.	chr2:176164051-176188958[-]	.	.	HGNC:43755	.	.	ENSG00000224189	.	.	.	.	.
Mol01241	LncRNA	"Surfactant associated 1, LncRNA (SFTA1P)"	SFTA1P	"HOXD-AS1, MIR7704HG, Mdgt"	207107	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000660024.1, SFTA1P-209, 707; ENST00000652890.1, SFTA1P-206, 2459; ENST00000667544.1, SFTA1P-212, 781; ENST00000446372.3, SFTA1P-203, 710; ENST00000653216.1, SFTA1P-207, 686; ENST00000663743.1, SFTA1P-210, 675; ENST00000602763.6, SFTA1P-204, 633; ENST00000415590.7, SFTA1P-201, 601; ENST00000665724.1, SFTA1P-211, 570; ENST00000656654.1, SFTA1P-208, 570; ENST00000434919.6, SFTA1P-202, 465; ENST00000634899.2, SFTA1P-205, 412"	.	chr10:10784437-10795047[-]	.	.	HGNC:18383	.	.	ENSG00000225383	.	.	.	.	.
Mol01242	LncRNA	Novel transcript (RP3-508I15.14)	RP3-508I15.14	SFTPF	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000416406.1, -, 500"	.	chr22:38739003-38749041[+]	.	.	.	.	.	ENSG00000225450	.	.	.	.	.
Mol01243	LncRNA	Testis associated oncogenic LncRNA (THORLNC)	THORLNC	THORLNC	100506797	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000414886.5, THORLNC-201, 778; ENST00000669120.2, THORLNC-207, 1473; ENST00000648779.1, THORLNC-205, 1350; ENST00000647942.1, THORLNC-204, 764; ENST00000449075.3, THORLNC-202, 587; ENST00000449819.2, THORLNC-203, 584; ENST00000688717.1, THORLNC-210, 554; ENST00000661786.2, THORLNC-206, 488; ENST00000687658.1, THORLNC-209, 354; ENST00000693019.1, THORLNC-212, 354; ENST00000691060.1, THORLNC-211, 349; ENST00000686808.1, THORLNC-208, 349"	.	chr2:118132128-118222250[-]	.	.	HGNC:53788	.	.	ENSG00000226856	.	.	.	.	.
Mol01244	LncRNA	Long non-protein coding RNA 161 (LINC00161)	LINC00161	THOR	118421	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000412526.5, LINC00161-201, 870; ENST00000455939.1, LINC00161-202, 514"	.	chr21:28539318-28540355[+]	.	.	HGNC:17138	.	.	ENSG00000226935	.	.	.	.	.
Mol01245	LncRNA	Long non-protein coding RNA 511 (LINC00511)	LINC00511	"C21orf100, NCRNA00161"	400619	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650033.1, LINC00511-279, 3766; ENST00000650016.1, LINC00511-278, 508; ENST00000648631.1, LINC00511-244, 2929; ENST00000647652.1, LINC00511-220, 3700; ENST00000582712.2, LINC00511-215, 2586; ENST00000647706.2, LINC00511-221, 2532; ENST00000649350.1, LINC00511-261, 2527; ENST00000648623.2, LINC00511-243, 2522; ENST00000650131.3, LINC00511-283, 2292; ENST00000647953.1, LINC00511-225, 2292; ENST00000581549.2, LINC00511-213, 2266; ENST00000648401.1, LINC00511-235, 2214; ENST00000649793.2, LINC00511-274, 2208; ENST00000650051.1, LINC00511-280, 2207; ENST00000650212.1, LINC00511-289, 2174; ENST00000649881.1, LINC00511-276, 2078; ENST00000650371.1, LINC00511-294, 2061; ENST00000649647.1, LINC00511-272, 2060; ENST00000650550.2, LINC00511-302, 2041; ENST00000649366.1, LINC00511-262, 2028; ENST00000650313.1, LINC00511-292, 1995; ENST00000649250.1, LINC00511-255, 1978; ENST00000647871.2, LINC00511-224, 1958; ENST00000649074.1, LINC00511-252, 1905; ENST00000648952.1, LINC00511-249, 1893; ENST00000650483.1, LINC00511-299, 1888; ENST00000648520.1, LINC00511-240, 1888; ENST00000648411.1, LINC00511-237, 1843; ENST00000649433.1, LINC00511-264, 1836; ENST00000648297.1, LINC00511-234, 1823; ENST00000649311.1, LINC00511-257, 1815; ENST00000649172.1, LINC00511-253, 1788; ENST00000583460.2, LINC00511-216, 1778; ENST00000649833.1, LINC00511-275, 1772; ENST00000648667.1, LINC00511-245, 1751; ENST00000649733.1, LINC00511-273, 1742; ENST00000578206.2, LINC00511-205, 1732; ENST00000453722.6, LINC00511-201, 1716; ENST00000648069.1, LINC00511-227, 1713; ENST00000647593.1, LINC00511-218, 1690; ENST00000649489.1, LINC00511-266, 1682; ENST00000648176.2, LINC00511-230, 1647; ENST00000457958.7, LINC00511-202, 1626; ENST00000648403.1, LINC00511-236, 1556; ENST00000649343.1, LINC00511-260, 1552; ENST00000650602.2, LINC00511-306, 1510; ENST00000648248.1, LINC00511-233, 1468; ENST00000650423.1, LINC00511-296, 1455; ENST00000648522.1, LINC00511-241, 1351; ENST00000650083.1, LINC00511-281, 1329; ENST00000648104.2, LINC00511-229, 1264; ENST00000649597.1, LINC00511-270, 1206; ENST00000650482.1, LINC00511-298, 1202; ENST00000649440.2, LINC00511-265, 1159; ENST00000650227.1, LINC00511-290, 1126; ENST00000649614.1, LINC00511-271, 1098; ENST00000649532.1, LINC00511-267, 1045; ENST00000649407.1, LINC00511-263, 1045; ENST00000648054.1, LINC00511-226, 1027; ENST00000650211.1, LINC00511-288, 977; ENST00000650419.2, LINC00511-295, 952; ENST00000650191.1, LINC00511-286, 951; ENST00000649197.1, LINC00511-254, 937; ENST00000577773.3, LINC00511-203, 880; ENST00000650289.2, LINC00511-291, 862; ENST00000581183.3, LINC00511-212, 860; ENST00000581801.7, LINC00511-214, 855; ENST00000648672.2, LINC00511-246, 841; ENST00000650476.1, LINC00511-297, 826; ENST00000649553.1, LINC00511-268, 819; ENST00000649936.1, LINC00511-277, 796; ENST00000650161.1, LINC00511-284, 791; ENST00000649269.1, LINC00511-256, 789; ENST00000648428.1, LINC00511-238, 780; ENST00000647611.1, LINC00511-219, 762; ENST00000650194.2, LINC00511-287, 762; ENST00000648203.1, LINC00511-231, 746; ENST00000648907.1, LINC00511-248, 736; ENST00000580861.2, LINC00511-210, 701; ENST00000650510.1, LINC00511-301, 692; ENST00000650180.1, LINC00511-285, 691; ENST00000648954.1, LINC00511-250, 689; ENST00000580199.7, LINC00511-208, 678; ENST00000648088.1, LINC00511-228, 669; ENST00000648220.1, LINC00511-232, 668; ENST00000577828.6, LINC00511-204, 656; ENST00000650570.1, LINC00511-304, 617; ENST00000580500.5, LINC00511-209, 561; ENST00000650554.1, LINC00511-303, 514; ENST00000649332.1, LINC00511-259, 509; ENST00000648840.1, LINC00511-247, 502; ENST00000647735.1, LINC00511-222, 496; ENST00000580948.1, LINC00511-211, 475; ENST00000649595.2, LINC00511-269, 471; ENST00000579631.2, LINC00511-206, 448; ENST00000650357.1, LINC00511-293, 325; ENST00000649013.1, LINC00511-251, 266; ENST00000648559.1, LINC00511-242, 261; ENST00000650499.1, LINC00511-300, 231; ENST00000649330.1, LINC00511-258, 230; ENST00000648500.1, LINC00511-239, 219; ENST00000580175.2, LINC00511-207, 208; ENST00000584749.2, LINC00511-217, 173; ENST00000650600.1, LINC00511-305, 117; ENST00000647850.1, LINC00511-223, 111; ENST00000650121.1, LINC00511-282, 108"	.	chr17:72290091-72640472[-]	.	.	HGNC:43564	.	.	ENSG00000227036	.	.	.	.	.
Mol01246	LncRNA	PCGEM1 prostate-specific transcript (PCGEM1)	PCGEM1	onco-lncRNA-12	64002	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000454040.5, PCGEM1-201, 1590; ENST00000606314.1, PCGEM1-202, 759"	.	chr2:192749845-192776899[+]	.	.	HGNC:30145	.	.	ENSG00000227418	.	.	.	.	.
Mol01247	LncRNA	MACC1 antisense RNA 1 (MACC1-AS1)	MACC1-AS1	"LINC00071, NCRNA00071, PCAT9"	100874041	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000439285.1, MACC1-AS1-201, 639"	.	chr7:20141916-20153531[+]	.	.	HGNC:41257	.	.	ENSG00000228598	.	.	.	.	.
Mol01248	LncRNA	HOX transcript antisense RNA (HOTAIR)	HOTAIR	HOTAIR	100124700	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000424518.5, HOTAIR-201, 2421; ENST00000455246.5, HOTAIR-205, 918; ENST00000425595.5, HOTAIR-202, 572; ENST00000453875.5, HOTAIR-204, 562; ENST00000439545.1, HOTAIR-203, 560"	.	chr12:53962308-53974956[-]	.	.	HGNC:33510	.	.	ENSG00000228630	.	.	.	.	.
Mol01249	LncRNA	Carboxylesterase 1 pseudogene 1 (CES1P1)	CES1P1	"HOXC-AS4, HOXC11-AS1, NCRNA00072"	51716	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000571348.5, CES1P1-202, 2259; ENST00000573705.1, CES1P1-203, 1044; ENST00000574030.5, CES1P1-204, 877; ENST00000421606.6, CES1P1-201, 1704"	.	chr16:55760566-55793960[+]	.	.	HGNC:18546	.	.	ENSG00000228695	.	.	.	.	.
Mol01250	LncRNA	CCDC26 long non-coding RNA (CCDC26)	CCDC26	"CES1A3, CES4, CESR, PCE-3"	137196	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000675388.1, CCDC26-307, 1017; ENST00000643616.1, CCDC26-210, 20097; ENST00000676108.1, CCDC26-333, 2306; ENST00000675208.1, CCDC26-304, 2178; ENST00000675316.1, CCDC26-306, 2020; ENST00000676030.1, CCDC26-329, 2002; ENST00000675506.1, CCDC26-314, 1875; ENST00000675599.1, CCDC26-319, 1834; ENST00000674882.1, CCDC26-292, 1825; ENST00000663991.1, CCDC26-247, 1815; ENST00000674863.1, CCDC26-290, 1793; ENST00000675186.1, CCDC26-303, 1784; ENST00000674877.1, CCDC26-291, 1783; ENST00000676273.1, CCDC26-338, 1779; ENST00000675072.1, CCDC26-298, 1776; ENST00000667643.1, CCDC26-263, 1773; ENST00000676069.1, CCDC26-331, 1763; ENST00000667962.1, CCDC26-264, 1761; ENST00000675109.1, CCDC26-300, 1750; ENST00000663716.1, CCDC26-246, 1743; ENST00000658861.1, CCDC26-233, 1741; ENST00000674656.1, CCDC26-284, 1733; ENST00000676238.1, CCDC26-336, 1731; ENST00000675527.1, CCDC26-316, 1725; ENST00000446592.7, CCDC26-201, 1721; ENST00000675522.1, CCDC26-315, 1720; ENST00000657251.1, CCDC26-228, 1689; ENST00000668777.1, CCDC26-267, 1679; ENST00000674711.1, CCDC26-285, 1671; ENST00000676405.1, CCDC26-341, 1667; ENST00000642958.2, CCDC26-209, 1665; ENST00000676099.1, CCDC26-332, 1656; ENST00000644194.1, CCDC26-211, 1652; ENST00000657647.1, CCDC26-231, 1649; ENST00000652971.1, CCDC26-217, 1636; ENST00000667974.1, CCDC26-265, 1631; ENST00000663521.1, CCDC26-244, 1621; ENST00000674639.1, CCDC26-283, 1616; ENST00000671632.1, CCDC26-280, 1602; ENST00000661447.1, CCDC26-237, 1598; ENST00000675948.1, CCDC26-327, 1594; ENST00000674599.1, CCDC26-282, 1579; ENST00000674750.1, CCDC26-287, 1574; ENST00000675498.1, CCDC26-313, 1572; ENST00000675589.1, CCDC26-318, 1568; ENST00000663572.1, CCDC26-245, 1564; ENST00000665348.1, CCDC26-253, 1563; ENST00000664043.1, CCDC26-248, 1562; ENST00000662317.1, CCDC26-240, 1559; ENST00000675532.1, CCDC26-317, 1551; ENST00000675044.1, CCDC26-297, 1550; ENST00000654421.1, CCDC26-221, 1542; ENST00000664632.1, CCDC26-251, 1538; ENST00000668791.1, CCDC26-268, 1537; ENST00000666882.1, CCDC26-261, 1532; ENST00000675435.1, CCDC26-310, 1525; ENST00000676294.1, CCDC26-339, 1523; ENST00000660652.1, CCDC26-236, 1517; ENST00000675183.1, CCDC26-302, 1516; ENST00000675449.1, CCDC26-311, 1511; ENST00000660109.1, CCDC26-234, 1507; ENST00000667341.1, CCDC26-262, 1501; ENST00000675878.1, CCDC26-325, 1492; ENST00000657409.1, CCDC26-230, 1487; ENST00000523151.6, CCDC26-205, 1487; ENST00000666849.1, CCDC26-260, 1485; ENST00000676148.1, CCDC26-335, 1485; ENST00000671311.1, CCDC26-277, 1484; ENST00000675913.1, CCDC26-326, 1473; ENST00000664599.1, CCDC26-250, 1467; ENST00000662350.1, CCDC26-241, 1464; ENST00000665364.1, CCDC26-254, 1462; ENST00000664162.1, CCDC26-249, 1461; ENST00000670054.1, CCDC26-272, 1453; ENST00000656242.1, CCDC26-224, 1442; ENST00000669940.1, CCDC26-271, 1442; ENST00000674580.1, CCDC26-281, 1431; ENST00000669617.1, CCDC26-269, 1425; ENST00000668446.1, CCDC26-266, 1407; ENST00000670386.1, CCDC26-274, 1404; ENST00000657046.1, CCDC26-226, 1403; ENST00000674762.1, CCDC26-288, 1403; ENST00000675496.1, CCDC26-312, 1401; ENST00000675097.1, CCDC26-299, 1393; ENST00000654987.1, CCDC26-222, 1389; ENST00000666317.1, CCDC26-258, 1383; ENST00000666725.1, CCDC26-259, 1382; ENST00000675867.1, CCDC26-324, 1375; ENST00000670803.1, CCDC26-276, 1371; ENST00000676350.1, CCDC26-340, 1363; ENST00000674883.1, CCDC26-293, 1353; ENST00000662033.1, CCDC26-238, 1349; ENST00000671347.1, CCDC26-278, 1317; ENST00000653764.1, CCDC26-220, 1305; ENST00000646877.1, CCDC26-214, 1288; ENST00000657069.1, CCDC26-227, 1287; ENST00000653401.1, CCDC26-219, 1284; ENST00000671439.1, CCDC26-279, 1283; ENST00000676060.1, CCDC26-330, 1269; ENST00000662908.1, CCDC26-242, 1254; ENST00000645432.1, CCDC26-213, 1254; ENST00000675393.1, CCDC26-308, 1244; ENST00000675166.1, CCDC26-301, 1228; ENST00000655629.1, CCDC26-223, 1227; ENST00000653363.1, CCDC26-218, 1220; ENST00000674741.1, CCDC26-286, 1215; ENST00000676129.1, CCDC26-334, 1192; ENST00000656316.1, CCDC26-225, 1176; ENST00000509893.3, CCDC26-202, 1169; ENST00000660163.1, CCDC26-235, 1166; ENST00000674766.1, CCDC26-289, 1155; ENST00000644557.1, CCDC26-212, 1147; ENST00000664936.1, CCDC26-252, 1140; ENST00000670148.1, CCDC26-273, 1127; ENST00000675722.1, CCDC26-322, 1106; ENST00000670588.1, CCDC26-275, 1103; ENST00000669935.1, CCDC26-270, 1091; ENST00000658740.1, CCDC26-232, 1090; ENST00000652914.1, CCDC26-216, 1067; ENST00000675658.1, CCDC26-320, 1065; ENST00000666088.1, CCDC26-257, 1059; ENST00000674893.1, CCDC26-294, 1026; ENST00000657400.1, CCDC26-229, 1002; ENST00000674940.1, CCDC26-296, 984; ENST00000665935.1, CCDC26-256, 934; ENST00000665685.1, CCDC26-255, 916; ENST00000675815.1, CCDC26-323, 915; ENST00000520048.1, CCDC26-203, 904; ENST00000675970.1, CCDC26-328, 875; ENST00000630386.2, CCDC26-208, 866; ENST00000662207.1, CCDC26-239, 865; ENST00000676407.1, CCDC26-342, 816; ENST00000676248.1, CCDC26-337, 807; ENST00000625513.1, CCDC26-206, 783; ENST00000675669.1, CCDC26-321, 733; ENST00000674906.1, CCDC26-295, 722; ENST00000522667.1, CCDC26-204, 683; ENST00000647094.1, CCDC26-215, 677; ENST00000675432.1, CCDC26-309, 650; ENST00000663066.1, CCDC26-243, 640; ENST00000628064.3, CCDC26-207, 532; ENST00000675290.1, CCDC26-305, 374"	.	chr8:128634199-129683770[-]	.	.	HGNC:28416	.	.	ENSG00000229140	.	.	.	.	.
Mol01251	LncRNA	MBNL1 antisense RNA 1 (MBNL1-AS1)	MBNL1-AS1	"MGC27434, RAM"	401093	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000669594.1, MBNL1-AS1-204, 1934; ENST00000608395.2, MBNL1-AS1-202, 6595; ENST00000665663.1, MBNL1-AS1-203, 3244; ENST00000445466.2, MBNL1-AS1-201, 997"	.	chr3:152245262-152269565[-]	.	.	HGNC:44584	.	.	ENSG00000229619	.	.	.	.	.
Mol01252	LncRNA	X inactive specific transcript (XIST)	XIST	LOC401093	7503	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000429829.6, XIST-204, 19245; ENST00000650627.1, XIST-225, 13180; ENST00000650366.1, XIST-223, 12555; ENST00000650186.1, XIST-222, 8258; ENST00000648970.1, XIST-218, 8184; ENST00000648991.1, XIST-219, 7717; ENST00000647913.2, XIST-213, 6150; ENST00000648607.1, XIST-215, 5461; ENST00000649757.1, XIST-221, 5272; ENST00000669898.1, XIST-230, 4977; ENST00000666309.1, XIST-228, 4425; ENST00000647696.1, XIST-212, 4318; ENST00000650548.1, XIST-224, 4073; ENST00000650637.1, XIST-226, 3972; ENST00000648927.2, XIST-217, 3060; ENST00000434839.3, XIST-206, 2867; ENST00000635841.2, XIST-211, 2779; ENST00000421322.3, XIST-203, 2712; ENST00000648829.1, XIST-216, 2573; ENST00000665247.1, XIST-227, 2555; ENST00000648091.1, XIST-214, 2166; ENST00000649353.1, XIST-220, 2069; ENST00000416330.2, XIST-201, 908; ENST00000602495.1, XIST-208, 827; ENST00000417942.5, XIST-202, 724; ENST00000602863.2, XIST-210, 706; ENST00000666954.1, XIST-229, 662; ENST00000433732.2, XIST-205, 583; ENST00000602587.5, XIST-209, 583; ENST00000445814.2, XIST-207, 583"	.	chrX:73820649-73852723[-]	.	.	HGNC:12810	.	.	ENSG00000229807	.	.	.	.	.
Mol01253	LncRNA	TRPM2 antisense RNA (TRPM2-AS)	TRPM2-AS	"DXS1089, DXS399E, LINC00001, NCRNA00001, swd66"	101928607	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000423310.2, TRPM2-AS-201, 586; ENST00000456880.1, TRPM2-AS-202, 2056"	.	chr21:44414588-44425272[-]	.	.	HGNC:50758	.	.	ENSG00000230061	.	.	.	.	.
Mol01254	LncRNA	"Long non-protein coding RNA, p53 induced transcript (LINC-PINT)"	LINC-PINT	TRPM2-AS1	378805	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000429901.2, LINC-PINT-203, 900; ENST00000647388.1, LINC-PINT-222, 3404; ENST00000451786.5, LINC-PINT-208, 3505; ENST00000643135.1, LINC-PINT-212, 2205; ENST00000644804.1, LINC-PINT-217, 2101; ENST00000646587.1, LINC-PINT-220, 2003; ENST00000647288.1, LINC-PINT-221, 1559; ENST00000642156.1, LINC-PINT-209, 1340; ENST00000433079.5, LINC-PINT-205, 1262; ENST00000645248.1, LINC-PINT-218, 1241; ENST00000646429.1, LINC-PINT-219, 1216; ENST00000642602.1, LINC-PINT-211, 1106; ENST00000643855.1, LINC-PINT-214, 1002; ENST00000643373.1, LINC-PINT-213, 954; ENST00000642483.1, LINC-PINT-210, 953; ENST00000643874.1, LINC-PINT-215, 838; ENST00000431189.1, LINC-PINT-204, 803; ENST00000644188.1, LINC-PINT-216, 789; ENST00000423414.5, LINC-PINT-202, 616; ENST00000435523.5, LINC-PINT-206, 553; ENST00000443623.5, LINC-PINT-207, 453; ENST00000416999.1, LINC-PINT-201, 387"	.	chr7:130938963-131110176[-]	.	.	HGNC:26885	.	.	ENSG00000231721	.	.	.	.	.
Mol01255	LncRNA	Long non-protein coding RNA 210 (LINC00210)	LINC00210	"FLJ43663, LincRNA-Pint, MKLN1-AS1, PINT"	100885798	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000431637.2, LINC00210-201, 1584; ENST00000659987.1, LINC00210-202, 484"	.	chr1:217892900-217920804[+]	.	.	HGNC:37458	.	.	ENSG00000231814	.	.	.	.	.
Mol01256	LncRNA	Long non-protein coding RNA 665 (LINC00665)	LINC00665	"NCRNA00210, RP11-72L13.1"	100506930	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000675324.1, LINC00665-228, 976; ENST00000666182.3, LINC00665-219, 3595; ENST00000667829.1, LINC00665-222, 2880; ENST00000591372.3, LINC00665-208, 2868; ENST00000666458.1, LINC00665-220, 2797; ENST00000590657.2, LINC00665-207, 2622; ENST00000667789.1, LINC00665-221, 2586; ENST00000658991.1, LINC00665-214, 2540; ENST00000656137.1, LINC00665-210, 2310; ENST00000668768.1, LINC00665-223, 2111; ENST00000661195.1, LINC00665-216, 2047; ENST00000585356.6, LINC00665-205, 2038; ENST00000438368.7, LINC00665-203, 1903; ENST00000590622.5, LINC00665-206, 1749; ENST00000668927.1, LINC00665-224, 1676; ENST00000658042.1, LINC00665-211, 1657; ENST00000658126.2, LINC00665-212, 1581; ENST00000659786.2, LINC00665-215, 1571; ENST00000658301.1, LINC00665-213, 1514; ENST00000651681.2, LINC00665-209, 1397; ENST00000412740.7, LINC00665-201, 1358; ENST00000662398.1, LINC00665-217, 1233; ENST00000689532.1, LINC00665-232, 1207; ENST00000665982.1, LINC00665-218, 1194; ENST00000691592.1, LINC00665-233, 1103; ENST00000449434.8, LINC00665-204, 1019; ENST00000675074.1, LINC00665-226, 793; ENST00000676422.1, LINC00665-231, 729; ENST00000427868.6, LINC00665-202, 690; ENST00000676298.1, LINC00665-230, 669; ENST00000675167.1, LINC00665-227, 478; ENST00000674604.1, LINC00665-225, 434; ENST00000675914.1, LINC00665-229, 287"	.	chr19:36259540-36331770[-]	.	.	HGNC:44323	.	.	ENSG00000232677	.	.	.	.	.
Mol01257	LncRNA	ITGA6 antisense RNA 1 (ITGA6-AS1)	ITGA6-AS1	CIP2A-BP	101929947	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000458314.1, ITGA6-AS1-202, 512; ENST00000417539.1, ITGA6-AS1-201, 754"	.	chr2:172464262-172466022[-]	.	.	HGNC:40308	.	.	ENSG00000232788	.	.	.	.	.
Mol01258	LncRNA	Small nucleolar RNA host gene 15 (SNHG15)	SNHG15	AC078883.3	285958	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000580528.2, SNHG15-206, 2998; ENST00000667119.1, SNHG15-212, 3228; ENST00000577700.5, SNHG15-202, 3116; ENST00000653305.1, SNHG15-211, 2344; ENST00000582727.3, SNHG15-207, 1637; ENST00000668580.1, SNHG15-214, 1346; ENST00000667823.2, SNHG15-213, 1124; ENST00000578968.6, SNHG15-203, 986; ENST00000585030.6, SNHG15-210, 956; ENST00000579383.6, SNHG15-204, 732; ENST00000580458.5, SNHG15-205, 710; ENST00000584686.1, SNHG15-209, 541; ENST00000438705.3, SNHG15-201, 509; ENST00000584327.5, SNHG15-208, 505"	.	chr7:44983019-44986961[-]	.	.	HGNC:27797	.	.	ENSG00000232956	.	.	.	.	.
Mol01259	LncRNA	LncRNA regulator of Akt signaling associated with HCC and RCC (LNCARSR)	LNCARSR	"C7orf40, FLJ38860, Linc-Myo1g, MYO1GUT"	102723932	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000670754.1, LNCARSR-209, 927; ENST00000413352.3, LNCARSR-201, 2932; ENST00000665514.1, LNCARSR-207, 1012; ENST00000671232.1, LNCARSR-210, 990; ENST00000666862.1, LNCARSR-208, 931; ENST00000663687.1, LNCARSR-206, 872; ENST00000608561.1, LNCARSR-203, 856; ENST00000656806.1, LNCARSR-205, 834; ENST00000628133.1, LNCARSR-204, 589; ENST00000424980.5, LNCARSR-202, 328"	.	chr9:79505804-79567802[-]	.	.	HGNC:53864	.	.	ENSG00000233086	.	.	.	.	.
Mol01260	LncRNA	Long non-protein coding RNA 460 (LINC00460)	LINC00460	lnc-TALC	728192	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000647525.1, LINC00460-207, 2124; ENST00000642946.1, LINC00460-204, 1746; ENST00000643760.1, LINC00460-205, 1522; ENST00000644746.1, LINC00460-206, 1322; ENST00000435024.2, LINC00460-201, 1009; ENST00000444865.2, LINC00460-203, 915; ENST00000439790.6, LINC00460-202, 857"	.	chr13:106374477-106384315[+]	.	.	HGNC:42809	.	.	ENSG00000233532	.	.	.	.	.
Mol01261	LncRNA	Ribosomal protein L13a pseudogene 20 (RPL13AP20)	RPL13AP20	RPL13AP20	387841	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000459725.1, RPL13AP20-201, 609"	.	chr12:12875499-12876107[+]	.	.	HGNC:35709	.	.	ENSG00000234498	.	.	.	.	.
Mol01262	LncRNA	Growth arrest specific 5 (GAS5)	GAS5	HANR	60674	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650796.1, GAS5-230, 3145; ENST00000693469.1, GAS5-277, 1886; ENST00000431268.5, GAS5-210, 1698; ENST00000442067.6, GAS5-215, 1695; ENST00000693030.1, GAS5-273, 1364; ENST00000444470.6, GAS5-217, 1326; ENST00000687409.1, GAS5-246, 1194; ENST00000692671.1, GAS5-271, 1176; ENST00000455838.6, GAS5-226, 1158; ENST00000688895.1, GAS5-253, 1150; ENST00000421068.5, GAS5-204, 1060; ENST00000416952.6, GAS5-203, 1017; ENST00000412059.6, GAS5-201, 985; ENST00000458220.2, GAS5-229, 955; ENST00000422008.6, GAS5-205, 945; ENST00000443799.5, GAS5-216, 897; ENST00000449589.6, GAS5-220, 827; ENST00000436656.6, GAS5-214, 825; ENST00000436285.6, GAS5-213, 805; ENST00000689469.1, GAS5-256, 788; ENST00000422183.6, GAS5-206, 778; ENST00000456812.7, GAS5-228, 753; ENST00000422207.5, GAS5-207, 643; ENST00000454813.1, GAS5-225, 621; ENST00000456293.5, GAS5-227, 583; ENST00000434796.5, GAS5-212, 575; ENST00000651080.1, GAS5-231, 1071; ENST00000685107.1, GAS5-235, 1509; ENST00000691712.1, GAS5-269, 1466; ENST00000690941.1, GAS5-265, 1443; ENST00000689895.1, GAS5-258, 1271; ENST00000688557.1, GAS5-251, 1184; ENST00000691056.1, GAS5-266, 1169; ENST00000451607.5, GAS5-222, 1007; ENST00000693450.1, GAS5-275, 1003; ENST00000685008.1, GAS5-233, 990; ENST00000432536.5, GAS5-211, 959; ENST00000685159.1, GAS5-236, 916; ENST00000687063.1, GAS5-244, 821; ENST00000687710.1, GAS5-249, 817; ENST00000689860.1, GAS5-257, 774; ENST00000686918.1, GAS5-241, 763; ENST00000687189.1, GAS5-245, 731; ENST00000430245.5, GAS5-209, 723; ENST00000685758.1, GAS5-237, 692; ENST00000454068.5, GAS5-224, 688; ENST00000690172.1, GAS5-260, 657; ENST00000685039.1, GAS5-234, 652; ENST00000691213.1, GAS5-268, 650; ENST00000688573.1, GAS5-252, 633; ENST00000450589.6, GAS5-221, 631; ENST00000693521.1, GAS5-278, 630; ENST00000689958.1, GAS5-259, 619; ENST00000693348.1, GAS5-274, 619; ENST00000686460.1, GAS5-239, 613; ENST00000691137.1, GAS5-267, 612; ENST00000689238.1, GAS5-255, 607; ENST00000690761.1, GAS5-264, 605; ENST00000448718.6, GAS5-218, 592; ENST00000690448.1, GAS5-263, 583; ENST00000686995.1, GAS5-242, 580; ENST00000688952.1, GAS5-254, 580; ENST00000687022.1, GAS5-243, 566; ENST00000686878.1, GAS5-240, 566; ENST00000692994.1, GAS5-272, 564; ENST00000690228.1, GAS5-261, 563; ENST00000687987.1, GAS5-250, 554; ENST00000449289.6, GAS5-219, 543; ENST00000687549.1, GAS5-248, 539; ENST00000690349.1, GAS5-262, 527; ENST00000414075.6, GAS5-202, 519; ENST00000691982.1, GAS5-270, 518; ENST00000684949.1, GAS5-232, 518; ENST00000687435.1, GAS5-247, 500; ENST00000452197.5, GAS5-223, 483; ENST00000693459.1, GAS5-276, 479; ENST00000686231.1, GAS5-238, 465; ENST00000425771.6, GAS5-208, 426"	.	chr1:173858559-173868882[-]	.	.	HGNC:16355	.	.	ENSG00000234741	.	.	.	.	.
Mol01263	LncRNA	SLC25A25 antisense RNA 1 (SLC25A25-AS1)	SLC25A25-AS1	"NCRNA00030, SNHG2"	100289019	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000418747.2, SLC25A25-AS1-201, 6391"	.	chr9:128108581-128118693[-]	.	.	HGNC:27844	.	.	ENSG00000234771	.	.	.	.	.
Mol01264	LncRNA	MIR155 host gene (MIR155HG)	MIR155HG	HRCEG	114614	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000456917.2, MIR155HG-201, 1699; ENST00000659862.2, MIR155HG-202, 1571"	.	chr21:25561810-25575168[+]	.	.	HGNC:35460	.	.	ENSG00000234883	.	.	.	.	.
Mol01265	LncRNA	Long non-protein coding RNA 607 (LINC00607)	LINC00607	"BIC, MIRHG2, NCRNA00172, miPEP155"	646324	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000445174.5, LINC00607-205, 3690; ENST00000662624.1, LINC00607-212, 3218; ENST00000423530.5, LINC00607-204, 2104; ENST00000659768.1, LINC00607-210, 1940; ENST00000655131.1, LINC00607-209, 1752; ENST00000655043.1, LINC00607-208, 1697; ENST00000654368.1, LINC00607-207, 1404; ENST00000664275.1, LINC00607-213, 1123; ENST00000661231.1, LINC00607-211, 1024; ENST00000417922.2, LINC00607-202, 792; ENST00000451392.5, LINC00607-206, 581; ENST00000419922.1, LINC00607-203, 526; ENST00000413563.6, LINC00607-201, 453"	.	chr2:215611563-215848954[-]	.	.	HGNC:43944	.	.	ENSG00000235770	.	.	.	.	.
Mol01266	LncRNA	Eosinophil granule ontogeny transcript (EGOT)	EGOT	EGOT	100126791	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000414938.1, EGOT-201, 1464"	.	chr3:4749192-4751590[-]	.	.	HGNC:37129	.	.	ENSG00000235947	.	.	.	.	.
Mol01267	LncRNA	Gastric cancer associated transcript 3 (GACAT3)	GACAT3	"EGO, NCRNA00190"	104797537	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000652394.1, GACAT3-206, 1358; ENST00000667080.1, GACAT3-208, 2267; ENST00000651908.1, GACAT3-204, 1659; ENST00000651705.1, GACAT3-203, 1457; ENST00000652731.1, GACAT3-207, 1371; ENST00000651993.1, GACAT3-205, 1331; ENST00000426539.1, GACAT3-201, 1096; ENST00000442387.2, GACAT3-202, 472"	.	chr2:16013928-16087201[+]	.	.	HGNC:50847	.	.	ENSG00000236289	.	.	.	.	.
Mol01268	LncRNA	NR2F1 antisense RNA 1 (NR2F1-AS1)	NR2F1-AS1	"LINC01458, lncRNA-AC130710"	441094	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000660523.1, NR2F1-AS1-242, 1537; ENST00000653643.1, NR2F1-AS1-223, 8117; ENST00000655613.1, NR2F1-AS1-229, 3596; ENST00000654055.1, NR2F1-AS1-224, 3530; ENST00000607797.5, NR2F1-AS1-213, 3380; ENST00000653325.1, NR2F1-AS1-219, 3370; ENST00000658662.1, NR2F1-AS1-236, 3266; ENST00000669221.1, NR2F1-AS1-267, 3182; ENST00000653419.1, NR2F1-AS1-220, 3143; ENST00000670690.1, NR2F1-AS1-269, 3063; ENST00000661182.1, NR2F1-AS1-244, 3010; ENST00000664017.1, NR2F1-AS1-251, 3010; ENST00000661345.1, NR2F1-AS1-245, 2999; ENST00000653133.1, NR2F1-AS1-216, 2969; ENST00000665798.1, NR2F1-AS1-259, 2918; ENST00000654617.1, NR2F1-AS1-226, 2882; ENST00000671514.1, NR2F1-AS1-274, 2879; ENST00000504474.5, NR2F1-AS1-202, 2868; ENST00000670813.1, NR2F1-AS1-271, 2854; ENST00000667752.1, NR2F1-AS1-264, 2841; ENST00000668988.1, NR2F1-AS1-265, 2831; ENST00000670693.1, NR2F1-AS1-270, 2828; ENST00000661661.1, NR2F1-AS1-247, 2790; ENST00000666033.1, NR2F1-AS1-260, 2789; ENST00000654431.1, NR2F1-AS1-225, 2784; ENST00000510254.6, NR2F1-AS1-204, 2773; ENST00000656155.1, NR2F1-AS1-231, 2755; ENST00000606696.6, NR2F1-AS1-209, 2708; ENST00000659336.1, NR2F1-AS1-238, 2707; ENST00000661870.1, NR2F1-AS1-248, 2684; ENST00000665095.1, NR2F1-AS1-257, 2682; ENST00000670457.1, NR2F1-AS1-268, 2675; ENST00000666791.1, NR2F1-AS1-261, 2671; ENST00000656921.1, NR2F1-AS1-234, 2659; ENST00000665725.1, NR2F1-AS1-258, 2659; ENST00000671432.1, NR2F1-AS1-273, 2649; ENST00000661573.1, NR2F1-AS1-246, 2639; ENST00000671683.1, NR2F1-AS1-275, 2599; ENST00000606233.6, NR2F1-AS1-208, 2597; ENST00000664135.1, NR2F1-AS1-252, 2586; ENST00000671166.1, NR2F1-AS1-272, 2576; ENST00000656231.1, NR2F1-AS1-232, 2564; ENST00000669203.1, NR2F1-AS1-266, 2556; ENST00000664241.1, NR2F1-AS1-254, 2538; ENST00000656079.1, NR2F1-AS1-230, 2537; ENST00000659983.1, NR2F1-AS1-240, 2528; ENST00000663076.1, NR2F1-AS1-249, 2480; ENST00000659381.1, NR2F1-AS1-239, 2478; ENST00000660272.1, NR2F1-AS1-241, 2452; ENST00000663096.1, NR2F1-AS1-250, 2399; ENST00000660787.1, NR2F1-AS1-243, 2373; ENST00000664359.1, NR2F1-AS1-255, 2372; ENST00000657648.1, NR2F1-AS1-235, 2330; ENST00000652888.1, NR2F1-AS1-215, 2225; ENST00000665047.1, NR2F1-AS1-256, 2158; ENST00000667268.1, NR2F1-AS1-263, 2117; ENST00000503134.6, NR2F1-AS1-201, 2035; ENST00000607831.5, NR2F1-AS1-214, 1963; ENST00000655454.1, NR2F1-AS1-228, 1907; ENST00000654862.1, NR2F1-AS1-227, 1805; ENST00000656357.1, NR2F1-AS1-233, 1802; ENST00000606188.2, NR2F1-AS1-207, 1753; ENST00000664168.1, NR2F1-AS1-253, 1677; ENST00000666995.1, NR2F1-AS1-262, 1672; ENST00000606739.5, NR2F1-AS1-210, 1431; ENST00000653284.1, NR2F1-AS1-218, 1311; ENST00000653235.1, NR2F1-AS1-217, 1261; ENST00000653598.1, NR2F1-AS1-222, 1224; ENST00000513055.2, NR2F1-AS1-205, 1193; ENST00000659013.1, NR2F1-AS1-237, 1133; ENST00000507963.5, NR2F1-AS1-203, 922; ENST00000653510.1, NR2F1-AS1-221, 782; ENST00000607195.1, NR2F1-AS1-212, 591; ENST00000606165.5, NR2F1-AS1-206, 580; ENST00000607112.1, NR2F1-AS1-211, 271"	.	chr5:93360779-93585649[-]	.	.	HGNC:48622	.	.	ENSG00000237187	.	.	.	.	.
Mol01269	LncRNA	DiGeorge syndrome critical region gene 5 (DGCR5)	DGCR5	FLJ42709	26220	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000440005.6, DGCR5-205, 1299; ENST00000438934.5, DGCR5-204, 5492; ENST00000675214.1, DGCR5-209, 5074; ENST00000675671.1, DGCR5-210, 4432; ENST00000675978.1, DGCR5-211, 3828; ENST00000674913.1, DGCR5-208, 3823; ENST00000609630.2, DGCR5-206, 3724; ENST00000421572.2, DGCR5-202, 3581; ENST00000609839.2, DGCR5-207, 1006; ENST00000424407.1, DGCR5-203, 768"	.	chr22:18970439-19031242[+]	.	.	HGNC:16757	.	.	ENSG00000273032	.	.	.	.	.
Mol01270	LncRNA	POU class 5 homeobox 1 pseudogene 4 (POU5F1P4)	POU5F1P4	"DGCR10, DGCR9, DGS-A, DGS-B, LINC00037, NCRNA00037, POM121L5P, X91348"	645682	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000413175.2, POU5F1P4-201, 1085"	.	chr1:155433178-155434262[+]	.	.	HGNC:33310	.	.	ENSG00000237872	.	.	.	.	.
Mol01271	LncRNA	Long non-protein coding RNA 1589 (LINC01589)	LINC01589	"Oct4-pg4, POU5FLC1"	100506737	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000422971.1, LINC01589-201, 548"	.	chr22:45604432-45605621[-]	.	.	HGNC:51520	.	.	ENSG00000238120	.	.	.	.	.
Mol01272	LncRNA	NCK1 divergent transcript (NCK1-DT)	NCK1-DT	"CTA-941F9.9, TCONS_00029353"	101927597	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000661609.1, NCK1-DT-204, 2046; ENST00000666310.1, NCK1-DT-206, 2304; ENST00000470236.2, NCK1-DT-202, 1943; ENST00000461864.7, NCK1-DT-201, 1860; ENST00000670711.1, NCK1-DT-209, 1611; ENST00000663856.1, NCK1-DT-205, 1420; ENST00000667524.1, NCK1-DT-208, 1124; ENST00000474250.5, NCK1-DT-203, 827; ENST00000666660.1, NCK1-DT-207, 518"	.	chr3:136835345-136862618[-]	.	.	HGNC:49645	.	.	ENSG00000239213	.	.	.	.	.
Mol01273	LncRNA	LncRNA sorafenib resistance in renal cell carcinoma associated (LNCSRLR)	LNCSRLR	"NCK1-AS1, SLC35G2-AS1"	109729161	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000490375.1, LNCSRLR-201, 709"	.	chr3:146066344-146069185[-]	.	.	HGNC:52753	.	.	ENSG00000240032	.	.	.	.	.
Mol01274	LncRNA	CDKN2B antisense RNA 1 (CDKN2B-AS1)	CDKN2B-AS1	lncRNA-SRLR	100048912	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650946.1, CDKN2B-AS1-222, 1439; ENST00000652420.1, CDKN2B-AS1-227, 7173; ENST00000428597.6, CDKN2B-AS1-203, 3837; ENST00000651588.1, CDKN2B-AS1-224, 3573; ENST00000584351.5, CDKN2B-AS1-214, 2660; ENST00000468603.7, CDKN2B-AS1-205, 2359; ENST00000580576.6, CDKN2B-AS1-208, 2166; ENST00000645313.2, CDKN2B-AS1-221, 1948; ENST00000651519.1, CDKN2B-AS1-223, 1918; ENST00000644233.2, CDKN2B-AS1-219, 1651; ENST00000643286.1, CDKN2B-AS1-218, 1601; ENST00000585267.5, CDKN2B-AS1-217, 1337; ENST00000582072.5, CDKN2B-AS1-210, 1283; ENST00000580467.5, CDKN2B-AS1-207, 1260; ENST00000421632.2, CDKN2B-AS1-201, 1233; ENST00000651784.1, CDKN2B-AS1-225, 1150; ENST00000581051.5, CDKN2B-AS1-209, 1149; ENST00000577551.5, CDKN2B-AS1-206, 1013; ENST00000455933.7, CDKN2B-AS1-204, 962; ENST00000582301.5, CDKN2B-AS1-211, 956; ENST00000584637.5, CDKN2B-AS1-215, 949; ENST00000422420.2, CDKN2B-AS1-202, 939; ENST00000658981.1, CDKN2B-AS1-228, 929; ENST00000583719.5, CDKN2B-AS1-212, 856; ENST00000584020.5, CDKN2B-AS1-213, 813; ENST00000645223.3, CDKN2B-AS1-220, 813; ENST00000651904.1, CDKN2B-AS1-226, 608; ENST00000584816.5, CDKN2B-AS1-216, 602"	.	chr9:21994139-22128103[+]	.	.	HGNC:34341	.	.	ENSG00000240498	.	.	.	.	.
Mol01276	LncRNA	HOXA11 antisense RNA (HOXA11-AS)	HOXA11-AS	"ANRIL, CDKN2B-AS, CDKN2BAS, NCRNA00089, PCAT12, RP11-145E5.4, p15AS"	221883	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000520360.6, HOXA11-AS-202, 1431; ENST00000522863.2, HOXA11-AS-205, 1739; ENST00000522674.1, HOXA11-AS-204, 1549; ENST00000520395.2, HOXA11-AS-203, 1201; ENST00000648491.1, HOXA11-AS-208, 1100; ENST00000647680.1, HOXA11-AS-206, 851; ENST00000479766.2, HOXA11-AS-201, 824; ENST00000650141.1, HOXA11-AS-210, 822; ENST00000647851.1, HOXA11-AS-207, 710; ENST00000648499.1, HOXA11-AS-209, 498"	.	chr7:27184507-27189298[+]	.	.	HGNC:24957	.	.	ENSG00000240990	.	.	.	.	.
Mol01277	LncRNA	ADAMTS9 antisense RNA 2 (ADAMTS9-AS2)	ADAMTS9-AS2	"HOXA-AS5, HOXA11-AS1, HOXA11AS, HOXA11S, NCRNA00076"	100507098	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650103.1, ADAMTS9-AS2-205, 2261; ENST00000460833.1, ADAMTS9-AS2-201, 3691; ENST00000692372.1, ADAMTS9-AS2-207, 2926; ENST00000474768.5, ADAMTS9-AS2-202, 2388; ENST00000691998.1, ADAMTS9-AS2-206, 2146; ENST00000481312.2, ADAMTS9-AS2-203, 1984; ENST00000485174.5, ADAMTS9-AS2-204, 573"	.	chr3:64684909-65053439[+]	.	.	HGNC:42435	.	.	ENSG00000241684	.	.	.	.	.
Mol01278	LncRNA	Tumor suppressor candidate 7 (TUSC7)	TUSC7	TUSC7	285194	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000477805.1, TUSC7-204, 486; ENST00000477539.6, TUSC7-203, 2415; ENST00000496242.6, TUSC7-206, 2059; ENST00000660554.1, TUSC7-208, 1274; ENST00000496154.2, TUSC7-205, 1161; ENST00000466156.1, TUSC7-201, 1054; ENST00000609361.5, TUSC7-207, 873; ENST00000665622.1, TUSC7-209, 739; ENST00000466856.5, TUSC7-202, 557"	.	chr3:116709235-116723581[+]	.	.	HGNC:27701	.	.	ENSG00000243197	.	.	.	.	.
Mol01279	LncRNA	HOXA distal transcript antisense RNA (HOTTIP)	HOTTIP	"LINC00902, LOC285194, LSAMP-AS3, NCRNA00295"	100316868	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000521028.4, HOTTIP-203, 3343; ENST00000472494.1, HOTTIP-202, 2285; ENST00000605136.6, HOTTIP-204, 1287; ENST00000421733.1, HOTTIP-201, 781"	.	chr7:27198575-27207259[+]	.	.	HGNC:37461	.	.	ENSG00000243766	.	.	.	.	.
Mol01280	LncRNA	Mitosis associated long intergenic non-coding RNA 1 (MALINC1)	MALINC1	"HOXA-AS6, HOXA13-AS1, NCRNA00213, RP1-170O19.3"	100505636	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000663778.1, MALINC1-214, 2369; ENST00000654348.1, MALINC1-209, 3974; ENST00000499203.7, MALINC1-201, 3528; ENST00000660071.1, MALINC1-213, 3288; ENST00000671132.1, MALINC1-216, 3241; ENST00000656599.1, MALINC1-210, 3174; ENST00000522747.6, MALINC1-206, 2720; ENST00000659306.1, MALINC1-211, 2573; ENST00000521563.6, MALINC1-205, 2554; ENST00000653092.1, MALINC1-208, 2513; ENST00000659960.1, MALINC1-212, 2505; ENST00000671248.1, MALINC1-217, 1652; ENST00000668151.1, MALINC1-215, 1309; ENST00000518790.2, MALINC1-202, 1186; ENST00000520928.1, MALINC1-203, 648; ENST00000523452.5, MALINC1-207, 555; ENST00000521133.1, MALINC1-204, 454"	.	chr5:140071312-140109274[-]	.	.	HGNC:49009	.	.	ENSG00000245146	.	.	.	.	.
Mol01281	LncRNA	Nuclear paraspeckle assembly transcript 1 (NEAT1)	NEAT1	"LINC01024, MA-linc1"	283131	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000501122.2, NEAT1-202, 22743; ENST00000687132.1, NEAT1-211, 3736; ENST00000685861.1, NEAT1-210, 3732; ENST00000601801.3, NEAT1-203, 3524; ENST00000499732.3, NEAT1-201, 3441; ENST00000670617.1, NEAT1-209, 3301; ENST00000645023.1, NEAT1-207, 3300; ENST00000646243.1, NEAT1-208, 2994; ENST00000687943.1, NEAT1-212, 1204; ENST00000642367.1, NEAT1-206, 1145; ENST00000693290.1, NEAT1-214, 1116; ENST00000612303.2, NEAT1-204, 1053; ENST00000691530.1, NEAT1-213, 683; ENST00000693747.1, NEAT1-215, 683; ENST00000616315.2, NEAT1-205, 512"	.	chr11:65422774-65445540[+]	.	.	HGNC:30815	.	.	ENSG00000245532	.	.	.	.	.
Mol01283	LncRNA	Colorectal neoplasia differentially expressed (CRNDE)	CRNDE	"LINC00084, MENepsilon/beta, NCRNA00084, TncRNA, VINC"	643911	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000661493.1, CRNDE-222, 919; ENST00000557792.2, CRNDE-203, 6325; ENST00000657142.1, CRNDE-217, 6132; ENST00000558952.2, CRNDE-205, 4724; ENST00000668556.1, CRNDE-224, 3027; ENST00000613942.2, CRNDE-212, 2601; ENST00000689582.1, CRNDE-227, 2089; ENST00000658082.1, CRNDE-218, 2042; ENST00000689375.1, CRNDE-226, 2023; ENST00000660344.1, CRNDE-220, 1883; ENST00000559598.7, CRNDE-207, 1866; ENST00000502066.7, CRNDE-202, 1603; ENST00000661312.1, CRNDE-221, 1348; ENST00000637011.1, CRNDE-214, 865; ENST00000688921.1, CRNDE-225, 841; ENST00000501177.9, CRNDE-201, 790; ENST00000655114.1, CRNDE-216, 745; ENST00000560208.1, CRNDE-209, 735; ENST00000560029.5, CRNDE-208, 659; ENST00000558031.7, CRNDE-204, 656; ENST00000667913.1, CRNDE-223, 601; ENST00000560912.6, CRNDE-210, 579; ENST00000654070.1, CRNDE-215, 569; ENST00000635991.1, CRNDE-213, 546; ENST00000691307.1, CRNDE-228, 497; ENST00000561591.1, CRNDE-211, 420; ENST00000559432.6, CRNDE-206, 370; ENST00000659020.1, CRNDE-219, 359"	.	chr16:54845189-54929189[-]	.	.	HGNC:37078	.	.	ENSG00000245694	.	.	.	.	.
Mol01284	LncRNA	Small nucleolar RNA host gene 6 (SNHG6)	SNHG6	"CRNDEP, LINC00180, LOC643911"	641638	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000521127.1, SNHG6-204, 560; ENST00000686474.1, SNHG6-206, 1806; ENST00000520944.6, SNHG6-203, 639; ENST00000689720.1, SNHG6-207, 625; ENST00000520619.1, SNHG6-202, 479; ENST00000520348.6, SNHG6-201, 460; ENST00000521399.6, SNHG6-205, 366; ENST00000693345.1, SNHG6-208, 286"	.	chr8:66920561-66926398[-]	.	.	HGNC:32965	.	.	ENSG00000245910	.	.	.	.	.
Mol01285	LncRNA	SBF2 antisense RNA 1 (SBF2-AS1)	SBF2-AS1	"HBII-276HG, NCRNA00058, U87HG"	283104	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000663578.1, SBF2-AS1-209, 3714; ENST00000658574.1, SBF2-AS1-208, 3872; ENST00000650092.1, SBF2-AS1-207, 3693; ENST00000498905.2, SBF2-AS1-201, 2709; ENST00000664105.1, SBF2-AS1-210, 2000; ENST00000499953.6, SBF2-AS1-202, 854; ENST00000534671.1, SBF2-AS1-206, 767; ENST00000527406.1, SBF2-AS1-205, 666; ENST00000525636.5, SBF2-AS1-203, 638; ENST00000526617.1, SBF2-AS1-204, 488"	.	chr11:9758268-9811335[+]	.	.	HGNC:27438	.	.	ENSG00000246273	.	.	.	.	.
Mol01286	LncRNA	Long non-protein coding RNA 968 (LINC00968)	LINC00968	.	100507632	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000524338.2, LINC00968-207, 2229; ENST00000665904.2, LINC00968-209, 2421; ENST00000499425.1, LINC00968-201, 2366; ENST00000692050.1, LINC00968-210, 1938; ENST00000518943.1, LINC00968-202, 569; ENST00000519144.5, LINC00968-203, 564; ENST00000523786.5, LINC00968-206, 558; ENST00000521483.1, LINC00968-204, 554; ENST00000523664.1, LINC00968-205, 553; ENST00000653444.1, LINC00968-208, 519"	.	chr8:56494923-56559823[-]	.	.	HGNC:48727	.	.	ENSG00000246430	.	.	.	.	.
Mol01287	LncRNA	SOCS2 antisense RNA 1 (SOCS2-AS1)	SOCS2-AS1	.	144481	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000547845.5, SOCS2-AS1-203, 555; ENST00000500986.6, SOCS2-AS1-202, 2097; ENST00000499137.6, SOCS2-AS1-201, 3325; ENST00000668485.1, SOCS2-AS1-206, 1542; ENST00000662875.1, SOCS2-AS1-205, 1134; ENST00000551626.1, SOCS2-AS1-204, 618"	.	chr12:93542022-93571768[-]	.	.	HGNC:27054	.	.	ENSG00000246985	.	.	.	.	.
Mol01288	LncRNA	OIP5 antisense RNA 1 (OIP5-AS1)	OIP5-AS1	OIP5-AS1	729082	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000558457.5, OIP5-AS1-204, 676; ENST00000560545.1, OIP5-AS1-207, 566; ENST00000501665.2, OIP5-AS1-202, 1384; ENST00000500949.6, OIP5-AS1-201, 8829; ENST00000557993.5, OIP5-AS1-203, 1482; ENST00000558945.5, OIP5-AS1-205, 1269; ENST00000561275.5, OIP5-AS1-210, 821; ENST00000561226.5, OIP5-AS1-209, 775; ENST00000559368.5, OIP5-AS1-206, 642; ENST00000560706.5, OIP5-AS1-208, 473"	.	chr15:41283990-41309737[+]	.	.	HGNC:43563	.	.	ENSG00000247556	.	.	.	.	.
Mol01289	LncRNA	ENSG00000247844 (CCAT1)	CCAT1	"cyrano, linc-OIP5"	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	ENSG00000247844	.	.	.	.	.
Mol01290	LncRNA	NNT antisense RNA 1 (NNT-AS1)	NNT-AS1	.	100652772	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000513560.7, NNT-AS1-204, 4803; ENST00000606697.5, NNT-AS1-206, 1945; ENST00000668986.1, NNT-AS1-208, 852; ENST00000656020.1, NNT-AS1-207, 701; ENST00000503484.6, NNT-AS1-202, 599; ENST00000506247.1, NNT-AS1-203, 579; ENST00000515466.1, NNT-AS1-205, 557; ENST00000500258.2, NNT-AS1-201, 457"	.	chr5:43571594-43603230[-]	.	.	HGNC:49005	.	.	ENSG00000248092	.	.	.	.	.
Mol01291	LncRNA	Lung cancer associated transcript 1 (LUCAT1)	LUCAT1	RP11-159F24.1	100505994	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650150.1, LUCAT1-249, 1357; ENST00000513626.3, LUCAT1-203, 3072; ENST00000647761.1, LUCAT1-207, 3056; ENST00000648822.1, LUCAT1-224, 2666; ENST00000650017.1, LUCAT1-244, 2176; ENST00000649539.1, LUCAT1-235, 2059; ENST00000650067.1, LUCAT1-246, 2024; ENST00000648075.1, LUCAT1-211, 1977; ENST00000649702.1, LUCAT1-237, 1972; ENST00000650004.1, LUCAT1-242, 1913; ENST00000649304.1, LUCAT1-228, 1773; ENST00000650273.1, LUCAT1-251, 1757; ENST00000649969.1, LUCAT1-239, 1711; ENST00000648597.1, LUCAT1-218, 1687; ENST00000670581.1, LUCAT1-261, 1614; ENST00000648310.1, LUCAT1-214, 1505; ENST00000649467.1, LUCAT1-234, 1498; ENST00000650008.1, LUCAT1-243, 1457; ENST00000649654.1, LUCAT1-236, 1407; ENST00000668775.1, LUCAT1-260, 1359; ENST00000649392.2, LUCAT1-230, 1347; ENST00000650100.1, LUCAT1-248, 1337; ENST00000648923.1, LUCAT1-226, 1300; ENST00000650583.1, LUCAT1-255, 1278; ENST00000648031.1, LUCAT1-210, 1260; ENST00000648905.1, LUCAT1-225, 1227; ENST00000649138.1, LUCAT1-227, 1222; ENST00000650003.1, LUCAT1-241, 1212; ENST00000647807.1, LUCAT1-208, 1204; ENST00000649405.1, LUCAT1-231, 1179; ENST00000649447.2, LUCAT1-233, 1173; ENST00000648439.1, LUCAT1-216, 1149; ENST00000648137.2, LUCAT1-212, 1145; ENST00000650047.1, LUCAT1-245, 1080; ENST00000648683.1, LUCAT1-220, 1045; ENST00000648811.1, LUCAT1-223, 1043; ENST00000647745.1, LUCAT1-205, 1042; ENST00000650321.1, LUCAT1-252, 1012; ENST00000648773.1, LUCAT1-222, 1007; ENST00000660484.1, LUCAT1-258, 1004; ENST00000653155.1, LUCAT1-256, 991; ENST00000650261.1, LUCAT1-250, 969; ENST00000648636.1, LUCAT1-219, 967; ENST00000648385.1, LUCAT1-215, 960; ENST00000513492.6, LUCAT1-202, 935; ENST00000648015.1, LUCAT1-209, 917; ENST00000654784.1, LUCAT1-257, 901; ENST00000648199.1, LUCAT1-213, 881; ENST00000649322.1, LUCAT1-229, 857; ENST00000687742.1, LUCAT1-263, 842; ENST00000650529.1, LUCAT1-254, 820; ENST00000649976.1, LUCAT1-240, 809; ENST00000650381.1, LUCAT1-253, 798; ENST00000650098.1, LUCAT1-247, 793; ENST00000664701.1, LUCAT1-259, 768; ENST00000511918.6, LUCAT1-201, 737; ENST00000649968.1, LUCAT1-238, 646; ENST00000647759.1, LUCAT1-206, 604; ENST00000649424.1, LUCAT1-232, 601; ENST00000648751.2, LUCAT1-221, 570; ENST00000607854.1, LUCAT1-204, 549; ENST00000690504.1, LUCAT1-264, 518; ENST00000690915.1, LUCAT1-265, 464; ENST00000685632.1, LUCAT1-262, 409; ENST00000648457.1, LUCAT1-217, 374"	.	chr5:91054834-91314547[-]	.	.	HGNC:48498	.	.	ENSG00000248323	.	.	.	.	.
Mol01292	LncRNA	Cancer susceptibility 11 (CASC11)	CASC11	"SCAL1, SCAT5"	100270680	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000502463.7, CASC11-201, 3301; ENST00000672942.1, CASC11-205, 1095; ENST00000518376.2, CASC11-202, 907; ENST00000519071.6, CASC11-203, 780; ENST00000672637.1, CASC11-204, 655"	.	chr8:127686343-127738987[-]	.	.	HGNC:48939	.	.	ENSG00000249375	.	.	.	.	.
Mol01293	LncRNA	Cancer susceptibility 9 (CASC9)	CASC9	"CARLo-7, ENST00000518376, LINC00990, MYMLR, TCONS_00014535"	101805492	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000675539.1, CASC9-208, 386; ENST00000676364.1, CASC9-213, 668; ENST00000669950.1, CASC9-206, 1704; ENST00000670695.1, CASC9-207, 1513; ENST00000675897.1, CASC9-211, 1484; ENST00000504531.3, CASC9-201, 1453; ENST00000675884.1, CASC9-210, 1423; ENST00000654852.2, CASC9-205, 1218; ENST00000676127.1, CASC9-212, 1145; ENST00000521147.2, CASC9-202, 1120; ENST00000675549.1, CASC9-209, 1085; ENST00000523313.2, CASC9-204, 1048; ENST00000522183.2, CASC9-203, 847"	.	chr8:75120409-75352327[-]	.	.	HGNC:48906	.	.	ENSG00000249395	.	.	.	.	.
Mol01294	LncRNA	Pvt1 oncogene (PVT1)	PVT1	"ESCCAL-1, LINC00981, linc-JPH1"	5820	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000651587.1, PVT1-224, 2444; ENST00000660438.1, PVT1-293, 2450; ENST00000523068.2, PVT1-216, 2255; ENST00000664995.1, PVT1-323, 2230; ENST00000659106.1, PVT1-283, 2187; ENST00000660631.1, PVT1-295, 2161; ENST00000657449.1, PVT1-265, 2149; ENST00000667418.1, PVT1-347, 2143; ENST00000666147.1, PVT1-336, 2097; ENST00000656693.1, PVT1-254, 1990; ENST00000668098.1, PVT1-351, 1985; ENST00000665856.1, PVT1-331, 1965; ENST00000656532.1, PVT1-253, 1909; ENST00000670532.1, PVT1-368, 1840; ENST00000660456.1, PVT1-294, 1814; ENST00000670714.1, PVT1-372, 1756; ENST00000659912.1, PVT1-288, 1744; ENST00000658840.1, PVT1-282, 1738; ENST00000662413.1, PVT1-308, 1727; ENST00000664265.1, PVT1-317, 1720; ENST00000659326.1, PVT1-284, 1706; ENST00000667305.1, PVT1-346, 1701; ENST00000513868.6, PVT1-203, 1699; ENST00000657356.1, PVT1-263, 1697; ENST00000668619.1, PVT1-357, 1685; ENST00000662410.1, PVT1-307, 1668; ENST00000667630.1, PVT1-349, 1634; ENST00000666776.1, PVT1-340, 1628; ENST00000522963.6, PVT1-215, 1619; ENST00000652816.1, PVT1-229, 1610; ENST00000670204.1, PVT1-366, 1600; ENST00000656402.1, PVT1-250, 1585; ENST00000657289.1, PVT1-261, 1581; ENST00000661988.1, PVT1-305, 1580; ENST00000521122.2, PVT1-210, 1578; ENST00000666777.1, PVT1-341, 1555; ENST00000661160.1, PVT1-300, 1546; ENST00000521951.1, PVT1-212, 1535; ENST00000659666.1, PVT1-286, 1533; ENST00000661625.1, PVT1-303, 1519; ENST00000669416.1, PVT1-362, 1516; ENST00000517790.2, PVT1-205, 1513; ENST00000657112.1, PVT1-258, 1499; ENST00000661830.1, PVT1-304, 1490; ENST00000653853.1, PVT1-237, 1490; ENST00000669951.1, PVT1-364, 1485; ENST00000654369.1, PVT1-242, 1482; ENST00000666080.1, PVT1-334, 1481; ENST00000663461.1, PVT1-312, 1471; ENST00000523190.7, PVT1-217, 1466; ENST00000667149.1, PVT1-344, 1463; ENST00000654105.1, PVT1-240, 1460; ENST00000657596.1, PVT1-268, 1455; ENST00000657451.1, PVT1-266, 1454; ENST00000661205.1, PVT1-301, 1449; ENST00000668123.1, PVT1-352, 1433; ENST00000669272.1, PVT1-360, 1417; ENST00000654324.1, PVT1-241, 1411; ENST00000665737.1, PVT1-330, 1410; ENST00000658350.1, PVT1-279, 1402; ENST00000664299.1, PVT1-319, 1396; ENST00000671092.1, PVT1-375, 1393; ENST00000657667.1, PVT1-269, 1378; ENST00000659625.1, PVT1-285, 1363; ENST00000657211.1, PVT1-260, 1353; ENST00000670795.1, PVT1-373, 1348; ENST00000663059.1, PVT1-311, 1330; ENST00000653990.1, PVT1-238, 1329; ENST00000670223.1, PVT1-367, 1321; ENST00000656999.1, PVT1-257, 1314; ENST00000666353.1, PVT1-338, 1312; ENST00000654091.1, PVT1-239, 1311; ENST00000656411.1, PVT1-251, 1281; ENST00000669082.1, PVT1-358, 1280; ENST00000653497.1, PVT1-233, 1278; ENST00000653522.1, PVT1-234, 1275; ENST00000667714.1, PVT1-350, 1269; ENST00000653845.1, PVT1-236, 1262; ENST00000685634.1, PVT1-378, 1256; ENST00000657517.1, PVT1-267, 1253; ENST00000664293.1, PVT1-318, 1206; ENST00000663753.1, PVT1-314, 1206; ENST00000664742.1, PVT1-321, 1200; ENST00000660122.1, PVT1-290, 1199; ENST00000517525.2, PVT1-204, 1194; ENST00000671088.1, PVT1-374, 1191; ENST00000657183.1, PVT1-259, 1172; ENST00000656491.1, PVT1-252, 1167; ENST00000658556.1, PVT1-281, 1163; ENST00000692433.1, PVT1-382, 1163; ENST00000665721.1, PVT1-329, 1162; ENST00000669132.1, PVT1-359, 1156; ENST00000662766.1, PVT1-310, 1152; ENST00000660200.1, PVT1-292, 1139; ENST00000662061.1, PVT1-306, 1139; ENST00000522414.2, PVT1-213, 1132; ENST00000660896.1, PVT1-298, 1128; ENST00000652695.1, PVT1-227, 1126; ENST00000670602.1, PVT1-370, 1124; ENST00000655783.1, PVT1-246, 1118; ENST00000524165.6, PVT1-220, 1114; ENST00000664610.1, PVT1-320, 1114; ENST00000670626.1, PVT1-371, 1114; ENST00000512617.7, PVT1-202, 1109; ENST00000656077.1, PVT1-247, 1109; ENST00000665246.1, PVT1-326, 1096; ENST00000668479.1, PVT1-355, 1091; ENST00000657384.1, PVT1-264, 1068; ENST00000669509.1, PVT1-363, 1066; ENST00000666076.1, PVT1-333, 1062; ENST00000523328.6, PVT1-218, 1047; ENST00000667539.1, PVT1-348, 1041; ENST00000664139.1, PVT1-315, 1036; ENST00000650846.1, PVT1-221, 1020; ENST00000666842.1, PVT1-342, 1019; ENST00000652492.1, PVT1-226, 1017; ENST00000656880.1, PVT1-255, 1017; ENST00000504719.7, PVT1-201, 1017; ENST00000519481.6, PVT1-208, 1010; ENST00000685606.1, PVT1-377, 1004; ENST00000666452.1, PVT1-339, 1001; ENST00000665698.1, PVT1-328, 1000; ENST00000518528.2, PVT1-207, 995; ENST00000655594.1, PVT1-245, 978; ENST00000657693.1, PVT1-271, 977; ENST00000651568.1, PVT1-223, 971; ENST00000665166.1, PVT1-324, 965; ENST00000665175.1, PVT1-325, 964; ENST00000666223.1, PVT1-337, 963; ENST00000668480.1, PVT1-356, 956; ENST00000656396.1, PVT1-249, 938; ENST00000656168.1, PVT1-248, 935; ENST00000661391.1, PVT1-302, 924; ENST00000522875.5, PVT1-214, 922; ENST00000690350.1, PVT1-380, 922; ENST00000651664.1, PVT1-225, 914; ENST00000658158.1, PVT1-276, 909; ENST00000657297.1, PVT1-262, 907; ENST00000653608.1, PVT1-235, 906; ENST00000656948.1, PVT1-256, 904; ENST00000667204.1, PVT1-345, 897; ENST00000690788.1, PVT1-381, 891; ENST00000669407.1, PVT1-361, 890; ENST00000664924.1, PVT1-322, 886; ENST00000670535.1, PVT1-369, 876; ENST00000660069.1, PVT1-289, 870; ENST00000652993.1, PVT1-231, 866; ENST00000664214.1, PVT1-316, 861; ENST00000662709.1, PVT1-309, 858; ENST00000655099.1, PVT1-243, 855; ENST00000660781.1, PVT1-297, 854; ENST00000692980.1, PVT1-383, 851; ENST00000523427.2, PVT1-219, 837; ENST00000520913.2, PVT1-209, 835; ENST00000666878.1, PVT1-343, 830; ENST00000652883.1, PVT1-230, 821; ENST00000517838.6, PVT1-206, 821; ENST00000658018.1, PVT1-274, 820; ENST00000652728.1, PVT1-228, 812; ENST00000671587.1, PVT1-376, 803; ENST00000659892.1, PVT1-287, 782; ENST00000650930.1, PVT1-222, 777; ENST00000660146.1, PVT1-291, 764; ENST00000665372.1, PVT1-327, 762; ENST00000658429.1, PVT1-280, 760; ENST00000668351.1, PVT1-354, 759; ENST00000660912.1, PVT1-299, 754; ENST00000658065.1, PVT1-275, 745; ENST00000655148.1, PVT1-244, 724; ENST00000657945.1, PVT1-273, 678; ENST00000660659.1, PVT1-296, 673; ENST00000658305.1, PVT1-278, 641; ENST00000653406.1, PVT1-232, 619; ENST00000663715.1, PVT1-313, 615; ENST00000657682.1, PVT1-270, 611; ENST00000657844.1, PVT1-272, 609; ENST00000666105.1, PVT1-335, 608; ENST00000668215.1, PVT1-353, 590; ENST00000689722.1, PVT1-379, 573; ENST00000666039.1, PVT1-332, 520; ENST00000670009.1, PVT1-365, 456; ENST00000658242.1, PVT1-277, 432; ENST00000521600.5, PVT1-211, 408"	.	chr8:127794526-128187101[+]	.	.	HGNC:9709	.	.	ENSG00000249859	.	.	.	.	.
Mol01295	LncRNA	Long non-protein coding RNA 958 (LINC00958)	LINC00958	"LINC00079, MIR1204HG, NCRNA00079, onco-lncRNA-100"	100506305	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000658243.1, LINC00958-211, 1814; ENST00000653981.1, LINC00958-210, 2013; ENST00000526388.2, LINC00958-202, 1801; ENST00000671253.1, LINC00958-215, 1800; ENST00000663902.1, LINC00958-213, 1796; ENST00000662291.1, LINC00958-212, 1751; ENST00000653958.1, LINC00958-209, 1728; ENST00000671577.1, LINC00958-216, 1686; ENST00000653758.1, LINC00958-208, 1673; ENST00000531402.6, LINC00958-205, 1671; ENST00000504230.2, LINC00958-201, 1558; ENST00000534477.6, LINC00958-207, 1520; ENST00000532541.6, LINC00958-206, 1154; ENST00000527945.2, LINC00958-203, 1121; ENST00000667588.1, LINC00958-214, 807; ENST00000529328.1, LINC00958-204, 580"	.	chr11:12961541-12989597[-]	.	.	HGNC:48671	.	.	ENSG00000251381	.	.	.	.	.
Mol01296	LncRNA	Metastasis associated lung adenocarcinoma transcript 1 (MALAT1)	MALAT1	MALAT1	378938	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000619449.2, MALAT1-215, 5340; ENST00000534336.1, MALAT1-202, 8708; ENST00000688218.1, MALAT1-219, 2229; ENST00000689729.1, MALAT1-220, 2229; ENST00000693503.1, MALAT1-223, 2227; ENST00000692086.1, MALAT1-222, 2227; ENST00000685846.1, MALAT1-218, 2223; ENST00000690116.1, MALAT1-221, 2223; ENST00000508832.2, MALAT1-201, 1519; ENST00000618132.1, MALAT1-212, 725; ENST00000618227.1, MALAT1-213, 593; ENST00000616691.1, MALAT1-209, 587; ENST00000610851.1, MALAT1-205, 584; ENST00000616527.4, MALAT1-208, 572; ENST00000544868.2, MALAT1-203, 480; ENST00000618925.1, MALAT1-214, 424; ENST00000617791.1, MALAT1-211, 394; ENST00000610481.1, MALAT1-204, 353; ENST00000620902.1, MALAT1-217, 352; ENST00000620465.4, MALAT1-216, 333; ENST00000617489.1, MALAT1-210, 318; ENST00000612781.1, MALAT1-206, 234; ENST00000613376.1, MALAT1-207, 132"	.	chr11:65497688-65506516[+]	.	.	HGNC:29665	.	.	ENSG00000251562	.	.	.	.	.
Mol01297	LncRNA	Taurine up-regulated 1 (TUG1)	TUG1	"HCN, LINC00047, MALAT-1, NCRNA00047, NEAT2, PRO1073, mascRNA"	55000	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000644773.2, TUG1-217, 7469; ENST00000644027.1, TUG1-216, 7084; ENST00000643071.1, TUG1-210, 6154; ENST00000647354.1, TUG1-220, 5875; ENST00000643553.1, TUG1-213, 5412; ENST00000519077.4, TUG1-201, 5017; ENST00000643077.1, TUG1-211, 4752; ENST00000646496.1, TUG1-219, 4650; ENST00000643920.1, TUG1-215, 4449; ENST00000569384.2, TUG1-207, 4214; ENST00000569149.2, TUG1-206, 4207; ENST00000643280.1, TUG1-212, 3419; ENST00000540687.6, TUG1-203, 3308; ENST00000643877.1, TUG1-214, 3028; ENST00000563812.2, TUG1-204, 2787; ENST00000602393.1, TUG1-208, 2233; ENST00000521091.6, TUG1-202, 2110; ENST00000602971.2, TUG1-209, 1817; ENST00000566220.2, TUG1-205, 932; ENST00000646021.1, TUG1-218, 375"	.	chr22:30969245-30979395[+]	.	.	HGNC:26066	.	.	ENSG00000253352	.	.	.	.	.
Mol01298	LncRNA	Prostate cancer associated transcript 1 (PCAT1)	PCAT1	"FLJ20618, LINC00080, NCRNA00080"	100750225	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000645463.1, PCAT1-228, 906; ENST00000561978.1, PCAT1-208, 1992; ENST00000644627.1, PCAT1-221, 1565; ENST00000645215.1, PCAT1-227, 1562; ENST00000646670.1, PCAT1-230, 1538; ENST00000643101.1, PCAT1-211, 1530; ENST00000689472.1, PCAT1-233, 1511; ENST00000644588.1, PCAT1-219, 1460; ENST00000643742.1, PCAT1-215, 1402; ENST00000524320.2, PCAT1-207, 1393; ENST00000643079.1, PCAT1-210, 1326; ENST00000645490.1, PCAT1-229, 1309; ENST00000644570.1, PCAT1-218, 1280; ENST00000647190.2, PCAT1-232, 1256; ENST00000644842.1, PCAT1-223, 1101; ENST00000643594.2, PCAT1-214, 1075; ENST00000645198.1, PCAT1-226, 1057; ENST00000644733.1, PCAT1-222, 969; ENST00000643118.1, PCAT1-212, 961; ENST00000645130.1, PCAT1-225, 823; ENST00000642795.1, PCAT1-209, 770; ENST00000519319.2, PCAT1-203, 737; ENST00000690964.1, PCAT1-234, 730; ENST00000644594.1, PCAT1-220, 696; ENST00000644021.1, PCAT1-216, 662; ENST00000646972.1, PCAT1-231, 583; ENST00000519880.5, PCAT1-204, 574; ENST00000517915.2, PCAT1-202, 562; ENST00000644994.1, PCAT1-224, 528; ENST00000517773.5, PCAT1-201, 498; ENST00000643428.1, PCAT1-213, 484; ENST00000644323.1, PCAT1-217, 471; ENST00000521586.2, PCAT1-206, 420; ENST00000520512.1, PCAT1-205, 372"	.	chr8:126556323-127419050[+]	.	.	HGNC:43022	.	.	ENSG00000253438	.	.	.	.	.
Mol01299	LncRNA	HOXA cluster antisense RNA 2 (HOXA-AS2)	HOXA-AS2	"PCA1, PCAT-1, PiHL"	285943	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000669815.1, HOXA-AS2-213, 1050; ENST00000517635.2, HOXA-AS2-202, 2455; ENST00000517550.1, HOXA-AS2-201, 2022; ENST00000658768.1, HOXA-AS2-212, 1111; ENST00000523364.1, HOXA-AS2-209, 989; ENST00000521159.5, HOXA-AS2-206, 800; ENST00000521687.5, HOXA-AS2-207, 764; ENST00000593438.1, HOXA-AS2-211, 629; ENST00000517641.1, HOXA-AS2-203, 583; ENST00000518088.5, HOXA-AS2-205, 509; ENST00000524048.1, HOXA-AS2-210, 493; ENST00000518046.1, HOXA-AS2-204, 422; ENST00000522193.1, HOXA-AS2-208, 339"	.	chr7:27107777-27134302[+]	.	.	HGNC:43745	.	.	ENSG00000253552	.	.	.	.	.
Mol01300	LncRNA	SIRT1 regulating LncRNA tumor promoter (SIRLNT)	SIRLNT	HOXA3as	112543493	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000669842.1, SIRLNT-205, 829; ENST00000654202.1, SIRLNT-204, 924; ENST00000521363.1, SIRLNT-202, 881; ENST00000521030.1, SIRLNT-201, 663; ENST00000522486.1, SIRLNT-203, 505"	.	chr8:40298697-40353133[-]	.	.	HGNC:53902	.	.	ENSG00000253802	.	.	.	.	.
Mol01301	LncRNA	Mir-100-let-7a-2-mir-125b-1 cluster host gene (MIR100HG)	MIR100HG	lncRNA-PRLB	399959	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000533109.6, MIR100HG-219, 1794; ENST00000656682.1, MIR100HG-251, 4534; ENST00000666485.1, MIR100HG-278, 4195; ENST00000659296.1, MIR100HG-259, 4175; ENST00000668776.1, MIR100HG-280, 4133; ENST00000530072.7, MIR100HG-209, 3673; ENST00000528986.2, MIR100HG-205, 3514; ENST00000531071.6, MIR100HG-211, 3399; ENST00000654519.1, MIR100HG-242, 3378; ENST00000531381.1, MIR100HG-212, 3370; ENST00000529823.2, MIR100HG-208, 3337; ENST00000649216.1, MIR100HG-235, 3226; ENST00000647591.1, MIR100HG-225, 3218; ENST00000661848.1, MIR100HG-267, 3174; ENST00000648734.1, MIR100HG-234, 3137; ENST00000670198.1, MIR100HG-284, 3098; ENST00000664908.1, MIR100HG-271, 3066; ENST00000662950.1, MIR100HG-268, 3043; ENST00000658364.1, MIR100HG-257, 3034; ENST00000656226.1, MIR100HG-249, 3014; ENST00000670396.1, MIR100HG-286, 3004; ENST00000532319.2, MIR100HG-216, 3003; ENST00000669472.1, MIR100HG-282, 2976; ENST00000532890.6, MIR100HG-218, 2973; ENST00000649293.1, MIR100HG-236, 2971; ENST00000650497.1, MIR100HG-239, 2933; ENST00000655138.1, MIR100HG-245, 2867; ENST00000660148.1, MIR100HG-261, 2859; ENST00000663296.1, MIR100HG-269, 2848; ENST00000653167.1, MIR100HG-240, 2847; ENST00000665673.1, MIR100HG-275, 2811; ENST00000648209.1, MIR100HG-231, 2801; ENST00000656793.1, MIR100HG-252, 2789; ENST00000660603.1, MIR100HG-264, 2766; ENST00000524376.1, MIR100HG-201, 2684; ENST00000655814.1, MIR100HG-248, 2585; ENST00000647967.1, MIR100HG-227, 2549; ENST00000647749.1, MIR100HG-226, 2338; ENST00000637700.1, MIR100HG-224, 2262; ENST00000654629.1, MIR100HG-244, 2038; ENST00000648163.1, MIR100HG-230, 2021; ENST00000532350.6, MIR100HG-217, 1820; ENST00000648213.1, MIR100HG-232, 1734; ENST00000649544.1, MIR100HG-237, 1732; ENST00000654571.2, MIR100HG-243, 1720; ENST00000653565.1, MIR100HG-241, 1650; ENST00000657554.1, MIR100HG-254, 1609; ENST00000686059.1, MIR100HG-290, 1551; ENST00000531470.3, MIR100HG-213, 1522; ENST00000688615.1, MIR100HG-292, 1514; ENST00000649626.1, MIR100HG-238, 1491; ENST00000663802.1, MIR100HG-270, 1481; ENST00000690515.1, MIR100HG-297, 1465; ENST00000692224.1, MIR100HG-299, 1465; ENST00000636654.1, MIR100HG-223, 1434; ENST00000669306.2, MIR100HG-281, 1353; ENST00000669993.1, MIR100HG-283, 1315; ENST00000690198.1, MIR100HG-296, 1301; ENST00000670843.1, MIR100HG-288, 1257; ENST00000658183.1, MIR100HG-256, 1249; ENST00000659378.1, MIR100HG-260, 1249; ENST00000658452.1, MIR100HG-258, 1234; ENST00000529804.6, MIR100HG-207, 1217; ENST00000665305.1, MIR100HG-273, 1215; ENST00000655232.1, MIR100HG-246, 1186; ENST00000532315.1, MIR100HG-215, 1175; ENST00000670374.1, MIR100HG-285, 1164; ENST00000665051.1, MIR100HG-272, 1155; ENST00000690059.1, MIR100HG-294, 1144; ENST00000670951.1, MIR100HG-289, 1143; ENST00000692610.1, MIR100HG-300, 1123; ENST00000648082.1, MIR100HG-228, 1099; ENST00000667484.2, MIR100HG-279, 1071; ENST00000665519.1, MIR100HG-274, 1039; ENST00000661432.1, MIR100HG-265, 1019; ENST00000648084.1, MIR100HG-229, 995; ENST00000660329.2, MIR100HG-263, 993; ENST00000666085.1, MIR100HG-276, 982; ENST00000656387.1, MIR100HG-250, 980; ENST00000657990.1, MIR100HG-255, 972; ENST00000690151.1, MIR100HG-295, 965; ENST00000660311.1, MIR100HG-262, 960; ENST00000527474.5, MIR100HG-203, 959; ENST00000689894.1, MIR100HG-293, 941; ENST00000648576.1, MIR100HG-233, 922; ENST00000666347.1, MIR100HG-277, 905; ENST00000655288.1, MIR100HG-247, 869; ENST00000670520.1, MIR100HG-287, 847; ENST00000686772.1, MIR100HG-291, 800; ENST00000693154.1, MIR100HG-301, 788; ENST00000530955.2, MIR100HG-210, 775; ENST00000691884.1, MIR100HG-298, 745; ENST00000661695.1, MIR100HG-266, 635; ENST00000656868.1, MIR100HG-253, 623; ENST00000534195.1, MIR100HG-220, 586; ENST00000529733.5, MIR100HG-206, 584; ENST00000534297.2, MIR100HG-221, 572; ENST00000531629.1, MIR100HG-214, 562; ENST00000528381.1, MIR100HG-204, 554; ENST00000534782.4, MIR100HG-222, 494; ENST00000526674.1, MIR100HG-202, 310"	.	chr11:122028325-122556721[-]	.	.	HGNC:39522	.	.	ENSG00000255248	.	.	.	.	.
Mol01302	LncRNA	TTC36 and KMT2A antisense RNA 1 (TTC36-AS1)	TTC36-AS1	"AGD1, linc-NeD125, lncRNA-N2"	101929089	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000532597.6, TTC36-AS1-203, 2069; ENST00000554407.5, TTC36-AS1-204, 579; ENST00000525992.2, TTC36-AS1-201, 448; ENST00000528578.5, TTC36-AS1-202, 423; ENST00000556583.1, TTC36-AS1-205, 234"	.	chr11:118510273-118531094[-]	.	.	HGNC:55495	.	.	ENSG00000255435	.	.	.	.	.
Mol01303	LncRNA	Small nucleolar RNA host gene 1 (SNHG1)	SNHG1	SNHG1	23642	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000665371.1, SNHG1-245, 3294; ENST00000535076.6, SNHG1-201, 2812; ENST00000537965.6, SNHG1-207, 2772; ENST00000538654.6, SNHG1-209, 2769; ENST00000661616.1, SNHG1-237, 2336; ENST00000535689.6, SNHG1-202, 2173; ENST00000541416.6, SNHG1-216, 2078; ENST00000537024.6, SNHG1-203, 1727; ENST00000544550.6, SNHG1-220, 1689; ENST00000540865.5, SNHG1-214, 784; ENST00000545308.5, SNHG1-222, 646; ENST00000545688.5, SNHG1-224, 610; ENST00000540904.1, SNHG1-215, 594; ENST00000689147.1, SNHG1-266, 1162; ENST00000656268.1, SNHG1-231, 3771; ENST00000545920.2, SNHG1-225, 3527; ENST00000660960.1, SNHG1-236, 3500; ENST00000655919.1, SNHG1-228, 3489; ENST00000668309.1, SNHG1-249, 3302; ENST00000664307.1, SNHG1-244, 3228; ENST00000663237.1, SNHG1-242, 3119; ENST00000665512.1, SNHG1-246, 3065; ENST00000652879.1, SNHG1-226, 2982; ENST00000671236.1, SNHG1-254, 2843; ENST00000670729.1, SNHG1-253, 2763; ENST00000662400.1, SNHG1-240, 2560; ENST00000670469.1, SNHG1-251, 2470; ENST00000656240.1, SNHG1-229, 2456; ENST00000661936.1, SNHG1-238, 2345; ENST00000662229.1, SNHG1-239, 2309; ENST00000656589.1, SNHG1-232, 2152; ENST00000544983.2, SNHG1-221, 1968; ENST00000660730.1, SNHG1-235, 1944; ENST00000656241.1, SNHG1-230, 1828; ENST00000660547.1, SNHG1-234, 1785; ENST00000667655.1, SNHG1-247, 1782; ENST00000670502.1, SNHG1-252, 1752; ENST00000692454.1, SNHG1-272, 1735; ENST00000691324.1, SNHG1-271, 1551; ENST00000658540.1, SNHG1-233, 1513; ENST00000537925.5, SNHG1-206, 1487; ENST00000653690.1, SNHG1-227, 1438; ENST00000540725.6, SNHG1-213, 1394; ENST00000663092.1, SNHG1-241, 1320; ENST00000688102.1, SNHG1-265, 1300; ENST00000687029.1, SNHG1-263, 1282; ENST00000663967.1, SNHG1-243, 1202; ENST00000668048.1, SNHG1-248, 1158; ENST00000686478.1, SNHG1-259, 1147; ENST00000686670.1, SNHG1-261, 1132; ENST00000670323.1, SNHG1-250, 1112; ENST00000539921.7, SNHG1-211, 1105; ENST00000685229.1, SNHG1-255, 1100; ENST00000692887.1, SNHG1-273, 1092; ENST00000685577.1, SNHG1-256, 1089; ENST00000686500.1, SNHG1-260, 1073; ENST00000691255.1, SNHG1-270, 1073; ENST00000537869.6, SNHG1-205, 1069; ENST00000687243.1, SNHG1-264, 1033; ENST00000686081.1, SNHG1-258, 1018; ENST00000686740.1, SNHG1-262, 1011; ENST00000686008.1, SNHG1-257, 988; ENST00000693734.1, SNHG1-274, 974; ENST00000690476.1, SNHG1-268, 964; ENST00000539975.5, SNHG1-212, 955; ENST00000690542.1, SNHG1-269, 935; ENST00000541578.6, SNHG1-217, 897; ENST00000539303.6, SNHG1-210, 897; ENST00000689664.1, SNHG1-267, 843; ENST00000542112.5, SNHG1-219, 780; ENST00000545440.5, SNHG1-223, 754; ENST00000541615.5, SNHG1-218, 748; ENST00000537068.5, SNHG1-204, 629; ENST00000538266.5, SNHG1-208, 347"	.	chr11:62851978-62855953[-]	.	.	HGNC:32688	.	.	ENSG00000255717	.	.	.	.	.
Mol01304	LncRNA	AGAP2 antisense RNA 1 (AGAP2-AS1)	AGAP2-AS1	"LINC00057, NCRNA00057, UHG, lncRNA16"	100130776	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000542466.2, AGAP2-AS1-201, 1500"	.	chr12:57726271-57728356[+]	.	.	HGNC:48633	.	.	ENSG00000255737	.	.	.	.	.
Mol01305	LncRNA	P53 regulated carcinoma associated Stat3 activating long intergenic non-protein coding transcript (PRECSIT)	PRECSIT	"LOC100130776, PUNISHER"	283487	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000538077.2, PRECSIT-201, 6265; ENST00000687692.1, PRECSIT-202, 1118; ENST00000689874.1, PRECSIT-203, 1118; ENST00000693706.1, PRECSIT-206, 945; ENST00000690007.1, PRECSIT-204, 676; ENST00000690115.1, PRECSIT-205, 676"	.	chr13:110863987-110870330[-]	.	.	HGNC:27492	.	.	ENSG00000255874	.	.	.	.	.
Mol01306	LncRNA	"Novel transcript, antisense to MYRFL (ENST00000547547)"	ENST00000547547	"C13orf29, LINC00346, NCRNA00346"	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000547547.1, -, 434"	.	chr12:69946543-69947081[-]	.	.	.	.	.	ENSG00000257241	.	.	.	.	.
Mol01307	LncRNA	GIHCG inhibitor of miR-200b/200a/429 expression (GIHCG)	GIHCG	GIHCG	100506844	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000547492.1, GIHCG-202, 759; ENST00000553102.1, GIHCG-204, 705; ENST00000659090.1, GIHCG-209, 2214; ENST00000655210.2, GIHCG-206, 1965; ENST00000656617.1, GIHCG-208, 1830; ENST00000655884.1, GIHCG-207, 1284; ENST00000653595.1, GIHCG-205, 986; ENST00000668073.1, GIHCG-213, 894; ENST00000546580.2, GIHCG-201, 803; ENST00000664635.1, GIHCG-211, 672; ENST00000660297.1, GIHCG-210, 597; ENST00000667438.1, GIHCG-212, 495; ENST00000551421.1, GIHCG-203, 451; ENST00000688407.1, GIHCG-214, 411"	.	chr12:57930115-57936345[-]	.	.	HGNC:52649	.	.	ENSG00000257698	.	.	.	.	.
Mol01308	LncRNA	Long non-protein coding RNA 239 (LINC00239)	LINC00239	lncRNA-GIHCG	145200	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000556973.1, LINC00239-201, 639"	.	chr14:101730437-101732522[+]	.	.	HGNC:20119	.	.	ENSG00000258512	.	.	.	.	.
Mol01309	LncRNA	"Long non-protein coding RNA, regulator of reprogramming (LINC-ROR)"	LINC-ROR	"C14orf72, NCRNA00239"	100885779	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000553704.3, LINC-ROR-201, 2604; ENST00000645956.1, LINC-ROR-207, 2186; ENST00000646314.1, LINC-ROR-208, 935; ENST00000643706.1, LINC-ROR-203, 766; ENST00000644805.1, LINC-ROR-206, 737; ENST00000644575.1, LINC-ROR-205, 568; ENST00000642403.1, LINC-ROR-202, 544; ENST00000644118.1, LINC-ROR-204, 532"	.	chr18:57054558-57072119[-]	.	.	HGNC:43773	.	.	ENSG00000258609	.	.	.	.	.
Mol01311	LncRNA	HIF1A antisense RNA 3 (HIF1A-AS3)	HIF1A-AS3	"ROR, lincRNA-RoR, lincRNA-ST8SIA3"	105370526	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000660325.1, HIF1A-AS3-202, 1532; ENST00000554254.1, HIF1A-AS3-201, 533"	.	chr14:61707564-61751099[-]	.	.	HGNC:54284	.	.	ENSG00000258667	.	.	.	.	.
Mol01312	LncRNA	Papillary thyroid carcinoma susceptibility candidate 3 (PTCSC3)	PTCSC3	.	100886964	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000556013.2, PTCSC3-201, 571"	.	chr14:36136108-36176468[-]	.	.	HGNC:43959	.	.	ENSG00000259104	.	.	.	.	.
Mol01313	LncRNA	Long non-protein coding RNA 261 (LINC00261)	LINC00261	LINC00261	140828	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000564492.1, LINC00261-202, 4912; ENST00000638550.3, LINC00261-204, 1840; ENST00000420070.1, LINC00261-201, 795; ENST00000609300.1, LINC00261-203, 457"	.	chr20:22547671-22578642[-]	.	.	HGNC:16189	.	.	ENSG00000259974	.	.	.	.	.
Mol01314	LncRNA	"Novel transcript, overlapping ACER2 (RP11-363E7.4)"	RP11-363E7.4	"ALIEN, C20orf56, DEANR1, FALCOR, HCCDR1, NCRNA00261, TCONS_00027846, bA216C10.1, onco-lncRNA-17"	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000563205.1, -, 1965"	.	chr9:19453209-19455173[+]	.	.	.	.	.	ENSG00000260912	.	.	.	.	.
Mol01315	LncRNA	FOXC2 antisense RNA 1 (FOXC2-AS1)	FOXC2-AS1	FOXC2-AS1	103752587	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000563280.2, FOXC2-AS1-201, 403"	.	chr16:86565145-86567845[-]	.	.	HGNC:50665	.	.	ENSG00000260944	.	.	.	.	.
Mol01317	LncRNA	LOXL1 antisense RNA 1 (LOXL1-AS1)	LOXL1-AS1	ODRUL	100287616	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000685373.1, LOXL1-AS1-214, 984; ENST00000562739.6, LOXL1-AS1-202, 3429; ENST00000567257.5, LOXL1-AS1-210, 2358; ENST00000564194.5, LOXL1-AS1-204, 2301; ENST00000562965.1, LOXL1-AS1-203, 1183; ENST00000565756.5, LOXL1-AS1-208, 885; ENST00000568229.5, LOXL1-AS1-213, 765; ENST00000565689.5, LOXL1-AS1-207, 735; ENST00000688623.1, LOXL1-AS1-215, 701; ENST00000567644.5, LOXL1-AS1-211, 640; ENST00000565416.1, LOXL1-AS1-206, 588; ENST00000566675.5, LOXL1-AS1-209, 574; ENST00000568087.5, LOXL1-AS1-212, 565; ENST00000564963.1, LOXL1-AS1-205, 538; ENST00000562130.5, LOXL1-AS1-201, 533"	.	chr15:73908071-73928248[-]	.	.	HGNC:44169	.	.	ENSG00000261801	.	.	.	.	.
Mol01318	LncRNA	Breast cancer anti-estrogen resistance 4 (BCAR4)	BCAR4	BCAR4	400500	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000571158.5, BCAR4-201, 791; ENST00000573319.1, BCAR4-204, 1273; ENST00000573037.1, BCAR4-203, 887; ENST00000571259.5, BCAR4-202, 669; ENST00000574028.1, BCAR4-205, 470; ENST00000577041.1, BCAR4-206, 378; ENST00000615574.1, BCAR4-207, 366"	.	chr16:11819829-11828845[-]	.	.	HGNC:22170	.	.	ENSG00000262117	.	.	.	.	.
Mol01319	LncRNA	Long non-protein coding RNA 672 (LINC00672)	LINC00672	LINC00672	100505576	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000583195.2, LINC00672-201, 3692"	.	chr17:38925168-38929384[+]	.	.	HGNC:44353	.	.	ENSG00000263874	.	.	.	.	.
Mol01320	LncRNA	ENSG00000267194 (RP1-193H18.2 )	RP1-193H18.2	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	ENSG00000267194	.	.	.	.	.
Mol01321	LncRNA	FOXF1 adjacent non-coding developmental regulatory RNA (FENDRR)	FENDRR	FENDRR	400550	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000659025.1, FENDRR-208, 3705; ENST00000593604.2, FENDRR-201, 3510; ENST00000659545.1, FENDRR-210, 3330; ENST00000667117.1, FENDRR-212, 3277; ENST00000598996.3, FENDRR-205, 3192; ENST00000595886.1, FENDRR-203, 3095; ENST00000599749.5, FENDRR-206, 2843; ENST00000671115.1, FENDRR-214, 2762; ENST00000662100.1, FENDRR-211, 2671; ENST00000669311.1, FENDRR-213, 2103; ENST00000659486.1, FENDRR-209, 1896; ENST00000594398.1, FENDRR-202, 602; ENST00000597578.1, FENDRR-204, 553; ENST00000600553.5, FENDRR-207, 355"	.	chr16:86474529-86509099[-]	.	.	HGNC:43894	.	.	ENSG00000268388	.	.	.	.	.
Mol01322	LncRNA	KCNQ1 opposite strand/antisense transcript 1 (KCNQ1OT1)	KCNQ1OT1	"FOXF1-AS1, lincFOXF1, onco-lncRNA-21"	10984	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000597346.1, KCNQ1OT1-201, 91667"	.	chr11:2608328-2699994[-]	.	.	HGNC:6295	.	.	ENSG00000269821	.	.	.	.	.
Mol01323	LncRNA	NF-kappaB interacting LncRNA (NKILA)	NKILA	"KCNQ1-AS2, KvDMR1, KvLQT1-AS, LIT1, NCRNA00012"	105416157	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000614771.2, NKILA-202, 2625; ENST00000613231.1, NKILA-201, 537"	.	chr20:57710156-57712780[+]	.	.	HGNC:51599	.	.	ENSG00000278709	.	.	.	.	.
Mol01324	LncRNA	BRAF-activated non-protein coding RNA (BANCR)	BANCR	BANCR	100885775	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000625062.4, BANCR-202, 558; ENST00000691130.1, BANCR-204, 768; ENST00000624238.3, BANCR-201, 764; ENST00000693755.1, BANCR-205, 619; ENST00000690153.1, BANCR-203, 617"	.	chr9:69296678-69311111[-]	.	.	HGNC:43877	.	.	ENSG00000278910	.	.	.	.	.
Mol01325	LncRNA	E2F1-regulated inhibitor of cell death (ERICD)	ERICD	LINC00586	104355217	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000623655.2, ERICD-201, 2003"	.	chr8:140636281-140638283[+]	.	.	HGNC:49404	.	.	ENSG00000280303	.	.	.	.	.
Mol01326	LncRNA	PCBP2 overlapping transcript 1 (PCBP2-OT1)	PCBP2-OT1	"ERIC, LINC01130, TCONS_00014875"	102157401	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000634357.1, PCBP2-OT1-201, 590"	.	chr12:53464468-53465057[+]	.	.	HGNC:49150	.	.	ENSG00000282977	.	.	.	.	.
Mol01327	LncRNA	Hepatocellular carcinoma up-regulated long non-coding RNA (HULC)	HULC	"TUC.338, TUC338, uc.338"	728655	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000645747.1, HULC-270, 1783; ENST00000642357.1, HULC-207, 3568; ENST00000644837.1, HULC-255, 3529; ENST00000646231.1, HULC-284, 3469; ENST00000643788.1, HULC-236, 3387; ENST00000645474.1, HULC-266, 3341; ENST00000643985.1, HULC-241, 3302; ENST00000645379.1, HULC-264, 3277; ENST00000646996.1, HULC-305, 3163; ENST00000643058.1, HULC-218, 3147; ENST00000643136.1, HULC-221, 3133; ENST00000643126.1, HULC-220, 3014; ENST00000643036.1, HULC-217, 2976; ENST00000645365.1, HULC-263, 2976; ENST00000642163.1, HULC-203, 2936; ENST00000646490.1, HULC-292, 2925; ENST00000645344.1, HULC-262, 2883; ENST00000646431.1, HULC-290, 2882; ENST00000647365.1, HULC-312, 2851; ENST00000645047.1, HULC-258, 2843; ENST00000645808.1, HULC-274, 2836; ENST00000644654.1, HULC-252, 2821; ENST00000645464.1, HULC-265, 2806; ENST00000645976.1, HULC-280, 2805; ENST00000645486.1, HULC-267, 2793; ENST00000643545.1, HULC-232, 2777; ENST00000646792.1, HULC-301, 2638; ENST00000646295.1, HULC-286, 2635; ENST00000646718.1, HULC-295, 2611; ENST00000644248.1, HULC-246, 2604; ENST00000645611.1, HULC-268, 2563; ENST00000643473.1, HULC-230, 2543; ENST00000646007.1, HULC-281, 2528; ENST00000644778.1, HULC-253, 2466; ENST00000642534.1, HULC-209, 2463; ENST00000646521.1, HULC-293, 2415; ENST00000646876.1, HULC-303, 2369; ENST00000642760.1, HULC-213, 2257; ENST00000646073.1, HULC-283, 2225; ENST00000647156.1, HULC-309, 2218; ENST00000642798.1, HULC-214, 2151; ENST00000644363.1, HULC-247, 2079; ENST00000645322.1, HULC-261, 2060; ENST00000642666.2, HULC-212, 2016; ENST00000643311.1, HULC-225, 1856; ENST00000644892.1, HULC-256, 1844; ENST00000643761.1, HULC-235, 1831; ENST00000644070.1, HULC-243, 1727; ENST00000645796.1, HULC-273, 1714; ENST00000645087.1, HULC-259, 1694; ENST00000644213.2, HULC-245, 1686; ENST00000642859.1, HULC-215, 1641; ENST00000644038.1, HULC-242, 1623; ENST00000643259.1, HULC-224, 1599; ENST00000645715.1, HULC-269, 1596; ENST00000642622.1, HULC-210, 1569; ENST00000647466.1, HULC-313, 1556; ENST00000643141.1, HULC-222, 1547; ENST00000646706.1, HULC-294, 1542; ENST00000642458.1, HULC-208, 1528; ENST00000645820.1, HULC-275, 1505; ENST00000643635.1, HULC-234, 1490; ENST00000643526.1, HULC-231, 1458; ENST00000643571.1, HULC-233, 1457; ENST00000646403.1, HULC-288, 1429; ENST00000643938.1, HULC-239, 1412; ENST00000644364.1, HULC-248, 1396; ENST00000646488.1, HULC-291, 1368; ENST00000646749.1, HULC-297, 1339; ENST00000645758.1, HULC-272, 1337; ENST00000645940.1, HULC-278, 1330; ENST00000645970.1, HULC-279, 1317; ENST00000643404.1, HULC-226, 1296; ENST00000647175.1, HULC-310, 1288; ENST00000645017.1, HULC-257, 1286; ENST00000645925.1, HULC-277, 1281; ENST00000644610.1, HULC-251, 1274; ENST00000642345.1, HULC-206, 1274; ENST00000647306.1, HULC-311, 1269; ENST00000643414.1, HULC-227, 1252; ENST00000644111.1, HULC-244, 1238; ENST00000644441.1, HULC-249, 1226; ENST00000647039.1, HULC-306, 1218; ENST00000647052.1, HULC-307, 1214; ENST00000643431.1, HULC-229, 1208; ENST00000644800.1, HULC-254, 1205; ENST00000645750.1, HULC-271, 1204; ENST00000647135.1, HULC-308, 1196; ENST00000643415.1, HULC-228, 1191; ENST00000643083.1, HULC-219, 1184; ENST00000645321.1, HULC-260, 1171; ENST00000646406.1, HULC-289, 1167; ENST00000665267.1, HULC-314, 1161; ENST00000643953.1, HULC-240, 1150; ENST00000646868.1, HULC-302, 1145; ENST00000646741.1, HULC-296, 1145; ENST00000642340.1, HULC-205, 1127; ENST00000642665.1, HULC-211, 1103; ENST00000642877.1, HULC-216, 1077; ENST00000645863.1, HULC-276, 1069; ENST00000642168.1, HULC-204, 1055; ENST00000643201.1, HULC-223, 979; ENST00000646043.1, HULC-282, 958; ENST00000693633.1, HULC-316, 958; ENST00000646981.1, HULC-304, 948; ENST00000503668.2, HULC-202, 947; ENST00000643889.1, HULC-238, 919; ENST00000644605.1, HULC-250, 896; ENST00000643832.1, HULC-237, 890; ENST00000646774.1, HULC-299, 782; ENST00000646758.1, HULC-298, 734; ENST00000646377.1, HULC-287, 696; ENST00000665625.1, HULC-315, 664; ENST00000429060.2, HULC-201, 612; ENST00000646784.1, HULC-300, 581; ENST00000646294.1, HULC-285, 561"	.	chr6:8435568-9294133[+]	.	.	HGNC:34232	.	.	ENSG00000285219	.	.	.	.	.
Mol01328	Precursor miRNA	hsa-let-7a	microRNA let-7a-1	"HCCAT1, LINC00078, NCRNA00078"	406881	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362295.3, MIRLET7A1-201, 80"	UGGGAUGAGGUAGUAGGUUGUAUAGUUUUAGGGUCACACCCACCACUGGGAGAUAACUAUACAAUCUACUGUCUUUCCUA	chr9:94175957-94176036[+]	.	.	HGNC:31476	.	.	ENSG00000199165	MI0000060	.	.	.	.
Mol01329	Precursor miRNA	hsa-let-7b	microRNA let-7b	MIRLET7B	406884	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385140.1, MIRLET7B-201, 83"	CGGGGUGAGGUAGUAGGUUGUGUGGUUUCAGGGCAGUGAUGUUGCCCCUCGGAAGAUAACUAUACAACCUACUGCCUUCCCUG	chr22:46113686-46113768[+]	.	.	HGNC:31479	.	.	ENSG00000284520	MI0000063	.	.	.	.
Mol01330	Precursor miRNA	hsa-let-7c	microRNA let-7c	MIRLET7C	406885	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362160.2, MIRLET7C-201, 84"	GCAUCCGGGUUGAGGUAGUAGGUUGUAUGGUUUAGAGUUACACCCUGGGAGUUAACUGUACAACCUUCUAGCUUUCCUUGGAGC	chr21:16539828-16539911[+]	.	.	HGNC:31480	.	.	ENSG00000199030	MI0000064	.	.	.	.
Mol01331	Precursor miRNA	hsa-let-7d	microRNA let-7d	MIRLET7D	406886	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362263.3, MIRLET7D-201, 87"	CCUAGGAAGAGGUAGUAGGUUGCAUAGUUUUAGGGCAGGGAUUUUGCCCACAAGGAGGUAACUAUACGACCUGCUGCCUUUCUUAGG	chr9:94178834-94178920[+]	.	.	HGNC:31481	.	.	ENSG00000199133	MI0000065	.	.	.	.
Mol01332	Precursor miRNA	hsa-let-7e	microRNA let-7e	MIRLET7E	406887	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362102.3, MIRLET7E-201, 79"	CCCGGGCUGAGGUAGGAGGUUGUAUAGUUGAGGAGGACACCCAAGGAGAUCACUAUACGGCCUCCUAGCUUUCCCCAGG	chr19:51692786-51692864[+]	.	.	HGNC:31482	.	.	ENSG00000198972	MI0000066	.	.	.	.
Mol01333	Precursor miRNA	hsa-let-7f-1	microRNA let-7f-1	MIRLET7F1	406888	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362202.3, MIRLET7F1-201, 87"	UCAGAGUGAGGUAGUAGAUUGUAUAGUUGUGGGGUAGUGAUUUUACCCUGUUCAGGAGAUAACUAUACAAUCUAUUGCCUUCCCUGA	chr9:94176347-94176433[+]	.	.	HGNC:31483	.	.	ENSG00000199072	MI0000067	.	.	.	.
Mol01334	Precursor miRNA	hsa-mir-15	microRNA 15a	MIR15A	406948	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000607334.3, MIR15A-201, 83"	CCUUGGAGUAAAGUAGCAGCACAUAAUGGUUUGUGGAUUUUGAAAAGGUGCAGGCCAUAUUGUGCUGCCUCAAAAAUACAAGG	chr13:50049119-50049201[-]	.	.	HGNC:31543	.	.	ENSG00000283785	MI0000069	.	.	.	.
Mol01335	Precursor miRNA	hsa-mir-15a	microRNA 15a	MIR15A	406948	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000607334.3, MIR15A-201, 83"	CCUUGGAGUAAAGUAGCAGCACAUAAUGGUUUGUGGAUUUUGAAAAGGUGCAGGCCAUAUUGUGCUGCCUCAAAAAUACAAGG	chr13:50049119-50049201[-]	.	.	HGNC:31543	.	.	ENSG00000283785	MI0000069	.	.	.	.
Mol01336	Precursor miRNA	hsa-mir-16	microRNA 16-1	MIR16-1	406950	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385271.1, MIR16-1-201, 89"	GUCAGCAGUGCCUUAGCAGCACGUAAAUAUUGGCGUUAAGAUUCUAAAAUUAUCUCCAGUAUUAACUGUGCUGCUGAAGUAAGGUUGAC	chr13:50048973-50049061[-]	.	.	HGNC:31545	.	.	ENSG00000208006	MI0000070	.	.	.	.
Mol01337	Precursor miRNA	hsa-mir-16-1	microRNA 16-1	MIR16-1	406950	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385271.1, MIR16-1-201, 89"	GUCAGCAGUGCCUUAGCAGCACGUAAAUAUUGGCGUUAAGAUUCUAAAAUUAUCUCCAGUAUUAACUGUGCUGCUGAAGUAAGGUUGAC	chr13:50048973-50049061[-]	.	.	HGNC:31545	.	.	ENSG00000208006	MI0000070	.	.	.	.
Mol01338	Precursor miRNA	hsa-mir-17	microRNA 17	MIR17	406952	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385012.1, MIR17-201, 84"	GUCAGAAUAAUGUCAAAGUGCUUACAGUGCAGGUAGUGAUAUGUGCAUCUACUGCAGUGAAGGCACUUGUAGCAUUAUGGUGAC	chr13:91350605-91350688[+]	.	.	HGNC:31547	.	.	ENSG00000284536	MI0000071	.	.	.	.
Mol01339	Precursor miRNA	hsa-mir-18a	microRNA 18a	MIR18A	406953	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362310.3, MIR18A-201, 71"	UGUUCUAAGGUGCAUCUAGUGCAGAUAGUGAAGUAGAUUAGCAUCUACUGCCCUAAGUGCUCCUUCUGGCA	chr13:91350751-91350821[+]	.	.	HGNC:31548	.	.	ENSG00000283815	MI0000072	.	.	.	.
Mol01340	Precursor miRNA	hsa-mir-19a	microRNA 19a	MIR19A	406979	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384878.1, MIR19A-201, 82"	GCAGUCCUCUGUUAGUUUUGCAUAGUUGCACUACAAGAAGAAUGUAGUUGUGCAAAUCUAUGCAAAACUGAUGGUGGCCUGC	chr13:91350891-91350972[+]	.	.	HGNC:31574	.	.	ENSG00000284204	MI0000073	.	.	.	.
Mol01341	Precursor miRNA	hsa-mir-19b	microRNA 19b-1	MIR19B1	406980	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384829.1, MIR19B1-201, 87"	CACUGUUCUAUGGUUAGUUUUGCAGGUUUGCAUCCAGCUGUGUGAUAUUCUGCUGUGCAAAUCCAUGCAAAACUGACUGUGGUAGUG	chr13:91351192-91351278[+]	.	.	HGNC:31575	.	.	ENSG00000284375	MI0000074	.	.	.	.
Mol01342	Precursor miRNA	hsa-mir-20a	microRNA 20a	MIR20A	406982	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362279.1, MIR20A-201, 71"	GUAGCACUAAAGUGCUUAUAGUGCAGGUAGUGUUUAGUUAUCUACUGCAUUAUGAGCACUUAAAGUACUGC	chr13:91351065-91351135[+]	.	.	HGNC:31577	.	.	ENSG00000283762	MI0000076	.	.	.	.
Mol01343	Precursor miRNA	hsa-mir-21	microRNA 21	MIR21	406991	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362134.1, MIR21-201, 72"	UGUCGGGUAGCUUAUCAGACUGAUGUUGACUGUUGAAUCUCAUGGCAACACCAGUCGAUGGGCUGUCUGACA	chr17:59841266-59841337[+]	.	.	HGNC:31586	.	.	ENSG00000284190	MI0000077	.	.	.	.
Mol01344	Precursor miRNA	hsa-mir-22	microRNA 22	MIR22	407004	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362190.3, MIR22-201, 85"	GGCUGAGCCGCAGUAGUUCUUCAGUGGCAAGCUUUAUGUCCUGACCCAGCUAAAGCUGCCAGUUGAAGAACUGUUGCCCUCUGCC	chr17:1713903-1713987[-]	.	.	HGNC:31599	.	.	ENSG00000283824	MI0000078	.	.	.	.
Mol01345	Precursor miRNA	hsa-mir-23a	microRNA 23a	MIR23A	407010	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385245.1, MIR23A-201, 73"	GGCCGGCUGGGGUUCCUGGGGAUGGGAUUUGCUUCCUGUCACAAAUCACAUUGCCAGGGAUUUCCAACCGACC	chr19:13836587-13836659[-]	.	.	HGNC:31605	.	.	ENSG00000207980	MI0000079	.	.	.	.
Mol01346	Precursor miRNA	hsa-mir-24	microRNA 24-1	MIR24-1	407012	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000637495.1, MIR24-1-201, 68"	CUCCGGUGCCUACUGAGCUGAUAUCAGUUCUCAUUUUACACACUGGCUCAGUUCAGCAGGAACAGGAG	chr9:95086021-95086088[+]	.	.	HGNC:31607	.	.	ENSG00000284459	MI0000080	.	.	.	.
Mol01347	Precursor miRNA	hsa-mir-25	microRNA 25	MIR25	407014	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384816.1, MIR25-201, 84"	GGCCAGUGUUGAGAGGCGGAGACUUGGGCAAUUGCUGGACGCUGCCCUGGGCAUUGCACUUGUCUCGGUCUGACAGUGCCGGCC	chr7:100093560-100093643[-]	.	.	HGNC:31609	.	.	ENSG00000207547	MI0000082	.	.	.	.
Mol01348	Precursor miRNA	hsa-mir-26a	microRNA 26a-1	MIR26A1	407015	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362205.1, MIR26A1-201, 77"	GUGGCCUCGUUCAAGUAAUCCAGGAUAGGCUGUGCAGGUCCCAAUGGGCCUAUUCUUGGUUACUUGCACGGGGACGC	chr3:37969404-37969480[+]	.	.	HGNC:31610	.	.	ENSG00000199075	MI0000083	.	.	.	.
Mol01349	Precursor miRNA	hsa-mir-26b	microRNA 26b	MIR26B	407017	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362251.4, MIR26B-201, 77"	CCGGGACCCAGUUCAAGUAAUUCAGGAUAGGUUGUGUGCUGUCCAGCCUGUUCUCCAUUACUUGGCUCGGGGACCGG	chr2:218402646-218402722[+]	.	.	HGNC:31612	.	.	ENSG00000199121	MI0000084	.	.	.	.
Mol01350	Precursor miRNA	hsa-mir-27a	microRNA 27a	MIR27A	407018	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385073.1, MIR27A-201, 78"	CUGAGGAGCAGGGCUUAGCUGCUUGUGAGCAGGGUCCACACCAAGUCGUGUUCACAGUGGCUAAGUUCCGCCCCCCAG	chr19:13836440-13836517[-]	.	.	HGNC:31613	.	.	ENSG00000207808	MI0000085	.	.	.	.
Mol01351	Precursor miRNA	hsa-mir-29a	microRNA 29a	MIR29A	407021	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362111.4, MIR29A-201, 64"	AUGACUGAUUUCUUUUGGUGUUCAGAGUCAAUAUAAUUUUCUAGCACCAUCUGAAAUCGGUUAU	chr7:130876747-130876810[-]	.	.	HGNC:31616	.	.	ENSG00000284032	MI0000087	.	.	.	.
Mol01352	Precursor miRNA	hsa-mir-30a	microRNA 30a	MIR30A	407029	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385092.1, MIR30A-201, 71"	GCGACUGUAAACAUCCUCGACUGGAAGCUGUGAAGCCACAGAUGGGCUUUCAGUCGGAUGUUUGCAGCUGC	chr6:71403551-71403621[-]	.	.	HGNC:31624	.	.	ENSG00000207827	MI0000088	.	.	.	.
Mol01353	Precursor miRNA	hsa-mir-31	microRNA 31	MIR31	407035	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362307.1, MIR31-201, 71"	GGAGAGGAGGCAAGAUGCUGGCAUAGCUGUUGAACUGGGAACCUGCUAUGCCAACAUAUUGCCAUCUUUCC	chr9:21512115-21512185[-]	.	.	HGNC:31630	.	.	ENSG00000199177	MI0000089	.	.	.	.
Mol01354	Precursor miRNA	hsa-mir-32	microRNA 32	MIR32	407036	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384965.1, MIR32-201, 70"	GGAGAUAUUGCACAUUACUAAGUUGCAUGUUGUCACGGCCUCAAUGCAAUUUAGUGUGUGUGAUAUUUUC	chr9:109046229-109046298[-]	.	.	HGNC:31631	.	.	ENSG00000207698	MI0000090	.	.	.	.
Mol01355	Precursor miRNA	hsa-mir-33a	microRNA 33a	MIR33A	407039	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385197.1, MIR33A-201, 69"	CUGUGGUGCAUUGUAGUUGCAUUGCAUGUUCUGGUGGUACCCAUGCAAUGUUUCCACAGUGCAUCACAG	chr22:41900944-41901012[+]	.	.	HGNC:31634	.	.	ENSG00000207932	MI0000091	.	.	.	.
Mol01356	Precursor miRNA	hsa-mir-92a	microRNA 92a-1	MIR92A1	407048	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385233.3, MIR92A1-201, 78"	CUUUCUACACAGGUUGGGAUCGGUUGCAAUGCUGUGUUUCUGUAUGGUAUUGCACUUGUCCCGGCCUGUUGAGUUUGG	chr13:91351314-91351391[+]	.	.	HGNC:31643	.	.	ENSG00000283705	MI0000093	.	.	.	.
Mol01357	Precursor miRNA	hsa-mir-93	microRNA 93	MIR93	407050	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385024.1, MIR93-201, 80"	CUGGGGGCUCCAAAGUGCUGUUCGUGCAGGUAGUGUGAUUACCCAACCUACUGCUGAGCUAGCACUUCCCGAGCCCCCGG	chr7:100093768-100093847[-]	.	.	HGNC:31645	.	.	ENSG00000207757	MI0000095	.	.	.	.
Mol01358	Precursor miRNA	hsa-mir-96	microRNA 96	MIR96	407053	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362288.1, MIR96-201, 78"	UGGCCGAUUUUGGCACUAGCACAUUUUUGCUUGUGUCUCUCCGCUCUGAGCAAUCAUGUGCAGUGCCAAUAUGGGAAA	chr7:129774692-129774769[-]	.	.	HGNC:31648	.	.	ENSG00000199158	MI0000098	.	.	.	.
Mol01359	Precursor miRNA	hsa-mir-98	microRNA 98	MIR98	407054	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000606724.1, MIR98-201, 119"	AGGAUUCUGCUCAUGCCAGGGUGAGGUAGUAAGUUGUAUUGUUGUGGGGUAGGGAUAUUAGGCCCCAAUUAGAAGAUAACUAUACAACUUACUACUUUCCCUGGUGUGUGGCAUAUUCA	chrX:53556223-53556341[-]	.	.	HGNC:31649	.	.	ENSG00000271886	MI0000100	.	.	.	.
Mol01360	Precursor miRNA	hsa-mir-99a	microRNA 99a	MIR99A	407055	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384906.1, MIR99A-201, 81"	CCCAUUGGCAUAAACCCGUAGAUCCGAUCUUGUGGUGAAGUGGACCGCACAAGCUCGCUUCUAUGGGUCUGUGUCAGUGUG	chr21:16539089-16539169[+]	.	.	HGNC:31650	.	.	ENSG00000207638	MI0000101	.	.	.	.
Mol01361	Precursor miRNA	hsa-mir-100	microRNA 100	MIR100	406892	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385259.1, MIR100-201, 80"	CCUGUUGCCACAAACCCGUAGAUCCGAACUUGUGGUAUUAGUCCGCACAAGCUUGUAUCUAUAGGUAUGUGUCUGUUAGG	chr11:122152229-122152308[-]	.	.	HGNC:31487	.	.	ENSG00000207994	MI0000102	.	.	.	.
Mol01362	Precursor miRNA	hsa-mir-101	microRNA 101-1	MIR101-1	406893	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362265.1, MIR101-1-201, 75"	UGCCCUGGCUCAGUUAUCACAGUGCUGAUGCUGUCUAUUCUAAAGGUACAGUACUGUGAUAACUGAAGGAUGGCA	chr1:65058434-65058508[-]	.	.	HGNC:31488	.	.	ENSG00000199135	MI0000103	.	.	.	.
Mol01363	Precursor miRNA	hsa-mir-29b	microRNA 29b-1	MIR29B1	407024	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385015.1, MIR29B1-201, 81"	CUUCAGGAAGCUGGUUUCAUAUGGUGGUUUAGAUUUAAAUAGUGAUUGUCUAGCACCAUUUGAAAUCAGUGUUCUUGGGGG	chr7:130877459-130877539[-]	.	.	HGNC:31619	.	.	ENSG00000283797	MI0000105	.	.	.	.
Mol01364	Precursor miRNA	hsa-mir-29b-1	microRNA 29b-1	MIR29B1	407024	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385015.1, MIR29B1-201, 81"	CUUCAGGAAGCUGGUUUCAUAUGGUGGUUUAGAUUUAAAUAGUGAUUGUCUAGCACCAUUUGAAAUCAGUGUUCUUGGGGG	chr7:130877459-130877539[-]	.	.	HGNC:31619	.	.	ENSG00000283797	MI0000105	.	.	.	.
Mol01365	Precursor miRNA	hsa-mir-103	microRNA 103a-1	MIR103A1	406895	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362165.2, MIR103A1-201, 78"	UACUGCCCUCGGCUUCUUUACAGUGCUGCCUUGUUGCAUAUGGAUCAAGCAGCAUUGUACAGGGCUAUGAAGGCAUUG	chr5:168560896-168560973[-]	.	.	HGNC:31490	.	.	ENSG00000199035	MI0000109	.	.	.	.
Mol01366	Precursor miRNA	hsa-mir-105	microRNA 105-1	MIR105-1	406897	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385222.1, MIR105-1-201, 81"	UGUGCAUCGUGGUCAAAUGCUCAGACUCCUGUGGUGGCUGCUCAUGCACCACGGAUGUUUGAGCAUGUGCUACGGUGUCUA	chrX:152392219-152392299[-]	.	.	HGNC:31492	.	.	ENSG00000207957	MI0000111	.	.	.	.
Mol01367	Precursor miRNA	hsa-mir-106a	microRNA 106a	MIR106A	406899	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384870.1, MIR106A-201, 81"	CCUUGGCCAUGUAAAAGUGCUUACAGUGCAGGUAGCUUUUUGAGAUCUACUGCAAUGUAAGCACUUCUUACAUUACCAUGG	chrX:134170198-134170278[-]	.	.	HGNC:31494	.	.	ENSG00000284157	MI0000113	.	.	.	.
Mol01368	Precursor miRNA	hsa-mir-192	microRNA 192	MIR192	406967	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384915.3, MIR192-201, 110"	GCCGAGACCGAGUGCACAGGGCUCUGACCUAUGAAUUGACAGCCAGUGCUCUCGUCUCCCCUCUGGCUGCCAAUUCCAUAGGUCACAGGUAUGUUCGCCUCAAUGCCAGC	chr11:64891137-64891246[-]	.	.	HGNC:31562	.	.	ENSG00000283926	MI0000234	.	.	.	.
Mol01369	Precursor miRNA	hsa-mir-196a	microRNA 196a-1	MIR196A1	406972	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000388006.1, MIR196A1-201, 70"	GUGAAUUAGGUAGUUUCAUGUUGUUGGGCCUGGGUUUCUGAACACAACAACAUUAAACCACCCGAUUCAC	chr17:48632490-48632559[-]	.	.	HGNC:31567	.	.	ENSG00000210741	MI0000238	.	.	.	.
Mol01370	Precursor miRNA	hsa-mir-197	microRNA 197	MIR197	406974	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384976.2, MIR197-201, 75"	GGCUGUGCCGGGUAGAGAGGGCAGUGGGAGGUAAGAGCUCUUCACCCUUCACCACCUUCUCCACCCAGCAUGGCC	chr1:109598893-109598967[+]	.	.	HGNC:31569	.	.	ENSG00000284443	MI0000239	.	.	.	.
Mol01371	Precursor miRNA	hsa-mir-199a	microRNA 199a-1	MIR199A1	406976	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385019.1, MIR199A1-201, 71"	GCCAACCCAGUGUUCAGACUACCUGUUCAGGAGGCUCUCAAUGUGUACAGUAGUCUGCACAUUGGUUAGGC	chr19:10817426-10817496[-]	.	.	HGNC:31571	.	.	ENSG00000207752	MI0000242	.	.	.	.
Mol01372	Precursor miRNA	hsa-mir-129	microRNA 129-1	MIR129-1	406917	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384972.2, MIR129-1-201, 72"	GGAUCUUUUUGCGGUCUGGGCUUGCUGUUCCUCUCAACAGUAGUCAGGAAGCCCUUACCCCAAAAAGUAUCU	chr7:128207872-128207943[+]	.	.	HGNC:31512	.	.	ENSG00000207705	MI0000252	.	.	.	.
Mol01373	Precursor miRNA	hsa-mir-148a	microRNA 148a	MIR148A	406940	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362215.3, MIR148A-201, 68"	GAGGCAAAGUUCUGAGACACUCCGACUCUGAGUAUGAUAGAAGUCAGUGCACUACAGAACUUUGUCUC	chr7:25949919-25949986[-]	.	.	HGNC:31535	.	.	ENSG00000199085	MI0000253	.	.	.	.
Mol01374	Precursor miRNA	hsa-mir-30c	microRNA 30c-2	MIR30C2	407032	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362224.3, MIR30C2-201, 72"	AGAUACUGUAAACAUCCUACACUCUCAGCUGUGGAAAGUAAGAAAGCUGGGAGAAGGCUGUUUACUCUUUCU	chr6:71376960-71377031[-]	.	.	HGNC:31627	.	.	ENSG00000199094	MI0000254	.	.	.	.
Mol01375	Precursor miRNA	hsa-mir-30d	microRNA 30d	MIR30D	407033	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362283.1, MIR30D-201, 70"	GUUGUUGUAAACAUCCCCGACUGGAAGCUGUAAGACACAGCUAAGCUUUCAGUCAGAUGUUUGCUGCUAC	chr8:134804876-134804945[-]	.	.	HGNC:31628	.	.	ENSG00000199153	MI0000255	.	.	.	.
Mol01376	Precursor miRNA	hsa-mir-139	microRNA 139	MIR139	406931	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000606837.1, MIR139-201, 68"	GUGUAUUCUACAGUGCACGUGUCUCCAGUGUGGCUCGGAGGCUGGAGACGCGGCCCUGUUGGAGUAAC	chr11:72615063-72615130[-]	.	.	HGNC:31526	.	.	ENSG00000272036	MI0000261	.	.	.	.
Mol01377	Precursor miRNA	hsa-mir-147	microRNA 147a	MIR147A	406939	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385079.1, MIR147A-201, 72"	AAUCUAAAGACAACAUUUCUGCACACACACCAGACUAUGGAAGCCAGUGUGUGGAAAUGCUUCUGCUAGAUU	chr9:120244979-120245050[-]	.	.	HGNC:31534	.	.	ENSG00000207814	MI0000262	.	.	.	.
Mol01378	Precursor miRNA	hsa-mir-7	microRNA 7-1	MIR7-1	407043	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384871.1, MIR7-1-201, 110"	UUGGAUGUUGGCCUAGUUCUGUGUGGAAGACUAGUGAUUUUGUUGUUUUUAGAUAACUAAAUCGACAACAAAUCACAGUCUGCCAUAUGGCACAGGCCAUGCCUCUACAG	chr9:83969748-83969857[-]	.	.	HGNC:31638	.	.	ENSG00000284179	MI0000263	.	.	.	.
Mol01379	Precursor miRNA	hsa-mir-10a	microRNA 10a	MIR10A	406902	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385043.1, MIR10A-201, 110"	GAUCUGUCUGUCUUCUGUAUAUACCCUGUAGAUCCGAAUUUGUGUAAGGAAUUUUGUGGUCACAAAUUCGUAUCUAGGGGAAUAUGUAGUUGACAUAAACACUCCGCUCU	chr17:48579838-48579947[-]	.	.	HGNC:31497	.	.	ENSG00000284038	MI0000266	.	.	.	.
Mol01380	Precursor miRNA	hsa-mir-10b	microRNA 10b	MIR10B	406903	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385011.1, MIR10B-201, 110"	CCAGAGGUUGUAACGUUGUCUAUAUAUACCCUGUAGAACCGAAUUUGUGUGGUAUCCGUAUAGUCACAGAUUCGAUUCUAGGGGAAUAUAUGGUCGAUGCAAAAACUUCA	chr2:176150303-176150412[+]	.	.	HGNC:31498	.	.	ENSG00000207744	MI0000267	.	.	.	.
Mol01381	Precursor miRNA	hsa-mir-34	microRNA 34a	MIR34A	407040	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385130.1, MIR34A-201, 110"	GGCCAGCUGUGAGUGUUUCUUUGGCAGUGUCUUAGCUGGUUGUUGUGAGCAAUAGUAAGGAAGCAAUCAGCAAGUAUACUGCCCUAGAAGUGCUGCACGUUGUGGGGCCC	chr1:9151668-9151777[-]	.	.	HGNC:31635	.	.	ENSG00000284357	MI0000268	.	.	.	.
Mol01382	Precursor miRNA	hsa-mir-34a	microRNA 34a	MIR34A	407040	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385130.1, MIR34A-201, 110"	GGCCAGCUGUGAGUGUUUCUUUGGCAGUGUCUUAGCUGGUUGUUGUGAGCAAUAGUAAGGAAGCAAUCAGCAAGUAUACUGCCCUAGAAGUGCUGCACGUUGUGGGGCCC	chr1:9151668-9151777[-]	.	.	HGNC:31635	.	.	ENSG00000284357	MI0000268	.	.	.	.
Mol01383	Precursor miRNA	hsa-mir-181a	microRNA 181a-2	MIR181A2	406954	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384863.1, MIR181A2-201, 110"	AGAAGGGCUAUCAGGCCAGCCUUCAGAGGACUCCAAGGAACAUUCAACGCUGUCGGUGAGUUUGGGAUUUGAAAAAACCACUGACCGUUGACUGUACCUUGGGGUCCUUA	chr9:124692442-124692551[+]	.	.	HGNC:31549	.	.	ENSG00000207595	MI0000269	.	.	.	.
Mol01384	Precursor miRNA	hsa-mir-181	microRNA 181b-1	MIR181B1	406955	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385240.1, MIR181B1-201, 110"	CCUGUGCAGAGAUUAUUUUUUAAAAGGUCACAAUCAACAUUCAUUGCUGUCGGUGGGUUGAACUGUGUGGACAAGCUCACUGAACAAUGAAUGCAACUGUGGCCCCGCUU	chr1:198858873-198858982[-]	.	.	HGNC:31550	.	.	ENSG00000207975	MI0000270	.	.	.	.
Mol01385	Precursor miRNA	hsa-mir-181b-1	microRNA 181b-1	MIR181B1	406955	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385240.1, MIR181B1-201, 110"	CCUGUGCAGAGAUUAUUUUUUAAAAGGUCACAAUCAACAUUCAUUGCUGUCGGUGGGUUGAACUGUGUGGACAAGCUCACUGAACAAUGAAUGCAACUGUGGCCCCGCUU	chr1:198858873-198858982[-]	.	.	HGNC:31550	.	.	ENSG00000207975	MI0000270	.	.	.	.
Mol01386	Precursor miRNA	hsa-mir-181c	microRNA 181c	MIR181C	406957	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384881.1, MIR181C-201, 110"	CGGAAAAUUUGCCAAGGGUUUGGGGGAACAUUCAACCUGUCGGUGAGUUUGGGCAGCUCAGGCAAACCAUCGACCGUUGAGUGGACCCUGAGGCCUGGAAUUGCCAUCCU	chr19:13874699-13874808[+]	.	.	HGNC:31552	.	.	ENSG00000207613	MI0000271	.	.	.	.
Mol01387	Precursor miRNA	hsa-mir-182	microRNA 182	MIR182	406958	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385255.3, MIR182-201, 110"	GAGCUGCUUGCCUCCCCCCGUUUUUGGCAAUGGUAGAACUCACACUGGUGAGGUAACAGGAUCCGGUGGUUCUAGACUUGCCAACUAUGGGGCGAGGACUCAGCCGGCAC	chr7:129770383-129770492[-]	.	.	HGNC:31553	.	.	ENSG00000207990	MI0000272	.	.	.	.
Mol01388	Precursor miRNA	hsa-mir-183	microRNA 183	MIR183	406959	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384958.1, MIR183-201, 110"	CCGCAGAGUGUGACUCCUGUUCUGUGUAUGGCACUGGUAGAAUUCACUGUGAACAGUCUCAGUCAGUGAAUUACCGAAGGGCCAUAAACAGAGCAGAGACAGAUCCACGA	chr7:129774905-129775014[-]	.	.	HGNC:31554	.	.	ENSG00000207691	MI0000273	.	.	.	.
Mol01389	Precursor miRNA	hsa-mir-187	microRNA 187	MIR187	406963	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385062.1, MIR187-201, 109"	GGUCGGGCUCACCAUGACACAGUGUGAGACCUCGGGCUACAACACAGGACCCGGGCGCUGCUCUGACCCCUCGUGUCUUGUGUUGCAGCCGGAGGGACGCAGGUCCGCA	chr18:35904818-35904926[-]	.	.	HGNC:31558	.	.	ENSG00000207797	MI0000274	.	.	.	.
Mol01390	Precursor miRNA	hsa-mir-199b	microRNA 199b	MIR199B	406978	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384849.1, MIR199B-201, 110"	CCAGAGGACACCUCCACUCCGUCUACCCAGUGUUUAGACUAUCUGUUCAGGACUCCCAAAUUGUACAGUAGUCUGCACAUUGGUUAGGCUGGGCUGGGUUAGACCCUCGG	chr9:128244721-128244830[-]	.	.	HGNC:31573	.	.	ENSG00000207581	MI0000282	.	.	.	.
Mol01391	Precursor miRNA	hsa-mir-203	microRNA 203a	MIR203A	406986	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384836.1, MIR203A-201, 110"	GUGUUGGGGACUCGCGCGCUGGGUCCAGUGGUUCUUAACAGUUCAACAGUUCUGUAGCGCAAUUGUGAAAUGUUUAGGACCACUAGACCCGGCGGGCGCGGCGACAGCGA	chr14:104117405-104117514[+]	.	.	HGNC:31581	.	.	ENSG00000207568	MI0000283	.	.	.	.
Mol01392	Precursor miRNA	hsa-mir-204	microRNA 204	MIR204	406987	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385200.3, MIR204-201, 110"	GGCUACAGUCUUUCUUCAUGUGACUCGUGGACUUCCCUUUGUCAUCCUAUGCCUGAGAAUAUAUGAAGGAGGCUGGGAAGGCAAAGGGACGUUCAAUUGUCAUCACUGGC	chr9:70809975-70810084[-]	.	.	HGNC:31582	.	.	ENSG00000207935	MI0000284	.	.	.	.
Mol01393	Precursor miRNA	hsa-mir-205	microRNA 205	MIR205	406988	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384891.1, MIR205-201, 110"	AAAGAUCCUCAGACAAUCCAUGUGCUUCUCUUGUCCUUCAUUCCACCGGAGUCUGUCUCAUACCCAACCAGAUUUCAGUGGAGUGAAGUUCAGGAGGCAUGGAGCUGACA	chr1:209432133-209432242[+]	.	.	HGNC:31583	.	.	ENSG00000284485	MI0000285	.	.	.	.
Mol01394	Precursor miRNA	hsa-mir-210	microRNA 210	MIR210	406992	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362168.1, MIR210-201, 110"	ACCCGGCAGUGCCUCCAGGCGCAGGGCAGCCCCUGCCCACCGCACACUGCGCUGCCCCAGACCCACUGUGCGUGUGACAGCGGCUGAUCUGUGCCUGGGCAGCGCGACCC	chr11:568089-568198[-]	.	.	HGNC:31587	.	.	ENSG00000199038	MI0000286	.	.	.	.
Mol01395	Precursor miRNA	hsa-mir-211	microRNA 211	MIR211	406993	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384969.1, MIR211-201, 110"	UCACCUGGCCAUGUGACUUGUGGGCUUCCCUUUGUCAUCCUUCGCCUAGGGCUCUGAGCAGGGCAGGGACAGCAAAGGGGUGCUCAGUUGUCACUUCCCACAGCACGGAG	chr15:31065032-31065141[-]	.	.	HGNC:31588	.	.	ENSG00000207702	MI0000287	.	.	.	.
Mol01396	Precursor miRNA	hsa-mir-212	microRNA 212	MIR212	406994	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000586026.1, MIR212-201, 110"	CGGGGCACCCCGCCCGGACAGCGCGCCGGCACCUUGGCUCUAGACUGCUUACUGCCCGGGCCGCCCUCAGUAACAGUCUCCAGUCACGGCCACCGACGCCUGGCCCCGCC	chr17:2050271-2050380[-]	.	.	HGNC:31589	.	.	ENSG00000267195	MI0000288	.	.	.	.
Mol01397	Precursor miRNA	hsa-mir-214	microRNA 214	MIR214	406996	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385214.1, MIR214-201, 110"	GGCCUGGCUGGACAGAGUUGUCAUGUGUCUGCCUGUCUACACUUGCUGUGCAGAACAUCCGCUCACCUGUACAGCAGGCACAGACAGGCAGUCACAUGACAACCCAGCCU	chr1:172138798-172138907[-]	.	.	HGNC:31591	.	.	ENSG00000283844	MI0000290	.	.	.	.
Mol01398	Precursor miRNA	hsa-mir-215	microRNA 215	MIR215	406997	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384858.1, MIR215-201, 110"	AUCAUUCAGAAAUGGUAUACAGGAAAAUGACCUAUGAAUUGACAGACAAUAUAGCUGAGUUUGUCUGUCAUUUCUUUAGGCCAAUAUUCUGUAUGACUGUGCUACUUCAA	chr1:220117853-220117962[-]	.	.	HGNC:31592	.	.	ENSG00000207590	MI0000291	.	.	.	.
Mol01399	Precursor miRNA	hsa-mir-216a	microRNA 216a	MIR216A	406998	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385063.1, MIR216A-201, 110"	GAUGGCUGUGAGUUGGCUUAAUCUCAGCUGGCAACUGUGAGAUGUUCAUACAAUCCCUCACAGUGGUCUCUGGGAUUAUGCUAAACAGAGCAAUUUCCUAGCCCUCACGA	chr2:55988950-55989059[-]	.	.	HGNC:31593	.	.	ENSG00000207798	MI0000292	.	.	.	.
Mol01400	Precursor miRNA	hsa-mir-217	microRNA 217	MIR217	406999	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384817.3, MIR217-201, 110"	AGUAUAAUUAUUACAUAGUUUUUGAUGUCGCAGAUACUGCAUCAGGAACUGAUUGGAUAAGAAUCAGUCACCAUCAGUUCCUAAUGCAUUGCCUUCAGCAUCUAAACAAG	chr2:55982967-55983076[-]	.	.	HGNC:31594	.	.	ENSG00000207548	MI0000293	.	.	.	.
Mol01401	Precursor miRNA	hsa-mir-218	microRNA 218-1	MIR218-1	407000	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384999.1, MIR218-1-201, 110"	GUGAUAAUGUAGCGAGAUUUUCUGUUGUGCUUGAUCUAACCAUGUGGUUGCGAGGUAUGAGUAAAACAUGGUUCCGUCAAGCACCAUGGAACGUCACGCAGCUUUCUACA	chr4:20528275-20528384[+]	.	.	HGNC:31595	.	.	ENSG00000207732	MI0000294	.	.	.	.
Mol01402	Precursor miRNA	hsa-mir-218-2	microRNA 218-2	MIR218-2	407001	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385006.1, MIR218-2-201, 110"	GACCAGUCGCUGCGGGGCUUUCCUUUGUGCUUGAUCUAACCAUGUGGUGGAACGAUGGAAACGGAACAUGGUUCUGUCAAGCACCGCGGAAAGCACCGUGCUCUCCUGCA	chr5:168768146-168768255[-]	.	.	HGNC:31596	.	.	ENSG00000207739	MI0000295	.	.	.	.
Mol01403	Precursor miRNA	hsa-mir-221	microRNA 221	MIR221	407006	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385135.1, MIR221-201, 110"	UGAACAUCCAGGUCUGGGGCAUGAACCUGGCAUACAAUGUAGAUUUCUGUGUUCGUUAGGCAACAGCUACAUUGUCUGCUGGGUUUCAGGCUACCUGGAAACAUGUUCUC	chrX:45746157-45746266[-]	.	.	HGNC:31601	.	.	ENSG00000207870	MI0000298	.	.	.	.
Mol01404	Precursor miRNA	hsa-mir-222	microRNA 222	MIR222	407007	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384992.3, MIR222-201, 110"	GCUGCUGGAAGGUGUAGGUACCCUCAAUGGCUCAGUAGCCAGUGUAGAUCCUGUCUUUCGUAAUCAGCAGCUACAUCUGGCUACUGGGUCUCUGAUGGCAUCUUCUAGCU	chrX:45747015-45747124[-]	.	.	HGNC:31602	.	.	ENSG00000207725	MI0000299	.	.	.	.
Mol01405	Precursor miRNA	hsa-mir-223	microRNA 223	MIR223	407008	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385204.1, MIR223-201, 110"	CCUGGCCUCCUGCAGUGCCACGCUCCGUGUAUUUGACAAGCUGAGUUGGACACUCCAUGUGGUAGAGUGUCAGUUUGUCAAAUACCCCAAGUGCGGCACAUGCUUACCAG	chrX:66018870-66018979[+]	.	.	HGNC:31603	.	.	ENSG00000284567	MI0000300	.	.	.	.
Mol01406	Precursor miRNA	hsa-mir-224	microRNA 224	MIR224	407009	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384889.1, MIR224-201, 81"	GGGCUUUCAAGUCACUAGUGGUUCCGUUUAGUAGAUGAUUGUGCAUUGUUUCAAAAUGGUGCCCUAGUGACUACAAAGCCC	chrX:151958578-151958658[-]	.	.	HGNC:31604	.	.	ENSG00000284363	MI0000301	.	.	.	.
Mol01407	Precursor miRNA	hsa-mir-200b	microRNA 200b	MIR200B	406984	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384997.3, MIR200B-201, 95"	CCAGCUCGGGCAGCCGUGGCCAUCUUACUGGGCAGCAUUGGAUGGAGUCAGGUCUCUAAUACUGCCUGGUAAUGAUGACGGCGGAGCCCUGCACG	chr1:1167104-1167198[+]	.	.	HGNC:31579	.	.	ENSG00000207730	MI0000342	.	.	.	.
Mol01408	Precursor miRNA	hsa-let-7g	microRNA let-7g	MIRLET7G	406890	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362280.3, MIRLET7G-201, 84"	AGGCUGAGGUAGUAGUUUGUACAGUUUGAGGGUCUAUGAUACCACCCGGUACAGGAGAUAACUGUACAGGCCACUGCCUUGCCA	chr3:52268278-52268361[-]	.	.	HGNC:31485	.	.	ENSG00000199150	MI0000433	.	.	.	.
Mol01409	Precursor miRNA	hsa-let-7i	microRNA let-7i	MIRLET7I	406891	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362309.3, MIRLET7I-201, 84"	CUGGCUGAGGUAGUAGUUUGUGCUGUUGGUCGGGUUGUGACAUUGCCCGCUGUGGAGAUAACUGCGCAAGCUACUGCCUUGCUA	chr12:62603686-62603769[+]	.	.	HGNC:31486	.	.	ENSG00000199179	MI0000434	.	.	.	.
Mol01410	Precursor miRNA	hsa-mir-15b	microRNA 15b	MIR15B	406949	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385045.1, MIR15B-201, 98"	UUGAGGCCUUAAAGUACUGUAGCAGCACAUCAUGGUUUACAUGCUACAGUCAAGAUGCGAAUCAUUAUUUGCUGCUCUAGAAAUUUAAGGAAAUUCAU	chr3:160404588-160404685[+]	.	.	HGNC:31544	.	.	ENSG00000207779	MI0000438	.	.	.	.
Mol01411	Precursor miRNA	hsa-mir-23b	microRNA 23b	MIR23B	407011	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384832.1, MIR23B-201, 97"	CUCAGGUGCUCUGGCUGCUUGGGUUCCUGGCAUGCUGAUUUGUGACUUAAGAUUAAAAUCACAUUGCCAGGGAUUACCACGCAACCACGACCUUGGC	chr9:95085208-95085304[+]	.	.	HGNC:31606	.	.	ENSG00000207563	MI0000439	.	.	.	.
Mol01412	Precursor miRNA	hsa-mir-27b	microRNA 27b	MIR27B	407019	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385129.3, MIR27B-201, 97"	ACCUCUCUAACAAGGUGCAGAGCUUAGCUGAUUGGUGAACAGUGAUUGGUUUCCGCUUUGUUCACAGUGGCUAAGUUCUGCACCUGAAGAGAAGGUG	chr9:95085445-95085541[+]	.	.	HGNC:31614	.	.	ENSG00000207864	MI0000440	.	.	.	.
Mol01413	Precursor miRNA	hsa-mir-30b	microRNA 30b	MIR30B	407030	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384850.1, MIR30B-201, 88"	ACCAAGUUUCAGUUCAUGUAAACAUCCUACACUCAGCUGUAAUACAUGGAUUGGCUGGGAGGUGGAUGUUUACUUCAGCUGACUUGGA	chr8:134800520-134800607[-]	.	.	HGNC:31625	.	.	ENSG00000207582	MI0000441	.	.	.	.
Mol01414	Precursor miRNA	hsa-mir-122	microRNA 122	MIR122	406906	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385044.3, MIR122-201, 85"	CCUUAGCAGAGCUGUGGAGUGUGACAAUGGUGUUUGUGUCUAAACUAUCAAACGCCAUUAUCACACUAAAUAGCUACUGCUAGGC	chr18:58451074-58451158[+]	.	.	HGNC:31501	.	.	ENSG00000284440	MI0000442	.	.	.	.
Mol01415	Precursor miRNA	hsa-mir-124	microRNA 124-1	MIR124-1	406907	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385275.1, MIR124-1-201, 85"	AGGCCUCUCUCUCCGUGUUCACAGCGGACCUUGAUUUAAAUGUCCAUACAAUUAAGGCACGCGGUGAAUGCCAAGAAUGGGGCUG	chr8:9903388-9903472[-]	.	.	HGNC:31502	.	.	ENSG00000284321	MI0000443	.	.	.	.
Mol01416	Precursor miRNA	hsa-mir-125b	microRNA 125b-1	MIR125B1	406911	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385236.1, MIR125B1-201, 88"	UGCGCUCCUCUCAGUCCCUGAGACCCUAACUUGUGAUGUUUACCGUUUAAAUCCACGGGUUAGGCUCUUGGGAGCUGCGAGUCGUGCU	chr11:122099757-122099844[-]	.	.	HGNC:31506	.	.	ENSG00000207971	MI0000446	.	.	.	.
Mol01417	Precursor miRNA	hsa-mir-125b-1	microRNA 125b-1	MIR125B1	406911	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385236.1, MIR125B1-201, 88"	UGCGCUCCUCUCAGUCCCUGAGACCCUAACUUGUGAUGUUUACCGUUUAAAUCCACGGGUUAGGCUCUUGGGAGCUGCGAGUCGUGCU	chr11:122099757-122099844[-]	.	.	HGNC:31506	.	.	ENSG00000207971	MI0000446	.	.	.	.
Mol01418	Precursor miRNA	hsa-mir-128a	microRNA 128-1	MIR128-1	406915	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384921.4, MIR128-1-201, 82"	UGAGCUGUUGGAUUCGGGGCCGUAGCACUGUCUGAGAGGUUUACAUUUCUCACAGUGAACCGGUCUCUUUUUCAGCUGCUUC	chr2:135665397-135665478[+]	.	.	HGNC:31510	.	.	ENSG00000207654	MI0000447	.	.	.	.
Mol01419	Precursor miRNA	hsa-mir-130a	microRNA 130a	MIR130A	406919	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385274.1, MIR130A-201, 89"	UGCUGCUGGCCAGAGCUCUUUUCACAUUGUGCUACUGUCUGCACCUGUCACUAGCAGUGCAAUGUUAAAAGGGCAUUGGCCGUGUAGUG	chr11:57641198-57641286[+]	.	.	HGNC:31514	.	.	ENSG00000208009	MI0000448	.	.	.	.
Mol01420	Precursor miRNA	hsa-mir-132	microRNA 132	MIR132	406921	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000591554.1, MIR132-201, 101"	CCGCCCCCGCGUCUCCAGGGCAACCGUGGCUUUCGAUUGUUACUGUGGGAACUGGAGGUAACAGUCUACAGCCAUGGUCGCCCCGCAGCACGCCCACGCGC	chr17:2049908-2050008[-]	.	.	HGNC:31516	.	.	ENSG00000267200	MI0000449	.	.	.	.
Mol01421	Precursor miRNA	hsa-mir-133a	microRNA 133a-1	MIR133A1	406922	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385052.1, MIR133A1-201, 88"	ACAAUGCUUUGCUAGAGCUGGUAAAAUGGAACCAAAUCGCCUCUUCAAUGGAUUUGGUCCCCUUCAACCAGCUGUAGCUAUGCAUUGA	chr18:21825698-21825785[-]	.	.	HGNC:31517	.	.	ENSG00000283927	MI0000450	.	.	.	.
Mol01422	Precursor miRNA	hsa-mir-135a	microRNA 135a-1	MIR135A1	406925	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385191.1, MIR135A1-201, 90"	AGGCCUCGCUGUUCUCUAUGGCUUUUUAUUCCUAUGUGAUUCUACUGCUCACUCAUAUAGGGAUUGGAGCCGUGGCGCACGGCGGGGACA	chr3:52294219-52294308[-]	.	.	HGNC:31520	.	.	ENSG00000207926	MI0000452	.	.	.	.
Mol01423	Precursor miRNA	hsa-mir-135a-1	microRNA 135a-1	MIR135A1	406925	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385191.1, MIR135A1-201, 90"	AGGCCUCGCUGUUCUCUAUGGCUUUUUAUUCCUAUGUGAUUCUACUGCUCACUCAUAUAGGGAUUGGAGCCGUGGCGCACGGCGGGGACA	chr3:52294219-52294308[-]	.	.	HGNC:31520	.	.	ENSG00000207926	MI0000452	.	.	.	.
Mol01424	Precursor miRNA	hsa-mir-137	microRNA 137	MIR137	406928	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385223.1, MIR137-201, 102"	GGUCCUCUGACUCUCUUCGGUGACGGGUAUUCUUGGGUGGAUAAUACGGAUUACGUUGUUAUUGCUUAAGAAUACGCGUAGUCGAGGAGAGUACCAGCGGCA	chr1:98046070-98046171[-]	.	.	HGNC:31523	.	.	ENSG00000284202	MI0000454	.	.	.	.
Mol01425	Precursor miRNA	hsa-mir-138	microRNA 138-2	MIR138-2	406930	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384916.3, MIR138-2-201, 84"	CGUUGCUGCAGCUGGUGUUGUGAAUCAGGCCGACGAGCAGCGCAUCCUCUUACCCGGCUAUUUCACGACACCAGGGUUGCAUCA	chr16:56858518-56858601[+]	.	.	HGNC:31525	.	.	ENSG00000207649	MI0000455	.	.	.	.
Mol01426	Precursor miRNA	hsa-mir-138-2	microRNA 138-2	MIR138-2	406930	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384916.3, MIR138-2-201, 84"	CGUUGCUGCAGCUGGUGUUGUGAAUCAGGCCGACGAGCAGCGCAUCCUCUUACCCGGCUAUUUCACGACACCAGGGUUGCAUCA	chr16:56858518-56858601[+]	.	.	HGNC:31525	.	.	ENSG00000207649	MI0000455	.	.	.	.
Mol01427	Precursor miRNA	hsa-mir-140	microRNA 140	MIR140	406932	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385282.3, MIR140-201, 100"	UGUGUCUCUCUCUGUGUCCUGCCAGUGGUUUUACCCUAUGGUAGGUUACGUCAUGCUGUUCUACCACAGGGUAGAACCACGGACAGGAUACCGGGGCACC	chr16:69933081-69933180[+]	.	.	HGNC:31527	.	.	ENSG00000208017	MI0000456	.	.	.	.
Mol01428	Precursor miRNA	hsa-mir-141	microRNA 141	MIR141	406933	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384975.1, MIR141-201, 95"	CGGCCGGCCCUGGGUCCAUCUUCCAGUACAGUGUUGGAUGGUCUAAUUGUGAAGCUCCUAACACUGUCUGGUAAAGAUGGCUCCCGGGUGGGUUC	chr12:6964097-6964191[+]	.	.	HGNC:31528	.	.	ENSG00000207708	MI0000457	.	.	.	.
Mol01429	Precursor miRNA	hsa-mir-143	microRNA 143	MIR143	406935	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385300.1, MIR143-201, 106"	GCGCAGCGCCCUGUCUCCCAGCCUGAGGUGCAGUGCUGCAUCUCUGGUCAGUUGGGAGUCUGAGAUGAAGCACUGUAGCUCAGGAAGAGAGAAGUUGUUCUGCAGC	chr5:149428918-149429023[+]	.	.	HGNC:31530	.	.	ENSG00000284182	MI0000459	.	.	.	.
Mol01430	Precursor miRNA	hsa-mir-144	microRNA 144	MIR144	406936	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384886.3, MIR144-201, 86"	UGGGGCCCUGGCUGGGAUAUCAUCAUAUACUGUAAGUUUGCGAUGAGACACUACAGUAUAGAUGAUGUACUAGUCCGGGCACCCCC	chr17:28861533-28861618[-]	.	.	HGNC:31531	.	.	ENSG00000283819	MI0000460	.	.	.	.
Mol01431	Precursor miRNA	hsa-mir-145	microRNA 145	MIR145	406937	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384967.1, MIR145-201, 88"	CACCUUGUCCUCACGGUCCAGUUUUCCCAGGAAUCCCUUAGAUGCUAAGAUGGGGAUUCCUGGAAAUACUGUUCUUGAGGUCAUGGUU	chr5:149430646-149430733[+]	.	.	HGNC:31532	.	.	ENSG00000276365	MI0000461	.	.	.	.
Mol01432	Precursor miRNA	hsa-mir-152	microRNA 152	MIR152	406943	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385212.3, MIR152-201, 87"	UGUCCCCCCCGGCCCAGGUUCUGUGAUACACUCCGACUCGGGCUCUGGAGCAGUCAGUGCAUGACAGAACUUGGGCCCGGAAGGACC	chr17:48037161-48037247[-]	.	.	HGNC:31538	.	.	ENSG00000207947	MI0000462	.	.	.	.
Mol01433	Precursor miRNA	hsa-mir-153	microRNA 153-1	MIR153-1	406944	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384914.1, MIR153-1-201, 90"	CUCACAGCUGCCAGUGUCAUUUUUGUGAUCUGCAGCUAGUAUUCUCACUCCAGUUGCAUAGUCACAAAAGUGAUCAUUGGCAGGUGUGGC	chr2:219294111-219294200[-]	.	.	HGNC:31539	.	.	ENSG00000207647	MI0000463	.	.	.	.
Mol01434	Precursor miRNA	hsa-mir-9	microRNA 9-1	MIR9-1	407046	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385198.3, MIR9-1-201, 89"	CGGGGUUGGUUGUUAUCUUUGGUUAUCUAGCUGUAUGAGUGGUGUGGAGUCUUCAUAAAGCUAGAUAACCGAAAGUAAAAAUAACCCCA	chr1:156420341-156420429[-]	.	.	HGNC:31641	.	.	ENSG00000207933	MI0000466	.	.	.	.
Mol01435	Precursor miRNA	hsa-mir-125a	microRNA 125a	MIR125A	406910	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385273.1, MIR125A-201, 86"	UGCCAGUCUCUAGGUCCCUGAGACCCUUUAACCUGUGAGGACAUCCAGGGUCACAGGUGAGGUUCUUGGGAGCCUGGCGUCUGGCC	chr19:51693254-51693339[+]	.	.	HGNC:31505	.	.	ENSG00000208008	MI0000469	.	.	.	.
Mol01436	Precursor miRNA	hsa-mir-125b-2	microRNA 125b-2	MIR125B2	406912	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385128.1, MIR125B2-201, 89"	ACCAGACUUUUCCUAGUCCCUGAGACCCUAACUUGUGAGGUAUUUUAGUAACAUCACAAGUCAGGCUCUUGGGACCUAGGCGGAGGGGA	chr21:16590237-16590325[+]	.	.	HGNC:31507	.	.	ENSG00000207863	MI0000470	.	.	.	.
Mol01437	Precursor miRNA	hsa-mir-126	microRNA 126	MIR126	406913	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362291.1, MIR126-201, 85"	CGCUGGCGACGGGACAUUAUUACUUUUGGUACGCGCUGUGACACUUCAAACUCGUACCGUGAGUAAUAAUGCGCCGUCCACGGCA	chr9:136670602-136670686[+]	.	.	HGNC:31508	.	.	ENSG00000199161	MI0000471	.	.	.	.
Mol01438	Precursor miRNA	hsa-mir-127	microRNA 127	MIR127	406914	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384876.3, MIR127-201, 97"	UGUGAUCACUGUCUCCAGCCUGCUGAAGCUCAGAGGGCUCUGAUUCAGAAAGAUCAUCGGAUCCGUCUGAGCUUGGCUGGUCGGAAGUCUCAUCAUC	chr14:100882979-100883075[+]	.	.	HGNC:31509	.	.	ENSG00000207608	MI0000472	.	.	.	.
Mol01439	Precursor miRNA	hsa-mir-134	microRNA 134	MIR134	406924	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385258.3, MIR134-201, 73"	CAGGGUGUGUGACUGGUUGACCAGAGGGGCAUGCACUGUGUUCACCCUGUGGGCCACCUAGUCACCAACCCUC	chr14:101054687-101054759[+]	.	.	HGNC:31519	.	.	ENSG00000207993	MI0000474	.	.	.	.
Mol01440	Precursor miRNA	hsa-mir-136	microRNA 136	MIR136	406927	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385207.2, MIR136-201, 82"	UGAGCCCUCGGAGGACUCCAUUUGUUUUGAUGAUGGAUUCUUAUGCUCCAUCAUCGUCUCAAAUGAGUCUUCAGAGGGUUCU	chr14:100884702-100884783[+]	.	.	HGNC:31522	.	.	ENSG00000207942	MI0000475	.	.	.	.
Mol01441	Precursor miRNA	hsa-mir-146a	microRNA 146a	MIR146A	406938	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385201.1, MIR146A-201, 99"	CCGAUGUGUAUCCUCAGCUUUGAGAACUGAAUUCCAUGGGUUGUGUCAGUGUCAGACCUCUGAAAUUCAGUUCUUCAGCUGGGAUAUCUCUGUCAUCGU	chr5:160485352-160485450[+]	.	.	HGNC:31533	.	.	ENSG00000283733	MI0000477	.	.	.	.
Mol01442	Precursor miRNA	hsa-mir-149	microRNA 149	MIR149	406941	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384879.1, MIR149-201, 89"	GCCGGCGCCCGAGCUCUGGCUCCGUGUCUUCACUCCCGUGCUUGUCCGAGGAGGGAGGGAGGGACGGGGGCUGUGCUGGGGCAGCUGGA	chr2:240456001-240456089[+]	.	.	HGNC:31536	.	.	ENSG00000207611	MI0000478	.	.	.	.
Mol01443	Precursor miRNA	hsa-mir-150	microRNA 150	MIR150	406942	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385048.3, MIR150-201, 84"	CUCCCCAUGGCCCUGUCUCCCAACCCUUGUACCAGUGCUGGGCUCAGACCCUGGUACAGGCCUGGGGGACAGGGACCUGGGGAC	chr19:49500785-49500868[-]	.	.	HGNC:31537	.	.	ENSG00000207782	MI0000479	.	.	.	.
Mol01444	Precursor miRNA	hsa-mir-185	microRNA 185	MIR185	406961	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385288.3, MIR185-201, 82"	AGGGGGCGAGGGAUUGGAGAGAAAGGCAGUUCCUGAUGGUCCCCUCCCCAGGGGCUGGCUUUCCUCUGGUCCUUCCCUCCCA	chr22:20033139-20033220[+]	.	.	HGNC:31556	.	.	ENSG00000208023	MI0000482	.	.	.	.
Mol01445	Precursor miRNA	hsa-mir-186	microRNA 186	MIR186	406962	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384988.1, MIR186-201, 86"	UGCUUGUAACUUUCCAAAGAAUUCUCCUUUUGGGCUUUCUGGUUUUAUUUUAAGCCCAAAGGUGAAUUUUUUGGGAAGUUUGAGCU	chr1:71067631-71067716[-]	.	.	HGNC:31557	.	.	ENSG00000207721	MI0000483	.	.	.	.
Mol01446	Precursor miRNA	hsa-mir-193a	microRNA 193a	MIR193A	406968	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384882.1, MIR193A-201, 88"	CGAGGAUGGGAGCUGAGGGCUGGGUCUUUGCGGGCGAGAUGAGGGUGUCGGAUCAACUGGCCUACAAAGUCCCAGUUCUCGGCCCCCG	chr17:31559996-31560083[+]	.	.	HGNC:31563	.	.	ENSG00000207614	MI0000487	.	.	.	.
Mol01447	Precursor miRNA	hsa-mir-194	microRNA 194-1	MIR194-1	406969	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384892.1, MIR194-1-201, 85"	AUGGUGUUAUCAAGUGUAACAGCAACUCCAUGUGGACUGUGUACCAAUUUCCAGUGGAGAUGCUGUUACUUUUGAUGGUUACCAA	chr1:220118157-220118241[-]	.	.	HGNC:31564	.	.	ENSG00000207624	MI0000488	.	.	.	.
Mol01448	Precursor miRNA	hsa-mir-195	microRNA 195	MIR195	406971	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385194.1, MIR195-201, 87"	AGCUUCCCUGGCUCUAGCAGCACAGAAAUAUUGGCACAGGGAAGCGAGUCUGCCAAUAUUGGCUGUGCUGCUCCAGGCAGGGUGGUG	chr17:7017615-7017701[-]	.	.	HGNC:31566	.	.	ENSG00000284112	MI0000489	.	.	.	.
Mol01449	Precursor miRNA	hsa-mir-320	microRNA 320a	MIR320A	407037	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385302.1, MIR320A-201, 82"	CUCCCCUCCGCCUUCUCUUCCCGGUUCUUCCCGGAGUCGGGAAAAGCUGGGUUGAGAGGGCGAAAAAGGAUG	chr8:22244962-22245043[-]	.	.	HGNC:31632	.	.	ENSG00000208037	MI0000542	.	.	.	.
Mol01450	Precursor miRNA	hsa-mir-320a	microRNA 320a	MIR320A	407037	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385302.1, MIR320A-201, 82"	CUCCCCUCCGCCUUCUCUUCCCGGUUCUUCCCGGAGUCGGGAAAAGCUGGGUUGAGAGGGCGAAAAAGGAUG	chr8:22244962-22245043[-]	.	.	HGNC:31632	.	.	ENSG00000208037	MI0000542	.	.	.	.
Mol01451	Precursor miRNA	hsa-mir-200c	microRNA 200c	MIR200C	406985	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384980.3, MIR200C-201, 68"	CCCUCGUCUUACCCAGCAGUGUUUGGGUGCGGUUGGGAGUCUCUAAUACUGCCGGGUAAUGAUGGAGG	chr12:6963699-6963766[+]	.	.	HGNC:31580	.	.	ENSG00000207713	MI0000650	.	.	.	.
Mol01452	Precursor miRNA	hsa-mir-1	microRNA 1-1	MIR1-1	406904	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362147.2, MIR1-1-201, 71"	UGGGAAACAUACUUCUUUAUAUGCCCAUAUGGACCUGCUAAGCUAUGGAAUGUAAAGAAGUAUGUAUCUCA	chr20:62554306-62554376[+]	.	.	HGNC:31499	.	.	ENSG00000199017	MI0000651	.	.	.	.
Mol01453	Precursor miRNA	hsa-mir-155	microRNA 155	MIR155	406947	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385060.1, MIR155-201, 65"	CUGUUAAUGCUAAUCGUGAUAGGGGUUUUUGCCUCCAACUGACUCCUACAUAUUAGCAUUAACAG	chr21:25573980-25574044[+]	.	.	HGNC:31542	.	.	ENSG00000283904	MI0000681	.	.	.	.
Mol01454	Precursor miRNA	hsa-mir-128	microRNA 128-2	MIR128-2	406916	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384893.1, MIR128-2-201, 84"	UGAGCUGUUGGAUUCGGGGCCGUAGCACUGUCUGAGAGGUUUACAUUUCUCACAGUGAACCGGUCUCUUUUUCAGCUGCUUC	chr3:35744476-35744559[+]	.	.	HGNC:31511	.	.	ENSG00000207625	MI0000727	.	.	.	.
Mol01455	Precursor miRNA	hsa-mir-128-2	microRNA 128-2	MIR128-2	406916	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384893.1, MIR128-2-201, 84"	UGUGCAGUGGGAAGGGGGGCCGAUACACUGUACGAGAGUGAGUAGCAGGUCUCACAGUGAACCGGUCUCUUUCCCUACUGUGUC	chr3:35744476-35744559[+]	.	.	HGNC:31511	.	.	ENSG00000207625	MI0000727	.	.	.	.
Mol01456	Precursor miRNA	hsa-mir-29c	microRNA 29c	MIR29C	407026	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385231.3, MIR29C-201, 88"	AUCUCUUACACAGGCUGACCGAUUUCUCCUGGUGUUCAGAGUCUGUUUUUGUCUAGCACCAUUUGAAAUCGGUUAUGAUGUAGGGGGA	chr1:207801852-207801939[-]	.	.	HGNC:31621	.	.	ENSG00000284214	MI0000735	.	.	.	.
Mol01457	Precursor miRNA	hsa-mir-200a	microRNA 200a	MIR200A	406983	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384875.3, MIR200A-201, 90"	CCGGGCCCCUGUGAGCAUCUUACCGGACAGUGCUGGAUUUCCCAGCUUGACUCUAACACUGUCUGGUAACGAUGUUCAAAGGUGACCCGC	chr1:1167863-1167952[+]	.	.	HGNC:31578	.	.	ENSG00000207607	MI0000737	.	.	.	.
Mol01458	Precursor miRNA	hsa-mir-302a	microRNA 302a	MIR302A	407028	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385192.1, MIR302A-201, 69"	CCACCACUUAAACGUGGAUGUACUUGCUUUGAAACUAAAGAAGUAAGUGCUUCCAUGUUUUGGUGAUGG	chr4:112648183-112648251[-]	.	.	HGNC:31623	.	.	ENSG00000207927	MI0000738	.	.	.	.
Mol01459	Precursor miRNA	hsa-mir-34c	microRNA 34c	MIR34C	407042	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384831.3, MIR34C-201, 77"	AGUCUAGUUACUAGGCAGUGUAGUUAGCUGAUUGCUAAUAGUACCAAUCACUAACCACACGGCCAGGUAAAAAGAUU	chr11:111513439-111513515[+]	.	.	HGNC:31637	.	.	ENSG00000207562	MI0000743	.	.	.	.
Mol01460	Precursor miRNA	hsa-mir-301	microRNA 301a	MIR301A	407027	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385261.1, MIR301A-201, 86"	ACUGCUAACGAAUGCUCUGACUUUAUUGCACUACUGUACUUUACAGCUAGCAGUGCAAUAGUAUUGUCAAAGCAUCUGAAAGCAGG	chr17:59151136-59151221[-]	.	.	HGNC:31622	.	.	ENSG00000207996	MI0000745	.	.	.	.
Mol01461	Precursor miRNA	hsa-mir-301a	microRNA 301a	MIR301A	407027	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385261.1, MIR301A-201, 86"	ACUGCUAACGAAUGCUCUGACUUUAUUGCACUACUGUACUUUACAGCUAGCAGUGCAAUAGUAUUGUCAAAGCAUCUGAAAGCAGG	chr17:59151136-59151221[-]	.	.	HGNC:31622	.	.	ENSG00000207996	MI0000745	.	.	.	.
Mol01462	Precursor miRNA	hsa-mir-296	microRNA 296	MIR296	407022	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385215.1, MIR296-201, 80"	AGGACCCUUCCAGAGGGCCCCCCCUCAAUCCUGUUGUGCCUAAUUCAGAGGGUUGGGUGGAGGCUCUCCUGAAGGGCUCU	chr20:58817615-58817694[-]	.	.	HGNC:31617	.	.	ENSG00000284040	MI0000747	.	.	.	.
Mol01463	Precursor miRNA	hsa-mir-130b	microRNA 130b	MIR130B	406920	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385018.1, MIR130B-201, 82"	GGCCUGCCCGACACUCUUUCCCUGUUGCACUACUAUAGGCCGCUGGGAAGCAGUGCAAUGAUGAAAGGGCAUCGGUCAGGUC	chr22:21653304-21653385[+]	.	.	HGNC:31515	.	.	ENSG00000283871	MI0000748	.	.	.	.
Mol01464	Precursor miRNA	hsa-mir-30e	microRNA 30e	MIR30E	407034	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362104.3, MIR30E-201, 92"	GGGCAGUCUUUGCUACUGUAAACAUCCUUGACUGGAAGCUGUAAGGUGUUCAGAGGAGCUUUCAGUCGGAUGUUUACAGCGGCAGGCUGCCA	chr1:40754355-40754446[+]	.	.	HGNC:31629	.	.	ENSG00000198974	MI0000749	.	.	.	.
Mol01465	Precursor miRNA	hsa-mir-361	microRNA 361	MIR361	494323	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362181.3, MIR361-201, 72"	GGAGCUUAUCAGAAUCUCCAGGGGUACUUUAUAAUUUCAAAAAGUCCCCCAGGUGUGAUUCUGAUUUGCUUC	chrX:85903636-85903707[-]	.	.	HGNC:31867	.	.	ENSG00000199051	MI0000760	.	.	.	.
Mol01466	Precursor miRNA	hsa-mir-363	microRNA 363	MIR363	574031	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384840.3, MIR363-201, 75"	UGUUGUCGGGUGGAUCACGAUGCAAUUUUGAUGAGUAUCAUAGGAGAAAAAUUGCACGGUAUCCAUCUGUAAACC	chrX:134169378-134169452[-]	.	.	HGNC:32023	.	.	ENSG00000284499	MI0000764	.	.	.	.
Mol01467	Precursor miRNA	hsa-mir-365	microRNA 365a	MIR365A	100126355	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362260.3, MIR365A-201, 87"	ACCGCAGGGAAAAUGAGGGACUUUUGGGGGCAGAUGUGUUUCCAUUCCACUAUCAUAAUGCCCCUAAAAAUCCUUAUUGCUCUUGCA	chr16:14309285-14309371[+]	.	.	HGNC:33692	.	.	ENSG00000199130	MI0000767	.	.	.	.
Mol01468	Precursor miRNA	hsa-mir-302b	microRNA 302b	MIR302B	442894	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362188.1, MIR302B-201, 73"	GCUCCCUUCAACUUUAACAUGGAAGUGCUUUCUGUGACUUUAAAAGUAAGUGCUUCCAUGUUUUAGUAGGAGU	chr4:112648485-112648557[-]	.	.	HGNC:31763	.	.	ENSG00000284463	MI0000772	.	.	.	.
Mol01469	Precursor miRNA	hsa-mir-302c	microRNA 302c	MIR302C	442895	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362232.1, MIR302C-201, 68"	CCUUUGCUUUAACAUGGGGGUACCUGCUGUGUGAAACAAAAGUAAGUGCUUCCAUGUUUCAGUGGAGG	chr4:112648363-112648430[-]	.	.	HGNC:31764	.	.	ENSG00000199102	MI0000773	.	.	.	.
Mol01470	Precursor miRNA	hsa-mir-302d	microRNA 302d	MIR302D	442896	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362275.1, MIR302D-201, 68"	CCUCUACUUUAACAUGGAGGCACUUGCUGUGACAUGACAAAAAUAAGUGCUUCCAUGUUUGAGUGUGG	chr4:112648004-112648071[-]	.	.	HGNC:31765	.	.	ENSG00000199145	MI0000774	.	.	.	.
Mol01471	Precursor miRNA	hsa-mir-376c	microRNA 376c	MIR376C	442913	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000607441.3, MIR376C-201, 66"	AAAAGGUGGAUAUUCCUUCUAUGUUUAUGUUAUUUAUGGUUAAACAUAGAGGAAAUUCCACGUUUU	chr14:101039690-101039755[+]	.	.	HGNC:31782	.	.	ENSG00000283279	MI0000776	.	.	.	.
Mol01472	Precursor miRNA	hsa-mir-370	microRNA 370	MIR370	442915	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362135.4, MIR370-201, 75"	AGACAGAGAAGCCAGGUCACGUCUCUGCAGUUACACAGCUCACGAGUGCCUGCUGGGGUGGAACCUGGUCUGUCU	chr14:100911139-100911213[+]	.	.	HGNC:31784	.	.	ENSG00000199005	MI0000778	.	.	.	.
Mol01473	Precursor miRNA	hsa-mir-374a	microRNA 374a	MIR374A	442919	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362298.3, MIR374A-201, 72"	UACAUCGGCCAUUAUAAUACAACCUGAUAAGUGUUAUAGCACUUAUCAGAUUGUAUUGUAAUUGUCUGUGUA	chrX:74287286-74287357[-]	.	.	HGNC:31788	.	.	ENSG00000199168	MI0000782	.	.	.	.
Mol01474	Precursor miRNA	hsa-mir-375	microRNA 375	MIR375	494324	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362103.4, MIR375-201, 64"	CCCCGCGACGAGCCCCUCGCACAAACCGGACCUGAGCGUUUUGUUCGUUCGGCUCGCGUGAGGC	chr2:219001645-219001708[-]	.	.	HGNC:31868	.	.	ENSG00000198973	MI0000783	.	.	.	.
Mol01475	Precursor miRNA	hsa-mir-377	microRNA 377	MIR377	494326	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362145.4, MIR377-201, 69"	UUGAGCAGAGGUUGCCCUUGGUGAAUUCGCUUUAUUUAUGUUGAAUCACACAAAGGCAACUUUUGUUUG	chr14:101062050-101062118[+]	.	.	HGNC:31870	.	.	ENSG00000199015	MI0000785	.	.	.	.
Mol01476	Precursor miRNA	hsa-mir-378	microRNA 378a	MIR378A	494327	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362177.3, MIR378A-201, 66"	AGGGCUCCUGACUCCAGGUCCUGUGUGUUACCUAGAAAUAGCACUGGACUUGGAGUCAGAAGGCCU	chr5:149732825-149732890[+]	.	.	HGNC:31871	.	.	ENSG00000199047	MI0000786	.	.	.	.
Mol01477	Precursor miRNA	hsa-mir-378a	microRNA 378a	MIR378A	494327	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362177.3, MIR378A-201, 66"	AGGGCUCCUGACUCCAGGUCCUGUGUGUUACCUAGAAAUAGCACUGGACUUGGAGUCAGAAGGCCU	chr5:149732825-149732890[+]	.	.	HGNC:31871	.	.	ENSG00000199047	MI0000786	.	.	.	.
Mol01478	Precursor miRNA	hsa-mir-379	microRNA 379	MIR379	494328	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362218.5, MIR379-201, 67"	AGAGAUGGUAGACUAUGGAACGUAGGCGUUAUGAUUUCUGACCUAUGUAACAUGGUCCACUAACUCU	chr14:101022066-101022132[+]	.	.	HGNC:31872	.	.	ENSG00000199088	MI0000787	.	.	.	.
Mol01479	Precursor miRNA	hsa-mir-381	microRNA 381	MIR381	494330	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362150.3, MIR381-201, 75"	UACUUAAAGCGAGGUUGCCCUUUGUAUAUUCGGUUUAUUGACAUGGAAUAUACAAGGGCAAGCUCUCUGUGAGUA	chr14:101045920-101045994[+]	.	.	HGNC:31874	.	.	ENSG00000199020	MI0000789	.	.	.	.
Mol01480	Precursor miRNA	hsa-mir-382	microRNA 382	MIR382	494331	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000637119.1, MIR382-201, 76"	UACUUGAAGAGAAGUUGUUCGUGGUGGAUUCGCUUUACUUAUGACGAAUCAUUCACGGACAACACUUUUUUCAGUA	chr14:101054306-101054381[+]	.	.	HGNC:31875	.	.	ENSG00000283170	MI0000790	.	.	.	.
Mol01481	Precursor miRNA	hsa-mir-383	microRNA 383	MIR383	494332	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362257.1, MIR383-201, 73"	CUCCUCAGAUCAGAAGGUGAUUGUGGCUUUGGGUGGAUAUUAAUCAGCCACAGCACUGCCUGGUCAGAAAGAG	chr8:14853438-14853510[-]	.	.	HGNC:31876	.	.	ENSG00000199127	MI0000791	.	.	.	.
Mol01482	Precursor miRNA	hsa-mir-340	microRNA 340	MIR340	442908	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362125.3, MIR340-201, 95"	UUGUACCUGGUGUGAUUAUAAAGCAAUGAGACUGAUUGUCAUAUGUCGUUUGUGGGAUCCGUCUCAGUUACUUUAUAGCCAUACCUGGUAUCUUA	chr5:180015303-180015397[-]	.	.	HGNC:31777	.	.	ENSG00000198995	MI0000802	.	.	.	.
Mol01483	Precursor miRNA	hsa-mir-330	microRNA 330	MIR330	442902	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362196.1, MIR330-201, 94"	CUUUGGCGAUCACUGCCUCUCUGGGCCUGUGUCUUAGGCUCUGCAAGAUCAACCGAGCAAAGCACACGGCCUGCAGAGAGGCAGCGCUCUGCCC	chr19:45638994-45639087[-]	.	.	HGNC:31771	.	.	ENSG00000284544	MI0000803	.	.	.	.
Mol01484	Precursor miRNA	hsa-mir-328	microRNA 328	MIR328	442901	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385213.3, MIR328-201, 75"	UGGAGUGGGGGGGCAGGAGGGGCUCAGGGAGAAAGUGCAUACAGCCCCUGGCCCUCUCUGCCCUUCCGUCCCCUG	chr16:67202321-67202395[-]	.	.	HGNC:31770	.	.	ENSG00000207948	MI0000804	.	.	.	.
Mol01485	Precursor miRNA	hsa-mir-342	microRNA 342	MIR342	442909	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362212.1, MIR342-201, 99"	GAAACUGGGCUCAAGGUGAGGGGUGCUAUCUGUGAUUGAGGGACAUGGUUAAUGGAAUUGUCUCACACAGAAAUCGCACCCGUCACCUUGGCCUACUUA	chr14:100109655-100109753[+]	.	.	HGNC:31778	.	.	ENSG00000199082	MI0000805	.	.	.	.
Mol01486	Precursor miRNA	hsa-mir-323	microRNA 323a	MIR323A	442897	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362199.3, MIR323A-201, 86"	UUGGUACUUGGAGAGAGGUGGUCCGUGGCGCGUUCGCUUUAUUUAUGGCGCACAUUACACGGUCGACCUCUUUGCAGUAUCUAAUC	chr14:101025732-101025817[+]	.	.	HGNC:31766	.	.	ENSG00000199069	MI0000807	.	.	.	.
Mol01487	Precursor miRNA	hsa-mir-151a	microRNA 151a	MIR151A	442893	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000521276.3, MIR151A-201, 90"	UUUCCUGCCCUCGAGGAGCUCACAGUCUAGUAUGUCUCAUCCCCUACUAGACUGAAGCUCCUUGAGGACAGGGAUGGUCAUACUCACCUC	chr8:140732564-140732653[-]	.	.	HGNC:31762	.	.	ENSG00000254324	MI0000809	.	.	.	.
Mol01488	Precursor miRNA	hsa-mir-135b	microRNA 135b	MIR135B	442891	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362189.3, MIR135B-201, 97"	CACUCUGCUGUGGCCUAUGGCUUUUCAUUCCUAUGUGAUUGCUGUCCCAAACUCAUGUAGGGCUAAAAGCCAUGGGCUACAGUGAGGGGCGAGCUCC	chr1:205448302-205448398[-]	.	.	HGNC:31760	.	.	ENSG00000199059	MI0000810	.	.	.	.
Mol01489	Precursor miRNA	hsa-mir-148b	microRNA 148b	MIR148B	442892	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362252.3, MIR148B-201, 99"	CAAGCACGAUUAGCAUUUGAGGUGAAGUUCUGUUAUACACUCAGGCUGUGGCUCUCUGAAAGUCAGUGCAUCACAGAACUUUGUCUCGAAAGCUUUCUA	chr12:54337216-54337314[+]	.	.	HGNC:31761	.	.	ENSG00000199122	MI0000811	.	.	.	.
Mol01490	Precursor miRNA	hsa-mir-324	microRNA 324	MIR324	442898	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362183.3, MIR324-201, 83"	CUGACUAUGCCUCCCCGCAUCCCCUAGGGCAUUGGUGUAAAGCUGGAGACCCACUGCCCCAGGUGCUGCUGGGGGUUGUAGUC	chr17:7223297-7223379[-]	.	.	HGNC:31767	.	.	ENSG00000199053	MI0000813	.	.	.	.
Mol01491	Precursor miRNA	hsa-mir-335	microRNA 335	MIR335	442904	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362173.1, MIR335-201, 94"	UGUUUUGAGCGGGGGUCAAGAGCAAUAACGAAAAAUGUUUGUCAUAAACCGUUUUUCAUUAUUGCUCCUGACCUCCUCUCAUUUGCUAUAUUCA	chr7:130496111-130496204[+]	.	.	HGNC:31773	.	.	ENSG00000199043	MI0000816	.	.	.	.
Mol01492	Precursor miRNA	hsa-mir-196b	microRNA 196b	MIR196B	442920	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384852.2, MIR196B-201, 84"	ACUGGUCGGUGAUUUAGGUAGUUUCCUGUUGUUGGGAUCCACCUUUCUCUCGACAGCACGACACUGCCUUCAUUACUUCAGUUG	chr7:27169480-27169563[-]	.	.	HGNC:31790	.	.	ENSG00000283745	MI0001150	.	.	.	.
Mol01493	Precursor miRNA	hsa-mir-424	microRNA 424	MIR424	494336	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362227.3, MIR424-201, 98"	CGAGGGGAUACAGCAGCAAUUCAUGUUUUGAAGUGUUCUAAAUGGUUCAAAACGUGAGGCGCUGCUAUACCCCCUCGUGGGGAAGGUAGAAGGUGGGG	chrX:134546614-134546711[-]	.	.	HGNC:31881	.	.	ENSG00000284231	MI0001446	.	.	.	.
Mol01494	Precursor miRNA	hsa-mir-20b	microRNA 20b	MIR20B	574032	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384977.1, MIR20B-201, 69"	AGUACCAAAGUGCUCAUAGUGCAGGUAGUUUUGGCAUGACUCUACUGUAGUAUGGGCACUUCCAGUACU	chrX:134169809-134169877[-]	.	.	HGNC:32024	.	.	ENSG00000284043	MI0001519	.	.	.	.
Mol01495	Precursor miRNA	hsa-mir-431	microRNA 431	MIR431	574038	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385266.1, MIR431-201, 114"	UCCUGCUUGUCCUGCGAGGUGUCUUGCAGGCCGUCAUGCAGGCCACACUGACGGUAACGUUGCAGGUCGUCUUGCAGGGCUUCUCGCAAGACGACAUCCUCAUCACCAACGACG	chr14:100881007-100881120[+]	.	.	HGNC:32027	.	.	ENSG00000208001	MI0001721	.	.	.	.
Mol01496	Precursor miRNA	hsa-mir-451	microRNA 451a	MIR451A	574411	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385059.1, MIR451A-201, 72"	CUUGGGAAUGGCAAGGAAACCGUUACCAUUACUGAGUUUAGUAAUGGUAAUGGUUCUCUUGCUAUACCCAGA	chr17:28861369-28861440[-]	.	.	HGNC:32053	.	.	ENSG00000284565	MI0001729	.	.	.	.
Mol01497	Precursor miRNA	hsa-mir-452	microRNA 452	MIR452	574412	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385020.3, MIR452-201, 85"	GCUAAGCACUUACAACUGUUUGCAGAGGAAACUGAGACUUUGUAACUAUGUCUCAGUCUCAUCUGCAAAGAAGUAAGUGCUUUGC	chrX:151959628-151959712[-]	.	.	HGNC:32054	.	.	ENSG00000283751	MI0001733	.	.	.	.
Mol01498	Precursor miRNA	hsa-mir-410	microRNA 410	MIR410	574434	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362222.4, MIR410-201, 80"	GGUACCUGAGAAGAGGUUGUCUGUGAUGAGUUCGCUUUUAUUAAUGACGAAUAUAACACAGAUGGCCUGUUUUCAGUACC	chr14:101065912-101065991[+]	.	.	HGNC:32065	.	.	ENSG00000199092	MI0002465	.	.	.	.
Mol01499	Precursor miRNA	hsa-mir-483	microRNA 483	MIR483	619552	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385070.3, MIR483-201, 76"	GAGGGGGAAGACGGGAGGAAAGAAGGGAGUGGUUCCAUCACGCCUCCUCACUCCUCUCCUCCCGUCUUCUCCUCUC	chr11:2134134-2134209[-]	.	.	HGNC:32340	.	.	ENSG00000207805	MI0002467	.	.	.	.
Mol01500	Precursor miRNA	hsa-mir-487a	microRNA 487a	MIR487A	619555	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385009.3, MIR487A-201, 80"	GGUACUUGAAGAGUGGUUAUCCCUGCUGUGUUCGCUUAAUUUAUGACGAAUCAUACAGGGACAUCCAGUUUUUCAGUAUC	chr14:101052446-101052525[+]	.	.	HGNC:32343	.	.	ENSG00000207742	MI0002471	.	.	.	.
Mol01501	Precursor miRNA	hsa-mir-488	microRNA 488	MIR488	574441	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000365739.4, MIR488-201, 83"	GAGAAUCAUCUCUCCCAGAUAAUGGCACUCUCAAACAAGUUUCCAAAUUGUUUGAAAGGCUAUUUCUUGGUCAGAUGACUCUC	chr1:177029363-177029445[-]	.	.	HGNC:32073	.	.	ENSG00000202609	MI0003123	.	.	.	.
Mol01502	Precursor miRNA	hsa-mir-489	microRNA 489	MIR489	574442	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384923.1, MIR489-201, 84"	GUGGCAGCUUGGUGGUCGUAUGUGUGACGCCAUUUACUUGAACCUUUAGGAGUGACAUCACAUAUACGGCAGCUAAACUGCUAC	chr7:93483936-93484019[-]	.	.	HGNC:32074	.	.	ENSG00000207656	MI0003124	.	.	.	.
Mol01503	Precursor miRNA	hsa-mir-491	microRNA 491	MIR491	574444	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384877.3, MIR491-201, 84"	UUGACUUAGCUGGGUAGUGGGGAACCCUUCCAUGAGGAGUAGAACACUCCUUAUGCAAGAUUCCCUUCUACCUGGCUGGGUUGG	chr9:20716105-20716188[+]	.	.	HGNC:32076	.	.	ENSG00000207609	MI0003126	.	.	.	.
Mol01504	Precursor miRNA	hsa-mir-202	microRNA 202	MIR202	574448	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362219.2, MIR202-201, 110"	CGCCUCAGAGCCGCCCGCCGUUCCUUUUUCCUAUGCAUAUACUUCUUUGAGGAUCUGGCCUAAAGAGGUAUAGGGCAUGGGAAAACGGGGCGGUCGGGUCCUCCCCAGCG	chr10:133247511-133247620[-]	.	.	HGNC:32080	.	.	ENSG00000284219	MI0003130	.	.	.	.
Mol01505	Precursor miRNA	hsa-mir-493	microRNA 493	MIR493	574450	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385254.3, MIR493-201, 89"	CUGGCCUCCAGGGCUUUGUACAUGGUAGGCUUUCAUUCAUUCGUUUGCACAUUCGGUGAAGGUCUACUGUGUGCCAGGCCCUGUGCCAG	chr14:100869060-100869148[+]	.	.	HGNC:32082	.	.	ENSG00000207989	MI0003132	.	.	.	.
Mol01506	Precursor miRNA	hsa-mir-494	microRNA 494	MIR494	574452	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000349529.4, MIR494-201, 81"	GAUACUCGAAGGAGAGGUUGUCCGUGUUGUCUUCUCUUUAUUUAUGAUGAAACAUACACGGGAAACCUCUUUUUUAGUAUC	chr14:101029634-101029714[+]	.	.	HGNC:32084	.	.	ENSG00000194717	MI0003134	.	.	.	.
Mol01507	Precursor miRNA	hsa-mir-495	microRNA 495	MIR495	574453	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385010.3, MIR495-201, 82"	UGGUACCUGAAAAGAAGUUGCCCAUGUUAUUUUCGCUUUAUAUGUGACGAAACAAACAUGGUGCACUUCUUUUUCGGUAUCA	chr14:101033755-101033836[+]	.	.	HGNC:32085	.	.	ENSG00000207743	MI0003135	.	.	.	.
Mol01508	Precursor miRNA	hsa-mir-193b	microRNA 193b	MIR193B	574455	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384907.1, MIR193B-201, 83"	GUGGUCUCAGAAUCGGGGUUUUGAGGGCGAGAUGAGUUUAUGUUUUAUCCAACUGGCCCUCAAAGUCCCGCUUUUGGGGUCAU	chr16:14303967-14304049[+]	.	.	HGNC:32087	.	.	ENSG00000207639	MI0003137	.	.	.	.
Mol01509	Precursor miRNA	hsa-mir-497	microRNA 497	MIR497	574456	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385056.1, MIR497-201, 112"	CCACCCCGGUCCUGCUCCCGCCCCAGCAGCACACUGUGGUUUGUACGGCACUGUGGCCACGUCCAAACCACACUGUGGUGUUAGAGCGAGGGUGGGGGAGGCACCGCCGAGG	chr17:7017911-7018022[-]	.	.	HGNC:32088	.	.	ENSG00000284027	MI0003138	.	.	.	.
Mol01510	Precursor miRNA	hsa-mir-181d	microRNA 181d	MIR181D	574457	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384853.1, MIR181D-201, 137"	GUCCCCUCCCCUAGGCCACAGCCGAGGUCACAAUCAACAUUCAUUGUUGUCGGUGGGUUGUGAGGACUGAGGCCAGACCCACCGGGGGAUGAAUGUCACUGUGGCUGGGCCAGACACGGCUUAAGGGGAAUGGGGAC	chr19:13874875-13875011[+]	.	.	HGNC:32089	.	.	ENSG00000207585	MI0003139	.	.	.	.
Mol01511	Precursor miRNA	hsa-mir-520f	microRNA 520f	MIR520F	574464	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384824.3, MIR520F-201, 87"	UCUCAGGCUGUGACCCUCUAAAGGGAAGCGCUUUCUGUGGUCAGAAAGAAAAGCAAGUGCUUCCUUUUAGAGGGUUACCGUUUGGGA	chr19:53682159-53682245[+]	.	.	HGNC:32096	.	.	ENSG00000283540	MI0003146	.	.	.	.
Mol01512	Precursor miRNA	hsa-mir-519d	microRNA 519d	MIR519D	574480	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385246.1, MIR519D-201, 88"	UCCCAUGCUGUGACCCUCCAAAGGGAAGCGCUUUCUGUUUGUUUUCUCUUAAACAAAGUGCCUCCCUUUAGAGUGUUACCGUUUGGGA	chr19:53713347-53713434[+]	.	.	HGNC:32112	.	.	ENSG00000207981	MI0003162	.	.	.	.
Mol01513	Precursor miRNA	hsa-mir-520g	microRNA 520g	MIR520G	574484	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385064.1, MIR520G-201, 90"	UCCCAUGCUGUGACCCUCUAGAGGAAGCACUUUCUGUUUGUUGUCUGAGAAAAAACAAAGUGCUUCCCUUUAGAGUGUUACCGUUUGGGA	chr19:53722166-53722255[+]	.	.	HGNC:32116	.	.	ENSG00000207799	MI0003166	.	.	.	.
Mol01514	Precursor miRNA	hsa-mir-522	microRNA 522	MIR522	574495	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385071.3, MIR522-201, 87"	UCUCAGGCUGUGUCCCUCUAGAGGGAAGCGCUUUCUGUUGUCUGAAAGAAAAGAAAAUGGUUCCCUUUAGAGUGUUACGCUUUGAGA	chr19:53751211-53751297[+]	.	.	HGNC:32127	.	.	ENSG00000283685	MI0003177	.	.	.	.
Mol01515	Precursor miRNA	hsa-mir-519a	microRNA 519a-1	MIR519A1	574496	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385257.1, MIR519A1-201, 85"	CUCAGGCUGUGACACUCUAGAGGGAAGCGCUUUCUGUUGUCUGAAAGAAAGGAAAGUGCAUCCUUUUAGAGUGUUACUGUUUGAG	chr19:53752397-53752481[+]	.	.	HGNC:32128	.	.	ENSG00000207992	MI0003178	.	.	.	.
Mol01516	Precursor miRNA	hsa-mir-503	microRNA 503	MIR503	574506	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385270.1, MIR503-201, 71"	UGCCCUAGCAGCGGGAACAGUUCUGCAGUGAGCGAUCGGUGCUCUGGGGUAUUGUUUCCGCUGCCAGGGUA	chrX:134546328-134546398[-]	.	.	HGNC:32138	.	.	ENSG00000208005	MI0003188	.	.	.	.
Mol01517	Precursor miRNA	hsa-mir-505	microRNA 505	MIR505	574508	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384901.3, MIR505-201, 84"	GAUGCACCCAGUGGGGGAGCCAGGAAGUAUUGAUGUUUCUGCCAGUUUAGCGUCAACACUUGCUGGUUUCCUCUCUGGAGCAUC	chrX:139924148-139924231[-]	.	.	HGNC:32140	.	.	ENSG00000207633	MI0003190	.	.	.	.
Mol01518	Precursor miRNA	hsa-mir-506	microRNA 506	MIR506	574511	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384998.1, MIR506-201, 124"	GCCACCACCAUCAGCCAUACUAUGUGUAGUGCCUUAUUCAGGAAGGUGUUACUUAAUAGAUUAAUAUUUGUAAGGCACCCUUCUGAGUAGAGUAAUGUGCAACAUGGACAACAUUUGUGGUGGC	chrX:147230720-147230843[-]	.	.	HGNC:32143	.	.	ENSG00000207731	MI0003193	.	.	.	.
Mol01519	Precursor miRNA	hsa-mir-514	microRNA 514a-1	MIR514A1	574516	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385133.1, MIR514A1-201, 98"	AACAUGUUGUCUGUGGUACCCUACUCUGGAGAGUGACAAUCAUGUAUAAUUAAAUUUGAUUGACACUUCUGUGAGUAGAGUAACGCAUGACACGUACG	chrX:147279247-147279344[-]	.	.	HGNC:32148	.	.	ENSG00000207868	MI0003198	.	.	.	.
Mol01520	Precursor miRNA	hsa-mir-539	microRNA 539	MIR539	664612	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000365690.4, MIR539-201, 78"	AUACUUGAGGAGAAAUUAUCCUUGGUGUGUUCGCUUUAUUUAUGAUGAAUCAUACAAGGACAAUUUCUUUUUGAGUAU	chr14:101047321-101047398[+]	.	.	HGNC:32529	.	.	ENSG00000202560	MI0003514	.	.	.	.
Mol01521	Precursor miRNA	hsa-mir-487b	microRNA 487b	MIR487B	664616	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385021.3, MIR487B-201, 84"	UUGGUACUUGGAGAGUGGUUAUCCCUGUCCUGUUCGUUUUGCUCAUGUCGAAUCGUACAGGGUCAUCCACUUUUUCAGUAUCAA	chr14:101046455-101046538[+]	.	.	HGNC:32533	.	.	ENSG00000207754	MI0003530	.	.	.	.
Mol01522	Precursor miRNA	hsa-mir-92b	microRNA 92b	MIR92B	693235	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000607575.3, MIR92B-201, 96"	CGGGCCCCGGGCGGGCGGGAGGGACGGGACGCGGUGCAGUGUUGUUUUUUCCCCCGCCAAUAUUGCACUCGUCCCGGCCUCCGGCCCCCCCGGCCC	chr1:155195177-155195272[+]	.	.	HGNC:32920	.	.	ENSG00000284586	MI0003560	.	.	.	.
Mol01523	Precursor miRNA	hsa-mir-551b	microRNA 551b	MIR551B	693136	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384984.1, MIR551B-201, 96"	AGAUGUGCUCUCCUGGCCCAUGAAAUCAAGCGUGGGUGAGACCUGGUGCAGAACGGGAAGGCGACCCAUACUUGGUUUCAGAGGCUGUGAGAAUAA	chr3:168551854-168551949[+]	.	.	HGNC:32807	.	.	ENSG00000207717	MI0003575	.	.	.	.
Mol01524	Precursor miRNA	hsa-mir-574	microRNA 574	MIR574	693159	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385209.1, MIR574-201, 96"	GGGACCUGCGUGGGUGCGGGCGUGUGAGUGUGUGUGUGUGAGUGUGUGUCGCUCCGGGUCCACGCUCAUGCACACACCCACACGCCCACACUCAGG	chr4:38868032-38868127[+]	.	.	HGNC:32830	.	.	ENSG00000207944	MI0003581	.	.	.	.
Mol01525	Precursor miRNA	hsa-mir-548b	microRNA 548b	MIR548B	693128	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385247.1, MIR548B-201, 97"	CAGACUAUAUAUUUAGGUUGGCGCAAAAGUAAUUGUGGUUUUGGCCUUUAUUUUCAAUGGCAAGAACCUCAGUUGCUUUUGUGCCAACCUAAUACUU	chr6:119069047-119069143[-]	.	.	HGNC:32799	.	.	ENSG00000207982	MI0003596	.	.	.	.
Mol01526	Precursor miRNA	hsa-mir-629	microRNA 629	MIR629	693214	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385230.1, MIR629-201, 97"	UCCCUUUCCCAGGGGAGGGGCUGGGUUUACGUUGGGAGAACUUUUACGGUGAACCAGGAGGUUCUCCCAACGUAAGCCCAGCCCCUCCCCUCUGCCU	chr15:70079372-70079468[-]	.	.	HGNC:32885	.	.	ENSG00000207965	MI0003643	.	.	.	.
Mol01527	Precursor miRNA	hsa-mir-33b	microRNA 33b	MIR33B	693120	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385104.1, MIR33B-201, 96"	GCGGGCGGCCCCGCGGUGCAUUGCUGUUGCAUUGCACGUGUGUGAGGCGGGUGCAGUGCCUCGGCAGUGCAGCCCGGAGCCGGCCCCUGGCACCAC	chr17:17813836-17813931[-]	.	.	HGNC:32791	.	.	ENSG00000207839	MI0003646	.	.	.	.
Mol01528	Precursor miRNA	hsa-mir-663	microRNA 663a	MIR663A	724033	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385250.1, MIR663A-201, 93"	CCUUCCGGCGUCCCAGGCGGGGCGCCGCGGGACCGCCCUCGUGUCUGUGGCGGUGGGAUCCCGCGGCCGUGUUUUCCUGGUGGCCCGGCCAUG	chr20:26208186-26208278[-]	.	.	HGNC:32919	.	.	ENSG00000284419	MI0003672	.	.	.	.
Mol01529	Precursor miRNA	hsa-mir-411	microRNA 411	MIR411	693121	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362239.4, MIR411-201, 96"	UGGUACUUGGAGAGAUAGUAGACCGUAUAGCGUACGCUUUAUCUGUGACGUAUGUAACACGGUCCACUAACCCUCAGUAUCAAAUCCAUCCCCGAG	chr14:101023325-101023420[+]	.	.	HGNC:32792	.	.	ENSG00000199109	MI0003675	.	.	.	.
Mol01530	Precursor miRNA	hsa-mir-1271	microRNA 1271	MIR1271	100302203	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408537.1, MIR1271-201, 86"	CACCCAGAUCAGUGCUUGGCACCUAGCAAGCACUCAGUAAAUAUUUGUUGAGUGCCUGCUAUGUGCCAGGCAUUGUGCUGAGGGCU	chr5:176367946-176368031[+]	.	.	HGNC:35252	.	.	ENSG00000221464	MI0003814	.	.	.	.
Mol01531	Precursor miRNA	hsa-mir-1301	microRNA 1301	MIR1301	100302246	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408518.3, MIR1301-201, 82"	GGAUUGUGGGGGGUCGCUCUAGGCACCGCAGCACUGUGCUGGGGAUGUUGCAGCUGCCUGGGAGUGACUUCACACAGUCCUC	chr2:25328640-25328721[-]	.	.	HGNC:35253	.	.	ENSG00000221445	MI0003815	.	.	.	.
Mol01532	Precursor miRNA	hsa-mir-770	microRNA 770	MIR770	768222	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390219.1, MIR770-201, 98"	AGGAGCCACCUUCCGAGCCUCCAGUACCACGUGUCAGGGCCACAUGAGCUGGGCCUCGUGGGCCUGAUGUGGUGCUGGGGCCUCAGGGGUCUGCUCUU	chr14:100852390-100852487[+]	.	.	HGNC:33143	.	.	ENSG00000211574	MI0005118	.	.	.	.
Mol01533	Precursor miRNA	hsa-mir-675	microRNA 675	MIR675	100033819	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390168.6, MIR675-201, 73"	CCCAGGGUCUGGUGCGGAGAGGGCCCACAGUGGACUUGGUGACGCUGUAUGCCCUCACCGCUCAGCCCCUGGG	chr11:1996759-1996831[-]	.	.	HGNC:33351	.	.	ENSG00000284010	MI0005416	.	.	.	.
Mol01534	Precursor miRNA	hsa-mir-874	microRNA 874	MIR874	100126343	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401190.3, MIR874-201, 78"	UUAGCCCUGCGGCCCCACGCACCAGGGUAAGAGAGACUCUCGCUUCCUGCCCUGGCCCGAGGGACCGACUGGCUGGGC	chr5:137647572-137647649[-]	.	.	HGNC:33643	.	.	ENSG00000216009	MI0005532	.	.	.	.
Mol01535	Precursor miRNA	hsa-mir-708	microRNA 708	MIR708	100126333	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390708.1, MIR708-201, 88"	AACUGCCCUCAAGGAGCUUACAAUCUAGCUGGGGGUAAAUGACUUGCACAUGAACACAACUAGACUGUGAGCUUCUAGAGGGCAGGGA	chr11:79402022-79402109[-]	.	.	HGNC:33654	.	.	ENSG00000211997	MI0005543	.	.	.	.
Mol01536	Precursor miRNA	hsa-mir-873	microRNA 873	MIR873	100126316	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401120.3, MIR873-201, 77"	GUGUGCAUUUGCAGGAACUUGUGAGUCUCCUAUUGAAAAUGAACAGGAGACUGAUGAGUUCCCGGGAACACCCACAA	chr9:28888879-28888955[-]	.	.	HGNC:33663	.	.	ENSG00000215939	MI0005564	.	.	.	.
Mol01537	Precursor miRNA	hsa-mir-374b	microRNA 374b	MIR374B	100126317	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390738.3, MIR374B-201, 72"	ACUCGGAUGGAUAUAAUACAACCUGCUAAGUGUCCUAGCACUUAGCAGGUUGUAUUAUCAUUGUCCGUGUCU	chrX:74218547-74218618[-]	.	.	HGNC:33665	.	.	ENSG00000212027	MI0005566	.	.	.	.
Mol01538	Precursor miRNA	hsa-mir-216b	microRNA 216b	MIR216B	100126319	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390186.2, MIR216B-201, 82"	GCAGACUGGAAAAUCUCUGCAGGCAAAUGUGAUGUCACUGAGGAAAUCACACACUUACCCGUAGAGAUUCUACAGUCUGACA	chr2:56000714-56000795[-]	.	.	HGNC:33668	.	.	ENSG00000211520	MI0005569	.	.	.	.
Mol01539	Precursor miRNA	hsa-mir-939	microRNA 939	MIR939	100126351	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401314.1, MIR939-201, 82"	UGUGGGCAGGGCCCUGGGGAGCUGAGGCUCUGGGGGUGGCCGGGGCUGACCCUGGGCCUCUGCUCCCCAGUGUCUGACCGCG	chr8:144394149-144394230[-]	.	.	HGNC:33682	.	.	ENSG00000284310	MI0005761	.	.	.	.
Mol01540	Precursor miRNA	hsa-mir-942	microRNA 942	MIR942	100126331	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401111.1, MIR942-201, 86"	AUUAGGAGAGUAUCUUCUCUGUUUUGGCCAUGUGUGUACUCACAGCCCCUCACACAUGGCCGAAACAGAGAAGUUACUUUCCUAAU	chr1:117094643-117094728[+]	.	.	HGNC:33688	.	.	ENSG00000215930	MI0005767	.	.	.	.
Mol01541	Precursor miRNA	hsa-mir-1307	microRNA 1307	MIR1307	100302174	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408840.1, MIR1307-201, 149"	CAUCAAGACCCAGCUGAGUCACUGUCACUGCCUACCAAUCUCGACCGGACCUCGACCGGCUCGUCUGUGUUGCCAAUCGACUCGGCGUGGCGUCGGUCGUGGUAGAUAGGCGGUCAUGCAUACGAAUUUUCAGCUCUUGUUCUGGUGAC	chr10:103394253-103394401[-]	.	.	HGNC:35372	.	.	ENSG00000283867	MI0006444	.	.	.	.
Mol01542	Precursor miRNA	hsa-mir-1915	microRNA 1915	MIR1915	100302129	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000410139.1, MIR1915-201, 80"	UGAGAGGCCGCACCUUGCCUUGCUGCCCGGGCCGUGCACCCGUGGGCCCCAGGGCGACGCGGCGGGGGCGGCCCUAGCGA	chr10:21496562-21496641[-]	.	.	HGNC:35399	.	.	ENSG00000222071	MI0008336	.	.	.	.
Mol01543	Precursor miRNA	hsa-mir-3656	microRNA 3656	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	CUUUCGGCCAGCGGGACGGCAUCCGAGGUGGGCUAGGCUCGGGCCCGUGGCGGGUGCGGGGGUGGGAGG	.	.	.	HGNC:38889	.	.	.	MI0016056	.	.	.	.
Mol01544	Mature miRNA	hsa-let-7a-5p	microRNA let-7a-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362295.3, MIRLET7A1-201, 80"	UGAGGUAGUAGGUUGUAUAGUU	.	.	.	HGNC:31476	.	.	ENSG00000199165	.	MIMAT0000062	"hsa-let-7a-1,MI0000060,chr9:94175957-94176036(+),chr9:94175962-94175983(+); hsa-let-7a-2,MI0000061,chr11:122146522-122146593(-),chr11:122146568-122146589(-); hsa-let-7a-3,MI0000062,chr22:46112749-46112822(+),chr22:46112752-46112773(+)"	.	.
Mol01545	Mature miRNA	hsa-miR-17-5p	microRNA 17	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385012.1, MIR17-201, 84"	CAAAGUGCUUACAGUGCAGGUAG	.	.	.	HGNC:31547	.	.	ENSG00000284536	.	MIMAT0000070	"hsa-mir-17,MI0000071,chr13:91350605-91350688(+),chr13:91350618-91350640(+)"	.	.
Mol01546	Mature miRNA	hsa-miR-19a-3p	microRNA 19a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384878.1, MIR19A-201, 82"	UGUGCAAAUCUAUGCAAAACUGA	.	.	.	HGNC:31574	.	.	ENSG00000284204	.	MIMAT0000073	"hsa-mir-19a,MI0000073,chr13:91350891-91350972(+),chr13:91350939-91350961(+)"	.	.
Mol01547	Mature miRNA	hsa-miR-19b-3p	microRNA 19b-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384829.1, MIR19B1-201, 87"	UGUGCAAAUCCAUGCAAAACUGA	.	.	.	HGNC:31575	.	.	ENSG00000284375	.	MIMAT0000074	"hsa-mir-19b-1,MI0000074,chr13:91351192-91351278(+),chr13:91351245-91351267(+); hsa-mir-19b-2,MI0000075,chrX:134169671-134169766(-),chrX:134169683-134169705(-)"	.	.
Mol01548	Mature miRNA	hsa-miR-20a-5p	microRNA 20a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362279.1, MIR20A-201, 71"	UAAAGUGCUUAUAGUGCAGGUAG	.	.	.	HGNC:31577	.	.	ENSG00000283762	.	MIMAT0000075	"hsa-mir-20a,MI0000076,chr13:91351065-91351135(+),chr13:91351072-91351094(+)"	.	.
Mol01549	Mature miRNA	hsa-miR-21-5p	microRNA 21	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362134.1, MIR21-201, 72"	UAGCUUAUCAGACUGAUGUUGA	.	.	.	HGNC:31586	.	.	ENSG00000284190	.	MIMAT0000076	"hsa-mir-21,MI0000077,chr17:59841266-59841337(+),chr17:59841273-59841294(+)"	.	.
Mol01550	Mature miRNA	hsa-miR-22-3p	microRNA 22	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362190.3, MIR22-201, 85"	AAGCUGCCAGUUGAAGAACUGU	.	.	.	HGNC:31599	.	.	ENSG00000283824	.	MIMAT0000077	"hsa-mir-22,MI0000078,chr17:1713903-1713987(-),chr17:1713914-1713935(-)"	.	.
Mol01551	Mature miRNA	hsa-miR-24-3p	microRNA 24-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000637495.1, MIR24-1-201, 68"	UGGCUCAGUUCAGCAGGAACAG	.	.	.	HGNC:31607	.	.	ENSG00000284459	.	MIMAT0000080	"hsa-mir-24-1,MI0000080,chr9:95086021-95086088(+),chr9:95086064-95086085(+); hsa-mir-24-2,MI0000081,chr19:13836287-13836359(-),chr19:13836289-13836310(-)"	.	.
Mol01552	Mature miRNA	hsa-miR-29a-3p	microRNA 29a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362111.4, MIR29A-201, 64"	UAGCACCAUCUGAAAUCGGUUA	.	.	.	HGNC:31616	.	.	ENSG00000284032	.	MIMAT0000086	"hsa-mir-29a,MI0000087,chr7:130876747-130876810(-),chr7:130876748-130876769(-)"	.	.
Mol01553	Mature miRNA	hsa-miR-30a-5p	microRNA 30a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385092.1, MIR30A-201, 71"	UGUAAACAUCCUCGACUGGAAG	.	.	.	HGNC:31624	.	.	ENSG00000207827	.	MIMAT0000087	"hsa-mir-30a,MI0000088,chr6:71403551-71403621(-),chr6:71403595-71403616(-)"	.	.
Mol01554	Mature miRNA	hsa-miR-32-5p	microRNA 32	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384965.1, MIR32-201, 70"	UAUUGCACAUUACUAAGUUGCA	.	.	.	HGNC:31631	.	.	ENSG00000207698	.	MIMAT0000090	"hsa-mir-32,MI0000090,chr9:109046229-109046298(-),chr9:109046272-109046293(-)"	.	.
Mol01555	Mature miRNA	hsa-miR-33a-5p	microRNA 33a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385197.1, MIR33A-201, 69"	GUGCAUUGUAGUUGCAUUGCA	.	.	.	HGNC:31634	.	.	ENSG00000207932	.	MIMAT0000091	"hsa-mir-33a,MI0000091,chr22:41900944-41901012(+),chr22:41900949-41900969(+)"	.	.
Mol01556	Mature miRNA	hsa-miR-96-5p	microRNA 96	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362288.1, MIR96-201, 78"	UUUGGCACUAGCACAUUUUUGCU	.	.	.	HGNC:31648	.	.	ENSG00000199158	.	MIMAT0000095	"hsa-mir-96,MI0000098,chr7:129774692-129774769(-),chr7:129774739-129774761(-)"	.	.
Mol01557	Mature miRNA	hsa-miR-98-5p	microRNA 98	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000606724.1, MIR98-201, 119"	UGAGGUAGUAAGUUGUAUUGUU	.	.	.	HGNC:31649	.	.	ENSG00000271886	.	MIMAT0000096	"hsa-mir-98,MI0000100,chrX:53556223-53556341(-),chrX:53556299-53556320(-)"	.	.
Mol01558	Mature miRNA	hsa-miR-99a-5p	microRNA 99a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384906.1, MIR99A-201, 81"	AACCCGUAGAUCCGAUCUUGUG	.	.	.	HGNC:31650	.	.	ENSG00000207638	.	MIMAT0000097	"hsa-mir-99a,MI0000101,chr21:16539089-16539169(+),chr21:16539101-16539122(+)"	.	.
Mol01559	Mature miRNA	hsa-miR-100-5p	microRNA 100	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385259.1, MIR100-201, 80"	AACCCGUAGAUCCGAACUUGUG	.	.	.	HGNC:31487	.	.	ENSG00000207994	.	MIMAT0000098	"hsa-mir-100,MI0000102,chr11:122152229-122152308(-),chr11:122152275-122152296(-)"	.	.
Mol01560	Mature miRNA	hsa-miR-101-3p	microRNA 101-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362265.1, MIR101-1-201, 75"	UACAGUACUGUGAUAACUGAA	.	.	.	HGNC:31488	.	.	ENSG00000199135	.	MIMAT0000099	"hsa-mir-101-1,MI0000103,chr1:65058434-65058508(-),chr1:65058442-65058462(-); hsa-mir-101-2,MI0000739,chr9:4850297-4850375(+),chr9:4850345-4850365(+)"	.	.
Mol01561	Mature miRNA	hsa-miR-29b-3p	microRNA 29b-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385015.1, MIR29B1-201, 81"	UAGCACCAUUUGAAAUCAGUGUU	.	.	.	HGNC:31619	.	.	ENSG00000283797	.	MIMAT0000100	"hsa-mir-29b-1,MI0000105,chr7:130877459-130877539(-),chr7:130877467-130877489(-); hsa-mir-29b-2,MI0000107,chr1:207802443-207802523(-),chr1:207802450-207802472(-)"	.	.
Mol01562	Mature miRNA	hsa-miR-107	microRNA 107	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362127.2, MIR107-201, 81"	AGCAGCAUUGUACAGGGCUAUCA	.	.	.	HGNC:31496	.	.	ENSG00000198997	.	MIMAT0000104	"hsa-mir-107,MI0000114,chr10:89592747-89592827(-),chr10:89592756-89592778(-)"	.	.
Mol01563	Mature miRNA	hsa-miR-196a-5p	microRNA 196a-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000388006.1, MIR196A1-201, 70"	UAGGUAGUUUCAUGUUGUUGGG	.	.	.	HGNC:31567	.	.	ENSG00000210741	.	MIMAT0000226	"hsa-mir-196a-1,MI0000238,chr17:48632490-48632559(-),chr17:48632532-48632553(-); hsa-mir-196a-2,MI0000279,chr12:53991738-53991847(+),chr12:53991762-53991783(+)"	.	.
Mol01564	Mature miRNA	hsa-miR-197-3p	microRNA 197	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384976.2, MIR197-201, 75"	UUCACCACCUUCUCCACCCAGC	.	.	.	HGNC:31569	.	.	ENSG00000284443	.	MIMAT0000227	"hsa-mir-197,MI0000239,chr1:109598893-109598967(+),chr1:109598940-109598961(+)"	.	.
Mol01565	Mature miRNA	hsa-miR-198	microRNA 198	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000637333.1, MIR198-201, 62"	GGUCCAGAGGGGAGAUAGGUUC	.	.	.	HGNC:31570	.	.	ENSG00000284121	.	MIMAT0000228	"hsa-mir-198,MI0000240,chr3:120395668-120395729(-),chr3:120395703-120395724(-)"	.	.
Mol01566	Mature miRNA	hsa-miR-199a-5p	microRNA 199a-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385019.1, MIR199A1-201, 71"	CCCAGUGUUCAGACUACCUGUUC	.	.	.	HGNC:31571	.	.	ENSG00000207752	.	MIMAT0000231	"hsa-mir-199a-1,MI0000242,chr19:10817426-10817496(-),chr19:10817469-10817491(-); hsa-mir-199a-2,MI0000281,chr1:172144535-172144644(-),chr1:172144592-172144614(-)"	.	.
Mol01567	Mature miRNA	hsa-miR-199a-3p	microRNA 199a-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385019.1, MIR199A1-201, 71"	ACAGUAGUCUGCACAUUGGUUA	.	.	.	HGNC:31571	.	.	ENSG00000207752	.	MIMAT0000232	"hsa-mir-199a-1,MI0000242,chr19:10817426-10817496(-),chr19:10817429-10817450(-); hsa-mir-199a-2,MI0000281,chr1:172144535-172144644(-),chr1:172144554-172144575(-)"	.	.
Mol01568	Mature miRNA	hsa-miR-129-5p	microRNA 129-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384972.2, MIR129-1-201, 72"	CUUUUUGCGGUCUGGGCUUGC	.	.	.	HGNC:31512	.	.	ENSG00000207705	.	MIMAT0000242	"hsa-mir-129-1,MI0000252,chr7:128207872-128207943(+),chr7:128207876-128207896(+); hsa-mir-129-2,MI0000473,chr11:43581394-43581483(+),chr11:43581408-43581428(+)"	.	.
Mol01569	Mature miRNA	hsa-miR-148a-3p	microRNA 148a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362215.3, MIR148A-201, 68"	UCAGUGCACUACAGAACUUUGU	.	.	.	HGNC:31535	.	.	ENSG00000199085	.	MIMAT0000243	"hsa-mir-148a,MI0000253,chr7:25949919-25949986(-),chr7:25949922-25949943(-)"	.	.
Mol01570	Mature miRNA	hsa-miR-30c-5p	microRNA 30c-2	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362224.3, MIR30C2-201, 72"	UGUAAACAUCCUACACUCUCAGC	.	.	.	HGNC:31627	.	.	ENSG00000199094	.	MIMAT0000244	"hsa-mir-30c-1,MI0000736,chr1:40757284-40757372(+),chr1:40757300-40757322(+); hsa-mir-30c-2,MI0000254,chr6:71376960-71377031(-),chr6:71377003-71377025(-)"	.	.
Mol01571	Mature miRNA	hsa-miR-139-5p	microRNA 139	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000606837.1, MIR139-201, 68"	UCUACAGUGCACGUGUCUCCAGU	.	.	.	HGNC:31526	.	.	ENSG00000272036	.	MIMAT0000250	"hsa-mir-139,MI0000261,chr11:72615063-72615130(-),chr11:72615102-72615124(-)"	.	.
Mol01572	Mature miRNA	hsa-miR-7-5p	microRNA 7-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384871.1, MIR7-1-201, 110"	UGGAAGACUAGUGAUUUUGUUGUU	.	.	.	HGNC:31638	.	.	ENSG00000284179	.	MIMAT0000252	"hsa-mir-7-1,MI0000263,chr9:83969748-83969857(-),chr9:83969811-83969834(-); hsa-mir-7-2,MI0000264,chr15:88611825-88611934(+),chr15:88611856-88611879(+); hsa-mir-7-3,MI0000265,chr19:4770670-4770779(+),chr19:4770700-4770723(+)"	.	.
Mol01573	Mature miRNA	hsa-miR-10a-5p	microRNA 10a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385043.1, MIR10A-201, 110"	UACCCUGUAGAUCCGAAUUUGUG	.	.	.	HGNC:31497	.	.	ENSG00000284038	.	MIMAT0000253	"hsa-mir-10a,MI0000266,chr17:48579838-48579947(-),chr17:48579904-48579926(-)"	.	.
Mol01574	Mature miRNA	hsa-miR-34a-5p	microRNA 34a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385130.1, MIR34A-201, 110"	UGGCAGUGUCUUAGCUGGUUGU	.	.	.	HGNC:31635	.	.	ENSG00000284357	.	MIMAT0000255	"hsa-mir-34a,MI0000268,chr1:9151668-9151777(-),chr1:9151735-9151756(-)"	.	.
Mol01575	Mature miRNA	hsa-miR-181a-5p	microRNA 181a-2	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384863.1, MIR181A2-201, 110"	AACAUUCAACGCUGUCGGUGAGU	.	.	.	HGNC:31549	.	.	ENSG00000207595	.	MIMAT0000256	"hsa-mir-181a-1,MI0000289,chr1:198859044-198859153(-),chr1:198859108-198859130(-); hsa-mir-181a-2,MI0000269,chr9:124692442-124692551(+),chr9:124692480-124692502(+)"	.	.
Mol01576	Mature miRNA	hsa-miR-181b-5p	microRNA 181b-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385240.1, MIR181B1-201, 110"	AACAUUCAUUGCUGUCGGUGGGU	.	.	.	HGNC:31550	.	.	ENSG00000207975	.	MIMAT0000257	"hsa-mir-181b-1,MI0000270,chr1:198858873-198858982(-),chr1:198858925-198858947(-); hsa-mir-181b-2,MI0000683,chr9:124693710-124693798(+),chr9:124693725-124693747(+)"	.	.
Mol01577	Mature miRNA	hsa-miR-181c-5p	microRNA 181c	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384881.1, MIR181C-201, 110"	AACAUUCAACCUGUCGGUGAGU	.	.	.	HGNC:31552	.	.	ENSG00000207613	.	MIMAT0000258	"hsa-mir-181c,MI0000271,chr19:13874699-13874808(+),chr19:13874725-13874746(+)"	.	.
Mol01578	Mature miRNA	hsa-miR-182-5p	microRNA 182	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385255.3, MIR182-201, 110"	UUUGGCAAUGGUAGAACUCACACU	.	.	.	HGNC:31553	.	.	ENSG00000207990	.	MIMAT0000259	"hsa-mir-182,MI0000272,chr7:129770383-129770492(-),chr7:129770447-129770470(-)"	.	.
Mol01579	Mature miRNA	hsa-miR-183-5p	microRNA 183	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384958.1, MIR183-201, 110"	UAUGGCACUGGUAGAAUUCACU	.	.	.	HGNC:31554	.	.	ENSG00000207691	.	MIMAT0000261	"hsa-mir-183,MI0000273,chr7:129774905-129775014(-),chr7:129774967-129774988(-)"	.	.
Mol01580	Mature miRNA	hsa-miR-199b-5p	microRNA 199b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384849.1, MIR199B-201, 110"	CCCAGUGUUUAGACUAUCUGUUC	.	.	.	HGNC:31573	.	.	ENSG00000207581	.	MIMAT0000263	"hsa-mir-199b,MI0000282,chr9:128244721-128244830(-),chr9:128244783-128244805(-)"	.	.
Mol01581	Mature miRNA	hsa-miR-204-5p	microRNA 204	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385200.3, MIR204-201, 110"	UUCCCUUUGUCAUCCUAUGCCU	.	.	.	HGNC:31582	.	.	ENSG00000207935	.	MIMAT0000265	"hsa-mir-204,MI0000284,chr9:70809975-70810084(-),chr9:70810031-70810052(-)"	.	.
Mol01582	Mature miRNA	hsa-miR-205-5p	microRNA 205	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384891.1, MIR205-201, 110"	UCCUUCAUUCCACCGGAGUCUG	.	.	.	HGNC:31583	.	.	ENSG00000284485	.	MIMAT0000266	"hsa-mir-205,MI0000285,chr1:209432133-209432242(+),chr1:209432166-209432187(+)"	.	.
Mol01583	Mature miRNA	hsa-miR-210-3p	microRNA 210	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362168.1, MIR210-201, 110"	CUGUGCGUGUGACAGCGGCUGA	.	.	.	HGNC:31587	.	.	ENSG00000199038	.	MIMAT0000267	"hsa-mir-210,MI0000286,chr11:568089-568198(-),chr11:568112-568133(-)"	.	.
Mol01584	Mature miRNA	hsa-miR-211-5p	microRNA 211	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384969.1, MIR211-201, 110"	UUCCCUUUGUCAUCCUUCGCCU	.	.	.	HGNC:31588	.	.	ENSG00000207702	.	MIMAT0000268	"hsa-mir-211,MI0000287,chr15:31065032-31065141(-),chr15:31065095-31065116(-)"	.	.
Mol01585	Mature miRNA	hsa-miR-214-3p	microRNA 214	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385214.1, MIR214-201, 110"	ACAGCAGGCACAGACAGGCAGU	.	.	.	HGNC:31591	.	.	ENSG00000283844	.	MIMAT0000271	"hsa-mir-214,MI0000290,chr1:172138798-172138907(-),chr1:172138816-172138837(-)"	.	.
Mol01586	Mature miRNA	hsa-miR-218-5p	microRNA 218-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384999.1, MIR218-1-201, 110"	UUGUGCUUGAUCUAACCAUGU	.	.	.	HGNC:31595	.	.	ENSG00000207732	.	MIMAT0000275	"hsa-mir-218-1,MI0000294,chr4:20528275-20528384(+),chr4:20528299-20528319(+); hsa-mir-218-2,MI0000295,chr5:168768146-168768255(-),chr5:168768211-168768231(-)"	.	.
Mol01587	Mature miRNA	hsa-miR-219a-5p	microRNA 219a-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362166.1, MIR219A1-201, 110"	UGAUUGUCCAAACGCAAUUCU	.	.	.	HGNC:31597	.	.	ENSG00000199036	.	MIMAT0000276	"hsa-mir-219a-1,MI0000296,chr6:33207835-33207944(+),chr6:33207855-33207875(+); hsa-mir-219a-2,MI0000740,chr9:128392618-128392714(-),chr9:128392676-128392696(-)"	.	.
Mol01589	Mature miRNA	hsa-miR-221-3p	microRNA 221	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385135.1, MIR221-201, 110"	AGCUACAUUGUCUGCUGGGUUUC	.	.	.	HGNC:31601	.	.	ENSG00000207870	.	MIMAT0000278	"hsa-mir-221,MI0000298,chrX:45746157-45746266(-),chrX:45746180-45746202(-)"	.	.
Mol01590	Mature miRNA	hsa-miR-223-3p	microRNA 223	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385204.1, MIR223-201, 110"	UGUCAGUUUGUCAAAUACCCCA	.	.	.	HGNC:31603	.	.	ENSG00000284567	.	MIMAT0000280	"hsa-mir-223,MI0000300,chrX:66018870-66018979(+),chrX:66018937-66018958(+)"	.	.
Mol01591	Mature miRNA	hsa-miR-224-5p	microRNA 224	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384889.1, MIR224-201, 81"	UCAAGUCACUAGUGGUUCCGUUUAG	.	.	.	HGNC:31604	.	.	ENSG00000284363	.	MIMAT0000281	"hsa-mir-224,MI0000301,chrX:151958578-151958658(-),chrX:151958628-151958652(-)"	.	.
Mol01592	Mature miRNA	hsa-miR-15b-5p	microRNA 15b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385045.1, MIR15B-201, 98"	UAGCAGCACAUCAUGGUUUACA	.	.	.	HGNC:31544	.	.	ENSG00000207779	.	MIMAT0000417	"hsa-mir-15b,MI0000438,chr3:160404588-160404685(+),chr3:160404607-160404628(+)"	.	.
Mol01593	Mature miRNA	hsa-miR-23b-3p	microRNA 23b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384832.1, MIR23B-201, 97"	AUCACAUUGCCAGGGAUUACCAC	.	.	.	HGNC:31606	.	.	ENSG00000207563	.	MIMAT0000418	"hsa-mir-23b,MI0000439,chr9:95085208-95085304(+),chr9:95085265-95085287(+)"	.	.
Mol01594	Mature miRNA	hsa-miR-27b-3p	microRNA 27b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385129.3, MIR27B-201, 97"	UUCACAGUGGCUAAGUUCUGC	.	.	.	HGNC:31614	.	.	ENSG00000207864	.	MIMAT0000419	"hsa-mir-27b,MI0000440,chr9:95085445-95085541(+),chr9:95085505-95085525(+)"	.	.
Mol01595	Mature miRNA	hsa-miR-124-3p	microRNA 124-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385275.1, MIR124-1-201, 85"	UAAGGCACGCGGUGAAUGCCAA	.	.	.	HGNC:31502	.	.	ENSG00000284321	.	MIMAT0000422	"hsa-mir-124-1,MI0000443,chr8:9903388-9903472(-),chr8:9903399-9903420(-); hsa-mir-124-2,MI0000444,chr8:64379149-64379257(+),chr8:64379210-64379231(+); hsa-mir-124-3,MI0000445,chr20:63178500-63178586(+),chr20:63178552-63178573(+)"	.	.
Mol01596	Mature miRNA	hsa-miR-125b-5p	microRNA 125b-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385236.1, MIR125B1-201, 88"	UCCCUGAGACCCUAACUUGUGA	.	.	.	HGNC:31506	.	.	ENSG00000207971	.	MIMAT0000423	"hsa-mir-125b-1,MI0000446,chr11:122099757-122099844(-),chr11:122099809-122099830(-); hsa-mir-125b-2,MI0000470,chr21:16590237-16590325(+),chr21:16590253-16590274(+)"	.	.
Mol01597	Mature miRNA	hsa-miR-130a-3p	microRNA 130a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385274.1, MIR130A-201, 89"	CAGUGCAAUGUUAAAAGGGCAU	.	.	.	HGNC:31514	.	.	ENSG00000208009	.	MIMAT0000425	"hsa-mir-130a,MI0000448,chr11:57641198-57641286(+),chr11:57641252-57641273(+)"	.	.
Mol01598	Mature miRNA	hsa-miR-135a-5p	microRNA 135a-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385191.1, MIR135A1-201, 90"	UAUGGCUUUUUAUUCCUAUGUGA	.	.	.	HGNC:31520	.	.	ENSG00000207926	.	MIMAT0000428	"hsa-mir-135a-1,MI0000452,chr3:52294219-52294308(-),chr3:52294270-52294292(-); hsa-mir-135a-2,MI0000453,chr12:97563812-97563911(+),chr12:97563834-97563856(+)"	.	.
Mol01599	Mature miRNA	hsa-miR-138-5p	microRNA 138-2	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384916.3, MIR138-2-201, 84"	AGCUGGUGUUGUGAAUCAGGCCG	.	.	.	HGNC:31525	.	.	ENSG00000207649	.	MIMAT0000430	"hsa-mir-138-1,MI0000476,chr3:44114212-44114310(+),chr3:44114234-44114256(+); hsa-mir-138-2,MI0000455,chr16:56858518-56858601(+),chr16:56858527-56858549(+)"	.	.
Mol01600	Mature miRNA	hsa-miR-140-5p	microRNA 140	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385282.3, MIR140-201, 100"	CAGUGGUUUUACCCUAUGGUAG	.	.	.	HGNC:31527	.	.	ENSG00000208017	.	MIMAT0000431	"hsa-mir-140,MI0000456,chr16:69933081-69933180(+),chr16:69933103-69933124(+)"	.	.
Mol01601	Mature miRNA	hsa-miR-141-3p	microRNA 141	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384975.1, MIR141-201, 95"	UAACACUGUCUGGUAAAGAUGG	.	.	.	HGNC:31528	.	.	ENSG00000207708	.	MIMAT0000432	"hsa-mir-141,MI0000457,chr12:6964097-6964191(+),chr12:6964155-6964176(+)"	.	.
Mol01602	Mature miRNA	hsa-miR-142-5p	microRNA 142	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384835.3, MIR142-201, 87"	CAUAAAGUAGAAAGCACUACU	.	.	.	HGNC:31529	.	.	ENSG00000284353	.	MIMAT0000433	"hsa-mir-142,MI0000458,chr17:58331232-58331318(-),chr17:58331283-58331303(-)"	.	.
Mol01603	Mature miRNA	hsa-miR-142-3p	microRNA 142	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384835.3, MIR142-201, 87"	UGUAGUGUUUCCUACUUUAUGGA	.	.	.	HGNC:31529	.	.	ENSG00000284353	.	MIMAT0000434	"hsa-mir-142,MI0000458,chr17:58331232-58331318(-),chr17:58331245-58331267(-)"	.	.
Mol01604	Mature miRNA	hsa-miR-143-3p	microRNA 143	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385300.1, MIR143-201, 106"	UGAGAUGAAGCACUGUAGCUC	.	.	.	HGNC:31530	.	.	ENSG00000284182	.	MIMAT0000435	"hsa-mir-143,MI0000459,chr5:149428918-149429023(+),chr5:149428978-149428998(+)"	.	.
Mol01605	Mature miRNA	hsa-miR-144-3p	microRNA 144	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384886.3, MIR144-201, 86"	UACAGUAUAGAUGAUGUACU	.	.	.	HGNC:31531	.	.	ENSG00000283819	.	MIMAT0000436	"hsa-mir-144,MI0000460,chr17:28861533-28861618(-),chr17:28861548-28861567(-)"	.	.
Mol01606	Mature miRNA	hsa-miR-145-5p	microRNA 145	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384967.1, MIR145-201, 88"	GUCCAGUUUUCCCAGGAAUCCCU	.	.	.	HGNC:31532	.	.	ENSG00000276365	.	MIMAT0000437	"hsa-mir-145,MI0000461,chr5:149430646-149430733(+),chr5:149430661-149430683(+)"	.	.
Mol01607	Mature miRNA	hsa-miR-125a-5p	microRNA 125a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385273.1, MIR125A-201, 86"	UCCCUGAGACCCUUUAACCUGUGA	.	.	.	HGNC:31505	.	.	ENSG00000208008	.	MIMAT0000443	"hsa-mir-125a,MI0000469,chr19:51693254-51693339(+),chr19:51693268-51693291(+)"	.	.
Mol01608	Mature miRNA	hsa-miR-126-5p	microRNA 126	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362291.1, MIR126-201, 85"	CAUUAUUACUUUUGGUACGCG	.	.	.	HGNC:31508	.	.	ENSG00000199161	.	MIMAT0000444	"hsa-mir-126,MI0000471,chr9:136670602-136670686(+),chr9:136670616-136670636(+)"	.	.
Mol01609	Mature miRNA	hsa-miR-126-3p	microRNA 126	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362291.1, MIR126-201, 85"	UCGUACCGUGAGUAAUAAUGCG	.	.	.	HGNC:31508	.	.	ENSG00000199161	.	MIMAT0000445	"hsa-mir-126,MI0000471,chr9:136670602-136670686(+),chr9:136670653-136670674(+)"	.	.
Mol01610	Mature miRNA	hsa-miR-127-3p	microRNA 127	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384876.3, MIR127-201, 97"	UCGGAUCCGUCUGAGCUUGGCU	.	.	.	HGNC:31509	.	.	ENSG00000207608	.	MIMAT0000446	"hsa-mir-127,MI0000472,chr14:100882979-100883075(+),chr14:100883035-100883056(+)"	.	.
Mol01611	Mature miRNA	hsa-miR-134-5p	microRNA 134	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385258.3, MIR134-201, 73"	UGUGACUGGUUGACCAGAGGGG	.	.	.	HGNC:31519	.	.	ENSG00000207993	.	MIMAT0000447	"hsa-mir-134,MI0000474,chr14:101054687-101054759(+),chr14:101054694-101054715(+)"	.	.
Mol01612	Mature miRNA	hsa-miR-146a-5p	microRNA 146a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385201.1, MIR146A-201, 99"	UGAGAACUGAAUUCCAUGGGUU	.	.	.	HGNC:31533	.	.	ENSG00000283733	.	MIMAT0000449	"hsa-mir-146a,MI0000477,chr5:160485352-160485450(+),chr5:160485372-160485393(+)"	.	.
Mol01613	Mature miRNA	hsa-miR-149-5p	microRNA 149	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384879.1, MIR149-201, 89"	UCUGGCUCCGUGUCUUCACUCCC	.	.	.	HGNC:31536	.	.	ENSG00000207611	.	MIMAT0000450	"hsa-mir-149,MI0000478,chr2:240456001-240456089(+),chr2:240456015-240456037(+)"	.	.
Mol01614	Mature miRNA	hsa-miR-184	microRNA 184	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384962.1, MIR184-201, 84"	UGGACGGAGAACUGAUAAGGGU	.	.	.	HGNC:31555	.	.	ENSG00000207695	.	MIMAT0000454	"hsa-mir-184,MI0000481,chr15:79209788-79209871(+),chr15:79209840-79209861(+)"	.	.
Mol01615	Mature miRNA	hsa-miR-185-5p	microRNA 185	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385288.3, MIR185-201, 82"	UGGAGAGAAAGGCAGUUCCUGA	.	.	.	HGNC:31556	.	.	ENSG00000208023	.	MIMAT0000455	"hsa-mir-185,MI0000482,chr22:20033139-20033220(+),chr22:20033153-20033174(+)"	.	.
Mol01616	Mature miRNA	hsa-miR-193a-3p	microRNA 193a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384882.1, MIR193A-201, 88"	AACUGGCCUACAAAGUCCCAGU	.	.	.	HGNC:31563	.	.	ENSG00000207614	.	MIMAT0000459	"hsa-mir-193a,MI0000487,chr17:31559996-31560083(+),chr17:31560050-31560071(+)"	.	.
Mol01617	Mature miRNA	hsa-miR-194-5p	microRNA 194-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384892.1, MIR194-1-201, 85"	UGUAACAGCAACUCCAUGUGGA	.	.	.	HGNC:31564	.	.	ENSG00000207624	.	MIMAT0000460	"hsa-mir-194-1,MI0000488,chr1:220118157-220118241(-),chr1:220118206-220118227(-); hsa-mir-194-2,MI0000732,chr11:64891355-64891439(-),chr11:64891404-64891425(-)"	.	.
Mol01618	Mature miRNA	hsa-miR-195-5p	microRNA 195	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385194.1, MIR195-201, 87"	UAGCAGCACAGAAAUAUUGGC	.	.	.	HGNC:31566	.	.	ENSG00000284112	.	MIMAT0000461	"hsa-mir-195,MI0000489,chr17:7017615-7017701(-),chr17:7017667-7017687(-)"	.	.
Mol01619	Mature miRNA	hsa-miR-206	microRNA 206	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384872.3, MIR206-201, 86"	UGGAAUGUAAGGAAGUGUGUGG	.	.	.	HGNC:31584	.	.	ENSG00000207604	.	MIMAT0000462	"hsa-mir-206,MI0000490,chr6:52144349-52144434(+),chr6:52144401-52144422(+)"	.	.
Mol01620	Mature miRNA	hsa-miR-200c-3p	microRNA 200c	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384980.3, MIR200C-201, 68"	UAAUACUGCCGGGUAAUGAUGGA	.	.	.	HGNC:31580	.	.	ENSG00000207713	.	MIMAT0000617	"hsa-mir-200c,MI0000650,chr12:6963699-6963766(+),chr12:6963742-6963764(+)"	.	.
Mol01621	Mature miRNA	hsa-miR-155-5p	microRNA 155	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385060.1, MIR155-201, 65"	UUAAUGCUAAUCGUGAUAGGGGUU	.	.	.	HGNC:31542	.	.	ENSG00000283904	.	MIMAT0000646	"hsa-mir-155,MI0000681,chr21:25573980-25574044(+),chr21:25573983-25574006(+)"	.	.
Mol01622	Mature miRNA	hsa-miR-106b-5p	microRNA 106b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385301.1, MIR106B-201, 82"	UAAAGUGCUGACAGUGCAGAU	.	.	.	HGNC:31495	.	.	ENSG00000208036	.	MIMAT0000680	"hsa-mir-106b,MI0000734,chr7:100093993-100094074(-),chr7:100094043-100094063(-)"	.	.
Mol01623	Mature miRNA	hsa-miR-29c-3p	microRNA 29c	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385231.3, MIR29C-201, 88"	UAGCACCAUUUGAAAUCGGUUA	.	.	.	HGNC:31621	.	.	ENSG00000284214	.	MIMAT0000681	"hsa-mir-29c,MI0000735,chr1:207801852-207801939(-),chr1:207801865-207801886(-)"	.	.
Mol01624	Mature miRNA	hsa-miR-200a-3p	microRNA 200a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384875.3, MIR200A-201, 90"	UAACACUGUCUGGUAACGAUGU	.	.	.	HGNC:31578	.	.	ENSG00000207607	.	MIMAT0000682	"hsa-mir-200a,MI0000737,chr1:1167863-1167952(+),chr1:1167916-1167937(+)"	.	.
Mol01625	Mature miRNA	hsa-miR-34c-5p	microRNA 34c	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384831.3, MIR34C-201, 77"	AGGCAGUGUAGUUAGCUGAUUGC	.	.	.	HGNC:31637	.	.	ENSG00000207562	.	MIMAT0000686	"hsa-mir-34c,MI0000743,chr11:111513439-111513515(+),chr11:111513451-111513473(+)"	.	.
Mol01626	Mature miRNA	hsa-miR-299-3p	microRNA 299	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385016.4, MIR299-201, 63"	UAUGUGGGAUGGUAAACCGCUU	.	.	.	HGNC:31618	.	.	ENSG00000207749	.	MIMAT0000687	"hsa-mir-299,MI0000744,chr14:101023794-101023856(+),chr14:101023832-101023853(+)"	.	.
Mol01627	Mature miRNA	hsa-miR-365a-3p	microRNA 365a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362260.3, MIR365A-201, 87"	UAAUGCCCCUAAAAAUCCUUAU	.	.	.	HGNC:33692	.	.	ENSG00000199130	.	MIMAT0000710	"hsa-mir-365a,MI0000767,chr16:14309285-14309371(+),chr16:14309340-14309361(+)"	.	.
Mol01628	Mature miRNA	hsa-miR-367-3p	microRNA 367	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362299.1, MIR367-201, 68"	AAUUGCACUUUAGCAAUGGUGA	.	.	.	HGNC:31781	.	.	ENSG00000199169	.	MIMAT0000719	"hsa-mir-367,MI0000775,chr4:112647874-112647941(-),chr4:112647877-112647898(-)"	.	.
Mol01629	Mature miRNA	hsa-miR-369-3p	microRNA 369	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362155.4, MIR369-201, 70"	AAUAAUACAUGGUUGAUCUUU	.	.	.	HGNC:31783	.	.	ENSG00000199025	.	MIMAT0000721	"hsa-mir-369,MI0000777,chr14:101065598-101065667(+),chr14:101065641-101065661(+)"	.	.
Mol01630	Mature miRNA	hsa-miR-370-3p	microRNA 370	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362135.4, MIR370-201, 75"	GCCUGCUGGGGUGGAACCUGGU	.	.	.	HGNC:31784	.	.	ENSG00000199005	.	MIMAT0000722	"hsa-mir-370,MI0000778,chr14:100911139-100911213(+),chr14:100911186-100911207(+)"	.	.
Mol01631	Mature miRNA	hsa-miR-373-3p	microRNA 373	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362273.1, MIR373-201, 69"	GAAGUGCUUCGAUUUUGGGGUGU	.	.	.	HGNC:31787	.	.	ENSG00000199143	.	MIMAT0000726	"hsa-mir-373,MI0000781,chr19:53788705-53788773(+),chr19:53788748-53788770(+)"	.	.
Mol01632	Mature miRNA	hsa-miR-378a-3p	microRNA 378a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362177.3, MIR378A-201, 66"	ACUGGACUUGGAGUCAGAAGGC	.	.	.	HGNC:31871	.	.	ENSG00000199047	.	MIMAT0000732	"hsa-mir-378a,MI0000786,chr5:149732825-149732890(+),chr5:149732867-149732888(+)"	.	.
Mol01633	Mature miRNA	hsa-miR-381-3p	microRNA 381	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362150.3, MIR381-201, 75"	UAUACAAGGGCAAGCUCUCUGU	.	.	.	HGNC:31874	.	.	ENSG00000199020	.	MIMAT0000736	"hsa-mir-381,MI0000789,chr14:101045920-101045994(+),chr14:101045968-101045989(+)"	.	.
Mol01634	Mature miRNA	hsa-miR-383-5p	microRNA 383	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362257.1, MIR383-201, 73"	AGAUCAGAAGGUGAUUGUGGCU	.	.	.	HGNC:31876	.	.	ENSG00000199127	.	MIMAT0000738	"hsa-mir-383,MI0000791,chr8:14853438-14853510(-),chr8:14853483-14853504(-)"	.	.
Mol01635	Mature miRNA	hsa-miR-342-3p	microRNA 342	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362212.1, MIR342-201, 99"	UCUCACACAGAAAUCGCACCCGU	.	.	.	HGNC:31778	.	.	ENSG00000199082	.	MIMAT0000753	"hsa-mir-342,MI0000805,chr14:100109655-100109753(+),chr14:100109715-100109737(+)"	.	.
Mol01636	Mature miRNA	hsa-miR-337-3p	microRNA 337	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362281.3, MIR337-201, 93"	CUCCUAUAUGAUGCCUUUCUUC	.	.	.	HGNC:31774	.	.	ENSG00000199151	.	MIMAT0000754	"hsa-mir-337,MI0000806,chr14:100874493-100874585(+),chr14:100874553-100874574(+)"	.	.
Mol01637	Mature miRNA	hsa-miR-326	microRNA 326	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362220.1, MIR326-201, 95"	CCUCUGGGCCCUUCCUCCAG	.	.	.	HGNC:31769	.	.	ENSG00000199090	.	MIMAT0000756	"hsa-mir-326,MI0000808,chr11:75335092-75335186(-),chr11:75335108-75335127(-)"	.	.
Mol01638	Mature miRNA	hsa-miR-151a-3p	microRNA 151a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000521276.3, MIR151A-201, 90"	CUAGACUGAAGCUCCUUGAGG	.	.	.	HGNC:31762	.	.	ENSG00000254324	.	MIMAT0000757	"hsa-mir-151a,MI0000809,chr8:140732564-140732653(-),chr8:140732587-140732607(-)"	.	.
Mol01639	Mature miRNA	hsa-miR-135b-5p	microRNA 135b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362189.3, MIR135B-201, 97"	UAUGGCUUUUCAUUCCUAUGUGA	.	.	.	HGNC:31760	.	.	ENSG00000199059	.	MIMAT0000758	"hsa-mir-135b,MI0000810,chr1:205448302-205448398(-),chr1:205448361-205448383(-)"	.	.
Mol01640	Mature miRNA	hsa-miR-324-5p	microRNA 324	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362183.3, MIR324-201, 83"	CGCAUCCCCUAGGGCAUUGGUG	.	.	.	HGNC:31767	.	.	ENSG00000199053	.	MIMAT0000761	"hsa-mir-324,MI0000813,chr17:7223297-7223379(-),chr17:7223343-7223364(-)"	.	.
Mol01641	Mature miRNA	hsa-miR-338-3p	microRNA 338	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000636369.1, MIR338-201, 67"	UCCAGCAUCAGUGAUUUUGUUG	.	.	.	HGNC:31775	.	.	ENSG00000283604	.	MIMAT0000763	"hsa-mir-338,MI0000814,chr17:81125883-81125949(-),chr17:81125887-81125908(-)"	.	.
Mol01642	Mature miRNA	hsa-miR-335-5p	microRNA 335	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362173.1, MIR335-201, 94"	UCAAGAGCAAUAACGAAAAAUGU	.	.	.	HGNC:31773	.	.	ENSG00000199043	.	MIMAT0000765	"hsa-mir-335,MI0000816,chr7:130496111-130496204(+),chr7:130496126-130496148(+)"	.	.
Mol01643	Mature miRNA	hsa-miR-133b	microRNA 133b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362210.1, MIR133B-201, 119"	UUUGGUCCCCUUCAACCAGCUA	.	.	.	HGNC:31759	.	.	ENSG00000199080	.	MIMAT0000770	"hsa-mir-133b,MI0000822,chr6:52148923-52149041(+),chr6:52148988-52149009(+)"	.	.
Mol01644	Mature miRNA	hsa-miR-346	microRNA 346	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362234.2, MIR346-201, 95"	UGUCUGCCCGCAUGCCUGCCUCU	.	.	.	HGNC:31780	.	.	ENSG00000199104	.	MIMAT0000773	"hsa-mir-346,MI0000826,chr10:86264694-86264788(-),chr10:86264747-86264769(-)"	.	.
Mol01645	Mature miRNA	hsa-miR-196b-5p	microRNA 196b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384852.2, MIR196B-201, 84"	UAGGUAGUUUCCUGUUGUUGGG	.	.	.	HGNC:31790	.	.	ENSG00000283745	.	MIMAT0001080	"hsa-mir-196b,MI0001150,chr7:27169480-27169563(-),chr7:27169528-27169549(-)"	.	.
Mol01646	Mature miRNA	hsa-miR-422a	microRNA 422a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362286.1, MIR422A-201, 90"	ACUGGACUUAGGGUCAGAAGGC	.	.	.	HGNC:31879	.	.	ENSG00000199156	.	MIMAT0001339	"hsa-mir-422a,MI0001444,chr15:63870930-63871019(-),chr15:63870989-63871010(-)"	.	.
Mol01647	Mature miRNA	hsa-miR-425-3p	microRNA 425	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362162.1, MIR425-201, 87"	AUCGGGAAUGUCGUGUCCGCCC	.	.	.	HGNC:31882	.	.	ENSG00000199032	.	MIMAT0001343	"hsa-mir-425,MI0001448,chr3:49020148-49020234(-),chr3:49020159-49020180(-)"	.	.
Mol01648	Mature miRNA	hsa-miR-429	microRNA 429	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362106.1, MIR429-201, 83"	UAAUACUGUCUGGUAAAACCGU	.	.	.	HGNC:13784	.	.	ENSG00000198976	.	MIMAT0001536	"hsa-mir-429,MI0001641,chr1:1169005-1169087(+),chr1:1169055-1169076(+)"	.	.
Mol01649	Mature miRNA	hsa-miR-449a	microRNA 449a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362113.1, MIR449A-201, 91"	UGGCAGUGUAUUGUUAGCUGGU	.	.	.	HGNC:27645	.	.	ENSG00000198983	.	MIMAT0001541	"hsa-mir-449a,MI0001648,chr5:55170532-55170622(-),chr5:55170586-55170607(-)"	.	.
Mol01650	Mature miRNA	hsa-miR-433-3p	microRNA 433	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384837.2, MIR433-201, 93"	AUCAUGAUGGGCUCCUCGGUGU	.	.	.	HGNC:32026	.	.	ENSG00000207569	.	MIMAT0001627	"hsa-mir-433,MI0001723,chr14:100881886-100881978(+),chr14:100881949-100881970(+)"	.	.
Mol01651	Mature miRNA	hsa-miR-451a	microRNA 451a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385059.1, MIR451A-201, 72"	AAACCGUUACCAUUACUGAGUU	.	.	.	HGNC:32053	.	.	ENSG00000284565	.	MIMAT0001631	"hsa-mir-451a,MI0001729,chr17:28861369-28861440(-),chr17:28861403-28861424(-)"	.	.
Mol01652	Mature miRNA	hsa-miR-409-3p	microRNA 409	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362237.3, MIR409-201, 79"	GAAUGUUGCUCGGUGAACCCCU	.	.	.	HGNC:32055	.	.	ENSG00000199107	.	MIMAT0001639	"hsa-mir-409,MI0001735,chr14:101065300-101065378(+),chr14:101065346-101065367(+)"	.	.
Mol01653	Mature miRNA	hsa-miR-483-3p	microRNA 483	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385070.3, MIR483-201, 76"	UCACUCCUCUCCUCCCGUCUU	.	.	.	HGNC:32340	.	.	ENSG00000207805	.	MIMAT0002173	"hsa-mir-483,MI0002467,chr11:2134134-2134209(-),chr11:2134142-2134162(-)"	.	.
Mol01654	Mature miRNA	hsa-miR-484	microRNA 484	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000606601.3, MIR484-201, 79"	UCAGGCUCAGUCCCCUCCCGAU	.	.	.	HGNC:32341	.	.	ENSG00000283736	.	MIMAT0002174	"hsa-mir-484,MI0002468,chr16:15643294-15643372(+),chr16:15643301-15643322(+)"	.	.
Mol01655	Mature miRNA	hsa-miR-485-5p	microRNA 485	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385292.4, MIR485-201, 73"	AGAGGCUGGCCGUGAUGAAUUC	.	.	.	HGNC:32067	.	.	ENSG00000208027	.	MIMAT0002175	"hsa-mir-485,MI0002469,chr14:101055419-101055491(+),chr14:101055427-101055448(+)"	.	.
Mol01656	Mature miRNA	hsa-miR-485-3p	microRNA 485	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385292.4, MIR485-201, 73"	GUCAUACACGGCUCUCCUCUCU	.	.	.	HGNC:32067	.	.	ENSG00000208027	.	MIMAT0002176	"hsa-mir-485,MI0002469,chr14:101055419-101055491(+),chr14:101055464-101055485(+)"	.	.
Mol01657	Mature miRNA	hsa-miR-486-5p	microRNA 486-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000612171.2, MIR486-1-201, 68"	UCCUGUACUGAGCUGCCCCGAG	.	.	.	HGNC:32342	.	.	ENSG00000274705	.	MIMAT0002177	"hsa-mir-486-1,MI0002470,chr8:41660441-41660508(-),chr8:41660484-41660505(-); hsa-mir-486-2,MI0023622,chr8:41660444-41660507(+),chr8:41660444-41660465(+)"	.	.
Mol01658	Mature miRNA	hsa-miR-490-3p	microRNA 490	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384865.1, MIR490-201, 128"	CAACCUGGAGGACUCCAUGCUG	.	.	.	HGNC:32075	.	.	ENSG00000207597	.	MIMAT0002806	"hsa-mir-490,MI0003125,chr7:136903167-136903294(+),chr7:136903242-136903263(+)"	.	.
Mol01659	Mature miRNA	hsa-miR-146b-5p	microRNA 146b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000365699.4, MIR146B-201, 73"	UGAGAACUGAAUUCCAUAGGCUG	.	.	.	HGNC:32079	.	.	ENSG00000202569	.	MIMAT0002809	"hsa-mir-146b,MI0003129,chr10:102436512-102436584(+),chr10:102436520-102436542(+)"	.	.
Mol01660	Mature miRNA	hsa-miR-494-3p	microRNA 494	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000349529.4, MIR494-201, 81"	UGAAACAUACACGGGAAACCUC	.	.	.	HGNC:32084	.	.	ENSG00000194717	.	MIMAT0002816	"hsa-mir-494,MI0003134,chr14:101029634-101029714(+),chr14:101029681-101029702(+)"	.	.
Mol01661	Mature miRNA	hsa-miR-193b-3p	microRNA 193b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384907.1, MIR193B-201, 83"	AACUGGCCCUCAAAGUCCCGCU	.	.	.	HGNC:32087	.	.	ENSG00000207639	.	MIMAT0002819	"hsa-mir-193b,MI0003137,chr16:14303967-14304049(+),chr16:14304017-14304038(+)"	.	.
Mol01662	Mature miRNA	hsa-miR-519b-3p	microRNA 519b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385090.1, MIR519B-201, 81"	AAAGUGCAUCCUUUUAGAGGUU	.	.	.	HGNC:32101	.	.	ENSG00000207825	.	MIMAT0002837	"hsa-mir-519b,MI0003151,chr19:53695213-53695293(+),chr19:53695263-53695284(+)"	.	.
Mol01663	Mature miRNA	hsa-miR-520c-3p	microRNA 520c	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385005.1, MIR520C-201, 87"	AAAGUGCUUCCUUUUAGAGGGU	.	.	.	HGNC:32108	.	.	ENSG00000207738	.	MIMAT0002846	"hsa-mir-520c,MI0003158,chr19:53707453-53707539(+),chr19:53707506-53707527(+)"	.	.
Mol01664	Mature miRNA	hsa-miR-524-5p	microRNA 524	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385242.3, MIR524-201, 87"	CUACAAAGGGAAGCACUUUCUC	.	.	.	HGNC:32110	.	.	ENSG00000283289	.	MIMAT0002849	"hsa-mir-524,MI0003160,chr19:53711002-53711088(+),chr19:53711017-53711038(+)"	.	.
Mol01665	Mature miRNA	hsa-miR-520h	microRNA 520h	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385126.1, MIR520H-201, 88"	ACAAAGUGCUUCCCUUUAGAGU	.	.	.	HGNC:32125	.	.	ENSG00000207861	.	MIMAT0002867	"hsa-mir-520h,MI0003175,chr19:53742512-53742599(+),chr19:53742566-53742587(+)"	.	.
Mol01666	Mature miRNA	hsa-miR-503-5p	microRNA 503	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385270.1, MIR503-201, 71"	UAGCAGCGGGAACAGUUCUGCAG	.	.	.	HGNC:32138	.	.	ENSG00000208005	.	MIMAT0002874	"hsa-mir-503,MI0003188,chrX:134546328-134546398(-),chrX:134546371-134546393(-)"	.	.
Mol01667	Mature miRNA	hsa-miR-506-3p	microRNA 506	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384998.1, MIR506-201, 124"	UAAGGCACCCUUCUGAGUAGA	.	.	.	HGNC:32143	.	.	ENSG00000207731	.	MIMAT0002878	"hsa-mir-506,MI0003193,chrX:147230720-147230843(-),chrX:147230753-147230773(-)"	.	.
Mol01668	Mature miRNA	hsa-miR-509-3p	microRNA 509-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385265.1, MIR509-1-201, 94"	UGAUUGGUACGUCUGUGGGUAG	.	.	.	HGNC:32146	.	.	ENSG00000208000	.	MIMAT0002881	"hsa-mir-509-1,MI0003196,chrX:147260532-147260625(-),chrX:147260550-147260571(-); hsa-mir-509-2,MI0005530,chrX:147258760-147258850(-),chrX:147258775-147258796(-); hsa-mir-509-3,MI0005717,chrX:147259652-147259726(-),chrX:147259662-147259683(-)"	.	.
Mol01669	Mature miRNA	hsa-miR-299-5p	microRNA 299	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385016.4, MIR299-201, 63"	UGGUUUACCGUCCCACAUACAU	.	.	.	HGNC:31618	.	.	ENSG00000207749	.	MIMAT0002890	"hsa-mir-299,MI0000744,chr14:101023794-101023856(+),chr14:101023800-101023821(+)"	.	.
Mol01670	Mature miRNA	hsa-miR-574-3p	microRNA 574	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385209.1, MIR574-201, 96"	CACGCUCAUGCACACACCCACA	.	.	.	HGNC:32830	.	.	ENSG00000207944	.	MIMAT0003239	"hsa-mir-574,MI0003581,chr4:38868032-38868127(+),chr4:38868092-38868113(+)"	.	.
Mol01671	Mature miRNA	hsa-miR-577	microRNA 577	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385196.1, MIR577-201, 96"	UAGAUAAAAUAUUGGUACCUG	.	.	.	HGNC:32833	.	.	ENSG00000207931	.	MIMAT0003242	"hsa-mir-577,MI0003584,chr4:114656759-114656854(+),chr4:114656774-114656794(+)"	.	.
Mol01672	Mature miRNA	hsa-miR-582-5p	microRNA 582	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000365731.4, MIR582-201, 98"	UUACAGUUGUUCAACCAGUUACU	.	.	.	HGNC:32838	.	.	ENSG00000202601	.	MIMAT0003247	"hsa-mir-582,MI0003589,chr5:59703606-59703703(-),chr5:59703666-59703688(-)"	.	.
Mol01673	Mature miRNA	hsa-miR-587	microRNA 587	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384845.1, MIR587-201, 96"	UUUCCAUAGGUGAUGAGUCAC	.	.	.	HGNC:32843	.	.	ENSG00000207577	.	MIMAT0003253	"hsa-mir-587,MI0003595,chr6:106784125-106784220(+),chr6:106784140-106784160(+)"	.	.
Mol01674	Mature miRNA	hsa-miR-590-5p	microRNA 590	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385008.1, MIR590-201, 97"	GAGCUUAUUCAUAAAAGUGCAG	.	.	.	HGNC:32846	.	.	ENSG00000207741	.	MIMAT0003258	"hsa-mir-590,MI0003602,chr7:74191198-74191294(+),chr7:74191213-74191234(+)"	.	.
Mol01675	Mature miRNA	hsa-miR-591	microRNA 591	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385290.1, MIR591-201, 95"	AGACCAUGGGUUCUCAUUGU	.	.	.	HGNC:32847	.	.	ENSG00000208025	.	MIMAT0003259	"hsa-mir-591,MI0003603,chr7:96219662-96219756(-),chr7:96219722-96219741(-)"	.	.
Mol01676	Mature miRNA	hsa-miR-595	microRNA 595	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384905.1, MIR595-201, 96"	GAAGUGUGCCGUGGUGUGUCU	.	.	.	HGNC:32851	.	.	ENSG00000207637	.	MIMAT0003263	"hsa-mir-595,MI0003607,chr7:158532718-158532813(-),chr7:158532733-158532753(-)"	.	.
Mol01677	Mature miRNA	hsa-miR-613	microRNA 613	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385248.1, MIR613-201, 95"	AGGAAUGUUCCUUCUUUGCC	.	.	.	HGNC:32869	.	.	ENSG00000207983	.	MIMAT0003281	"hsa-mir-613,MI0003626,chr12:12764649-12764743(+),chr12:12764709-12764728(+)"	.	.
Mol01678	Mature miRNA	hsa-miR-620	microRNA 620	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385232.1, MIR620-201, 95"	AUGGAGAUAGAUAUAGAAAU	.	.	.	HGNC:32876	.	.	ENSG00000207967	.	MIMAT0003289	"hsa-mir-620,MI0003634,chr12:116148560-116148654(-),chr12:116148575-116148594(-)"	.	.
Mol01679	Mature miRNA	hsa-miR-623	microRNA 623	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384986.1, MIR623-201, 98"	AUCCCUUGCAGGGGCUGUUGGGU	.	.	.	HGNC:32879	.	.	ENSG00000207719	.	MIMAT0003292	"hsa-mir-623,MI0003637,chr13:99356131-99356228(+),chr13:99356146-99356168(+)"	.	.
Mol01680	Mature miRNA	hsa-miR-630	microRNA 630	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384957.1, MIR630-201, 97"	AGUAUUCUGUACCAGGGAAGGU	.	.	.	HGNC:32886	.	.	ENSG00000283798	.	MIMAT0003299	"hsa-mir-630,MI0003644,chr15:72587217-72587313(+),chr15:72587277-72587298(+)"	.	.
Mol01681	Mature miRNA	hsa-miR-631	microRNA 631	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384904.1, MIR631-201, 75"	AGACCUGGCCCAGACCUCAGC	.	.	.	HGNC:32887	.	.	ENSG00000284343	.	MIMAT0003300	"hsa-mir-631,MI0003645,chr15:75353611-75353685(-),chr15:75353650-75353670(-)"	.	.
Mol01682	Mature miRNA	hsa-miR-33b-5p	microRNA 33b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385104.1, MIR33B-201, 96"	GUGCAUUGCUGUUGCAUUGC	.	.	.	HGNC:32791	.	.	ENSG00000207839	.	MIMAT0003301	"hsa-mir-33b,MI0003646,chr17:17813836-17813931(-),chr17:17813897-17813916(-)"	.	.
Mol01683	Mature miRNA	hsa-miR-633	microRNA 33b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385104.1, MIR33B-201, 96"	CUAAUAGUAUCUACCACAAUAAA	.	.	.	HGNC:32791	.	.	ENSG00000207839	.	MIMAT0003303	"hsa-mir-633,MI0003648,chr17:62944215-62944312(+),chr17:62944275-62944297(+)"	.	.
Mol01684	Mature miRNA	hsa-miR-634	microRNA 634	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385208.1, MIR634-201, 97"	AACCAGCACCCCAACUUUGGAC	.	.	.	HGNC:32890	.	.	ENSG00000207943	.	MIMAT0003304	"hsa-mir-634,MI0003649,chr17:66787072-66787168(+),chr17:66787132-66787153(+)"	.	.
Mol01685	Mature miRNA	hsa-miR-638	microRNA 638	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385237.1, MIR638-201, 100"	AGGGAUCGCGGGCGGGUGGCGGCCU	.	.	.	HGNC:32894	.	.	ENSG00000207972	.	MIMAT0003308	"hsa-mir-638,MI0003653,chr19:10718404-10718503(+),chr19:10718419-10718443(+)"	.	.
Mol01686	Mature miRNA	hsa-miR-644a	microRNA 644a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385262.1, MIR644A-201, 94"	AGUGUGGCUUUCUUAGAGC	.	.	.	HGNC:32900	.	.	ENSG00000207997	.	MIMAT0003314	"hsa-mir-644a,MI0003659,chr20:34466325-34466418(+),chr20:34466385-34466403(+)"	.	.
Mol01687	Mature miRNA	hsa-miR-645	microRNA 645	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385283.1, MIR645-201, 94"	UCUAGGCUGGUACUGCUGA	.	.	.	HGNC:32901	.	.	ENSG00000208018	.	MIMAT0003315	"hsa-mir-645,MI0003660,chr20:50585786-50585879(+),chr20:50585846-50585864(+)"	.	.
Mol01688	Mature miRNA	hsa-miR-647	microRNA 647	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384823.1, MIR647-201, 96"	GUGGCUGCACUCACUUCCUUC	.	.	.	HGNC:32903	.	.	ENSG00000207554	.	MIMAT0003317	"hsa-mir-647,MI0003662,chr20:63942631-63942726(-),chr20:63942691-63942711(-)"	.	.
Mol01689	Mature miRNA	hsa-miR-650	microRNA 650	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385101.1, MIR650-201, 96"	AGGAGGCAGCGCUCUCAGGAC	.	.	.	HGNC:32906	.	.	ENSG00000284049	.	MIMAT0003320	"hsa-mir-650,MI0003665,chr22:22822776-22822871(+),chr22:22822791-22822811(+)"	.	.
Mol01690	Mature miRNA	hsa-miR-662	microRNA 662	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384847.1, MIR662-201, 95"	UCCCACGUUGUGGCCCAGCAG	.	.	.	HGNC:32918	.	.	ENSG00000207579	.	MIMAT0003325	"hsa-mir-662,MI0003670,chr16:770183-770277(+),chr16:770243-770263(+)"	.	.
Mol01691	Mature miRNA	hsa-miR-663a	microRNA 663a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385250.1, MIR663A-201, 93"	AGGCGGGGCGCCGCGGGACCGC	.	.	.	HGNC:32919	.	.	ENSG00000284419	.	MIMAT0003326	"hsa-mir-663a,MI0003672,chr20:26208186-26208278(-),chr20:26208243-26208264(-)"	.	.
Mol01692	Mature miRNA	hsa-miR-654-5p	microRNA 654	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385199.1, MIR654-201, 81"	UGGUGGGCCGCAGAACAUGUGC	.	.	.	HGNC:32910	.	.	ENSG00000207934	.	MIMAT0003330	"hsa-mir-654,MI0003676,chr14:101040219-101040299(+),chr14:101040234-101040255(+)"	.	.
Mol01693	Mature miRNA	hsa-miR-660-5p	microRNA 660	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385235.3, MIR660-201, 97"	UACCCAUUGCAUAUCGGAGUUG	.	.	.	HGNC:32916	.	.	ENSG00000207970	.	MIMAT0003338	"hsa-mir-660,MI0003684,chrX:50013241-50013337(+),chrX:50013256-50013277(+)"	.	.
Mol01694	Mature miRNA	hsa-miR-421	microRNA 421	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000365696.4, MIR421-201, 85"	AUCAACAGACAUUAAUUGGGCGC	.	.	.	HGNC:32793	.	.	ENSG00000202566	.	MIMAT0003339	"hsa-mir-421,MI0003685,chrX:74218377-74218461(-),chrX:74218392-74218414(-)"	.	.
Mol01695	Mature miRNA	hsa-miR-542-3p	microRNA 542	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385050.3, MIR542-201, 97"	UGUGACAGAUUGAUAACUGAAA	.	.	.	HGNC:32534	.	.	ENSG00000207784	.	MIMAT0003389	"hsa-mir-542,MI0003686,chrX:134541341-134541437(-),chrX:134541364-134541385(-)"	.	.
Mol01696	Mature miRNA	hsa-miR-425-5p	microRNA 425	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362162.1, MIR425-201, 87"	AAUGACACGAUCACUCCCGUUGA	.	.	.	HGNC:31882	.	.	ENSG00000199032	.	MIMAT0003393	"hsa-mir-425,MI0001448,chr3:49020148-49020234(-),chr3:49020199-49020221(-)"	.	.
Mol01697	Mature miRNA	hsa-miR-454-3p	microRNA 454	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390180.1, MIR454-201, 115"	UAGUGCAAUAUUGCUUAUAGGGU	.	.	.	HGNC:33137	.	.	ENSG00000211514	.	MIMAT0003885	"hsa-mir-454,MI0003820,chr17:59137758-59137872(-),chr17:59137787-59137809(-)"	.	.
Mol01698	Mature miRNA	hsa-miR-769-5p	microRNA 769	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390225.1, MIR769-201, 118"	UGAGACCUCUGGGUUCUGAGCU	.	.	.	HGNC:33138	.	.	ENSG00000211580	.	MIMAT0003886	"hsa-mir-769,MI0003834,chr19:46018932-46019049(+),chr19:46018961-46018982(+)"	.	.
Mol01699	Mature miRNA	hsa-miR-765	microRNA 765	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390226.1, MIR765-201, 114"	UGGAGGAGAAGGAAGGUGAUG	.	.	.	HGNC:33141	.	.	ENSG00000211581	.	MIMAT0003945	"hsa-mir-765,MI0005116,chr1:156936131-156936244(-),chr1:156936156-156936176(-)"	.	.
Mol01700	Mature miRNA	hsa-miR-770-5p	microRNA 770	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390219.1, MIR770-201, 98"	UCCAGUACCACGUGUCAGGGCCA	.	.	.	HGNC:33143	.	.	ENSG00000211574	.	MIMAT0003948	"hsa-mir-770,MI0005118,chr14:100852390-100852487(+),chr14:100852409-100852431(+)"	.	.
Mol01701	Mature miRNA	hsa-miR-675-5p	microRNA 675	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390168.6, MIR675-201, 73"	UGGUGCGGAGAGGGCCCACAGUG	.	.	.	HGNC:33351	.	.	ENSG00000284010	.	MIMAT0004284	"hsa-mir-675,MI0005416,chr11:1996759-1996831(-),chr11:1996800-1996822(-)"	.	.
Mol01702	Mature miRNA	hsa-miR-297	microRNA 297	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401142.1, MIR297-201, 66"	AUGUAUGUGUGCAUGUGCAUG	.	.	.	HGNC:33691	.	.	ENSG00000215961	.	MIMAT0004450	"hsa-mir-297,MI0005775,chr4:110860582-110860647(-),chr4:110860624-110860644(-)"	.	.
Mol01703	Mature miRNA	hsa-miR-19b-1-5p	microRNA 19b-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384829.1, MIR19B1-201, 87"	AGUUUUGCAGGUUUGCAUCCAGC	.	.	.	HGNC:31575	.	.	ENSG00000284375	.	MIMAT0004491	"hsa-mir-19b-1,MI0000074,chr13:91351192-91351278(+),chr13:91351207-91351229(+)"	.	.
Mol01704	Mature miRNA	hsa-miR-21-3p	microRNA 21	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362134.1, MIR21-201, 72"	CAACACCAGUCGAUGGGCUGU	.	.	.	HGNC:31586	.	.	ENSG00000284190	.	MIMAT0004494	"hsa-mir-21,MI0000077,chr17:59841266-59841337(+),chr17:59841311-59841331(+)"	.	.
Mol01705	Mature miRNA	hsa-miR-93-3p	microRNA 93	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385024.1, MIR93-201, 80"	ACUGCUGAGCUAGCACUUCCCG	.	.	.	HGNC:31645	.	.	ENSG00000207757	.	MIMAT0004509	"hsa-mir-93,MI0000095,chr7:100093768-100093847(-),chr7:100093777-100093798(-)"	.	.
Mol01706	Mature miRNA	hsa-miR-106a-3p	microRNA 106a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384870.1, MIR106A-201, 81"	CUGCAAUGUAAGCACUUCUUAC	.	.	.	HGNC:31494	.	.	ENSG00000284157	.	MIMAT0004517	"hsa-mir-106a,MI0000113,chrX:134170198-134170278(-),chrX:134170208-134170229(-)"	.	.
Mol01707	Mature miRNA	hsa-miR-30c-2-3p	microRNA 30c-2	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362224.3, MIR30C2-201, 72"	CUGGGAGAAGGCUGUUUACUCU	.	.	.	HGNC:31627	.	.	ENSG00000199094	.	MIMAT0004550	"hsa-mir-30c-2,MI0000254,chr6:71376960-71377031(-),chr6:71376964-71376985(-)"	.	.
Mol01708	Mature miRNA	hsa-miR-130a-5p	microRNA 130a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385274.1, MIR130A-201, 89"	GCUCUUUUCACAUUGUGCUACU	.	.	.	HGNC:31514	.	.	ENSG00000208009	.	MIMAT0004593	"hsa-mir-130a,MI0000448,chr11:57641198-57641286(+),chr11:57641212-57641233(+)"	.	.
Mol01709	Mature miRNA	hsa-miR-125a-3p	microRNA 125a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385273.1, MIR125A-201, 86"	ACAGGUGAGGUUCUUGGGAGCC	.	.	.	HGNC:31505	.	.	ENSG00000208008	.	MIMAT0004602	"hsa-mir-125a,MI0000469,chr19:51693254-51693339(+),chr19:51693306-51693327(+)"	.	.
Mol01710	Mature miRNA	hsa-miR-188-3p	microRNA 188	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385034.3, MIR188-201, 86"	CUCCCACAUGCAGGGUUUGCA	.	.	.	HGNC:31559	.	.	ENSG00000207768	.	MIMAT0004613	"hsa-mir-188,MI0000484,chrX:50003503-50003588(+),chrX:50003556-50003576(+)"	.	.
Mol01711	Mature miRNA	hsa-miR-193a-5p	microRNA 193a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384882.1, MIR193A-201, 88"	UGGGUCUUUGCGGGCGAGAUGA	.	.	.	HGNC:31563	.	.	ENSG00000207614	.	MIMAT0004614	"hsa-mir-193a,MI0000487,chr17:31559996-31560083(+),chr17:31560016-31560037(+)"	.	.
Mol01712	Mature miRNA	hsa-miR-155-3p	microRNA 155	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385060.1, MIR155-201, 65"	CUCCUACAUAUUAGCAUUAACA	.	.	.	HGNC:31542	.	.	ENSG00000283904	.	MIMAT0004658	"hsa-mir-155,MI0000681,chr21:25573980-25574044(+),chr21:25574022-25574043(+)"	.	.
Mol01713	Mature miRNA	hsa-miR-34b-3p	microRNA 34b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385076.3, MIR34B-201, 84"	CAAUCACUAACUCCACUGCCAU	.	.	.	HGNC:31636	.	.	ENSG00000207811	.	MIMAT0004676	"hsa-mir-34b,MI0000742,chr11:111512938-111513021(+),chr11:111512987-111513008(+)"	.	.
Mol01714	Mature miRNA	hsa-miR-296-3p	microRNA 296	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385215.1, MIR296-201, 80"	GAGGGUUGGGUGGAGGCUCUCC	.	.	.	HGNC:31617	.	.	ENSG00000284040	.	MIMAT0004679	"hsa-mir-296,MI0000747,chr20:58817615-58817694(-),chr20:58817626-58817647(-)"	.	.
Mol01715	Mature miRNA	hsa-miR-340-5p	microRNA 340	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362125.3, MIR340-201, 95"	UUAUAAAGCAAUGAGACUGAUU	.	.	.	HGNC:31777	.	.	ENSG00000198995	.	MIMAT0004692	"hsa-mir-340,MI0000802,chr5:180015303-180015397(-),chr5:180015361-180015382(-)"	.	.
Mol01716	Mature miRNA	hsa-miR-331-5p	microRNA 331	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362302.3, MIR331-201, 94"	CUAGGUAUGGUCCCAGGGAUCC	.	.	.	HGNC:31772	.	.	ENSG00000199172	.	MIMAT0004700	"hsa-mir-331,MI0000812,chr12:95308420-95308513(+),chr12:95308445-95308466(+)"	.	.
Mol01717	Mature miRNA	hsa-miR-335-3p	microRNA 335	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362173.1, MIR335-201, 94"	UUUUUCAUUAUUGCUCCUGACC	.	.	.	HGNC:31773	.	.	ENSG00000199043	.	MIMAT0004703	"hsa-mir-335,MI0000816,chr7:130496111-130496204(+),chr7:130496162-130496183(+)"	.	.
Mol01718	Mature miRNA	hsa-miR-423-5p	microRNA 423	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362201.2, MIR423-201, 94"	UGAGGGGCAGAGAGCGAGACUUU	.	.	.	HGNC:31880	.	.	ENSG00000283935	.	MIMAT0004748	"hsa-mir-423,MI0001445,chr17:30117079-30117172(+),chr17:30117095-30117117(+)"	.	.
Mol01719	Mature miRNA	hsa-miR-424-3p	microRNA 424	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362227.3, MIR424-201, 98"	CAAAACGUGAGGCGCUGCUAU	.	.	.	HGNC:31881	.	.	ENSG00000284231	.	MIMAT0004749	"hsa-mir-424,MI0001446,chrX:134546614-134546711(-),chrX:134546644-134546664(-)"	.	.
Mol01720	Mature miRNA	hsa-miR-20b-3p	microRNA 20b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384977.1, MIR20B-201, 69"	ACUGUAGUAUGGGCACUUCCAG	.	.	.	HGNC:32024	.	.	ENSG00000284043	.	MIMAT0004752	"hsa-mir-20b,MI0001519,chrX:134169809-134169877(-),chrX:134169813-134169834(-)"	.	.
Mol01721	Mature miRNA	hsa-miR-483-5p	microRNA 483	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385070.3, MIR483-201, 76"	AAGACGGGAGGAAAGAAGGGAG	.	.	.	HGNC:32340	.	.	ENSG00000207805	.	MIMAT0004761	"hsa-mir-483,MI0002467,chr11:2134134-2134209(-),chr11:2134181-2134202(-)"	.	.
Mol01722	Mature miRNA	hsa-miR-488-3p	microRNA 488	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000365739.4, MIR488-201, 83"	UUGAAAGGCUAUUUCUUGGUC	.	.	.	HGNC:32073	.	.	ENSG00000202609	.	MIMAT0004763	"hsa-mir-488,MI0003123,chr1:177029363-177029445(-),chr1:177029374-177029394(-)"	.	.
Mol01723	Mature miRNA	hsa-miR-501-3p	microRNA 501	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390204.1, MIR501-201, 84"	AAUGCACCCGGGCAAGGAUUCU	.	.	.	HGNC:32135	.	.	ENSG00000211538	.	MIMAT0004774	"hsa-mir-501,MI0003185,chrX:50009722-50009805(+),chrX:50009772-50009793(+)"	.	.
Mol01724	Mature miRNA	hsa-miR-513a-3p	microRNA 513a-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385138.1, MIR513A1-201, 129"	UAAAUUUCACCUUUCUGAGAAGG	.	.	.	HGNC:32141	.	.	ENSG00000207873	.	MIMAT0004777	"hsa-mir-513a-1,MI0003191,chrX:147213463-147213591(-),chrX:147213498-147213520(-); hsa-mir-513a-2,MI0003192,chrX:147225826-147225952(-),chrX:147225860-147225882(-)"	.	.
Mol01725	Mature miRNA	hsa-miR-508-5p	microRNA 508	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384857.1, MIR508-201, 115"	UACUCCAGAGGGCGUCACUCAUG	.	.	.	HGNC:32145	.	.	ENSG00000207589	.	MIMAT0004778	"hsa-mir-508,MI0003195,chrX:147236913-147237027(-),chrX:147236980-147237002(-)"	.	.
Mol01726	Mature miRNA	hsa-miR-509-5p	microRNA 509-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385265.1, MIR509-1-201, 94"	UACUGCAGACAGUGGCAAUCA	.	.	.	HGNC:32146	.	.	ENSG00000208000	.	MIMAT0004779	"hsa-mir-509-1,MI0003196,chrX:147260532-147260625(-),chrX:147260586-147260606(-); hsa-mir-509-2,MI0005530,chrX:147258760-147258850(-),chrX:147258811-147258831(-)"	.	.
Mol01727	Mature miRNA	hsa-miR-455-3p	microRNA 455	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384993.3, MIR455-201, 96"	GCAGUCCAUGGGCAUAUACAC	.	.	.	HGNC:32344	.	.	ENSG00000207726	.	MIMAT0004784	"hsa-mir-455,MI0003513,chr9:114209434-114209529(+),chr9:114209487-114209507(+)"	.	.
Mol01728	Mature miRNA	hsa-miR-576-3p	microRNA 576	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385253.1, MIR576-201, 98"	AAGAUGUGGAAAAAUUGGAAUC	.	.	.	HGNC:32832	.	.	ENSG00000207988	.	MIMAT0004796	"hsa-mir-576,MI0003583,chr4:109488698-109488795(+),chr4:109488752-109488773(+)"	.	.
Mol01729	Mature miRNA	hsa-miR-589-5p	microRNA 589	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385238.1, MIR589-201, 99"	UGAGAACCACGUCUGCUCUGAG	.	.	.	HGNC:32845	.	.	ENSG00000207973	.	MIMAT0004799	"hsa-mir-589,MI0003599,chr7:5495819-5495917(-),chr7:5495873-5495894(-)"	.	.
Mol01730	Mature miRNA	hsa-miR-625-3p	microRNA 625	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385047.1, MIR625-201, 85"	GACUAUAGAACUUUCCCCCUCA	.	.	.	HGNC:32881	.	.	ENSG00000207781	.	MIMAT0004808	"hsa-mir-625,MI0003639,chr14:65471102-65471186(+),chr14:65471153-65471174(+)"	.	.
Mol01731	Mature miRNA	hsa-miR-628-5p	microRNA 628	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385229.3, MIR628-201, 95"	AUGCUGACAUAUUUACUAGAGG	.	.	.	HGNC:32884	.	.	ENSG00000283891	.	MIMAT0004809	"hsa-mir-628,MI0003642,chr15:55372940-55373034(-),chr15:55372991-55373012(-)"	.	.
Mol01732	Mature miRNA	hsa-miR-33b-3p	microRNA 33b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385104.1, MIR33B-201, 96"	CAGUGCCUCGGCAGUGCAGCCC	.	.	.	HGNC:32791	.	.	ENSG00000207839	.	MIMAT0004811	"hsa-mir-33b,MI0003646,chr17:17813836-17813931(-),chr17:17813857-17813878(-)"	.	.
Mol01733	Mature miRNA	hsa-miR-298	microRNA 298	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401212.1, MIR298-201, 88"	AGCAGAAGCAGGGAGGUUCUCCCA	.	.	.	HGNC:33634	.	.	ENSG00000216031	.	MIMAT0004901	"hsa-mir-298,MI0005523,chr20:58818226-58818313(-),chr20:58818280-58818303(-)"	.	.
Mol01734	Mature miRNA	hsa-miR-450b-5p	microRNA 450b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401182.3, MIR450B-201, 78"	UUUUGCAAUAUGUUCCUGAAUA	.	.	.	HGNC:33642	.	.	ENSG00000216001	.	MIMAT0004909	"hsa-mir-450b,MI0005531,chrX:134540185-134540262(-),chrX:134540231-134540252(-)"	.	.
Mol01735	Mature miRNA	hsa-miR-874-3p	microRNA 874	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401190.3, MIR874-201, 78"	CUGCCCUGGCCCGAGGGACCGA	.	.	.	HGNC:33643	.	.	ENSG00000216009	.	MIMAT0004911	"hsa-mir-874,MI0005532,chr5:137647572-137647649(-),chr5:137647582-137647603(-)"	.	.
Mol01736	Mature miRNA	hsa-miR-891b	microRNA 891b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401245.1, MIR891B-201, 79"	UGCAACUUACCUGAGUCAUUGA	.	.	.	HGNC:33645	.	.	ENSG00000216064	.	MIMAT0004913	"hsa-mir-891b,MI0005534,chrX:146001053-146001131(-),chrX:146001100-146001121(-)"	.	.
Mol01737	Mature miRNA	hsa-miR-876-3p	microRNA 876	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401147.1, MIR876-201, 81"	UGGUGGUUUACAAAGUAAUUCA	.	.	.	HGNC:33653	.	.	ENSG00000215966	.	MIMAT0004925	"hsa-mir-876,MI0005542,chr9:28863626-28863706(-),chr9:28863636-28863657(-)"	.	.
Mol01738	Mature miRNA	hsa-miR-708-3p	microRNA 708	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390708.1, MIR708-201, 88"	CAACUAGACUGUGAGCUUCUAG	.	.	.	HGNC:33654	.	.	ENSG00000211997	.	MIMAT0004927	"hsa-mir-708,MI0005543,chr11:79402022-79402109(-),chr11:79402032-79402053(-)"	.	.
Mol01739	Mature miRNA	hsa-miR-543	microRNA 543	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390751.3, MIR543-201, 78"	AAACAUUCGCGGUGCACUUCUU	.	.	.	HGNC:33664	.	.	ENSG00000212040	.	MIMAT0004954	"hsa-mir-543,MI0005565,chr14:101031987-101032064(+),chr14:101032033-101032054(+)"	.	.
Mol01740	Mature miRNA	hsa-miR-760	microRNA 760	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390220.3, MIR760-201, 80"	CGGCUCUGGGUCUGUGGGGA	.	.	.	HGNC:33666	.	.	ENSG00000211575	.	MIMAT0004957	"hsa-mir-760,MI0005567,chr1:93846832-93846911(+),chr1:93846880-93846899(+)"	.	.
Mol01741	Mature miRNA	hsa-miR-301b-3p	microRNA 301b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390813.1, MIR301B-201, 78"	CAGUGCAAUGAUAUUGUCAAAGC	.	.	.	HGNC:33667	.	.	ENSG00000212102	.	MIMAT0004958	"hsa-mir-301b,MI0005568,chr22:21652981-21653058(+),chr22:21653025-21653047(+)"	.	.
Mol01742	Mature miRNA	hsa-miR-216b-5p	microRNA 216b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390186.2, MIR216B-201, 82"	AAAUCUCUGCAGGCAAAUGUGA	.	.	.	HGNC:33668	.	.	ENSG00000211520	.	MIMAT0004959	"hsa-mir-216b,MI0005569,chr2:56000714-56000795(-),chr2:56000764-56000785(-)"	.	.
Mol01743	Mature miRNA	hsa-miR-935	microRNA 935	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000401179.1, MIR935-201, 91"	CCAGUUACCGCUUCCGCUACCGC	.	.	.	HGNC:33678	.	.	ENSG00000284583	.	MIMAT0004978	"hsa-mir-935,MI0005757,chr19:53982307-53982397(+),chr19:53982362-53982384(+)"	.	.
Mol01744	Mature miRNA	hsa-miR-1236-3p	microRNA 1236	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408340.1, MIR1236-201, 102"	CCUCUUCCCCUUGUCUCUCCAG	.	.	.	HGNC:33925	.	.	ENSG00000284446	.	MIMAT0005591	"hsa-mir-1236,MI0006326,chr6:31956839-31956940(-),chr6:31956839-31956860(-)"	.	.
Mol01745	Mature miRNA	hsa-miR-320c	microRNA 320c-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408566.1, MIR320C1-201, 88"	AAAAGCUGGGUUGAGAGGGU	.	.	.	HGNC:35248	.	.	ENSG00000221493	.	MIMAT0005793	"hsa-mir-320c-1,MI0003778,chr18:21683518-21683589(+),chr18:21683559-21683578(+); hsa-mir-320c-2,MI0008191,chr18:24321675-24321746(+),chr18:24321716-24321735(+)"	.	.
Mol01746	Mature miRNA	hsa-miR-1182	microRNA 1182	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408363.1, MIR1182-201, 97"	GAGGGUCUUGGGAGGGAUGUGAC	.	.	.	HGNC:35263	.	.	ENSG00000283799	.	MIMAT0005827	"hsa-mir-1182,MI0006275,chr1:231019828-231019924(-),chr1:231019841-231019863(-)"	.	.
Mol01747	Mature miRNA	hsa-miR-1183	microRNA 1183	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408856.1, MIR1183-201, 89"	CACUGUAGGUGAUGGUGAGAGUGGGCA	.	.	.	HGNC:35264	.	.	ENSG00000221783	.	MIMAT0005828	"hsa-mir-1183,MI0006276,chr7:21471058-21471146(+),chr7:21471105-21471131(+)"	.	.
Mol01748	Mature miRNA	hsa-miR-663b	microRNA 663b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408361.1, MIR663B-201, 115"	GGUGGCCCGGCCGUGCCUGAGG	.	.	.	HGNC:35270	.	.	ENSG00000221288	.	MIMAT0005867	"hsa-mir-663b,MI0006336,chr2:132256966-132257080(-),chr2:132256970-132256991(-)"	.	.
Mol01749	Mature miRNA	hsa-miR-1204	microRNA 1204	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408388.1, MIR1204-201, 67"	UCGUGGCCUGGUCUCCAUUAU	.	.	.	HGNC:37059	.	.	ENSG00000283710	.	MIMAT0005868	"hsa-mir-1204,MI0006337,chr8:127795962-127796028(+),chr8:127795965-127795985(+)"	.	.
Mol01750	Mature miRNA	hsa-miR-1207-5p	microRNA 1207	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408249.1, MIR1207-201, 87"	UGGCAGGGAGGCUGGGAGGGG	.	.	.	HGNC:35273	.	.	ENSG00000221176	.	MIMAT0005871	"hsa-mir-1207,MI0006340,chr8:128049152-128049238(+),chr8:128049159-128049179(+)"	.	.
Mol01751	Mature miRNA	hsa-miR-1291	microRNA 1291	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000627649.2, MIR1291-201, 87"	UGGCCCUGACUGAAGACCAGCAGU	.	.	.	HGNC:35284	.	.	ENSG00000281842	.	MIMAT0005881	"hsa-mir-1291,MI0006353,chr12:48654444-48654530(-),chr12:48654494-48654517(-)"	.	.
Mol01752	Mature miRNA	hsa-miR-1294	microRNA 1294	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408503.1, MIR1294-201, 142"	UGUGAGGUUGGCAUUGUUGUCU	.	.	.	HGNC:35287	.	.	ENSG00000221430	.	MIMAT0005884	"hsa-mir-1294,MI0006356,chr5:154347106-154347247(+),chr5:154347153-154347174(+)"	.	.
Mol01753	Mature miRNA	hsa-miR-1243	microRNA 1243	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000636083.1, MIR1243-201, 93"	AACUGGAUCAAUUAUAGGAGUG	.	.	.	HGNC:35304	.	.	ENSG00000283193	.	MIMAT0005894	"hsa-mir-1243,MI0006373,chr4:113106863-113106955(+),chr4:113106867-113106888(+)"	.	.
Mol01754	Mature miRNA	hsa-miR-1244	microRNA 1244-1	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000612829.5, MIR1244-1-201, 85"	AAGUAGUUGGUUUGUAUGAGAUGGUU	.	.	.	HGNC:35310	.	.	ENSG00000284378	.	MIMAT0005896	"hsa-mir-1244-1,MI0006379,chr2:231713314-231713398(+),chr2:231713368-231713393(+); hsa-mir-1244-2,MI0015974,chr5:118974586-118974670(+),chr5:118974640-118974665(+); hsa-mir-1244-3,MI0015975,chr12:9239467-9239551(-),chr12:9239472-9239497(-); hsa-mir-1244-4,MI0031511,chr12:12111952-12112036(+),chr12:12112006-12112031(+)"	.	.
Mol01755	Mature miRNA	hsa-miR-1246	microRNA 1246	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000636535.1, MIR1246-201, 73"	AAUGGAUUUUUGGAGCAGG	.	.	.	HGNC:35312	.	.	ENSG00000283203	.	MIMAT0005898	"hsa-mir-1246,MI0006381,chr2:176600980-176601052(-),chr2:176601024-176601042(-)"	.	.
Mol01756	Mature miRNA	hsa-miR-1268a	microRNA 1268a	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408714.1, MIR1268A-201, 52"	CGGGCGUGGUGGUGGGGG	.	.	.	HGNC:35336	.	.	ENSG00000221641	.	MIMAT0005922	"hsa-mir-1268a,MI0006405,chr15:22225278-22225329(-),chr15:22225308-22225325(-)"	.	.
Mol01757	Mature miRNA	hsa-miR-1284	microRNA 1284	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408337.1, MIR1284-201, 120"	UCUAUACAGACCCUGGCUUUUC	.	.	.	HGNC:35362	.	.	ENSG00000221264	.	MIMAT0005941	"hsa-mir-1284,MI0006431,chr3:71541970-71542089(-),chr3:71542039-71542060(-)"	.	.
Mol01758	Mature miRNA	hsa-miR-224-3p	microRNA 224	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000384889.1, MIR224-201, 81"	AAAAUGGUGCCCUAGUGACUACA	.	.	.	HGNC:31604	.	.	ENSG00000284363	.	MIMAT0009198	"hsa-mir-224,MI0000301,chrX:151958578-151958658(-),chrX:151958584-151958606(-)"	.	.
Mol01759	Mature miRNA	hsa-miR-761	microRNA 761	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000390787.2, MIR761-201, 59"	GCAGCAGGGUGAAACUGACACA	.	.	.	HGNC:37305	.	.	ENSG00000283899	.	MIMAT0010364	"hsa-mir-761,MI0003941,chr1:51836344-51836402(-),chr1:51836375-51836396(-)"	.	.
Mol01760	Mature miRNA	hsa-miR-3127-5p	microRNA 3127	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000583925.3, MIR3127-201, 76"	AUCAGGGCUUGUGGAAUGGGAAG	.	.	.	HGNC:38269	.	.	ENSG00000264157	.	MIMAT0014990	"hsa-mir-3127,MI0014144,chr2:96798278-96798353(+),chr2:96798288-96798310(+)"	.	.
Mol01761	Mature miRNA	hsa-miR-3163	microRNA 3163	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000581592.1, MIR3163-201, 73"	UAUAAAAUGAGGGCAGUAAGAC	.	.	.	HGNC:38209	.	.	ENSG00000266423	.	MIMAT0015037	"hsa-mir-3163,MI0014193,chr11:66934434-66934506(-),chr11:66934476-66934497(-)"	.	.
Mol01762	Mature miRNA	hsa-miR-3182	microRNA 3182	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000580839.1, MIR3182-201, 63"	GCUUCUGUAGUGUAGUC	.	.	.	HGNC:38317	.	.	ENSG00000263785	.	MIMAT0015062	"hsa-mir-3182,MI0014224,chr16:83508346-83508408(+),chr16:83508349-83508365(+)"	.	.
Mol01763	Mature miRNA	hsa-miR-3188	microRNA 3188	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000583494.1, MIR3188-201, 85"	AGAGGCUUUGUGCGGAUACGGGG	.	.	.	HGNC:38226	.	.	ENSG00000267959	.	MIMAT0015070	"hsa-mir-3188,MI0014232,chr19:18282077-18282161(+),chr19:18282129-18282151(+)"	.	.
Mol01764	Mature miRNA	hsa-miR-3190-5p	microRNA 3190	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000577414.1, MIR3190-201, 80"	UCUGGCCAGCUACGUCCCCA	.	.	.	HGNC:38190	.	.	ENSG00000265134	.	MIMAT0015073	"hsa-mir-3190,MI0014235,chr19:47226942-47227021(+),chr19:47226955-47226974(+)"	.	.
Mol01765	Mature miRNA	hsa-miR-3609	microRNA 3609	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000582661.1, MIR3609-201, 80"	CAAAGUGAUGAGUAAUACUGGCUG	.	.	.	HGNC:38956	.	.	ENSG00000266019	.	MIMAT0017986	"hsa-mir-3609,MI0015999,chr7:98881650-98881729(+),chr7:98881700-98881723(+)"	.	.
Mol01766	Mature miRNA	hsa-miR-3646	microRNA 3646	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000578301.1, MIR3646-201, 84"	AAAAUGAAAUGAGCCCAGCCCA	.	.	.	HGNC:38935	.	.	ENSG00000266151	.	MIMAT0018065	"hsa-mir-3646,MI0016046,chr20:44408120-44408203(+),chr20:44408177-44408198(+)"	.	.
Mol01767	Mature miRNA	hsa-miR-1268b	microRNA 1268b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000579691.2, MIR1268B-201, 50"	CGGGCGUGGUGGUGGGGGUG	.	.	.	HGNC:41581	.	.	ENSG00000265561	.	MIMAT0018925	"hsa-mir-1268b,MI0016748,chr17:80098828-80098877(+),chr17:80098831-80098850(+)"	.	.
Mol01768	Mature miRNA	hsa-miR-4443	microRNA 4443	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000585052.1, MIR4443-201, 53"	UUGGAGGCGUGGGUUUU	.	.	.	HGNC:41830	.	.	ENSG00000265483	.	MIMAT0018961	"hsa-mir-4443,MI0016786,chr3:48196564-48196616(+),chr3:48196572-48196588(+)"	.	.
Mol01769	Mature miRNA	hsa-miR-5100	microRNA 5100	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000579544.1, MIR5100-201, 119"	UUCAGAUCCCAGCGGUGCCUCU	.	.	.	HGNC:43540	.	.	ENSG00000263795	.	MIMAT0022259	"hsa-mir-5100,MI0019116,chr10:42997563-42997681(+),chr10:42997630-42997651(+)"	.	.
Mol01770	Mature miRNA	hsa-miR-1229-5p	microRNA 1229	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408467.1, MIR1229-201, 69"	GUGGGUAGGGUUUGGGGGAGAGCG	.	.	.	HGNC:33924	.	.	ENSG00000221394	.	MIMAT0022942	"hsa-mir-1229,MI0006319,chr5:179798278-179798346(-),chr5:179798323-179798346(-)"	.	.
Mol01771	Mature miRNA	hsa-miR-153-5p	microRNA 153-2	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385225.1, MIR153-2-201, 87"	UCAUUUUUGUGAUGUUGCAGCU	.	.	.	HGNC:31540	.	.	ENSG00000207960	.	MIMAT0026480	"hsa-mir-153-2,MI0000464,chr7:157574336-157574422(-),chr7:157574387-157574408(-)"	.	.
Mol01772	Mature miRNA	hsa-miR-487b-5p	microRNA 487b	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000385021.3, MIR487B-201, 84"	GUGGUUAUCCCUGUCCUGUUCG	.	.	.	HGNC:32533	.	.	ENSG00000207754	.	MIMAT0026614	"hsa-mir-487b,MI0003530,chr14:101046455-101046538(+),chr14:101046469-101046490(+)"	.	.
Mol01773	Mature miRNA	hsa-miR-6825-5p	microRNA 6825	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000618505.1, MIR6825-201, 66"	UGGGGAGGUGUGGAGUCAGCAU	.	.	.	HGNC:50208	.	.	ENSG00000275067	.	MIMAT0027550	"hsa-mir-6825,MI0022670,chr3:127575266-127575331(-),chr3:127575305-127575326(-)"	.	.
Mol01774	Mature miRNA	hsa-miR-6845-5p	microRNA 6845	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000613182.1, MIR6845-201, 61"	CGGGGCCAGAGCAGAGAGC	.	.	.	HGNC:49956	.	.	ENSG00000284142	.	MIMAT0027590	"hsa-mir-6845,MI0022691,chr8:143837756-143837816(-),chr8:143837793-143837811(-)"	.	.
Mol01775	Mature miRNA	hsa-miR-6886-3p	microRNA 6886	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000619864.1, MIR6886-201, 61"	UGCCCUUCUCUCCUCCUGCCU	.	.	.	HGNC:50121	.	.	ENSG00000284553	.	MIMAT0027673	"hsa-mir-6886,MI0022733,chr19:11113474-11113534(+),chr19:11113511-11113531(+)"	.	.
Mol01776	Circular RNA	hsa_circ_0025202	.	GAPDH	2597	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000229239.10, GAPDH-201, 1285"	.	chr12:6646474-6647162	.	.	HGNC:4141	.	.	ENSG00000111640	.	.	.	hsa_circ_0025202	.
Mol01777	Circular RNA	hsa_circ_0005379	.	GDI2	2665	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000380191.9, GDI2-203, 2297"	.	chr10:5827104-5842668	.	.	HGNC:4227	.	.	ENSG00000057608	.	.	.	hsa_circ_0005379	.
Mol01778	Circular RNA	hsa_circ_0004015	.	CDK14	5218	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	chr7:90355880-90377090	.	.	HGNC:8883	.	.	ENSG00000058091	.	.	.	hsa_circ_0004015	.
Mol01779	Circular RNA	hsa_circ_0001946	.	CDR1	1038	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	chrX:139865339-139866824	.	.	HGNC:1798	.	.	.	.	.	.	hsa_circ_0001946	.
Mol01780	Circular RNA	hsa_circ_0000199	.	AKT3	10000	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	chr1:243708811-243736350	.	.	HGNC:393	.	.	ENSG00000117020	.	.	.	hsa_circ_0000199	.
Mol01781	Circular RNA	hsa_circ_104075	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01782	Circular RNA	hsa_circ_BA9.3	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01783	Circular RNA	hsa_circ_MTO1	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01784	Circular RNA	hsa_circ_PAN3	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01785	Circular RNA	hsa_circ_PVT1	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01786	Piwi-interacting RNA	piR-hsa-54265	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000315396, ODAD1; ENST00000474199, ODAD1; ENST00000504608, ODAD1; ENST00000674207, ODAD1; ENST00000674294, ODAD1"	ATCTGCTGCGGATCGACAGGAACC	.	.	.	.	.	.	.	.	.	.	.	piR-hsa-54265
Mol01787	Piwi-interacting RNA	piR-hsa-39980	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000353267, CREB1; ENST00000425132, METTL21A; ENST00000432329, CREB1; ENST00000432416, METTL21A; ENST00000458426, METTL21A"	AAGAACATATGTGGCCACATTACC	.	.	.	.	.	.	.	.	.	.	.	piR-hsa-39980
Mol01788	Piwi-interacting RNA	piR-hsa-36712	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000247026, NSRP1; ENST00000394826, NSRP1; ENST00000467446, NSRP1; ENST00000475652, NSRP1; ENST00000540900, NSRP1; ENST00000577289, NSRP1; ENST00000580103, NSRP1; ENST00000581048, NSRP1; ENST00000584154, NSRP1; ENST00000584317, NSRP1; ENST00000585881, NSRP1; ENST00000588614, NSRP1; ENST00000589608, NSRP1; ENST00000612959, NSRP1"	AAAAAGAAAGAAATGAATGCTTGGGACCAGAAGT	.	.	.	.	.	.	.	.	.	.	.	piR-hsa-36712
Mol01789	Piwi-interacting RNA	piR-l-138	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01790	LncRNA	Long non-protein coding RNA (AC090952.4.1)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01791	LncRNA	Long non-protein coding RNA (AK022798)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01792	LncRNA	Long non-protein coding RNA (AK126698)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01793	LncRNA	Long non-protein coding RNA (BDLNR)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01794	LncRNA	Long non-protein coding RNA (CCAL)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01795	LncRNA	Long non-protein coding RNA (CILA1)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01796	LncRNA	Long non-protein coding RNA (D63785)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01797	LncRNA	Long non-protein coding RNA (FAM84B-AS)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01798	LncRNA	Long non-protein coding RNA (GBCDRlnc1)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01799	LncRNA	Long non-protein coding RNA (KRAL)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01800	LncRNA	Long non-protein coding RNA (LEIGC)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01801	LncRNA	Long non-protein coding RNA (LINC00515)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01802	LncRNA	Long non-protein coding RNA (Lnc-ATB)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01803	LncRNA	Long non-protein coding RNA (AK123263)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01805	LncRNA	Long non-protein coding RNA (BX537613)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01806	LncRNA	Long non-protein coding RNA (NONHSAT101069)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01807	LncRNA	Long non-protein coding RNA (NRAL)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01808	LncRNA	Long non-protein coding RNA (RP11-134G8.8)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01809	LncRNA	Long non-protein coding RNA (RP11-708H21.4)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01810	LncRNA	Long non-protein coding RNA (RP11-838N2.4)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01811	LncRNA	Long non-protein coding RNA (snaR)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01812	LncRNA	Long non-protein coding RNA (uc.57)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01813	LncRNA	Long non-protein coding RNA (UCA1a)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01814	LncRNA	Long non-protein coding RNA (XLOC_006753)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01815	Mature miRNA	hsa-miR-17-92	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01816	Mature miRNA	hsa-miR-106b~25	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol01817	Protein	HIV1 Protease (HIV1 PR)	Pr160Gag-Pol; MA; CA; SP1; p2; NC; TF; p6*; PR; Retropepsin; Exoribonuclease H; p66 RT; IN	gag-pol	155348	Human immunodeficiency virus type 1	11676	Human immunodeficiency virus 1	Lentivirus	11646	Retroviridae	11632	Ortervirales	2169561	Revtraviricetes	2732514	Artverviricota	2732409	Pararnavirae	2732397	.	PQVTLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNF	.	"Aspartyl protease that mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins"	PDB: 1A30; PDB: 1BV7; PDB: 1BV9; PDB: 1BVE; PDB: 1BVG; PDB: 1BWA; PDB: 1BWB; PDB: 1C0T; PDB: 1C0U; PDB: 1C1B; PDB: 1C1C; PDB: 1DMP; PDB: 1DTQ; PDB: 1DTT; PDB: 1E6J; PDB: 1EP4; PDB: 1ESK; PDB: 1EX4; PDB: 1EXQ; PDB: 1FB7; PDB: 1FK9; PDB: 1FKO; PDB: 1FKP; PDB: 1G6L; PDB: 1HIV; PDB: 1HVH; PDB: 1HVR; PDB: 1HWR; PDB: 1HXB; PDB: 1JKH; PDB: 1JLA; PDB: 1JLB; PDB: 1JLC; PDB: 1JLE; PDB: 1JLF; PDB: 1JLG; PDB: 1JLQ; PDB: 1KLM; PDB: 1LV1; PDB: 1LW0; PDB: 1LW2; PDB: 1LWC; PDB: 1LWE; PDB: 1LWF; PDB: 1NCP; PDB: 1O1W; PDB: 1ODW; PDB: 1ODY; PDB: 1QBR; PDB: 1QBS; PDB: 1QBT; PDB: 1QBU; PDB: 1REV; PDB: 1RT1; PDB: 1RT2; PDB: 1RT3; PDB: 1RT4; PDB: 1RT5; PDB: 1RT6; PDB: 1RT7; PDB: 1RTD; PDB: 1RTH; PDB: 1RTI; PDB: 1RTJ; PDB: 1S1T; PDB: 1S1U; PDB: 1S1V; PDB: 1S1W; PDB: 1S1X; PDB: 1T05; PDB: 1TAM; PDB: 1TKT; PDB: 1TKX; PDB: 1TKZ; PDB: 1TL1; PDB: 1TL3; PDB: 1VRT; PDB: 1VRU; PDB: 2HND; PDB: 2HNY; PDB: 2HNZ; PDB: 2KOD; PDB: 2NPH; PDB: 2OPP; PDB: 2OPQ; PDB: 2OPR; PDB: 2OPS; PDB: 2RF2; PDB: 2RKI; PDB: 2WHH; PDB: 2WOM; PDB: 2WON; PDB: 2YNF; PDB: 2YNG; PDB: 2YNH; PDB: 2YNI; PDB: 3AO2; PDB: 3C6T; PDB: 3C6U; PDB: 3DI6; PDB: 3DLE; PDB: 3DLG; PDB: 3DM2; PDB: 3DMJ; PDB: 3DOK; PDB: 3DOL; PDB: 3DOX; PDB: 3DRP; PDB: 3DRR; PDB: 3DRS; PDB: 3DYA; PDB: 3E01; PDB: 3FFI; PDB: 3I0R; PDB: 3I0S; PDB: 3KJV; PDB: 3KK1; PDB: 3KK2; PDB: 3KK3; PDB: 3KT2; PDB: 3KT5; PDB: 3LAK; PDB: 3LAL; PDB: 3LAM; PDB: 3LAN; PDB: 3LP0; PDB: 3LP1; PDB: 3LP2; PDB: 3M8P; PDB: 3M8Q; PDB: 3MEC; PDB: 3MED; PDB: 3MEE; PDB: 3MEG; PDB: 3N3I; PDB: 3NBP; PDB: 3PHV; PDB: 3QIN; PDB: 3QIO; PDB: 3QIP; PDB: 3T19; PDB: 3T1A; PDB: 3TAM; PDB: 4B3O; PDB: 4B3P; PDB: 4B3Q; PDB: 4I7F; PDB: 4KSE; PDB: 4KV8; PDB: 4NCG; PDB: 4Q1W; PDB: 4Q1X; PDB: 4Q1Y; PDB: 4Q5M; PDB: 4QLH; PDB: 4U1H; PDB: 4U1I; PDB: 4U1J; PDB: 4U7Q; PDB: 4U7V; PDB: 5DGU; PDB: 5DGW; PDB: 5EU7; PDB: 5HRN; PDB: 5HRP; PDB: 5HRR; PDB: 5HRS; PDB: 5IM7; PDB: 5J2M; PDB: 5J2N; PDB: 5J2P; PDB: 5J2Q; PDB: 5K14; PDB: 5KAO; PDB: 5T82; PDB: 5TC2; PDB: 5VZ6; PDB: 5XOS; PDB: 5XOT; PDB: 5YRS; PDB: 6BJ2; PDB: 6BJ3; PDB: 6BSG; PDB: 6BSH; PDB: 6BSI; PDB: 6BSJ; PDB: 6DIF; PDB: 6DIL; PDB: 6DJ1; PDB: 6DJ2; PDB: 6DJ5; PDB: 6DJ7; PDB: 6DV0; PDB: 6DV4; PDB: 6E7J; PDB: 6E9A; PDB: 6EWA; PDB: 6EX9; PDB: 6GL1; PDB: 6J1V; PDB: 6J1W; PDB: 6OR7; PDB: 6OTZ; PDB: 6P1I; PDB: 6P1X; PDB: 6P2G; PDB: 6PYL; PDB: 6SKK; PDB: 6SKM; PDB: 6SKN; PDB: 6SLQ; PDB: 6SLU; PDB: 6SMU; PDB: 6UIR; PDB: 6UIS; PDB: 6UIT; PDB: 6UJX; PDB: 6UJY; PDB: 6UJZ; PDB: 6UK0; PDB: 6VPZ; PDB: 6VQ2; PDB: 6VQD; PDB: 6VQE; PDB: 6VQY; PDB: 6VQZ; PDB: 6WAZ; PDB: 6WB1; PDB: 6WPF; PDB: 6WPH; PDB: 6WPJ	.	POL_HV1H2 (489-587)	Reviewed	.	.	.	.	.	.
Mol01818	Protein	HIV1 Integrase (HIV1 IT)	Pr160Gag-Pol; MA; CA; SP1; p2; NC; TF; p6*; PR; Retropepsin; Exoribonuclease H; p66 RT; IN	gag-pol	155348	Human immunodeficiency virus type 1	11676	Human immunodeficiency virus 1	Lentivirus	11646	Retroviridae	11632	Ortervirales	2169561	Revtraviricetes	2732514	Artverviricota	2732409	Pararnavirae	2732397	.	FLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTGATVRAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED	.	"Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration."	PDB: 1A30; PDB: 1BV7; PDB: 1BV9; PDB: 1BVE; PDB: 1BVG; PDB: 1BWA; PDB: 1BWB; PDB: 1C0T; PDB: 1C0U; PDB: 1C1B; PDB: 1C1C; PDB: 1DMP; PDB: 1DTQ; PDB: 1DTT; PDB: 1E6J; PDB: 1EP4; PDB: 1ESK; PDB: 1EX4; PDB: 1EXQ; PDB: 1FB7; PDB: 1FK9; PDB: 1FKO; PDB: 1FKP; PDB: 1G6L; PDB: 1HIV; PDB: 1HVH; PDB: 1HVR; PDB: 1HWR; PDB: 1HXB; PDB: 1JKH; PDB: 1JLA; PDB: 1JLB; PDB: 1JLC; PDB: 1JLE; PDB: 1JLF; PDB: 1JLG; PDB: 1JLQ; PDB: 1KLM; PDB: 1LV1; PDB: 1LW0; PDB: 1LW2; PDB: 1LWC; PDB: 1LWE; PDB: 1LWF; PDB: 1NCP; PDB: 1O1W; PDB: 1ODW; PDB: 1ODY; PDB: 1QBR; PDB: 1QBS; PDB: 1QBT; PDB: 1QBU; PDB: 1REV; PDB: 1RT1; PDB: 1RT2; PDB: 1RT3; PDB: 1RT4; PDB: 1RT5; PDB: 1RT6; PDB: 1RT7; PDB: 1RTD; PDB: 1RTH; PDB: 1RTI; PDB: 1RTJ; PDB: 1S1T; PDB: 1S1U; PDB: 1S1V; PDB: 1S1W; PDB: 1S1X; PDB: 1T05; PDB: 1TAM; PDB: 1TKT; PDB: 1TKX; PDB: 1TKZ; PDB: 1TL1; PDB: 1TL3; PDB: 1VRT; PDB: 1VRU; PDB: 2HND; PDB: 2HNY; PDB: 2HNZ; PDB: 2KOD; PDB: 2NPH; PDB: 2OPP; PDB: 2OPQ; PDB: 2OPR; PDB: 2OPS; PDB: 2RF2; PDB: 2RKI; PDB: 2WHH; PDB: 2WOM; PDB: 2WON; PDB: 2YNF; PDB: 2YNG; PDB: 2YNH; PDB: 2YNI; PDB: 3AO2; PDB: 3C6T; PDB: 3C6U; PDB: 3DI6; PDB: 3DLE; PDB: 3DLG; PDB: 3DM2; PDB: 3DMJ; PDB: 3DOK; PDB: 3DOL; PDB: 3DOX; PDB: 3DRP; PDB: 3DRR; PDB: 3DRS; PDB: 3DYA; PDB: 3E01; PDB: 3FFI; PDB: 3I0R; PDB: 3I0S; PDB: 3KJV; PDB: 3KK1; PDB: 3KK2; PDB: 3KK3; PDB: 3KT2; PDB: 3KT5; PDB: 3LAK; PDB: 3LAL; PDB: 3LAM; PDB: 3LAN; PDB: 3LP0; PDB: 3LP1; PDB: 3LP2; PDB: 3M8P; PDB: 3M8Q; PDB: 3MEC; PDB: 3MED; PDB: 3MEE; PDB: 3MEG; PDB: 3N3I; PDB: 3NBP; PDB: 3PHV; PDB: 3QIN; PDB: 3QIO; PDB: 3QIP; PDB: 3T19; PDB: 3T1A; PDB: 3TAM; PDB: 4B3O; PDB: 4B3P; PDB: 4B3Q; PDB: 4I7F; PDB: 4KSE; PDB: 4KV8; PDB: 4NCG; PDB: 4Q1W; PDB: 4Q1X; PDB: 4Q1Y; PDB: 4Q5M; PDB: 4QLH; PDB: 4U1H; PDB: 4U1I; PDB: 4U1J; PDB: 4U7Q; PDB: 4U7V; PDB: 5DGU; PDB: 5DGW; PDB: 5EU7; PDB: 5HRN; PDB: 5HRP; PDB: 5HRR; PDB: 5HRS; PDB: 5IM7; PDB: 5J2M; PDB: 5J2N; PDB: 5J2P; PDB: 5J2Q; PDB: 5K14; PDB: 5KAO; PDB: 5T82; PDB: 5TC2; PDB: 5VZ6; PDB: 5XOS; PDB: 5XOT; PDB: 5YRS; PDB: 6BJ2; PDB: 6BJ3; PDB: 6BSG; PDB: 6BSH; PDB: 6BSI; PDB: 6BSJ; PDB: 6DIF; PDB: 6DIL; PDB: 6DJ1; PDB: 6DJ2; PDB: 6DJ5; PDB: 6DJ7; PDB: 6DV0; PDB: 6DV4; PDB: 6E7J; PDB: 6E9A; PDB: 6EWA; PDB: 6EX9; PDB: 6GL1; PDB: 6J1V; PDB: 6J1W; PDB: 6OR7; PDB: 6OTZ; PDB: 6P1I; PDB: 6P1X; PDB: 6P2G; PDB: 6PYL; PDB: 6SKK; PDB: 6SKM; PDB: 6SKN; PDB: 6SLQ; PDB: 6SLU; PDB: 6SMU; PDB: 6UIR; PDB: 6UIS; PDB: 6UIT; PDB: 6UJX; PDB: 6UJY; PDB: 6UJZ; PDB: 6UK0; PDB: 6VPZ; PDB: 6VQ2; PDB: 6VQD; PDB: 6VQE; PDB: 6VQY; PDB: 6VQZ; PDB: 6WAZ; PDB: 6WB1; PDB: 6WPF; PDB: 6WPH; PDB: 6WPJ	.	POL_HV1H2 (1148-1435)	Reviewed	.	.	.	.	.	.
Mol01819	Protein	Interleukin-1alpha (IL1A)	Hematopoietin-1	IL1A	3552	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263339.4, IL1A-201, 2017"	MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA	.	"Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells."	PDB: 2KKI; PDB: 2L5X; PDB: 5UC6	HGNC:5991	IL1A_HUMAN 	.	ENSG00000115008	.	.	.	.	.
Mol01821	Protein	SARS-CoV-2 RNA-directed RNA polymerase (SARS-CoV-2 nsp12)	Replicase polyprotein 1ab (SARS-CoV-2 nsp12)	rep	43740578	Severe acute respiratory syndrome coronavirus 2 	2697049	Severe acute respiratory syndrome coronavirus	Betacoronavirus	694002	Coronaviridae	11118	Nidovirales	76804	Pisoniviricetes	2732506	Pisuviricota	2732408	Orthornavirae	2732396	.	SADAQSFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYNLLKDCPAVAKHDFFKFRIDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQ	.	Responsible for replication and transcription of the viral RNA genome.	PDB: 5R7Z; PDB: 5R80; PDB: 5R81; PDB: 5R82; PDB: 5R83; PDB: 5R84; PDB: 5R8T; PDB: 5RE4; PDB: 5RE5; PDB: 5RE6; PDB: 5RE7; PDB: 5RE8; PDB: 5RE9; PDB: 5REA; PDB: 5REB; PDB: 5REC; PDB: 5RED; PDB: 5REE; PDB: 5REF; PDB: 5REG; PDB: 5REH; PDB: 5REI; PDB: 5REJ; PDB: 5REK; PDB: 5REL; PDB: 5REM; PDB: 5REN; PDB: 5REO; PDB: 5REP; PDB: 5RER; PDB: 5RES; PDB: 5RET; PDB: 5REU; PDB: 5REV; PDB: 5REW; PDB: 5REX; PDB: 5REY; PDB: 5REZ; PDB: 5RF0; PDB: 5RF1; PDB: 5RF2; PDB: 5RF3; PDB: 5RF4; PDB: 5RF5; PDB: 5RF6; PDB: 5RF7; PDB: 5RF8; PDB: 5RF9; PDB: 5RFA; PDB: 5RFB; PDB: 5RFC; PDB: 5RFD; PDB: 5RFE; PDB: 5RFF; PDB: 5RFG; PDB: 5RFH; PDB: 5RFI; PDB: 5RFJ; PDB: 5RFK; PDB: 5RFL; PDB: 5RFM; PDB: 5RFN; PDB: 5RFO; PDB: 5RFP; PDB: 5RFQ; PDB: 5RFR; PDB: 5RFS; PDB: 5RFT; PDB: 5RFU; PDB: 5RFV; PDB: 5RFW; PDB: 5RFX; PDB: 5RFY; PDB: 5RFZ; PDB: 5RG0; PDB: 5RG1; PDB: 5RG2; PDB: 5RG3; PDB: 5RGG; PDB: 5RGH; PDB: 5RGI; PDB: 5RGJ; PDB: 5RGK; PDB: 5RGL; PDB: 5RGM; PDB: 5RGN; PDB: 5RGO; PDB: 5RGP; PDB: 5RGQ; PDB: 5RGR; PDB: 5RGS; PDB: 5RGT; PDB: 5RGU; PDB: 5RGV; PDB: 5RGW; PDB: 5RGX; PDB: 5RGY; PDB: 5RGZ; PDB: 5RH0; PDB: 5RH1; PDB: 5RH2; PDB: 5RH3; PDB: 5RH4; PDB: 5RH5; PDB: 5RH6; PDB: 5RH7; PDB: 5RH8; PDB: 5RH9; PDB: 5RHA; PDB: 5RHB; PDB: 5RHC; PDB: 5RHD; PDB: 5RHE; PDB: 5RHF; PDB: 5RL0; PDB: 5RL1; PDB: 5RL2; PDB: 5RL3; PDB: 5RL4; PDB: 5RL5; PDB: 5RL6; PDB: 5RL7; PDB: 5RL8; PDB: 5RL9; PDB: 5RLB; PDB: 5RLC; PDB: 5RLD; PDB: 5RLE; PDB: 5RLF; PDB: 5RLG; PDB: 5RLH; PDB: 5RLI; PDB: 5RLJ; PDB: 5RLK; PDB: 5RLL; PDB: 5RLM; PDB: 5RLN; PDB: 5RLO; PDB: 5RLP; PDB: 5RLQ; PDB: 5RLR; PDB: 5RLS; PDB: 5RLT; PDB: 5RLU; PDB: 5RLV; PDB: 5RLW; PDB: 5RLY; PDB: 5RLZ; PDB: 5RM0; PDB: 5RM1; PDB: 5RM2; PDB: 5RM3; PDB: 5RM4; PDB: 5RM5; PDB: 5RM6; PDB: 5RM7; PDB: 5RM8; PDB: 5RM9; PDB: 5RMA; PDB: 5RMB; PDB: 5RMC; PDB: 5RMD; PDB: 5RME; PDB: 5RMF; PDB: 5RMG; PDB: 5RMH; PDB: 5RMI; PDB: 5RMJ; PDB: 5RMK; PDB: 5RML; PDB: 5RMM; PDB: 5ROB; PDB: 5RS7; PDB: 5RS8; PDB: 5RS9; PDB: 5RSB; PDB: 5RSC; PDB: 5RSD; PDB: 5RSE; PDB: 5RSF; PDB: 5RSG; PDB: 5RSH; PDB: 5RSI; PDB: 5RSJ; PDB: 5RSK; PDB: 5RSL; PDB: 5RSM; PDB: 5RSN; PDB: 5RSO; PDB: 5RSP; PDB: 5RSQ; PDB: 5RSR; PDB: 5RSS; PDB: 5RST; PDB: 5RSU; PDB: 5RSV; PDB: 5RSW; PDB: 5RSX; PDB: 5RSY; PDB: 5RSZ; PDB: 5RT0; PDB: 5RT1; PDB: 5RT2; PDB: 5RT3; PDB: 5RT4; PDB: 5RT5; PDB: 5RT6; PDB: 5RT7; PDB: 5RT8; PDB: 5RT9; PDB: 5RTA; PDB: 5RTB; PDB: 5RTC; PDB: 5RTD; PDB: 5RTE; PDB: 5RTF; PDB: 5RTG; PDB: 5RTH; PDB: 5RTI; PDB: 5RTJ; PDB: 5RTK; PDB: 5RTL; PDB: 5RTM; PDB: 5RTN; PDB: 5RTO; PDB: 5RTP; PDB: 5RTQ; PDB: 5RTR; PDB: 5RTS; PDB: 5RTT; PDB: 5RTU; PDB: 5RTV; PDB: 5RTW; PDB: 5RTX; PDB: 5RTY; PDB: 5RTZ; PDB: 5RU0; PDB: 5RU1; PDB: 5RU2; PDB: 5RU3; PDB: 5RU4; PDB: 5RU5; PDB: 5RU6; PDB: 5RU7; PDB: 5RU8; PDB: 5RU9; PDB: 5RUA; PDB: 5RUC; PDB: 5RUD; PDB: 5RUE; PDB: 5RUF; PDB: 5RUG; PDB: 5RUH; PDB: 5RUI; PDB: 5RUJ; PDB: 5RUK; PDB: 5RUL; PDB: 5RUM; PDB: 5RUN; PDB: 5RUO; PDB: 5RUP; PDB: 5RUQ; PDB: 5RUR; PDB: 5RUS; PDB: 5RUT; PDB: 5RUU; PDB: 5RUV; PDB: 5RUW; PDB: 5RUX; PDB: 5RUY; PDB: 5RUZ; PDB: 5RV0; PDB: 5RV1; PDB: 5RV2; PDB: 5RV3; PDB: 5RV4; PDB: 5RV5; PDB: 5RV6; PDB: 5RV7; PDB: 5RV8; PDB: 5RV9; PDB: 5RVA; PDB: 5RVB; PDB: 5RVC; PDB: 5RVD; PDB: 5RVE; PDB: 5RVF; PDB: 5RVG; PDB: 5RVH; PDB: 5RVI; PDB: 5RVJ; PDB: 5RVK; PDB: 5RVL; PDB: 5RVM; PDB: 5RVN; PDB: 5RVO; PDB: 5RVP; PDB: 5RVQ; PDB: 5RVR; PDB: 5RVS; PDB: 5RVT; PDB: 5RVU; PDB: 5RVV; PDB: 5S18; PDB: 5S1A; PDB: 5S1C; PDB: 5S1E; PDB: 5S1G; PDB: 5S1I; PDB: 5S1K; PDB: 5S1M; PDB: 5S1O; PDB: 5S1Q; PDB: 5S1S; PDB: 5S1U; PDB: 5S1W; PDB: 5S1Y; PDB: 5S20; PDB: 5S22; PDB: 5S24; PDB: 5S26; PDB: 5S27; PDB: 5S28; PDB: 5S29; PDB: 5S2A; PDB: 5S2B; PDB: 5S2C; PDB: 5S2D; PDB: 5S2E; PDB: 5S2F; PDB: 5S2G; PDB: 5S2H; PDB: 5S2I; PDB: 5S2J; PDB: 5S2K; PDB: 5S2L; PDB: 5S2M; PDB: 5S2N; PDB: 5S2O; PDB: 5S2P; PDB: 5S2Q; PDB: 5S2R; PDB: 5S2S; PDB: 5S2T; PDB: 5S2U; PDB: 5S2V; PDB: 5S2W; PDB: 5S2X; PDB: 5S2Y; PDB: 5S2Z; PDB: 5S30; PDB: 5S31; PDB: 5S32; PDB: 5S33; PDB: 5S34; PDB: 5S35; PDB: 5S36; PDB: 5S37; PDB: 5S38; PDB: 5S39; PDB: 5S3A; PDB: 5S3B; PDB: 5S3C; PDB: 5S3D; PDB: 5S3E; PDB: 5S3F; PDB: 5S3G; PDB: 5S3H; PDB: 5S3I; PDB: 5S3J; PDB: 5S3K; PDB: 5S3L; PDB: 5S3M; PDB: 5S3N; PDB: 5S3O; PDB: 5S3P; PDB: 5S3Q; PDB: 5S3R; PDB: 5S3S; PDB: 5S3T; PDB: 5S3U; PDB: 5S3V; PDB: 5S3W; PDB: 5S3X; PDB: 5S3Y; PDB: 5S3Z; PDB: 5S40; PDB: 5S41; PDB: 5S42; PDB: 5S43; PDB: 5S44; PDB: 5S45; PDB: 5S46; PDB: 5S47; PDB: 5S48; PDB: 5S49; PDB: 5S4A; PDB: 5S4B; PDB: 5S4C; PDB: 5S4D; PDB: 5S4E; PDB: 5S4F; PDB: 5S4G; PDB: 5S4H; PDB: 5S4I; PDB: 5S4J; PDB: 5S4K; PDB: 5S6X; PDB: 5S6Y; PDB: 5S6Z; PDB: 5S70; PDB: 5S71; PDB: 5S72; PDB: 5S73; PDB: 5S74; PDB: 5SA4; PDB: 5SA5; PDB: 5SA6; PDB: 5SA7; PDB: 5SA8; PDB: 5SA9; PDB: 5SAA; PDB: 5SAB; PDB: 5SAC; PDB: 5SAD; PDB: 5SAE; PDB: 5SAF; PDB: 5SAG; PDB: 5SAH; PDB: 5SAI; PDB: 6LU7; PDB: 6LZE; PDB: 6M03; PDB: 6M0K; PDB: 6M2N; PDB: 6M2Q; PDB: 6M71; PDB: 6VWW; PDB: 6VXS; PDB: 6W01; PDB: 6W02; PDB: 6W4B; PDB: 6W4H; PDB: 6W61; PDB: 6W63; PDB: 6W6Y; PDB: 6W75; PDB: 6W9C; PDB: 6W9Q; PDB: 6WC1; PDB: 6WCF; PDB: 6WEN; PDB: 6WEY; PDB: 6WIQ; PDB: 6WJT; PDB: 6WKQ; PDB: 6WKS; PDB: 6WLC; PDB: 6WNP; PDB: 6WOJ; PDB: 6WQ3; PDB: 6WQD; PDB: 6WQF; PDB: 6WRH; PDB: 6WRZ; PDB: 6WTC; PDB: 6WTJ; PDB: 6WTK; PDB: 6WTM; PDB: 6WTT; PDB: 6WUU; PDB: 6WVN; PDB: 6WX4; PDB: 6WXC; PDB: 6WXD; PDB: 6WZU; PDB: 6X1B; PDB: 6X4I; PDB: 6XA4; PDB: 6XA9; PDB: 6XAA; PDB: 6XB0; PDB: 6XB1; PDB: 6XB2; PDB: 6XBG; PDB: 6XBH; PDB: 6XBI; PDB: 6XCH; PDB: 6XDH; PDB: 6XFN; PDB: 6XG3; PDB: 6XHM; PDB: 6XHU; PDB: 6XIP; PDB: 6XKF; PDB: 6XKH; PDB: 6XKM; PDB: 6XMK; PDB: 6XOA; PDB: 6XQS; PDB: 6XQT; PDB: 6XQU; PDB: 6XR3; PDB: 6Y2E; PDB: 6Y2F; PDB: 6Y2G; PDB: 6Y84; PDB: 6YB7; PDB: 6YNQ; PDB: 6YVA; PDB: 6YVF; PDB: 6YWK; PDB: 6YWL; PDB: 6YWM; PDB: 6YYT; PDB: 6YZ1; PDB: 6Z2E; PDB: 6Z5T; PDB: 6Z6I; PDB: 6Z72; PDB: 6ZCT; PDB: 6ZLW; PDB: 6ZM7; PDB: 6ZME; PDB: 6ZMI; PDB: 6ZMO; PDB: 6ZMT; PDB: 6ZN5; PDB: 6ZOJ; PDB: 6ZOK; PDB: 6ZON; PDB: 6ZP4; PDB: 6ZPE; PDB: 6ZRT; PDB: 6ZRU; PDB: 6ZSL; PDB: 7A1U; PDB: 7ABU; PDB: 7ADW; PDB: 7AEG; PDB: 7AF0; PDB: 7AGA; PDB: 7AHA; PDB: 7AK4; PDB: 7AKU; PDB: 7ALH; PDB: 7ALI; PDB: 7AMJ; PDB: 7ANS; PDB: 7AOL; PDB: 7AP6; PDB: 7APH; PDB: 7AQE; PDB: 7AQI; PDB: 7AQJ; PDB: 7AR5; PDB: 7AR6; PDB: 7ARF; PDB: 7AVD; PDB: 7AWR; PDB: 7AWS; PDB: 7AWU; PDB: 7AWW; PDB: 7AX6; PDB: 7AXM; PDB: 7AXO; PDB: 7AY7; PDB: 7B3E; PDB: 7B83; PDB: 7BAJ; PDB: 7BAK; PDB: 7BAL; PDB: 7BB2; PDB: 7BE7; PDB: 7BF3; PDB: 7BF4; PDB: 7BF5; PDB: 7BF6; PDB: 7BFB; PDB: 7BGP; PDB: 7BQ7; PDB: 7BQY; PDB: 7BRO; PDB: 7BRP; PDB: 7BTF; PDB: 7BUY; PDB: 7BV1; PDB: 7BV2; PDB: 7BWQ; PDB: 7BZF; PDB: 7C2I; PDB: 7C2J; PDB: 7C2K; PDB: 7C2Q; PDB: 7C2Y; PDB: 7C6S; PDB: 7C6U; PDB: 7C7P; PDB: 7C8B; PDB: 7C8R; PDB: 7C8T; PDB: 7C8U; PDB: 7CA8; PDB: 7CAM; PDB: 7CB7; PDB: 7CBT; PDB: 7CJD; PDB: 7CJM; PDB: 7CMD; PDB: 7COM; PDB: 7CUT; PDB: 7CUU; PDB: 7CWB; PDB: 7CWC; PDB: 7CX9; PDB: 7D1M; PDB: 7D1O; PDB: 7D7K; PDB: 7D7L; PDB: 7DDC; PDB: 7DG6; PDB: 7DIY; PDB: 7DVX; PDB: 7DVY; PDB: 7DW0; PDB: 7DW6; PDB: 7EQ4; PDB: 7JFQ; PDB: 7JHE; PDB: 7JIB; PDB: 7JKV; PDB: 7JME; PDB: 7JOY; PDB: 7JP0; PDB: 7JP1; PDB: 7JPE; PDB: 7JPY; PDB: 7JPZ; PDB: 7JQ0; PDB: 7JQ1; PDB: 7JQ2; PDB: 7JQ3; PDB: 7JQ4; PDB: 7JQ5; PDB: 7JQB; PDB: 7JQC; PDB: 7JR3; PDB: 7JR4; PDB: 7JST; PDB: 7JSU; PDB: 7JT0; PDB: 7JT7; PDB: 7JU7; PDB: 7JVZ; PDB: 7JW8; PDB: 7JYC; PDB: 7JYY; PDB: 7JZ0; PDB: 7K0E; PDB: 7K0F; PDB: 7K0R; PDB: 7K1L; PDB: 7K1O; PDB: 7K3N; PDB: 7K3T; PDB: 7K40; PDB: 7K5I; PDB: 7K6D; PDB: 7K6E; PDB: 7K7P; PDB: 7K9P; PDB: 7KAG; PDB: 7KEG; PDB: 7KEH; PDB: 7KF4; PDB: 7KFI; PDB: 7KG3; PDB: 7KHP; PDB: 7KOA; PDB: 7KPH; PDB: 7KQO; PDB: 7KQP; PDB: 7KQW; PDB: 7KR0; PDB: 7KR1; PDB: 7KRI; PDB: 7KVL; PDB: 7KVR; PDB: 7KX5; PDB: 7KXB; PDB: 7KYU; PDB: 7L0D; PDB: 7L10; PDB: 7L11; PDB: 7L12; PDB: 7L13; PDB: 7L14; PDB: 7L1F; PDB: 7L5D; PDB: 7L6R; PDB: 7L6T; PDB: 7L8I; PDB: 7L8J; PDB: 7LB7; PDB: 7LBN; PDB: 7LBR; PDB: 7LBS; PDB: 7LCO; PDB: 7LCS; PDB: 7LCT; PDB: 7LDL; PDB: 7LDX; PDB: 7LFE; PDB: 7LFP; PDB: 7LFZ; PDB: 7LG2; PDB: 7LG3; PDB: 7LG7; PDB: 7LGO; PDB: 7LKD; PDB: 7LKE; PDB: 7LKR; PDB: 7LKS; PDB: 7LKT; PDB: 7LKU; PDB: 7LKV; PDB: 7LKW; PDB: 7LKX; PDB: 7LLF; PDB: 7LLZ; PDB: 7LMD; PDB: 7LME; PDB: 7LMF; PDB: 7LOS; PDB: 7LTJ; PDB: 7LTN; PDB: 7LW3; PDB: 7LW4; PDB: 7LYH; PDB: 7LYI; PDB: 7LZT; PDB: 7LZU; PDB: 7LZV; PDB: 7LZW; PDB: 7LZX; PDB: 7LZY; PDB: 7LZZ; PDB: 7M00; PDB: 7M01; PDB: 7M02; PDB: 7M03; PDB: 7M04; PDB: 7M2P; PDB: 7M8M; PDB: 7M8N; PDB: 7M8O; PDB: 7M8P; PDB: 7M8X; PDB: 7M8Y; PDB: 7M8Z; PDB: 7M90; PDB: 7M91; PDB: 7MBG; PDB: 7MBI; PDB: 7MC5; PDB: 7MC6; PDB: 7ME0; PDB: 7MGR; PDB: 7MGS; PDB: 7MHF; PDB: 7MHG; PDB: 7MHH; PDB: 7MHI; PDB: 7MHJ; PDB: 7MHK; PDB: 7MHL; PDB: 7MHM; PDB: 7MHN; PDB: 7MHO; PDB: 7MHP; PDB: 7MHQ; PDB: 7MLF; PDB: 7MLG; PDB: 7MNG; PDB: 7MPB; PDB: 7MRR; PDB: 7MSW; PDB: 7MSX; PDB: 7N06; PDB: 7N0B; PDB: 7N0C; PDB: 7N0D; PDB: 7N33; PDB: 7N3K; PDB: 7N44; PDB: 7N5Z; PDB: 7N6N; PDB: 7N7R; PDB: 7N7U; PDB: 7N7W; PDB: 7N7Y; PDB: 7N83; PDB: 7N89; PDB: 7N8C; PDB: 7NBR; PDB: 7NBS; PDB: 7NBY; PDB: 7NEV; PDB: 7NF5; PDB: 7NFV; PDB: 7NG3; PDB: 7NG6; PDB: 7NIO; PDB: 7NN0; PDB: 7NNG; PDB: 7NTS; PDB: 7O7Y; PDB: 7O7Z; PDB: 7O80; PDB: 7O81; PDB: 7ORR; PDB: 7ORU; PDB: 7ORV; PDB: 7ORW; PDB: 7QGI; PDB: 7R7H; PDB: 7RB0; PDB: 7RB2; PDB: 7RBZ; PDB: 7RC0; PDB: 7RFR; PDB: 7RFS; PDB: 7RFU; PDB: 7RFW; PDB: 7RLS; PDB: 7RM2; PDB: 7RMB; PDB: 7RME; PDB: 7RMT; PDB: 7RMZ; PDB: 7RN0; PDB: 7RN1; PDB: 7RN4; PDB: 7RNH; PDB: 7RNK; PDB: 7RQG; PDB: 7S3K; PDB: 7S3S; PDB: 7S4B; PDB: 7SI9; PDB: 7T42; PDB: 7T43; PDB: 7T44; PDB: 7T45; PDB: 7T46; PDB: 7T48; PDB: 7T49; PDB: 7T4A; PDB: 7T4B; PDB: 7T9W; PDB: 7TE0; PDB: 7THH; PDB: 7TI9; 	.	R1AB_SARS2 (4393-5324)	Reviewed	.	.	.	.	.	.
Mol01822	Protein	Spike glycoprotein (S)	Peplomer protein; Spike protein S1; Spike protein S2; Spike protein S2'	S	43740568	Severe acute respiratory syndrome coronavirus 2 	2697049	Severe acute respiratory syndrome coronavirus	Betacoronavirus	694002	Coronaviridae	11118	Nidovirales	76804	Pisoniviricetes	2732506	Pisuviricota	2732408	Orthornavirae	2732396	.	MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYIWLGFIAGLIAIVMVTIMLCCMTSCCSCLKGCCSCGSCCKFDEDDSEPVLKGVKLHYT	.	"Spike protein S1: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein. Binding to host NRP1 and NRP2 via C-terminal polybasic sequence enhances virion entry into host cell. This interaction may explain virus tropism of human olfactory epithelium cells, which express high level of NRP1 and NRP2 but low level of ACE2. The stalk domain of S contains three hinges, giving the head unexpected orientational freedom. Uses human TMPRSS2 for priming in human lung cells which is an essential step for viral entry. Can be alternatively processed by host furin. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membrane fusion within endosomes. Spike protein S2: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes."	PDB: 6LVN; PDB: 6LXT; PDB: 6LZG; PDB: 6M0J; PDB: 6M17; PDB: 6M1V; PDB: 6VSB; PDB: 6VW1; PDB: 6VXX; PDB: 6VYB; PDB: 6W41; PDB: 6WPS; PDB: 6WPT; PDB: 6X29; PDB: 6X2A; PDB: 6X2B; PDB: 6X2C; PDB: 6X45; PDB: 6X6P; PDB: 6X79; PDB: 6XC2; PDB: 6XC3; PDB: 6XC4; PDB: 6XC7; PDB: 6XCM; PDB: 6XCN; PDB: 6XDG; PDB: 6XE1; PDB: 6XEY; PDB: 6XF5; PDB: 6XF6; PDB: 6XKL; PDB: 6XKP; PDB: 6XKQ; PDB: 6XLU; PDB: 6XM0; PDB: 6XM3; PDB: 6XM4; PDB: 6XM5; PDB: 6XR8; PDB: 6XRA; PDB: 6XS6; PDB: 6YLA; PDB: 6YM0; PDB: 6YOR; PDB: 6YZ5; PDB: 6YZ7; PDB: 6Z2M; PDB: 6Z43; PDB: 6Z97; PDB: 6ZB4; PDB: 6ZB5; PDB: 6ZBP; PDB: 6ZCZ; PDB: 6ZDG; PDB: 6ZDH; PDB: 6ZER; PDB: 6ZFO; PDB: 6ZGE; PDB: 6ZGG; PDB: 6ZGI; PDB: 6ZH9; PDB: 6ZHD; PDB: 6ZLR; PDB: 6ZOW; PDB: 6ZOX; PDB: 6ZOY; PDB: 6ZOZ; PDB: 6ZP0; PDB: 6ZP1; PDB: 6ZP2; PDB: 6ZP5; PDB: 6ZP7; PDB: 6ZWV; PDB: 6ZXN; PDB: 7A25; PDB: 7A29; PDB: 7A4N; PDB: 7A5R; PDB: 7A5S; PDB: 7A91; PDB: 7A92; PDB: 7A93; PDB: 7A94; PDB: 7A95; PDB: 7A96; PDB: 7A97; PDB: 7A98; PDB: 7AD1; PDB: 7AKD; PDB: 7B14; PDB: 7B17; PDB: 7B18; PDB: 7B3O; PDB: 7B62; PDB: 7BEH; PDB: 7BEI; PDB: 7BEJ; PDB: 7BEK; PDB: 7BEL; PDB: 7BEM; PDB: 7BEN; PDB: 7BEO; PDB: 7BEP; PDB: 7BH9; PDB: 7BNM; PDB: 7BNN; PDB: 7BNO; PDB: 7BWJ; PDB: 7BYR; PDB: 7BZ5; PDB: 7C01; PDB: 7C2L; PDB: 7C53; PDB: 7C8D; PDB: 7C8J; PDB: 7C8V; PDB: 7C8W; PDB: 7CAB; PDB: 7CAC; PDB: 7CAH; PDB: 7CAI; PDB: 7CAK; PDB: 7CAN; PDB: 7CDI; PDB: 7CDJ; PDB: 7CH4; PDB: 7CH5; PDB: 7CHB; PDB: 7CHC; PDB: 7CHE; PDB: 7CHF; PDB: 7CHH; PDB: 7CHO; PDB: 7CHP; PDB: 7CHS; PDB: 7CJF; PDB: 7CM4; PDB: 7CN4; PDB: 7CN9; PDB: 7CT5; PDB: 7CWL; PDB: 7CWM; PDB: 7CWN; PDB: 7CWO; PDB: 7CWS; PDB: 7CWT; PDB: 7CWU; PDB: 7CYH; PDB: 7CYP; PDB: 7CYV; PDB: 7CZP; PDB: 7CZQ; PDB: 7CZR; PDB: 7CZS; PDB: 7CZT; PDB: 7CZU; PDB: 7CZV; PDB: 7CZW; PDB: 7CZX; PDB: 7CZY; PDB: 7CZZ; PDB: 7D00; PDB: 7D03; PDB: 7D0B; PDB: 7D0C; PDB: 7D0D; PDB: 7D2Z; PDB: 7D30; PDB: 7D4G; PDB: 7D6I; PDB: 7DCC; PDB: 7DCX; PDB: 7DD2; PDB: 7DD8; PDB: 7DDD; PDB: 7DDN; PDB: 7DEO; PDB: 7DET; PDB: 7DEU; PDB: 7DF3; PDB: 7DF4; PDB: 7DHX; PDB: 7DJZ; PDB: 7DK0; PDB: 7DK2; PDB: 7DK3; PDB: 7DK4; PDB: 7DK5; PDB: 7DK6; PDB: 7DK7; PDB: 7DMU; PDB: 7DPM; PDB: 7DQA; PDB: 7DWX; PDB: 7DWY; PDB: 7DWZ; PDB: 7DX0; PDB: 7DX1; PDB: 7DX2; PDB: 7DX3; PDB: 7DX4; PDB: 7DX5; PDB: 7DX6; PDB: 7DX7; PDB: 7DX8; PDB: 7DX9; PDB: 7DZW; PDB: 7DZX; PDB: 7DZY; PDB: 7E+23; PDB: 7E+39; PDB: 7E3B; PDB: 7E3C; PDB: 7E3J; PDB: 7E3K; PDB: 7E3L; PDB: 7E3O; PDB: 7E5O; PDB: 7E5R; PDB: 7E5S; PDB: 7E5Y; PDB: 7E7B; PDB: 7E7D; PDB: 7E7X; PDB: 7E7Y; PDB: 7E+86; PDB: 7E+88; PDB: 7E8C; PDB: 7E8F; PDB: 7E8M; PDB: 7E9T; PDB: 7EAM; PDB: 7EAN; PDB: 7EAZ; PDB: 7EB0; PDB: 7EB3; PDB: 7EB4; PDB: 7EB5; PDB: 7EDF; PDB: 7EDG; PDB: 7EDH; PDB: 7EDI; PDB: 7EDJ; PDB: 7EFP; PDB: 7EFR; PDB: 7EH5; PDB: 7EJ4; PDB: 7EJ5; PDB: 7EK6; PDB: 7EKC; PDB: 7EKE; PDB: 7EKF; PDB: 7EKG; PDB: 7EKH; PDB: 7EY0; PDB: 7EY4; PDB: 7EY5; PDB: 7EYA; PDB: 7EZV; PDB: 7F62; PDB: 7F63; PDB: 7FAE; PDB: 7FAF; PDB: 7FCD; PDB: 7FCE; PDB: 7FDG; PDB: 7FDH; PDB: 7FDI; PDB: 7FDK; PDB: 7FEM; PDB: 7FET; PDB: 7FG2; PDB: 7FG3; PDB: 7FG7; PDB: 7JJC; PDB: 7JJI; PDB: 7JJJ; PDB: 7JMO; PDB: 7JMP; PDB: 7JMW; PDB: 7JV2; PDB: 7JV4; PDB: 7JV6; PDB: 7JVA; PDB: 7JVB; PDB: 7JVC; PDB: 7JW0; PDB: 7JWB; PDB: 7JWY; PDB: 7JX3; PDB: 7JZL; PDB: 7JZM; PDB: 7JZN; PDB: 7JZU; PDB: 7K43; PDB: 7K45; PDB: 7K4N; PDB: 7K8M; PDB: 7K8S; PDB: 7K8T; PDB: 7K8U; PDB: 7K8V; PDB: 7K8W; PDB: 7K8X; PDB: 7K8Y; PDB: 7K8Z; PDB: 7K90; PDB: 7K9H; PDB: 7K9I; PDB: 7K9J; PDB: 7K9K; PDB: 7K9Z; PDB: 7KDG; PDB: 7KDH; PDB: 7KDI; PDB: 7KDJ; PDB: 7KDK; PDB: 7KDL; PDB: 7KE4; PDB: 7KE6; PDB: 7KE7; PDB: 7KE8; PDB: 7KE9; PDB: 7KEA; PDB: 7KEB; PDB: 7KEC; PDB: 7KFV; PDB: 7KFW; PDB: 7KFX; PDB: 7KFY; PDB: 7KGJ; PDB: 7KGK; PDB: 7KJ2; PDB: 7KJ3; PDB: 7KJ4; PDB: 7KJ5; PDB: 7KKK; PDB: 7KKL; PDB: 7KL9; PDB: 7KLG; PDB: 7KLH; PDB: 7KLW; PDB: 7KM5; PDB: 7KMB; PDB: 7KMG; PDB: 7KMH; PDB: 7KMI; PDB: 7KMK; PDB: 7KML; PDB: 7KMS; PDB: 7KMZ; PDB: 7KN3; PDB: 7KN4; PDB: 7KN5; PDB: 7KN6; PDB: 7KN7; PDB: 7KNB; PDB: 7KNE; PDB: 7KNH; PDB: 7KNI; PDB: 7KQB; PDB: 7KQE; PDB: 7KRQ; PDB: 7KRR; PDB: 7KRS; PDB: 7KS9; PDB: 7KSG; PDB: 7KXJ; PDB: 7KXK; PDB: 7KZB; PDB: 7L02; PDB: 7L06; PDB: 7L09; PDB: 7L0N; PDB: 7L2C; PDB: 7L2D; PDB: 7L2E; PDB: 7L2F; PDB: 7L3N; PDB: 7L4Z; PDB: 7L56; PDB: 7L57; PDB: 7L58; PDB: 7L5B; PDB: 7L7D; PDB: 7L7E; PDB: 7L7F; PDB: 7L7K; PDB: 7LAA; PDB: 7LAB; PDB: 7LC8; PDB: 7LCN; PDB: 7LD1; PDB: 7LDJ; PDB: 7LJR; PDB: 7LM8; PDB: 7LO4; PDB: 7LOP; PDB: 7LQ7; PDB: 7LQV; PDB: 7LQW; PDB: 7LRS; PDB: 7LRT; PDB: 7LS9; PDB: 7LSS; PDB: 7LWI; PDB: 7LWJ; PDB: 7LWK; PDB: 7LWL; PDB: 7LWM; PDB: 7LWN; PDB: 7LWO; PDB: 7LWP; PDB: 7LWQ; PDB: 7LWS; PDB: 7LWT; PDB: 7LWU; PDB: 7LWV; PDB: 7LWW; PDB: 7LX5; PDB: 7LXW; PDB: 7LXX; PDB: 7LXY; PDB: 7LXZ; PDB: 7LY0; PDB: 7LY2; PDB: 7LY3; PDB: 7LYK; PDB: 7LYL; PDB: 7LYM; PDB: 7LYN; PDB: 7LYO; PDB: 7LYP; PDB: 7LYQ; PDB: 7M0J; PDB: 7M3I; PDB: 7M42; PDB: 7M53; PDB: 7M6D; PDB: 7M6E; PDB: 7M6F; PDB: 7M6G; PDB: 7M6H; PDB: 7M6I; PDB: 7M71; PDB: 7M7B; PDB: 7M7W; PDB: 7M8J; PDB: 7M8K; PDB: 7M8S; PDB: 7M8T; PDB: 7M8U; PDB: 7MDW; PDB: 7ME7; PDB: 7MEJ; PDB: 7MF1; PDB: 7MFU; PDB: 7MJG; PDB: 7MJH; PDB: 7MJI; PDB: 7MJJ; PDB: 7MJK; PDB: 7MJL; PDB: 7MJM; PDB: 7MJN; PDB: 7MKB; PDB: 7MKL; PDB: 7MKM; PDB: 7MLZ; PDB: 7MM0; PDB: 7MMO; PDB: 7MSQ; PDB: 7MTC; PDB: 7MTD; PDB: 7MTE; PDB: 7MY2; PDB: 7MY3; PDB: 7MY8; PDB: 7MZF; PDB: 7MZG; PDB: 7MZH; PDB: 7MZI; PDB: 7MZJ; PDB: 7MZK; PDB: 7MZL; PDB: 7MZM; PDB: 7MZN; PDB: 7N0G; PDB: 7N0H; PDB: 7N1A; PDB: 7N1B; PDB: 7N1E; PDB: 7N1F; PDB: 7N1Q; PDB: 7N1T; PDB: 7N1U; PDB: 7N1V; PDB: 7N1W; PDB: 7N1X; PDB: 7N1Y; PDB: 7N3I; PDB: 7N4I; PDB: 7N4J; PDB: 7N4L; PDB: 7N4M; PDB: 7N5H; PDB: 7N62; PDB: 7N64; PDB: 7N6D; PDB: 7N6E; PDB: 7N8H; PDB: 7N8I; PDB: 7N9A; PDB: 7N9B; PDB: 7N9C; PDB: 7N9E; PDB: 7N9T; PDB: 7NAB; PDB: 7ND3; PDB: 7ND4; PDB: 7ND5; PDB: 7ND6; PDB: 7ND7; PDB: 7ND8; PDB: 7ND9; PDB: 7NDA; PDB: 7NDB; PDB: 7NDC; PDB: 7NDD; PDB: 7NEG; PDB: 7NEH; PDB: 7NKT; PDB: 7NP1; PDB: 7NT9; PDB: 7NTA; PDB: 7NTC; PDB: 7NX6; PDB: 7NX7; PDB: 7NX8; PDB: 7NX9; PDB: 7NXA; PDB: 7NXB; PDB: 7NXC; PDB: 7OAN; PDB: 7OAO; PDB: 7OAP; PDB: 7OAQ; PDB: 7OAU; PDB: 7OAY; PDB: 7OD3; PDB: 7ODL; PDB: 7OLZ; PDB: 7OR9; PDB: 7ORA; PDB: 7ORB; PDB: 7P3D; PDB: 7P77; PDB: 7P78; PDB: 7P79; PDB: 7P7A; PDB: 7P7B; PDB: 7PRY; PDB: 7PRZ; PDB: 7PS0; PDB: 7PS1; PDB: 7PS2; PDB: 7PS4; PDB: 7PS5; PDB: 7PS6; PDB: 7PS7; PDB: 7Q0G; PDB: 7Q0H; PDB: 7Q0I; PDB: 7Q6E; PDB: 7Q9F; PDB: 7Q9G; PDB: 7Q9I; PDB: 7Q9J; PDB: 7Q9K; PDB: 7Q9M; PDB: 7Q9P; PDB: 7QO9; PDB: 7R6W; PDB: 7R6X; PDB: 7R7N; PDB: 7R8L; PDB: 7R8M; PDB: 7R8N; PDB: 7R8O; PDB: 7R95; PDB: 7RA8; PDB: 7RAL; PDB: 7RKU; PDB: 7RKV; PDB: 7RNJ; PDB: 7RPV; PDB: 7RR0; PDB: 7RTD; PDB: 7RTR; PDB: 7RW2; PDB: 7RXD; PDB: 7S0B; PDB: 7S0C; PDB: 7S0D; PDB: 7S0E; PDB: 7S4S; PDB: 7SBK; PDB: 7SBL; PDB: 7SBO; PDB: 7SBP; PDB: 7SBQ; PDB: 7SBR; PDB: 7SBS; PDB: 7SBT; PDB: 7SJS; PDB: 7SN2; PDB: 7SN3; PDB: 7SO9; PDB: 7SOA; PDB: 7SOB; PDB: 7SOC; PDB: 7SOD; PDB: 7SOE; PDB: 7SOF; PDB: 7SPO; PDB: 7SPP; PDB: 7SXR; PDB: 7SXS; PDB: 7SXT; PDB: 7SXU; PDB: 7SXV; PDB: 7SXW; PDB: 7SXX; PDB: 7SXY; PDB: 7SXZ; PDB: 7SY0; PDB: 7SY1; PDB: 7SY2; PDB: 7SY3; PDB: 7SY4; PDB: 7SY5; PDB: 7SY6; PDB: 7SY7; PDB: 7SY8; PDB: 7T9J; PDB: 7T9K; PDB: 7T9L; PDB: 7TAS; PDB: 7TAT; PDB: 7V26; PDB: 7V2A; PDB: 7V76; PDB: 7V77; PDB: 7V78; PDB: 7V79; PDB: 7V7A; PDB: 7V7D; PDB: 7V7E; PDB: 7V7F; PDB: 7V7G; PDB: 7V7H; PDB: 7V7I; PDB: 7V7J; PDB: 7V7N; PDB: 7V7O; PDB: 7V7P; PDB: 7V7Q; PDB: 7V7R; PDB: 7V7S; PDB: 7V7T; PDB: 7V7U; PDB: 7V7V; PDB: 7V7Z; PDB: 7V80; PDB: 7V81; PDB: 7V82; PDB: 7V83; PDB: 7V84; PDB: 7V85; PDB: 7V86; PDB: 7V87; PDB: 7V88; PDB: 7V89; PDB: 7V8A; PDB: 7V8B; PDB: 7V8C; PDB: 7VMU; PDB: 7VNB; PDB: 7VNC; PDB: 7VND; PDB: 7VNE; PDB: 7VX1; PDB: 7VX4; PDB: 7VX5; PDB: 7VX9; PDB: 7VXA; PDB: 7VXB; PDB: 7VXC; PDB: 7VXD; PDB: 7VXE; PDB: 7VXF; PDB: 7VXI; PDB: 7VXK; PDB: 7VXM; PDB: 7W92; PDB: 7W94; PDB: 7W98; PDB: 7W99; PDB: 7W9B; PDB: 7W9C; PDB: 7W9E; PDB: 7W9F; PDB: 7W9I; PDB: 7WBL; PDB: 7WBP; PDB: 7WBQ; PDB: 7WEV; PDB: 7WK2; PDB: 7WK3; PDB: 7WK8; PDB: 7WKA; 	.	SPIKE_SARS2	Reviewed	.	.	.	.	.	.
Mol01823	Protein	Myeloid cell surface antigen CD33 (CD33)	Sialic acid-binding Ig-like lectin 3; Siglec-3; gp67; CD antigen CD33; SIGLEC3	CD33	945	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262262.5, CD33-201, 1462; ENST00000391796.7, CD33-202, 1089; ENST00000421133.6, CD33-203, 1023; ENST00000436584.6, CD33-204, 1494; ENST00000600557.1, CD33-206, 536; ENST00000598473.1, CD33-205, 4728; ENST00000601785.5, CD33-207, 1522"	MPLLLLLPLLWAGALAMDPNFWLQVQESVTVQEGLCVLVPCTFFHPIPYYDKNSPVHGYWFREGAIISRDSPVATNKLDQEVQEETQGRFRLLGDPSRNNCSLSIVDARRRDNGSYFFRMERGSTKYSYKSPQLSVHVTDLTHRPKILIPGTLEPGHSKNLTCSVSWACEQGTPPIFSWLSAAPTSLGPRTTHSSVLIITPRPQDHGTNLTCQVKFAGAGVTTERTIQLNVTYVPQNPTTGIFPGDGSGKQETRAGVVHGAIGGAGVTALLALCLCLIFFIVKTHRRKAARTAVGRNDTHPTTGSASPKHQKKSKLHGPTETSSCSGAAPTVEMDEELHYASLNFHGMNPSKDTSTEYSEVRTQ	"chr19:51,225,064-51,243,860[+]"	"Sialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state. Preferentially recognizes and binds alpha-2,3- and more avidly alpha-2,6-linked sialic acid-bearing glycans. Upon engagement of ligands such as C1q or syalylated glycoproteins, two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) located in CD33 cytoplasmic tail are phosphorylated by Src-like kinases such as LCK. These phosphorylations provide docking sites for the recruitment and activation of protein-tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2. In turn, these phosphatases regulate downstream pathways through dephosphorylation of signaling molecules. One of the repressive effect of CD33 on monocyte activation requires phosphoinositide 3-kinase/PI3K."	PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:6D4A; PDB:5IHB; PDB:5IHB; PDB:5IHB; PDB:5IHB; PDB:5IHB; PDB:5IHB; PDB:5IHB; 	HGNC:1659	CD33_HUMAN	Reviewed	ENSG00000105383	.	.	.	.	.
Mol01824	Protein	B-cell receptor CD22 (CD22)	B-lymphocyte cell adhesion molecule; BL-CAM; Sialic acid-binding Ig-like lectin 2; Siglec-2; T-cell surface antigen Leu-14; CD antigen CD22	CD22	933	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000085219.10, CD22-201, 3274; ENST00000536635.6, CD22-204, 3004; ENST00000341773.10, CD22-202, 2755; ENST00000544992.6, CD22-205, 2698; ENST00000419549.6, CD22-203, 2642; ENST00000594250.5, CD22-209, 2107; ENST00000593867.5, CD22-207, 831; ENST00000613136.1, CD22-234, 609; ENST00000600131.5, CD22-224, 603; ENST00000597916.5, CD22-216, 592; ENST00000599811.5, CD22-223, 559; ENST00000595780.5, CD22-213, 558; ENST00000598537.5, CD22-219, 554; ENST00000600424.5, CD22-225, 542; ENST00000601769.5, CD22-231, 3060; ENST00000594125.1, CD22-208, 954; ENST00000594349.1, CD22-210, 740; ENST00000599717.5, CD22-221, 567; ENST00000595419.5, CD22-212, 623; ENST00000598138.5, CD22-218, 598; ENST00000598815.5, CD22-220, 589; ENST00000597433.1, CD22-215, 579; ENST00000598028.5, CD22-217, 573; ENST00000601414.5, CD22-229, 563; ENST00000601732.5, CD22-230, 562; ENST00000600905.5, CD22-227, 559; ENST00000601329.5, CD22-228, 556; ENST00000596492.5, CD22-214, 1061; ENST00000600655.1, CD22-226, 999; ENST00000594954.5, CD22-211, 605; ENST00000602224.5, CD22-233, 582; ENST00000599799.1, CD22-222, 581; ENST00000602123.1, CD22-232, 579; ENST00000593704.1, CD22-206, 569"	MHLLGPWLLLLVLEYLAFSDSSKWVFEHPETLYAWEGACVWIPCTYRALDGDLESFILFHNPEYNKNTSKFDGTRLYESTKDGKVPSEQKRVQFLGDKNKNCTLSIHPVHLNDSGQLGLRMESKTEKWMERIHLNVSERPFPPHIQLPPEIQESQEVTLTCLLNFSCYGYPIQLQWLLEGVPMRQAAVTSTSLTIKSVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSNDTVQLNVKHTPKLEIKVTPSDAIVREGDSVTMTCEVSSSNPEYTTVSWLKDGTSLKKQNTFTLNLREVTKDQSGKYCCQVSNDVGPGRSEEVFLQVQYAPEPSTVQILHSPAVEGSQVEFLCMSLANPLPTNYTWYHNGKEMQGRTEEKVHIPKILPWHAGTYSCVAENILGTGQRGPGAELDVQYPPKKVTTVIQNPMPIREGDTVTLSCNYNSSNPSVTRYEWKPHGAWEEPSLGVLKIQNVGWDNTTIACAACNSWCSWASPVALNVQYAPRDVRVRKIKPLSEIHSGNSVSLQCDFSSSHPKEVQFFWEKNGRLLGKESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSMSPGDQVMEGKSATLTCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQGTNSVGKGRSPLSTLTVYYSPETIGRRVAVGLGSCLAILILAICGLKLQRRWKRTQSQQGLQENSSGQSFFVRNKKVRRAPLSEGPHSLGCYNPMMEDGISYTTLRFPEMNIPRTGDAESSEMQRPPPDCDDTVTYSALHKRQVGDYENVIPDFPEDEGIHYSELIQFGVGERPQAQENVDYVILKH	"chr19:35,319,261-35,347,361[+]"	"Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules."	PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VL3; PDB:5VKM; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ; PDB:5VKJ	HGNC:1643	CD22_HUMAN	Reviewed	ENSG00000012124	.	.	.	.	.
Mol01825	Protein	B-lymphocyte antigen CD19 (CD19)	B-lymphocyte surface antigen B4; Differentiation antigen CD19; T-cell surface antigen Leu-12; CD antigen CD19	CD19	930	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000538922.8, CD19-202, 1918; ENST00000324662.8, CD19-201, 1922; ENST00000565089.5, CD19-203, 2322; ENST00000567368.1, CD19-205, 847; ENST00000566890.1, CD19-204, 590"	MPPPRLLFFLLFLTPMEVRPEEPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKPFLKLSLGLPGLGIHMRPLAIWLFIFNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGELFRWNVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCLPPRDSLNQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKDDRPARDMWVMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARPVLWHWLLRTGGWKVSAVTLAYLIFCLCSLVGILHLQRALVLRRKRKRMTDPTRRFFKVTPPPGSGPQNQYGNVLSLPTPTSGLGRAQRWAAGLGGTAPSYGNPSSDVQADGALGSRSPPGVGPEEEEGEGYEEPDSEEDSEFYENDSNLGQDQLSQDGSGYENPEDEPLGPEDEDSFSNAESYENEDEELTQPVARTMDFLSPHGSAWDPSREATSLGSQSYEDMRGILYAAPQLRSIRGQPGPNHEEDADSYENMDNPDGPDPAWGGGGRMGTWSTR	chr16:28931965-28939342[+]	"Functions as coreceptor for the B-cell antigen receptor complex (BCR) on B-lymphocytes. Decreases the threshold for activation of downstream signaling pathways and for triggering B-cell responses to antigens. Activates signaling pathways that lead to the activation of phosphatidylinositol 3-kinase and the mobilization of intracellular Ca(2+) stores. Is not required for early steps during B cell differentiation in the blood marrow. Required for normal differentiation of B-1 cells. Required for normal B cell differentiation and proliferation in response to antigen challenges. Required for normal levels of serum immunoglobulins, and for production of high-affinity antibodies in response to antigen challenge."	PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5; PDB:6AL5	HGNC:1633	CD19_HUMAN	Reviewed	ENSG00000177455	.	.	.	.	.
Mol01826	Protein	PI3-kinase beta (PIK3CB)	PI3-kinase subunit beta; PI3K-beta; PI3Kbeta; PtdIns-3-kinase subunit beta; Phosphatidylinositol 4;5-bisphosphate 3-kinase 110 kDa catalytic subunit beta; PtdIns-3-kinase subunit p110-beta; p110beta; PIK3CB; PIK3C1	PIK3CB	5291	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000674063.1,PIK3CB-214,6259; ENST00000289153.6,PIK3CB-201,5919; ENST00000477593.5,PIK3CB-207,4658; ENST00000544716.5,PIK3CB-213,3181; ENST00000493568.5,PIK3CB-212,2347; ENST00000483968.5,PIK3CB-209,721; ENST00000465581.1,PIK3CB-204,690; ENST00000462294.1,PIK3CB-202,542; ENST00000462898.5,PIK3CB-203,4747; ENST00000469284.6,PIK3CB-205,3164; ENST00000473435.1,PIK3CB-206,904; ENST00000481749.5,PIK3CB-208,2396; ENST00000485060.1,PIK3CB-210,612; ENST00000487552.1,PIK3CB-211,581"	MCFSFIMPPAMADILDIWAVDSQIASDGSIPVDFLLPTGIYIQLEVPREATISYIKQMLWKQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPGEKLDSKIGVLIGKGLHEFDSLKDPEVNEFRRKMRKFSEEKILSLVGLSWMDWLKQTYPPEHEPSIPENLEDKLYGGKLIVAVHFENCQDVFSFQVSPNMNPIKVNELAIQKRLTIHGKEDEVSPYDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRALPHFILVECCKIKKMYEQEMIAIEAAINRNSSNLPLPLPPKKTRIISHVWENNNPFQIVLVKGNKLNTEETVKVHVRAGLFHGTELLCKTIVSSEVSGKNDHIWNEPLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTINPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRTGDIILHSWSSFPDELEEMLNPMGTVQTNPYTENATALHVKFPENKKQPYYYPPFDKIIEKAAEIASSDSANVSSRGGKKFLPVLKEILDRDPLSQLCENEMDLIWTLRQDCREIFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPKLPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFLLERALGNRRIGQFLFWHLRSEVHIPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLKTLNSLIKLNAVKLNRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMDSKMKPLWLVYNNKVFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYGCLATGDRSGLIEVVSTSETIADIQLNSSNVAAAAAFNKDALLNWLKEYNSGDDLDRAIEEFTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFILTYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKDIQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS	"chr3:138,652,698-138,834,928[-]"	"Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol derivatives at position 3 of the inositol ring to produce 3-phosphoinositides. Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Involved in the activation of AKT1 upon stimulation by G-protein coupled receptors (GPCRs) ligands such as CXCL12, sphingosine 1-phosphate, and lysophosphatidic acid. May also act downstream receptor tyrosine kinases. Required in different signaling pathways for stable platelet adhesion and aggregation. Plays a role in platelet activation signaling triggered by GPCRs, alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) and ITAM (immunoreceptor tyrosine-based activation motif)-bearing receptors such as GP6. Regulates the strength of adhesion of ITGA2B/ ITGB3 activated receptors necessary for the cellular transmission of contractile forces. Required for platelet aggregation induced by F2 (thrombin) and thromboxane A2 (TXA2). Has a role in cell survival. May have a role in cell migration. Involved in the early stage of autophagosome formation. Modulates the intracellular level of PtdIns3P (phosphatidylinositol 3-phosphate) and activates PIK3C3 kinase activity. May act as a scaffold, independently of its lipid kinase activity to positively regulate autophagy. May have a role in insulin signaling as scaffolding protein in which the lipid kinase activity is not required. May have a kinase-independent function in regulating cell proliferation and in clathrin-mediated endocytosis. Mediator of oncogenic signal in cell lines lacking PTEN. The lipid kinase activity is necessary for its role in oncogenic transformation. Required for the growth of ERBB2 and RAS driven tumors."	.	HGNC:8976	PK3CB_HUMAN	Reviewed	ENSG00000051382	.	.	.	.	.
Mol01827	Protein	AMP-activated kinase alpha-2 (PRKAA2)	AMPK subunit alpha-2; Acetyl-CoA carboxylase kinase; ACACA kinase; Hydroxymethylglutaryl-CoA reductase kinase; HMGCR kinase; PRKAA2; AMPK; AMPK2	PRKAA2	5563	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371244.9,PRKAA2-201,9355"	MAEKQKHDGRVKIGHYVLGDTLGVGTFGKVKIGEHQLTGHKVAVKILNRQKIRSLDVVGKIKREIQNLKLFRHPHIIKLYQVISTPTDFFMVMEYVSGGELFDYICKHGRVEEMEARRLFQQILSAVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSCGVILYALLCGTLPFDDEHVPTLFKKIRGGVFYIPEYLNRSVATLLMHMLQVDPLKRATIKDIREHEWFKQDLPSYLFPEDPSYDANVIDDEAVKEVCEKFECTESEVMNSLYSGDPQDQLAVAYHLIIDNRRIMNQASEFYLASSPPSGSFMDDSAMHIPPGLKPHPERMPPLIADSPKARCPLDALNTTKPKSLAVKKAKWHLGIRSQSKPYDIMAEVYRAMKQLDFEWKVVNAYHLRVRRKNPVTGNYVKMSLQLYLVDNRSYLLDFKSIDDEVVEQRSGSSTPQRSCSAAGLHRPRSSFDSTTAESHSLSGSLTGSLTGSTLSSVSPRLGSHTMDFFEMCASLITTLAR	"chr3:56,645,314-56,715,335[+]"	"Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. Involved in insulin receptor/INSR internalization. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. In that process also activates WDR45. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation. Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1."	PDB: 2H6D; 2LTU; 2YZA; 3AQV; 4CFE; 4CFF; 4ZHX; 5EZV; 5ISO; 6B1U; 6B2E; 6BX6	HGNC:9377	AAPK2_HUMAN	Reviewed	ENSG00000162409	.	.	.	.	.
Mol01828	Protein	NT-3 growth factor receptor (TrkC)	GP145-TrkC; Trk-C; Neurotrophic tyrosine kinase receptor type 3; TrkC tyrosine kinase; NTRK3; TRKC	NTRK3	4916	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000394480.6,NTRK3-203,19984; ENST00000629765.3,NTRK3-217,20018; ENST00000558676.5,NTRK3-209,4670; ENST00000317501.8,NTRK3-201,4100; ENST00000695463.1,NTRK3-219,4075; ENST00000357724.6,NTRK3-202,2980; ENST00000695462.1,NTRK3-218,2901; ENST00000626019.2,NTRK3-216,2741; ENST00000557856.5,NTRK3-205,2622; ENST00000542733.6,NTRK3-204,2287; ENST00000558576.5,NTRK3-208,717; ENST00000559188.1,NTRK3-210,535; ENST00000560017.1,NTRK3-213,257; ENST00000558306.1,NTRK3-207,629; ENST00000560739.1,NTRK3-215,572; ENST00000559764.2,NTRK3-212,538; ENST00000559680.1,NTRK3-211,441; ENST00000560201.1,NTRK3-214,424; ENST00000557897.1,NTRK3-206,398"	MDVSLCPAKCSFWRIFLLGSVWLDYVGSVLACPANCVCSKTEINCRRPDDGNLFPLLEGQDSGNSNGNASINITDISRNITSIHIENWRSLHTLNAVDMELYTGLQKLTIKNSGLRSIQPRAFAKNPHLRYINLSSNRLTTLSWQLFQTLSLRELQLEQNFFNCSCDIRWMQLWQEQGEAKLNSQNLYCINADGSQLPLFRMNISQCDLPEISVSHVNLTVREGDNAVITCNGSGSPLPDVDWIVTGLQSINTHQTNLNWTNVHAINLTLVNVTSEDNGFTLTCIAENVVGMSNASVALTVYYPPRVVSLEEPELRLEHCIEFVVRGNPPPTLHWLHNGQPLRESKIIHVEYYQEGEISEGCLLFNKPTHYNNGNYTLIAKNPLGTANQTINGHFLKEPFPESTDNFILFDEVSPTPPITVTHKPEEDTFGVSIAVGLAAFACVLLVVLFVMINKYGRRSKFGMKGPVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVVIGMTRIPVIENPQYFRQGHNCHKPDTYVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYRLFNPSGNDFCIWCEVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATPIYLDILG	"chr15:87,859,75188,256,791[-]"	"Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation."	PDB: 1WWC; 3V5Q; 4YMJ; 6KZC; 6KZD	HGNC:8033	NTRK3_HUMAN	Reviewed	ENSG00000140538 	.	.	.	.	.
Mol01829	Protein	Janus kinase 1 (JAK-1)	Janus kinase 1; JAK-1; JAK1; JAK1A; JAK1B	JAK1	3716	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000342505.5,JAK1-201,5092; ENST00000672434.1,JAK1-212,5247; ENST00000672247.1,JAK1-211,5061; ENST00000671954.1,JAK1-208,5042; ENST00000671929.1,JAK1-207,5033; ENST00000673254.1,JAK1-219,4930; ENST00000673046.1,JAK1-216,4893; ENST00000672179.1,JAK1-210,4830; ENST00000673246.1,JAK1-218,4288; ENST00000672574.1,JAK1-213,2718; ENST00000673502.1,JAK1-221,2682; ENST00000672751.1,JAK1-214,1263; ENST00000672099.1,JAK1-209,904; ENST00000673220.1,JAK1-217,7780; ENST00000671746.1,JAK1-206,5243; ENST00000465376.6,JAK1-202,1859; ENST00000672903.1,JAK1-215,1653; ENST00000494904.1,JAK1-205,691; ENST00000673314.1,JAK1-220,5861; ENST00000471473.1,JAK1-203,645; ENST00000481702.1,JAK1-204,314"	MQYLNIKEDCNAMAFCAKMRSSKKTEVNLEAPEPGVEVIFYLSDREPLRLGSGEYTAEELCIRAAQACRISPLCHNLFALYDENTKLWYAPNRTITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKIPDATPLLDASSLEYLFAQGQYDLVKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENEMNWFHSNDGGNVLYYEVMVTGNLGIQWRHKPNVVSVEKEKNKLKRKKLENKHKKDEEKNKIREEWNNFSYFPEITHIVIKESVVSINKQDNKKMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVTCFEKSEQVQGAQKQFKNFQIEVQKGRYSLHGSDRSFPSLGDLMSHLKKQILRTDNISFMLKRCCQPKPREISNLLVATKKAQEWQPVYPMSQLSFDRILKKDLVQGEHLGRGTRTHIYSGTLMDYKDDEGTSEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSECGPFIKLSDPGIPITVLSRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKKPATEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLMQSKFYIASDVWSFGVTLHELLTYCDSDSSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLPCPPNCPDEVYQLMRKCWEFQPSNRTSFQNLIEGFEALLK	"chr1:64,833,22965,067,754[-]"	"Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor."	PDB: 3EYG; 3EYH; 4E4L; 4E4N; 4E5W; 4EHZ; 4EI4; 4FK6; 4GS0; 4I5C; 4IVB; 4IVC; 4IVD; 4K6Z; 4K77; 4L00; 4L01; 5E1E; 5HX8; 5IXD; 5IXI; 5KHW; 5KHX; 5L04; 5WO4; 6AAH; 6BBU; 6C7Y; 6DBN; 6ELR; 6GGH; 6HZU; 6N77; 6N78; 6N79; 6N7A; 6N7B; 6N7C; 6N7D; 6RSB; 6RSC; 6RSD; 6RSE; 6RSH; 6SM8; 6SMB; 6TPE; 6TPF; 6W8L	HGNC:6190	JAK1_HUMAN	Reviewed	ENSG00000162434	.	.	.	.	.
Mol01830	Protein	Proto-oncogene c-Ros (ROS1)	Proto-oncogene c-Ros; Proto-oncogene c-Ros-1; Receptor tyrosine kinase c-ros oncogene 1; c-Ros receptor tyrosine kinase; ROS1; MCF3; ROS	ROS1	6098	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368507.8,ROS1-201,8451; ENST00000368508.7,ROS1-202,7435; ENST00000403284.2,ROS1-203,681"	MKNIYCLIPKLVNFATLGCLWISVVQCTVLNSCLKSCVTNLGQQLDLGTPHNLSEPCIQGCHFWNSVDQKNCALKCRESCEVGCSSAEGAYEEEVLENADLPTAPFASSIGSHNMTLRWKSANFSGVKYIIQWKYAQLLGSWTYTKTVSRPSYVVKPLHPFTEYIFRVVWIFTAQLQLYSPPSPSYRTHPHGVPETAPLIRNIESSSPDTVEVSWDPPQFPGGPILGYNLRLISKNQKLDAGTQRTSFQFYSTLPNTIYRFSIAAVNEVGEGPEAESSITTSSSAVQQEEQWLFLSRKTSLRKRSLKHLVDEAHCLRLDAIYHNITGISVDVHQQIVYFSEGTLIWAKKAANMSDVSDLRIFYRGSGLISSISIDWLYQRMYFIMDELVCVCDLENCSNIEEITPPSISAPQKIVADSYNGYVFYLLRDGIYRADLPVPSGRCAEAVRIVESCTLKDFAIKPQAKRIIYFNDTAQVFMSTFLDGSASHLILPRIPFADVKSFACENNDFLVTDGKVIFQQDALSFNEFIVGCDLSHIEEFGFGNLVIFGSSSQLHPLPGRPQELSVLFGSHQALVQWKPPALAIGANVILISDIIELFELGPSAWQNWTYEVKVSTQDPPEVTHIFLNISGTMLNVPELQSAMKYKVSVRASSPKRPGPWSEPSVGTTLVPASEPPFIMAVKEDGLWSKPLNSFGPGEFLSSDIGNVSDMDWYNNSLYYSDTKGDVFVWLLNGTDISENYHLPSIAGAGALAFEWLGHFLYWAGKTYVIQRQSVLTGHTDIVTHVKLLVNDMVVDSVGGYLYWTTLYSVESTRLNGESSLVLQTQPWFSGKKVIALTLDLSDGLLYWLVQDSQCIHLYTAVLRGQSTGDTTITEFAAWSTSEISQNALMYYSGRLFWINGFRIITTQEIGQKTSVSVLEPARFNQFTIIQTSLKPLPGNFSFTPKVIPDSVQESSFRIEGNASSFQILWNGPPAVDWGVVFYSVEFSAHSKFLASEQHSLPVFTVEGLEPYALFNLSVTPYTYWGKGPKTSLSLRAPETVPSAPENPRIFILPSGKCCNKNEVVVEFRWNKPKHENGVLTKFEIFYNISNQSITNKTCEDWIAVNVTPSVMSFQLEGMSPRCFIAFQVRAFTSKGPGPYADVVKSTTSEINPFPHLITLLGNKIVFLDMDQNQVVWTFSAERVISAVCYTADNEMGYYAEGDSLFLLHLHNRSSSELFQDSLVFDITVITIDWISRHLYFALKESQNGMQVFDVDLEHKVKYPREVKIHNRNSTIISFSVYPLLSRLYWTEVSNFGYQMFYYSIISHTLHRILQPTATNQQNKRNQCSCNVTEFELSGAMAIDTSNLEKPLIYFAKAQEIWAMDLEGCQCWRVITVPAMLAGKTLVSLTVDGDLIYWIITAKDSTQIYQAKKGNGAIVSQVKALRSRHILAYSSVMQPFPDKAFLSLASDTVEPTILNATNTSLTIRLPLAKTNLTWYGITSPTPTYLVYYAEVNDRKNSSDLKYRILEFQDSIALIEDLQPFSTYMIQIAVKNYYSDPLEHLPPGKEIWGKTKNGVPEAVQLINTTVRSDTSLIISWRESHKPNGPKESVRYQLAISHLALIPETPLRQSEFPNGRLTLLVTRLSGGNIYVLKVLACHSEEMWCTESHPVTVEMFNTPEKPYSLVPENTSLQFNWKAPLNVNLIRFWVELQKWKYNEFYHVKTSCSQGPAYVCNITNLQPYTSYNVRVVVVYKTGENSTSLPESFKTKAGVPNKPGIPKLLEGSKNSIQWEKAEDNGCRITYYILEIRKSTSNNLQNQNLRWKMTFNGSCSSVCTWKSKNLKGIFQFRVVAANNLGFGEYSGISENIILVGDDFWIPETSFILTIIVGIFLVVTIPLTFVWHRRLKNQKSAKEGVTVLINEDKELAELRGLAAGVGLANACYAIHTLPTQEEIENLPAFPREKLTLRLLLGSGAFGEVYEGTAVDILGVGSGEIKVAVKTLKKGSTDQEKIEFLKEAHLMSKFNHPNILKQLGVCLLNEPQYIILELMEGGDLLTYLRKARMATFYGPLLTLVDLVDLCVDISKGCVYLERMHFIHRDLAARNCLVSVKDYTSPRIVKIGDFGLARDIYKNDYYRKRGEGLLPVRWMAPESLMDGIFTTQSDVWSFGILIWEILTLGHQPYPAHSNLDVLNYVQTGGRLEPPRNCPDDLWNLMTQCWAQEPDQRPTFHRIQDQLQLFRNFFLNSIYKSRDEANNSGVINESFEGEDGDVICLNSDDIMPVALMETKNREGLNYMVLATECGQGEEKSEGPLGSQESESCGLRKEEKEPHADKDFCQEKQVAYCPSGKPEGLNYACLTHSGYGDGSD	"chr6:117,287,353117,425,942[-]"	"Orphan receptor tyrosine kinase (RTK) that plays a role in epithelial cell differentiation and regionalization of the proximal epididymal epithelium. May activate several downstream signaling pathways related to cell differentiation, proliferation, growth and survival including the PI3 kinase-mTOR signaling pathway. Mediates the phosphorylation of PTPN11, an activator of this pathway. May also phosphorylate and activate the transcription factor STAT3 to control anchorage-independent cell growth. Mediates the phosphorylation and the activation of VAV3, a guanine nucleotide exchange factor regulating cell morphology. May activate other downstream signaling proteins including AKT1, MAPK1, MAPK3, IRS1 and PLCG2."	PDB: 3ZBF; 4UXL	HGNC:10261	ROS1_HUMAN	Reviewed	ENSG00000047936	.	.	.	.	.
Mol01831	Protein	Tropomyosin-related kinase A (TrkA)	Neurotrophic tyrosine kinase receptor type 1; TRK1-transforming tyrosine kinase protein; Tropomyosin-related kinase A; Tyrosine kinase receptor; Tyrosine kinase receptor A; Trk-A; gp140trk; p140-TrkA; NTRK1; MTC; TRK; TRKA	NTRK1	4914	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000524377.7,NTRK1-206,2669; ENST00000674537.1,NTRK1-211,2748; ENST00000368196.7,NTRK1-202,2701; ENST00000392302.7,NTRK1-203,2665; ENST00000358660.3,NTRK1-201,2492; ENST00000675461.1,NTRK1-212,1208; ENST00000497019.7,NTRK1-205,2508; ENST00000531606.2,NTRK1-208,658; ENST00000489021.6,NTRK1-204,570; ENST00000530298.5,NTRK1-207,3052; ENST00000534682.1,NTRK1-210,844; ENST00000533630.1,NTRK1-209,645"	MLRGGRRGQLGWHSWAAGPGSLLAWLILASAGAAPCPDACCPHGSSGLRCTRDGALDSLHHLPGAENLTELYIENQQHLQHLELRDLRGLGELRNLTIVKSGLRFVAPDAFHFTPRLSRLNLSFNALESLSWKTVQGLSLQELVLSGNPLHCSCALRWLQRWEEEGLGGVPEQKLQCHGQGPLAHMPNASCGVPTLKVQVPNASVDVGDDVLLRCQVEGRGLEQAGWILTELEQSATVMKSGGLPSLGLTLANVTSDLNRKNVTCWAENDVGRAEVSVQVNVSFPASVQLHTAVEMHHWCIPFSVDGQPAPSLRWLFNGSVLNETSFIFTEFLEPAANETVRHGCLRLNQPTHVNNGNYTLLAANPFGQASASIMAAFMDNPFEFNPEDPIPVSFSPVDTNSTSGDPVEKKDETPFGVSVAVGLAVFACLFLSTLLLVLNKCGRRNKFGINRPAVLAPEDGLAMSLHFMTLGGSSLSPTEGKGSGLQGHIIENPQYFSDACVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEASESARQDFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIMRGCWQREPQQRHSIKDVHARLQALAQAPPVYLDVLG	"chr1:156,815,640156,881,850[+]"	"Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand. Can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival. Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation. Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors.; [Isoform TrkA-III]: Resistant to NGF, it constitutively activates AKT1 and NF-kappa-B and is unable to activate the Ras-MAPK signaling cascade. Antagonizes the anti-proliferative NGF-NTRK1 signaling that promotes neuronal precursors differentiation. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed."	PDB: 1HE7; 1SHC; 1WWA; 1WWW; 2IFG; 2N90; 4AOJ; 4CRP; 4F0I; 4GT5; 4PMM; 4PMP; 4PMS; 4PMT; 4YNE; 4YPS; 5H3Q; 5I8A; 5JFS; 5JFV; 5JFW; 5JFX; 5KMI; 5KMJ; 5KMK; 5KML; 5KMM; 5KMN; 5KMO; 5KVT; 5WR7; 6D1Y; 6D1Z; 6D20; 6D22; 6DKB; 6DKG; 6DKI; 6DKW; 6IQN; 6J5L; 6NPT; 6NSP; 6NSS; 6PL1; 6PL2; 6PL3; 6PL4; 6PMA; 6PMB; 6PMC; 6PME	HGNC:8031	NTRK1_HUMAN	Reviewed	ENSG00000198400	.	.	.	.	.
Mol01832	Protein	VEGF-2 receptor (KDR)	VEGFR-2; Fetal liver kinase 1; FLK-1; Kinase insert domain receptor; KDR; Protein-tyrosine kinase receptor flk-1; CD antigen CD309; KDR; FLK1; VEGFR2	KDR	3791	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263923.5,KDR-201,5833; ENST00000647068.1,KDR-204,5494; ENST00000512566.1,KDR-203,2037; ENST00000509309.1,KDR-202,687"	MQSKVLLAVALWLCVETRAASVGLPSVSLDLPRLSIQKDILTIKANTTLQITCRGQRDLDWLWPNNQSGSEQRVEVTECSDGLFCKTLTIPKVIGNDTGAYKCFYRETDLASVIYVYVQDYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISWDSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVGEKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTRSDQGLYTCAASSGLMTKKNSTFVRVHEKPFVAFGSGMESLVEATVGERVRIPAKYLGYPPPEIKWYKNGIPLESNHTIKAGHVLTIMEVSERDTGNYTVILTNPISKEKQSHVVSLVVYVPPQIGEKSLISPVDSYQYGTTQTLTCTVYAIPPPHHIHWYWQLEEECANEPSQAVSVTNPYPCEEWRSVEDFQGGNKIEVNKNQFALIEGKNKTVSTLVIQAANVSALYKCEAVNKVGRGERVISFHVTRGPEITLQPDMQPTEQESVSLWCTADRSTFENLTWYKLGPQPLPIHVGELPTPVCKNLDTLWKLNATMFSNSTNDILIMELKNASLQDQGDYVCLAQDRKTKKRHCVVRQLTVLERVAPTITGNLENQTTSIGESIEVSCTASGNPPPQIMWFKDNETLVEDSGIVLKDGNRNLTIRRVRKEDEGLYTCQACSVLGCAKVEAFFIIEGAQEKTNLEIIILVGTAVIAMFFWLLLVIILRTVKRANGGELKTGYLSIVMDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYKTKGARFRQGKDYVGAIPVDLKRRLDSITSSQSSASSGFVEEKSLSDVEEEEAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLLQANAQQDGKDYIVLPISETLSMEEDSGLSLPTSPVSCMEEEEVCDPKFHYDNTAGISQYLQNSKRKSRPVSVKTFEDIPLEEPEVKVIPDDNQTDSGMVLASEELKTLEDRTKLSPSFGGMVPSKSRESVASEGSNQTSGYQSGYHSDDTDTTVYSSEEAELLKLIEIGVQTGSTAQILQPDSGTTLSSPPV	"chr4:55,078,48155,125,595 [-]"	"Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC."	PDB: 1VR2; 1Y6A; 1Y6B; 1YWN; 2M59; 2MET; 2MEU; 2OH4; 2P2H; 2P2I; 2QU5; 2QU6; 2RL5; 2X1W; 2X1X; 2XIR; 3B8Q; 3B8R; 3BE2; 3C7Q; 3CJF; 3CJG; 3CP9; 3CPB; 3CPC; 3DTW; 3EFL; 3EWH; 3KVQ; 3S35; 3S36; 3S37; 3U6J; 3V2A; 3V6B; 3VHE; 3VHK; 3VID; 3VNT; 3VO3; 3WZD; 3WZE; 4AG8; 4AGC; 4AGD; 4ASD; 4ASE; 5EW3; 5OYJ; 6GQO; 6GQP; 6GQQ; 6XVJ; 6XVK	HGNC:6307	VGFR2_HUMAN	Reviewed	ENSG00000128052	.	.	.	.	.
Mol01833	Protein	Calreticulin (CALR)	CRP55; Calregulin; Endoplasmic reticulum resident protein 60; ERp60; HACBP; grp60; CALR; CRTC	CALR	811	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000316448.10,CALR-201,1901; ENST00000588454.6,CALR-206,1661; ENST00000586760.2,CALR-202,1630; ENST00000586967.2,CALR-204,1678; ENST00000680816.1,CALR-208,1564; ENST00000587486.6,CALR-205,957; ENST00000590325.1,CALR-207,781; ENST00000586803.1,CALR-203,667"	MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL	"chr19:12,938,57812,944,489[+]"	"Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy."	PDB: 2CLR; 3DOW; 3POS; 3POW; 5LK5; 5V90; 6ENY	HGNC:1455	CALR_HUMAN	Reviewed	ENSG00000179218	.	.	.	.	.
Mol01834	Protein	Splicing factor 3B subunit 1 (SF3B1)	Splicing factor 3B subunit 1; (Pre-mRNA-splicing factor SF3b 155 kDa subunit; SF3b155; Spliceosome-associated protein 155; SAP 155	SF3B1	23451	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000335508.11,SF3B1-201,6463; ENST00000487698.5,SF3B1-211,2127; ENST00000424674.1,SF3B1-205,723; ENST00000414963.2,SF3B1-204,651; ENST00000652026.1,SF3B1-213,9283; ENST00000652738.1,SF3B1-214,8478; ENST00000409915.8,SF3B1-202,600; ENST00000414174.1,SF3B1-203,593; ENST00000462613.1,SF3B1-206,141; ENST00000470268.2,SF3B1-208,8308; ENST00000482158.1,SF3B1-210,772; ENST00000479532.1,SF3B1-209,587; ENST00000468925.1,SF3B1-207,510; ENST00000496458.1,SF3B1-212,475"	MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGGDSIGETPTPGASKRKSRWDETPASQMGGSTPVLTPGKTPIGTPAMNMATPTPGHIMSMTPEQLQAWRWEREIDERNRPLSDEELDAMFPEGYKVLPPPAGYVPIRTPARKLTATPTPLGGMTGFHMQTEDRTMKSVNDQPSGNLPFLKPDDIQYFDKLLVDVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCGTDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPRIYNDDKNTYIRYELDYIL	"chr2:197,388,515-197,435,079[-]"	"Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92. May also be involved in the assembly of the 'E' complex. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron."	PDB: 2F9D; PDB: 2F9J; PDB: 2FHO; PDB: 2PEH; PDB: 3LQV; PDB: 4OZ1; PDB: 5IFE; PDB: 5O9Z; PDB: 5Z56; PDB: 5Z57; PDB: 5Z58; PDB: 5ZYA; PDB: 6AH0; PDB: 6AHD; PDB: 6EN4; PDB: 6FF4; PDB: 6FF7; PDB: 6N3E; PDB: 6QX9; PDB: 6Y50; PDB: 6Y53; PDB: 6Y5Q; PDB: 7ABG; PDB: 7ABH; PDB: 7ABI; PDB: 7B0I; PDB: 7B91; PDB: 7B92; PDB: 7B9C; PDB: 7DVQ; PDB: 7OMF; PDB: 7ONB; PDB: 7OPI	HGNC:10768	SF3B1_HUMAN	Reviewed	ENSG00000115524	.	.	.	.	.
Mol01835	Protein	Guanine nucleotide-binding protein subunit alpha-11 (GNA11)	Guanine nucleotide-binding protein subunit alpha-11; G alpha-11; G-protein subunit alpha-11; Guanine nucleotide-binding protein G(y) subunit alpha; GNA11; GA11	GNA11	2767	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000078429.9,GNA11-201,4190; ENST00000587636.1,GNA11-204,733; ENST00000588401.1,GNA11-205,295; ENST00000586180.1,GNA11-202,739; ENST00000586763.1,GNA11-203,354; ENST00000590534.1,GNA11-206,2676; ENST00000591301.1,GNA11-207,389"	MTLESMMACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR IIHGAGYSEE DKRGFTKLVY QNIFTAMQAM IRAMETLKIL YKYEQNKANA LLIREVDVEK VTTFEHQYVS AIKTLWEDPG IQECYDRRRE YQLSDSAKYY LTDVDRIATL GYLPTQQDVL RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE DKILYSHLVD YFPEFDGPQR DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV	"chr19:3,094,362-3,123,999[+]"	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C. Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs).	PDB: 6OIJ; PDB: 7RKF	HGNC:4379	GNA11_HUMAN	Reviewed	ENSG00000088256	.	.	.	.	.
Mol01836	Protein	Fibroblast growth factor receptor 3 (FGFR3)	Fibroblast growth factor receptor 3; FGFR-3; CD antigen CD333; JTK4	FGFR3	2261	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000440486.8,FGFR3-205,4301; ENST00000412135.7,FGFR3-204,4294; ENST00000340107.8,FGFR3-202,4293; ENST00000481110.7,FGFR3-208,4149; ENST00000352904.6,FGFR3-203,2184; ENST00000507588.1,FGFR3-209,336; ENST00000260795.8,FGFR3-201,2841; ENST00000643463.1,FGFR3-210,417; ENST00000469068.1,FGFR3-206,821; ENST00000474521.1,FGFR3-207,545"	MGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT	"chr4:1,793,293-1,808,872[+]"	"Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling."	PDB: 1RY7; PDB: 2LZL; PDB: 4K33; PDB: 6LVM; PDB: 6PNX; PDB: 7DHL	HGNC:3690	FGFR3_HUMAN	Reviewed	ENSG00000068078	.	.	.	.	.
Mol01837	Protein	Fibroblast growth factor receptor 4 (FGFR4)	Fibroblast growth factor receptor 4; FGFR-4; CD antigen CD334; JTK2; TKF	FGFR4	2264	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000292408.9,FGFR4-201,3093; ENST00000393637.5,FGFR4-202,2418; ENST00000393648.6,FGFR4-203,2733; ENST00000426612.5,FGFR4-204,712; ENST00000430285.5,FGFR4-205,713; ENST00000483872.2,FGFR4-206,663; ENST00000502906.5,FGFR4-207,2638; ENST00000503708.5,FGFR4-208,770; ENST00000507708.1,FGFR4-209,476; ENST00000508139.1,FGFR4-210,720; ENST00000509511.5,FGFR4-211,1341; ENST00000510911.5,FGFR4-212,709; ENST00000511076.1,FGFR4-213,838; ENST00000513166.1,FGFR4-214,594; ENST00000513423.1,FGFR4-215,445; ENST00000514472.1,FGFR4-216,552"	MRLLLALLGVLLSVPGPPVLSLEASEEVELEPCLAPSLEQQEQELTVALGQPVRLCCGRAERGGHWYKEGSRLAPAGRVRGWRGRLEIASFLPEDAGRYLCLARGSMIVLQNLTLITGDSLTSSNDDEDPKSHRDPSNRHSYPQQAPYWTHPQRMEKKLHAVPAGNTVKFRCPAAGNPTPTIRWLKDGQAFHGENRIGGIRLRHQHWSLVMESVVPSDRGTYTCLVENAVGSIRYNYLLDVLERSPHRPILQAGLPANTTAVVGSDVELLCKVYSDAQPHIQWLKHIVINGSSFGADGFPYVQVLKTADINSSEVEVLYLRNVSAEDAGEYTCLAGNSIGLSYQSAWLTVLPEEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQALHGRHPRPPATVQKLSRFPLARQFSLESGSSGKSSSSLVRGVRLSSSGPALLAGLVSLDLPLDPLWEFPRDRLVLGKPLGEGCFGQVVRAEAFGMDPARPDQASTVAVKMLKDNASDKDLADLVSEMEVMKLIGRHKNIINLLGVCTQEGPLYVIVECAAKGNLREFLRARRPPGPDLSPDGPRSSEGPLSFPVLVSCAYQVARGMQYLESRKCIHRDLAARNVLVTEDNVMKIADFGLARGVHHIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILLWEIFTLGGSPYPGIPVEELFSLLREGHRMDRPPHCPPELYGLMRECWHAAPSQRPTFKQLVEALDKVLLAVSEEYLDLRLTFGPYSPSGGDASSTCSSSDSVFSHDPLPLGSSSFPFGSGVQT	"chr5:177,086,905-177,098,144[+]"	"Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling."	PDB: 4QQ5; PDB: 4QQC; PDB: 4QQJ; PDB: 4QQT; PDB: 4QRC; PDB: 4R6V; PDB: 4TYE; PDB: 4TYG; PDB: 4TYI; PDB: 4TYJ; PDB: 4UXQ; PDB: 4XCU; PDB: 5JKG; PDB: 5NUD; PDB: 5NWZ; PDB: 5XFF; PDB: 5XFJ; PDB: 6IUO; PDB: 6IUP; PDB: 6J6Y; PDB: 6JPE; PDB: 6JPJ; PDB: 6NVG; PDB: 6NVH; PDB: 6NVI; PDB: 6NVJ; PDB: 6NVK; PDB: 6V9C; PDB: 6YI8; PDB: 7DTZ; PDB: 7F3M	HGNC:3691	FGFR4_HUMAN	Reviewed	ENSG00000160867	.	.	.	.	.
Mol01838	Protein	Granulocyte colony-stimulating factor receptor (CSF3R)	Granulocyte colony-stimulating factor receptor; G-CSF receptor; G-CSF-R; CD antigen CD114; CSF3R; GCSFR	CSF3R	1441	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331941.6,CSF3R-201,2375; ENST00000361632.8,CSF3R-202,2847; ENST00000373103.5,CSF3R-203,3454; ENST00000373104.5,CSF3R-204,2953; ENST00000373106.6,CSF3R-205,3008; ENST00000464365.2,CSF3R-206,1659; ENST00000464465.6,CSF3R-207,1440; ENST00000466138.1,CSF3R-208,335; ENST00000469380.1,CSF3R-209,321; ENST00000480825.6,CSF3R-210,6074; ENST00000484762.1,CSF3R-211,677; ENST00000487540.6,CSF3R-212,1931; ENST00000489551.5,CSF3R-213,787; ENST00000526980.5,CSF3R-214,928; ENST00000533491.1,CSF3R-215,512"	MARLGNCSLTWAALIILLLPGSLEECGHISVSAPIVHLGDPITASCIIKQNCSHLDPEPQILWRLGAELQPGGRQQRLSDGTQESIITLPHLNHTQAFLSCCLNWGNSLQILDQVELRAGYPPAIPHNLSCLMNLTTSSLICQWEPGPETHLPTSFTLKSFKSRGNCQTQGDSILDCVPKDGQSHCCIPRKHLLLYQNMGIWVQAENALGTSMSPQLCLDPMDVVKLEPPMLRTMDPSPEAAPPQAGCLQLCWEPWQPGLHINQKCELRHKPQRGEASWALVGPLPLEALQYELCGLLPATAYTLQIRCIRWPLPGHWSDWSPSLELRTTERAPTVRLDTWWRQRQLDPRTVQLFWKPVPLEEDSGRIQGYVVSWRPSGQAGAILPLCNTTELSCTFHLPSEAQEVALVAYNSAGTSRPTPVVFSESRGPALTRLHAMARDPHSLWVGWEPPNPWPQGYVIEWGLGPPSASNSNKTWRMEQNGRATGFLLKENIRPFQLYEIIVTPLYQDTMGPSQHVYAYSQEMAPSHAPELHLKHIGKTWAQLEWVPEPPELGKSPLTHYTIFWTNAQNQSFSAILNASSRGFVLHGLEPASLYHIHLMAASQAGATNSTVLTLMTLTPEGSELHIILGLFGLLLLLTCLCGTAWLCCSPNRKNPLWPSVPDPAHSSLGSWVPTIMEEDAFQLPGLGTPPITKLTVLEEDEKKPVPWESHNSSETCGLPTLVQTYVLQGDPRAVSTQPQSQSGTSDQVLYGQLLGSPTSPGPGHYLRCDSTQPLLAGLTPSPKSYENLWFQASPLGTLVTPAPSQEDDCVFGPLLNFPLLQGIRVHGMEALGSF	"chr1:36,466,043-36,483,278[-]"	"Receptor for granulocyte colony-stimulating factor (CSF3), essential for granulocytic maturation. Plays a crucial role in the proliferation, differientation and survival of cells along the neutrophilic lineage. In addition it may function in some adhesion or recognition events at the cell surface."	PDB: 2D9Q	HGNC:2439	CSF3R_HUMAN	Reviewed	ENSG00000119535	.	.	.	.	.
Mol01839	Protein	Proto-oncogene tyrosine-protein kinase receptor Ret (RET)	Proto-oncogene tyrosine-protein kinase receptor Ret; Cadherin family member 12; Proto-oncogene c-Ret	RET	5979	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000684216.1,RET-212,737; ENST00000683872.1,RET-211,3004; ENST00000683278.1,RET-210,756; ENST00000683007.1,RET-209,6310; ENST00000672389.1,RET-208,2240; ENST00000671844.1,RET-207,3457; ENST00000640619.1,RET-206,608; ENST00000638465.1,RET-205,773; ENST00000615310.5,RET-204,6513; ENST00000498820.5,RET-203,729; ENST00000355710.8,RET-202,5617; ENST00000340058.6,RET-201,4159"	MAKATSGAAGLRLLLLLLLPLLGKVALGLYFSRDAYWEKLYVDQAAGTPLLYVHALRDAPEEVPSFRLGQHLYGTYRTRLHENNWICIQEDTGLLYLNRSLDHSSWEKLSVRNRGFPLLTVYLKVFLSPTSLREGECQWPGCARVYFSFFNTSFPACSSLKPRELCFPETRPSFRIRENRPPGTFHQFRLLPVQFLCPNISVAYRLLEGEGLPFRCAPDSLEVSTRWALDREQREKYELVAVCTVHAGAREEVVMVPFPVTVYDEDDSAPTFPAGVDTASAVVEFKRKEDTVVATLRVFDADVVPASGELVRRYTSTLLPGDTWAQQTFRVEHWPNETSVQANGSFVRATVHDYRLVLNRNLSISENRTMQLAVLVNDSDFQGPGAGVLLLHFNVSVLPVSLHLPSTYSLSVSRRARRFAQIGKVCVENCQAFSGINVQYKLHSSGANCSTLGVVTSAEDTSGILFVNDTKALRRPKCAELHYMVVATDQQTSRQAQAQLLVTVEGSYVAEEAGCPLSCAVSKRRLECEECGGLGSPTGRCEWRQGDGKGITRNFSTCSPSTKTCPDGHCDVVETQDINICPQDCLRGSIVGGHEPGEPRGIKAGYGTCNCFPEEEKCFCEPEDIQDPLCDELCRTVIAAAVLFSFIVSVLLSAFCIHCYHKFAHKPPISSAEMTFRRPAQAFPVSYSSSGARRPSLDSMENQVSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSLRGFLRESRKVGPGYLGSGGSRNSSSLDHPDERALTMGDLISFAWQISQGMQYLAEMKLVHRDLAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRRDYLDLAASTPSDSLIYDDGLSEEETPLVDCNNAPLPRALPSTWIENKLYGMSDPNWPGESPVPLTRADGTNTGFPRYPNDSVYANWMLSPSAAKLMDTFDS	"chr10:43,077,064-43,130,351[+]"	"Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration. Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which induces inhibition of food-intake. Activates MAPK- and AKT-signaling pathways. Isoform 1 in complex with GFRAL induces higher activation of MAPK-signaling pathway than isoform 2 in complex with GFRAL."	PDB: 2IVS; PDB: 2IVT; PDB: 2IVU; PDB: 2IVV; PDB: 2X2K; PDB: 2X2L; PDB: 2X2M; PDB: 2X2U; PDB: 4CKI; PDB: 4CKJ; PDB: 4UX8; PDB: 5AMN; PDB: 5FM2; PDB: 5FM3; PDB: 6FEK; PDB: 6GL7; PDB: 6I82; PDB: 6I83; PDB: 6NE7; PDB: 6NEC; PDB: 6NJA; PDB: 6Q2J; PDB: 6Q2N; PDB: 6Q2O; PDB: 6Q2R; PDB: 6Q2S; PDB: 6VHG; PDB: 7DU9; PDB: 7DUA; PDB: 7JU5; PDB: 7JU6; PDB: 7RUN	HGNC:9967	RET_HUMAN	Reviewed	ENSG00000165731	.	.	.	.	.
Mol01840	Protein	Transcription activator BRG1 (BRG1)	Transcription activator BRG1; ATP-dependent helicase SMARCA4; BRG1-associated factor 190A; BAF190A; Mitotic growth and transcription activator; Protein BRG-1; Protein brahma homolog 1; SNF2-beta; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4	SMARCA4	6597	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000647268.1,SMARCA4-252,3522; ENST00000647230.1,SMARCA4-251,5554; ENST00000647011.1,SMARCA4-250,487; ENST00000646889.1,SMARCA4-249,1659; ENST00000646746.1,SMARCA4-248,3680; ENST00000646693.2,SMARCA4-247,5670; ENST00000646593.1,SMARCA4-246,3206; ENST00000646513.1,SMARCA4-245,1127; ENST00000646510.1,SMARCA4-244,5595; ENST00000646484.1,SMARCA4-243,5579; ENST00000646236.1,SMARCA4-242,2802; ENST00000646183.1,SMARCA4-241,3496; ENST00000645648.1,SMARCA4-240,3250; ENST00000645460.1,SMARCA4-239,5457; ENST00000645387.1,SMARCA4-238,627; ENST00000645236.1,SMARCA4-237,1887; ENST00000645061.1,SMARCA4-236,4035; ENST00000644963.1,SMARCA4-235,4045; ENST00000644760.1,SMARCA4-234,740; ENST00000644737.1,SMARCA4-233,5777; ENST00000644327.1,SMARCA4-232,4237; ENST00000644290.1,SMARCA4-231,3355; ENST00000644267.1,SMARCA4-230,3382; ENST00000644065.1,SMARCA4-229,3802; ENST00000643995.1,SMARCA4-228,4817; ENST00000643929.1,SMARCA4-227,1865; ENST00000643857.1,SMARCA4-226,3637; ENST00000643549.1,SMARCA4-225,5609; ENST00000643534.1,SMARCA4-224,3426; ENST00000643296.1,SMARCA4-223,5563; ENST00000643208.1,SMARCA4-222,3940; ENST00000642726.1,SMARCA4-221,5675; ENST00000642628.1,SMARCA4-220,5637; ENST00000642508.1,SMARCA4-219,2612; ENST00000642350.1,SMARCA4-218,3750; ENST00000592604.6,SMARCA4-217,3358; ENST00000592158.2,SMARCA4-216,911; ENST00000591595.5,SMARCA4-215,3377; ENST00000591545.6,SMARCA4-214,5192; ENST00000590574.6,SMARCA4-213,5739; ENST00000589677.5,SMARCA4-212,5181; ENST00000587988.5,SMARCA4-211,552; ENST00000586985.2,SMARCA4-210,1968; ENST00000586921.1,SMARCA4-209,569; ENST00000586892.1,SMARCA4-208,559; ENST00000586122.5,SMARCA4-207,512; ENST00000585799.5,SMARCA4-206,3842; ENST00000541122.6,SMARCA4-205,5139; ENST00000538456.4,SMARCA4-204,1108; ENST00000444061.8,SMARCA4-203,5393; ENST00000429416.8,SMARCA4-202,5665; ENST00000344626.10,SMARCA4-201,5577"	MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED	"chr19:10,960,932-11,079,426[+]"	"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development, a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By similarity). Binds to RNA in a promiscuous manner (By similarity). Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4 ATPase and chromatin remodeling activities (By similarity)."	PDB: 2GRC; PDB: 2H60; PDB: 3UVD; PDB: 5DKD; PDB: 5EA1; PDB: 6BGH; PDB: 6HR2; PDB: 6LTH; PDB: 6LTJ; PDB: 6SY2; PDB: 6ZS2	HGNC:11100	SMCA4_HUMAN	Reviewed	ENSG00000127616	.	.	.	.	.
Mol01841	Protein	Guanine nucleotide-binding protein alpha-q (GNAQ)	Guanine nucleotide-binding protein G(q) subunit alpha; Guanine nucleotide-binding protein alpha-q; GNAQ; GAQ	GNAQ	2776	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000411677.1,GNAQ-202,551; ENST00000286548.9,GNAQ-201,6882"	MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV	"chr9:77,716,097-78,031,811[-]"	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs).	PDB: 6VU5; PDB: 7EZM; PDB: 7F6H; PDB: 7F6I; PDB: 7F8W	HGNC:4390	GNAQ_HUMAN	Reviewed	ENSG00000156052	.	.	.	.	.
Mol01842	Protein	Breast cancer type 2 susceptibility protein (BRCA2)	Fanconi anemia group D1 protein; BRCA2; FACD; FANCD1	BRCA2	675	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000680887.1,BRCA2-210,11880; ENST00000666593.1,BRCA2-209,523; ENST00000665585.1,BRCA2-208,2598; ENST00000614259.2,BRCA2-207,11763; ENST00000544455.6,BRCA2-206,11854; ENST00000533776.1,BRCA2-205,523; ENST00000530893.6,BRCA2-204,2011; ENST00000528762.1,BRCA2-203,495; ENST00000470094.1,BRCA2-202,842; ENST00000380152.8,BRCA2-201,11954"	MPIGSKERPTFFEIFKTRCNKADLGPISLNWFEELSSEAPPYNSEPAEESEHKNNNYEPNLFKTPQRKPSYNQLASTPIIFKEQGLTLPLYQSPVKELDKFKLDLGRNVPNSRHKSLRTVKTKMDQADDVSCPLLNSCLSESPVVLQCTHVTPQRDKSVVCGSLFHTPKFVKGRQTPKHISESLGAEVDPDMSWSSSLATPPTLSSTVLIVRNEEASETVFPHDTTANVKSYFSNHDESLKKNDRFIASVTDSENTNQREAASHGFGKTSGNSFKVNSCKDHIGKSMPNVLEDEVYETVVDTSEEDSFSLCFSKCRTKNLQKVRTSKTRKKIFHEANADECEKSKNQVKEKYSFVSEVEPNDTDPLDSNVANQKPFESGSDKISKEVVPSLACEWSQLTLSGLNGAQMEKIPLLHISSCDQNISEKDLLDTENKRKKDFLTSENSLPRISSLPKSEKPLNEETVVNKRDEEQHLESHTDCILAVKQAISGTSPVASSFQGIKKSIFRIRESPKETFNASFSGHMTDPNFKKETEASESGLEIHTVCSQKEDSLCPNLIDNGSWPATTTQNSVALKNAGLISTLKKKTNKFIYAIHDETSYKGKKIPKDQKSELINCSAQFEANAFEAPLTFANADSGLLHSSVKRSCSQNDSEEPTLSLTSSFGTILRKCSRNETCSNNTVISQDLDYKEAKCNKEKLQLFITPEADSLSCLQEGQCENDPKSKKVSDIKEEVLAAACHPVQHSKVEYSDTDFQSQKSLLYDHENASTLILTPTSKDVLSNLVMISRGKESYKMSDKLKGNNYESDVELTKNIPMEKNQDVCALNENYKNVELLPPEKYMRVASPSRKVQFNQNTNLRVIQKNQEETTSISKITVNPDSEELFSDNENNFVFQVANERNNLALGNTKELHETDLTCVNEPIFKNSTMVLYGDTGDKQATQVSIKKDLVYVLAEENKNSVKQHIKMTLGQDLKSDISLNIDKIPEKNNDYMNKWAGLLGPISNHSFGGSFRTASNKEIKLSEHNIKKSKMFFKDIEEQYPTSLACVEIVNTLALDNQKKLSKPQSINTVSAHLQSSVVVSDCKNSHITPQMLFSKQDFNSNHNLTPSQKAEITELSTILEESGSQFEFTQFRKPSYILQKSTFEVPENQMTILKTTSEECRDADLHVIMNAPSIGQVDSSKQFEGTVEIKRKFAGLLKNDCNKSASGYLTDENEVGFRGFYSAHGTKLNVSTEALQKAVKLFSDIENISEETSAEVHPISLSSSKCHDSVVSMFKIENHNDKTVSEKNNKCQLILQNNIEMTTGTFVEEITENYKRNTENEDNKYTAASRNSHNLEFDGSDSSKNDTVCIHKDETDLLFTDQHNICLKLSGQFMKEGNTQIKEDLSDLTFLEVAKAQEACHGNTSNKEQLTATKTEQNIKDFETSDTFFQTASGKNISVAKESFNKIVNFFDQKPEELHNFSLNSELHSDIRKNKMDILSYEETDIVKHKILKESVPVGTGNQLVTFQGQPERDEKIKEPTLLGFHTASGKKVKIAKESLDKVKNLFDEKEQGTSEITSFSHQWAKTLKYREACKDLELACETIEITAAPKCKEMQNSLNNDKNLVSIETVVPPKLLSDNLCRQTENLKTSKSIFLKVKVHENVEKETAKSPATCYTNQSPYSVIENSALAFYTSCSRKTSVSQTSLLEAKKWLREGIFDGQPERINTADYVGNYLYENNSNSTIAENDKNHLSEKQDTYLSNSSMSNSYSYHSDEVYNDSGYLSKNKLDSGIEPVLKNVEDQKNTSFSKVISNVKDANAYPQTVNEDICVEELVTSSSPCKNKNAAIKLSISNSNNFEVGPPAFRIASGKIVCVSHETIKKVKDIFTDSFSKVIKENNENKSKICQTKIMAGCYEALDDSEDILHNSLDNDECSTHSHKVFADIQSEEILQHNQNMSGLEKVSKISPCDVSLETSDICKCSIGKLHKSVSSANTCGIFSTASGKSVQVSDASLQNARQVFSEIEDSTKQVFSKVLFKSNEHSDQLTREENTAIRTPEHLISQKGFSYNVVNSSAFSGFSTASGKQVSILESSLHKVKGVLEEFDLIRTEHSLHYSPTSRQNVSKILPRVDKRNPEHCVNSEMEKTCSKEFKLSNNLNVEGGSSENNHSIKVSPYLSQFQQDKQQLVLGTKVSLVENIHVLGKEQASPKNVKMEIGKTETFSDVPVKTNIEVCSTYSKDSENYFETEAVEIAKAFMEDDELTDSKLPSHATHSLFTCPENEEMVLSNSRIGKRRGEPLILVGEPSIKRNLLNEFDRIIENQEKSLKASKSTPDGTIKDRRLFMHHVSLEPITCVPFRTTKERQEIQNPNFTAPGQEFLSKSHLYEHLTLEKSSSNLAVSGHPFYQVSATRNEKMRHLITTGRPTKVFVPPFKTKSHFHRVEQCVRNINLEENRQKQNIDGHGSDDSKNKINDNEIHQFNKNNSNQAVAVTFTKCEEEPLDLITSLQNARDIQDMRIKKKQRQRVFPQPGSLYLAKTSTLPRISLKAAVGGQVPSACSHKQLYTYGVSKHCIKINSKNAESFQFHTEDYFGKESLWTGKGIQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISRIWVYNHYRWIIWKLAAMECAFPKEFANRCLSPERVLLQLKYRYDTEIDRSRRSAIKKIMERDDTAAKTLVLCVSDIISLSANISETSSNKTSSADTQKVAIIELTDGWYAVKAQLDPPLLAVLKNGRLTVGQKIILHGAELVGSPDACTPLEAPESLMLKISANSTRPARWYTKLGFFPDPRPFPLPLSSLFSDGGNVGCVDVIIQRAYPIQWMEKTSSGLYIFRNEREEEKEAAKYVEAQQKRLEALFTKIQEEFEEHEENTTKPYLPSRALTRQQVRALQDGAELYEAVKNAADPAYLEGYFSEEQLRALNNHRQMLNDKKQAQIQLEIRKAMESAEQKEQGLSRDVTTVWKLRIVSYSKKEKDSVILSIWRPSSDLYSLLTEGKRYRIYHLATSKSKSKSERANIQLAATKKTQYQQLPVSDEILFQIYQPREPLHFSKFLDPDFQPSCSEVDLIGFVVSVVKKTGLAPFVYLSDECYNLLAIKFWIDLNEDIIKPHMLIAASNLQWRPESKSGLLTLFAGDFSVFSASPKEGHFQETFNKMKNTVENIDILCNEAENKLMHILHANDPKWSTPTKDCTSGPYTAQIIPGTGNKLLMSSPNCEIYYQSPLSLCMAKRKSVSTPVSAQMTSKSCKGEKEIDDQKNCKKRRALDFLSRLPLPPPVSPICTFVSPAAQKAFQPPRSCGTKYETPIKKKELNSPQMTPFKKFNEISLLESNSIADEELALINTQALLSGSTGEKQFISVSESTRTAPTSSEDYLRLKRRCTTSLIKEQESSQASTEECEKNKQDTITTKKYI	"chr13:32,315,086-32,400,268[+]"	"Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination."	PDB: 1N0W; PDB: 3EU7; PDB: 6GY2; PDB: 6HQU; PDB: 7BDX; PDB: 7LDG	HGNC:1101	BRCA2_HUMAN	Reviewed	ENSG00000139618	.	.	.	.	.
Mol01843	Protein	Serine/threonine-protein kinase STK11 (STK11) 	Serine/threonine-protein kinase STK11; (Liver kinase B1; LKB1; hLKB1; Renal carcinoma antigen NY-REN-19	STK11	6794	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000652231.1,STK11-209,2072; ENST00000593219.5,STK11-208,637; ENST00000591133.2,STK11-207,1011; ENST00000589152.5,STK11-206,3365; ENST00000586358.5,STK11-205,770; ENST00000585851.1,STK11-204,505; ENST00000585748.2,STK11-203,746; ENST00000585465.2,STK11-202,3554; ENST00000326873.12,STK11-201,3293"	MEVVDPQQLGMFTEGELMSVGMDTFIHRIDSTEVIYQPRRKRAKLIGKYLMGDLLGEGSYGKVKEVLDSETLCRRAVKILKKKKLRRIPNGEANVKKEIQLLRRLRHKNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFCQLIDGLEYLHSQGIVHKDIKPGNLLLTTGGTLKISDLGVAEALHPFAADDTCRTSQGSPAFQPPEIANGLDTFSGFKVDIWSAGVTLYNITTGLYPFEGDNIYKLFENIGKGSYAIPGDCGPPLSDLLKGMLEYEPAKRFSIRQIRQHSWFRKKHPPAEAPVPIPPSPDTKDRWRSMTVVPYLEDLHGADEDEDLFDIEDDIIYTQDFTVPGQVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAPNPARKACSASSKIRRLSACKQQ	"chr19:1,177,558-1,228,431[+]"	"Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair."	PDB: 2WTK; PDB: 4ZDR; PDB: 5WXN	HGNC:11389	STK11_HUMAN	Reviewed	ENSG00000118046	.	.	.	.	.
Mol01844	Protein	Von Hippel-Lindau disease tumor suppressor (VHL) 	Von Hippel-Lindau disease tumor suppressor; Protein G7; pVHL	VHL	7428	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000696153.1,VHL-206,4525; ENST00000696143.1,VHL-205,2858; ENST00000696142.1,VHL-204,2813; ENST00000477538.1,VHL-203,958; ENST00000345392.2,VHL-202,2696; ENST00000256474.3,VHL-201,4414"	MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD	"chr3:10,141,778-10,153,667[+]"	"Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as a target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia-inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2."	PDB: 1LM8; PDB: 1LQB; PDB: 1VCB; PDB: 3ZRC; PDB: 3ZRF; PDB: 3ZTC; PDB: 3ZTD; PDB: 3ZUN; PDB: 4AJY; PDB: 4AWJ; PDB: 4B95; PDB: 4B9K; PDB: 4BKS; PDB: 4BKT; PDB: 4W9C; PDB: 4W9D; PDB: 4W9E; PDB: 4W9F; PDB: 4W9G; PDB: 4W9H; PDB: 4W9I; PDB: 4W9J; PDB: 4W9K; PDB: 4W9L; PDB: 4WQO; PDB: 5LLI; PDB: 5N4W; PDB: 5NVV; PDB: 5NVW; PDB: 5NVX; PDB: 5NVY; PDB: 5NVZ; PDB: 5NW0; PDB: 5NW1; PDB: 5NW2; PDB: 5T35; PDB: 6BVB; PDB: 6FMI; PDB: 6FMJ; PDB: 6FMK; PDB: 6GFX; PDB: 6GFY; PDB: 6GFZ; PDB: 6GMN; PDB: 6GMQ; PDB: 6GMR; PDB: 6GMX; PDB: 6HAX; PDB: 6HAY; PDB: 6HR2; PDB: 6I7Q; PDB: 6I7R; PDB: 6R6H; PDB: 6R7F; PDB: 6SIS; PDB: 6ZHC; PDB: 7CJB; PDB: 7JTO; PDB: 7JTP; PDB: 7KHH; PDB: 7PI4; PDB: 7Q2J	HGNC:12687	VHL_HUMAN	Reviewed	ENSG00000134086	.	.	.	.	.
Mol01845	Protein	Protein phosphatase 1 regulatory subunit 15A (PPP1R15A)	Protein phosphatase 1 regulatory subunit 15A; Growth arrest and DNA damage-inducible protein GADD34; Myeloid differentiation primary response protein MyD116 homolog	PPP1R15A	23645	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000600406.1,PPP1R15A-202,1725; ENST00000200453.6,PPP1R15A-201,2350"	MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG	"chr19:48,872,421-48,876,058[+]"	"Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15'. Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux. Acts also a viral restriction factor by attenuating HIV-1 replication. Mechanistically, mediates the inhibition of HIV-1 TAR RNA-mediated translation."	PDB: 4XPN; PDB: 7NXV; PDB: 7NZM	HGNC:14375	PR15A_HUMAN	Reviewed	ENSG00000087074	.	.	.	.	.
Mol01846	Protein	Mismatch repair endonuclease PMS2 (PMS2)	Mismatch repair endonuclease PMS2; DNA mismatch repair protein PMS2; PMS1 protein homolog 2	PMS2	5395	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000644110.1,PMS2-211,2271; ENST00000643595.1,PMS2-210,2600; ENST00000642456.1,PMS2-209,2765; ENST00000642292.1,PMS2-208,2679; ENST00000469652.1,PMS2-207,93; ENST00000441476.6,PMS2-206,2730; ENST00000415839.2,PMS2-205,924; ENST00000406569.7,PMS2-204,1719; ENST00000382321.5,PMS2-203,1386; ENST00000380416.5,PMS2-202,1103; ENST00000265849.12,PMS2-201,5093"	MERAESSSTEPAKAIKPIDRKSVHQICSGQVVLSLSTAVKELVENSLDAGATNIDLKLKDYGVDLIEVSDNGCGVEEENFEGLTLKHHTSKIQEFADLTQVETFGFRGEALSSLCALSDVTISTCHASAKVGTRLMFDHNGKIIQKTPYPRPRGTTVSVQQLFSTLPVRHKEFQRNIKKEYAKMVQVLHAYCIISAGIRVSCTNQLGQGKRQPVVCTGGSPSIKENIGSVFGQKQLQSLIPFVQLPPSDSVCEEYGLSCSDALHNLFYISGFISQCTHGVGRSSTDRQFFFINRRPCDPAKVCRLVNEVYHMYNRHQYPFVVLNISVDSECVDINVTPDKRQILLQEEKLLLAVLKTSLIGMFDSDVNKLNVSQQPLLDVEGNLIKMHAADLEKPMVEKQDQSPSLRTGEEKKDVSISRLREAFSLRHTTENKPHSPKTPEPRRSPLGQKRGMLSSSTSGAISDKGVLRPQKEAVSSSHGPSDPTDRAEVEKDSGHGSTSVDSEGFSIPDTGSHCSSEYAASSPGDRGSQEHVDSQEKAPKTDDSFSDVDCHSNQEDTGCKFRVLPQPTNLATPNTKRFKKEEILSSSDICQKLVNTQDMSASQVDVAVKINKKVVPLDFSMSSLAKRIKQLHHEAQQSEGEQNYRKFRAKICPGENQAAEDELRKEISKTMFAEMEIIGQFNLGFIITKLNEDIFIVDQHATDEKYNFEMLQQHTVLQGQRLIAPQTLNLTAVNEAVLIENLEIFRKNGFDFVIDENAPVTERAKLISLPTSKNWTFGPQDVDELIFMLSDSPGVMCRPSRVKQMFASRACRKSVMIGTALNTSEMKKLITHMGEMDHPWNCPHGRPTMRHIANLGVISQN	"chr7:5,970,925-6,009,106[-]"	"Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages."	PDB: 1EA6; PDB: 1H7S; PDB: 1H7U; PDB: 5U5R; PDB: 6MFQ	HGNC:9122	PMS2_HUMAN	Reviewed	ENSG00000122512	.	.	.	.	.
Mol01847	Protein	Thrombopoietin receptor (TPOR)	Thrombopoietin receptor; TPO-R; Myeloproliferative leukemia protein; Proto-oncogene c-Mpl; CD antigen CD110; MPL	TPOR	4352	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000643351.1,MPL-204,530; ENST00000638732.1,MPL-203,1743; ENST00000413998.7,MPL-202,1887; ENST00000372470.9,MPL-201,3633"	MPSWALFMVTSCLLLAPQNLAQVSSQDVSLLASDSEPLKCFSRTFEDLTCFWDEEEAAPSGTYQLLYAYPREKPRACPLSSQSMPHFGTRYVCQFPDQEEVRLFFPLHLWVKNVFLNQTRTQRVLFVDSVGLPAPPSIIKAMGGSQPGELQISWEEPAPEISDFLRYELRYGPRDPKNSTGPTVIQLIATETCCPALQRPHSASALDQSPCAQPTMPWQDGPKQTSPSREASALTAEGGSCLISGLQPGNSYWLQLRSEPDGISLGGSWGSWSLPVTVDLPGDAVALGLQCFTLDLKNVTCQWQQQDHASSQGFFYHSRARCCPRDRYPIWENCEEEEKTNPGLQTPQFSRCHFKSRNDSIIHILVEVTTAPGTVHSYLGSPFWIHQAVRLPTPNLHWREISSGHLELEWQHPSSWAAQETCYQLRYTGEGHQDWKVLEPPLGARGGTLELRPRSRYRLQLRARLNGPTYQGPWSSWSDPTRVETATETAWISLVTALHLVLGLSAVLGLLLLRWQFPAHYRRLRHALWPSLPDLHRVLGQYLRDTAALSPPKATVSDTCEEVEPSLLEILPKSSERTPLPLCSSQAQMDYRRLQPSCLGTMPLSVCPPMAESGSCCTTHIANHSYLPLSYWQQP	"chr1:43,337,818-43,354,466[+]"	Receptor for thrombopoietin that acts as a primary regulator of megakaryopoiesis and platelet production. May represent a regulatory molecule specific for TPO-R-dependent immune responses.	.	HGNC:7217	TPOR_HUMAN	Reviewed	ENSG00000117400	.	.	.	.	.
Mol01848	Protein	Protein farnesyltransferase subunit beta (FNTB)	Protein farnesyltransferase subunit beta; FTase-beta; CAAX farnesyltransferase subunit beta; Ras proteins prenyltransferase subunit beta; FNTB	FNTB	2342	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000557300.1,FNTB-208,530; ENST00000556709.1,FNTB-207,509; ENST00000555742.5,FNTB-206,725; ENST00000555618.1,FNTB-205,297; ENST00000555372.5,FNTB-204,582; ENST00000554334.5,FNTB-203,2622; ENST00000554210.5,FNTB-202,575; ENST00000246166.3,FNTB-201,2711"	MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD	"chr14:64,986,895-65,062,652[+]"	Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.	PDB: 1JCQ; PDB: 1LD7; PDB: 1LD8; PDB: 1MZC; PDB: 1S63; PDB: 1SA4; PDB: 1TN6; PDB: 2F0Y; PDB: 2H6F; PDB: 2H6G; PDB: 2H6H; PDB: 2H6I; PDB: 2IEJ; PDB: 3E37	HGNC:3785	FNTB_HUMAN	Reviewed	ENSG00000257365	.	.	.	.	.
Mol01849	Protein	Protein kinase C eta type (PRKCH)	Protein kinase C eta type; PKC-L; nPKC-eta	PRKCH	5583	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000332981.11,PRKCH-201,3720; ENST00000536400.5,PRKCH-202,968; ENST00000552875.2,PRKCH-203,545; ENST00000553265.5,PRKCH-204,552; ENST00000553726.5,PRKCH-205,545; ENST00000553830.1,PRKCH-206,514; ENST00000553831.5,PRKCH-207,545; ENST00000553846.1,PRKCH-208,557; ENST00000553889.5,PRKCH-209,553; ENST00000554835.1,PRKCH-210,363; ENST00000555082.5,PRKCH-211,2932; ENST00000555110.1,PRKCH-212,268; ENST00000555185.5,PRKCH-213,582; ENST00000555233.5,PRKCH-214,582; ENST00000555382.5,PRKCH-215,691; ENST00000555542.5,PRKCH-216,521; ENST00000555604.1,PRKCH-217,361; ENST00000555628.5,PRKCH-218,569; ENST00000555906.5,PRKCH-219,459; ENST00000556164.5,PRKCH-220,429; ENST00000556245.1,PRKCH-221,2745; ENST00000556778.5,PRKCH-222,545; ENST00000557294.5,PRKCH-223,562; ENST00000557473.1,PRKCH-224,567; ENST00000557559.1,PRKCH-225,504; ENST00000557585.5,PRKCH-226,938; ENST00000557599.5,PRKCH-227,746"	MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP	"chr14:61,187,559-61,550,976[+]"	"Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization."	PDB: 2FK9; PDB: 3TXO	HGNC:9403	KPCL_HUMAN	Reviewed	ENSG00000027075	.	.	.	.	.
Mol01850	Protein	Serine/threonine-protein kinase A-Raf (ARAF)	ARAF; Proto-oncogene A-Raf; Proto-oncogene A-Raf-1; Proto-oncogene Pks; ARAF; ARAF1; PKS; PKS2	ARAF	369	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377039.2,ARAF-201,1271; ENST00000377045.9,ARAF-202,2378; ENST00000469505.1,ARAF-203,559; ENST00000470206.1,ARAF-204,646; ENST00000489496.1,ARAF-205,472"	MEPPRGPPANGAEPSRAVGTVKVYLPNKQRTVVTVRDGMSVYDSLDKALKVRGLNQDCCVVYRLIKGRKTVTAWDTAIAPLDGEELIVEVLEDVPLTMHNFVRKTFFSLAFCDFCLKFLFHGFRCQTCGYKFHQHCSSKVPTVCVDMSTNRQQFYHSVQDLSGGSRQHEAPSNRPLNELLTPQGPSPRTQHCDPEHFPFPAPANAPLQRIRSTSTPNVHMVSTTAPMDSNLIQLTGQSFSTDAAGSRGGSDGTPRGSPSPASVSSGRKSPHSKSPAEQRERKSLADDKKKVKNLGYRDSGYYWEVPPSEVQLLKRIGTGSFGTVFRGRWHGDVAVKVLKVSQPTAEQAQAFKNEMQVLRKTRHVNILLFMGFMTRPGFAIITQWCEGSSLYHHLHVADTRFDMVQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGAQPLEQPSGSVLWMAAEVIRMQDPNPYSFQSDVYAYGVVLYELMTGSLPYSHIGCRDQIIFMVGRGYLSPDLSKISSNCPKAMRRLLSDCLKFQREERPLFPQILATIELLQRSLPKIERSASEPSLHRTQADELPACLLSAARLVP	"chrX:47,561,205-47,571,908[+]"	Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade.	PDB: 1WXM; PDB: 2MSE	HGNC:646	ARAF_HUMAN	Reviewed	ENSG00000078061	.	.	.	.	.
Mol01851	Protein	G protein-activated inward rectifier potassium channel 4 (GIRK4) 	G protein-activated inward rectifier potassium channel 4; GIRK-4; Cardiac inward rectifier; CIR; Heart KATP channel; Inward rectifier K(+) channel Kir3.4); IRK-4; KATP-1; Potassium channel; inwardly rectifying subfamily J member 5; KCNJ5	GIRK4	3762	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000338350.4,KCNJ5-201,1734; ENST00000529694.6,KCNJ5-202,6068; ENST00000533599.1,KCNJ5-203,1350"	MAGDSRNAMNQDMEIGVTPWDPKKIPKQARDYVPIATDRTRLLAEGKKPRQRYMEKSGKCNVHHGNVQETYRYLSDLFTTLVDLKWRFNLLVFTMVYTVTWLFFGFIWWLIAYIRGDLDHVGDQEWIPCVENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQAILGSIVNAFMVGCMFVKISQPKKRAETLMFSNNAVISMRDEKLCLMFRVGDLRNSHIVEASIRAKLIKSRQTKEGEFIPLNQTDINVGFDTGDDRLFLVSPLIISHEINQKSPFWEMSQAQLHQEEFEVVVILEGMVEATGMTCQARSSYMDTEVLWGHRFTPVLTLEKGFYEVDYNTFHDTYETNTPSCCAKELAEMKREGRLLQYLPSPPLLGGCAEAGLDAEAEQNEEDEPKGLGGSREARGSV	"chr11:128,891,356-128,921,163[+]"	"This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium."	.	HGNC:6266	KCNJ5_HUMAN	Reviewed	ENSG00000120457	.	.	.	.	.
Mol01852	Protein	Protein-tyrosine phosphatase delta (PTPRD)	Receptor-type tyrosine-protein phosphatase delta; Protein-tyrosine phosphatase delta; R-PTP-delta	PTPRD	5789	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000355233.9,PTPRD-201,8251; ENST00000356435.9,PTPRD-202,9472; ENST00000381196.9,PTPRD-203,10389; ENST00000397606.7,PTPRD-204,5038; ENST00000397611.7,PTPRD-205,8242; ENST00000397617.8,PTPRD-206,8257; ENST00000463477.5,PTPRD-207,1697; ENST00000471274.1,PTPRD-208,1205; ENST00000477552.1,PTPRD-209,551; ENST00000481079.1,PTPRD-210,521; ENST00000486161.5,PTPRD-211,5039; ENST00000488774.1,PTPRD-212,420; ENST00000537002.5,PTPRD-213,8224; ENST00000540109.5,PTPRD-214,6210; ENST00000637354.1,PTPRD-215,891; ENST00000651105.1,PTPRD-216,8740"	MVHVARLLLLLLTFFLRTDAETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGSVLRIQPLRTPRDEAIYECVASNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRSESIGGTPIRGALQIEQSEESDQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVNITCVAVGSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAIAQITVKALPKPPGTPVVTESTATSITLTWDSGNPEPVSYYIIQHKPKNSEELYKEIDGVATTRYSVAGLSPYSDYEFRVVAVNNIGRGPPSEPVLTQTSEQAPSSAPRDVQARMLSSTTILVQWKEPEEPNGQIQGYRVYYTMDPTQHVNNWMKHNVADSQITTIGNLVPQKTYSVKVLAFTSIGDGPLSSDIQVITQTGVPGQPLNFKAEPESETSILLSWTPPRSDTIANYELVYKDGEHGEEQRITIEPGTSYRLQGLKPNSLYYFRLAARSPQGLGASTAEISARTMQSKPSAPPQDISCTSPSSTSILVSWQPPPVEKQNGIITEYSIKYTAVDGEDDKPHEILGIPSDTTKYLLEQLEKWTEYRITVTAHTDVGPGPESLSVLIRTNEDVPSGPPRKVEVEAVNSTSVKVSWRSPVPNKQHGQIRGYQVHYVRMENGEPKGQPMLKDVMLADAQWEFDDTTEHDMIISGLQPETSYSLTVTAYTTKGDGARSKPKLVSTTGAVPGKPRLVINHTQMNTALIQWHPPVDTFGPLQGYRLKFGRKDMEPLTTLEFSEKEDHFTATDIHKGASYVFRLSARNKVGFGEEMVKEISIPEEVPTGFPQNLHSEGTTSTSVQLSWQPPVLAERNGIITKYTLLYRDINIPLLPMEQLIVPADTTMTLTGLKPDTTYDVKVRAHTSKGPGPYSPSVQFRTLPVDQVFAKNFHVKAVMKTSVLLSWEIPENYNSAMPFKILYDDGKMVEEVDGRATQKLIVNLKPEKSYSFVLTNRGNSAGGLQHRVTAKTAPDVLRTKPAFIGKTNLDGMITVQLPEVPANENIKGYYIIIVPLKKSRGKFIKPWESPDEMELDELLKEISRKRRSIRYGREVELKPYIAAHFDVLPTEFTLGDDKHYGGFTNKQLQSGQEYVFFVLAVMEHAESKMYATSPYSDPVVSMDLDPQPITDEEEGLIWVVGPVLAVVFIICIVIAILLYKRKRAESDSRKSSIPNNKEIPSHHPTDPVELRRLNFQTPGMASHPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYVNANYIDGYRKQNAYIATQGSLPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETHGLVQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGNTEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFSYRAALEYLGSFDHYAT	"chr9:8,314,246-10,613,002[-]"	Can bidirectionally induce pre- and post-synaptic differentiation of neurons by mediating interaction with IL1RAP and IL1RAPL1 trans-synaptically. Involved in pre-synaptic differentiation through interaction with SLITRK2.	PDB: 1X5Z; PDB: 2DLH; PDB: 2YD6; PDB: 2YD7; PDB: 4RCA; PDB: 5WY8; PDB: 5XNP; PDB: 6X3A	HGNC:9668	PTPRD_HUMAN	Reviewed	ENSG00000153707	.	.	.	.	.
Mol01853	Protein	Nucleophosmin (NPM1)	Nucleophosmin; NPM; Nucleolar phosphoprotein B23; Nucleolar protein NO38; Numatrin	NPM1	4869	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000296930.10,NPM1-201,1320; ENST00000351986.10,NPM1-202,1237; ENST00000393820.2,NPM1-203,1598; ENST00000517671.5,NPM1-204,1338; ENST00000518587.2,NPM1-205,1382; ENST00000519955.1,NPM1-206,571; ENST00000521260.2,NPM1-207,1571; ENST00000521672.6,NPM1-208,1263; ENST00000521710.2,NPM1-209,1021; ENST00000523339.1,NPM1-210,268; ENST00000523622.1,NPM1-211,247; ENST00000524204.1,NPM1-212,640; ENST00000676504.1,NPM1-213,1936; ENST00000676589.1,NPM1-214,1338; ENST00000676613.1,NPM1-215,2676; ENST00000676625.1,NPM1-216,3605; ENST00000677297.1,NPM1-217,883; ENST00000677325.1,NPM1-218,2258; ENST00000677357.1,NPM1-219,1346; ENST00000677467.1,NPM1-220,2600; ENST00000677600.1,NPM1-221,2506; ENST00000677672.1,NPM1-222,2627; ENST00000677682.1,NPM1-223,2534; ENST00000677741.1,NPM1-224,2459; ENST00000677904.1,NPM1-225,1469; ENST00000677907.1,NPM1-226,1335; ENST00000678186.1,NPM1-227,2674; ENST00000678267.1,NPM1-228,2797; ENST00000678280.1,NPM1-229,1913; ENST00000678774.1,NPM1-230,1289; ENST00000679006.1,NPM1-231,1116; ENST00000679190.1,NPM1-232,794; ENST00000679233.1,NPM1-233,1072"	MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL	"chr5:171,387,116-171,411,810[+]"	"Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade. In complex with MYC enhances the transcription of MYC target genes."	PDB: 2LLH; PDB: 2P1B; PDB: 2VXD; PDB: 5EHD	HGNC:7910	NPM_HUMAN	Reviewed	ENSG00000181163	.	.	.	.	.
Mol01854	Protein	Interleukin-7 receptor subunit alpha (IL7R)	Interleukin-7 receptor subunit alpha; IL-7 receptor subunit alpha; IL-7R subunit alpha; IL-7R-alpha; IL-7RA; CDw127; CD antigen CD127; IL7R	IL7R	3575	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000303115.8,IL7R-201,4584; ENST00000505093.1,IL7R-202,917; ENST00000505875.1,IL7R-203,626; ENST00000506850.5,IL7R-204,1004; ENST00000508941.5,IL7R-205,562; ENST00000509668.1,IL7R-206,552; ENST00000511031.1,IL7R-207,515; ENST00000511982.1,IL7R-208,612; ENST00000514217.5,IL7R-209,1287; ENST00000515665.1,IL7R-210,551"	MTILGTTFGMVFSLLQVVSGESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVEVKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVYREGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAAMYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMDPILLTISILSFFSVALLVILACVLWKKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFLQDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSSSRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSNQEEAYVTMSSFYQNQ	"chr5:35,852,695-35,879,603[+]"	Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP).	PDB: 3DI2; PDB: 3DI3; PDB: 3UP1; PDB: 5J11; PDB: 6P50; PDB: 6P67	HGNC:6024	IL7RA_HUMAN	Reviewed	ENSG00000168685	.	.	.	.	.
Mol01855	Protein	CCAAT enhancer binding protein delta (CEBPD)	CEBPD	CEBPD	1052	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000408965.4,CEBPD-201,1252"	MSAALFSLDGPARGAPWPAEPAPFYEPGRAGKPGRGAEPGALGEPGAAAPAMYDDESAIDFSAYIDSMAAVPTLELCHDELFADLFNSNHKAGGAGPLELLPGGPARPLGPGPAAPRLLKREPDWGDGDAPGSLLPAQVAACAQTVVSLAAAGQPTPPTSPEPPRSSPRQTPAPGPAREKSAGKRGPDRGSPEYRQRRERNNIAVRKSRDKAKRRNQEMQQKLVELSAENEKLHQRVEQLTRDLAGLRQFFKQLPSPPFLPAAGTADCR	"chr8:47,736,913-47,738,164[-]"	Transcription activator that recognizes two different DNA motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Transcriptional activator that enhances IL6 transcription alone and as heterodimer with CEBPB.	.	HGNC:1835	CEBPD_HUMAN	reviewed	ENSG00000221869	.	.	.	.	.
Mol01856	Protein	Muscarinic acetylcholine receptor M3 (ACM3)	CHRM3	ACM3	1131	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000255380.8,CHRM3-201,8780; ENST00000448020.1,CHRM3-202,587; ENST00000468573.5,CHRM3-203,2005; ENST00000481779.1,CHRM3-204,1101; ENST00000487470.1,CHRM3-205,581; ENST00000492335.5,CHRM3-206,719; ENST00000615928.5,CHRM3-207,2433; ENST00000674678.1,CHRM3-208,2704; ENST00000675184.1,CHRM3-209,2740; ENST00000675709.1,CHRM3-210,1306; ENST00000676153.1,CHRM3-211,9179; ENST00000676433.1,CHRM3-212,2530"	MTLHNNSTTSPLFPNISSSWIHSPSDAGLPPGTVTHFGSYNVSRAAGNFSSPDGTTDDPLGGHTVWQVVFIAFLTGILALVTIIGNILVIVSFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLAIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAETENFVHPTGSSRSCSSYELQQQSMKRSNRRKYGRCHFWFTTKSWKPSSEQMDQDHSSSDSWNNNDAAASLENSASSDEEDIGSETRAIYSIVLKLPGHSTILNSTKLPSSDNLQVPEEELGMVDLERKADKLQAQKSVDDGGSFPKSFSKLPIQLESAVDTAKTSDVNSSVGKSTATLPLSFKEATLAKRFALKTRSQITKRKRMSLVKEKKAAQTLSAILLAFIITWTPYNIMVLVNTFCDSCIPKTFWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCDKKKRRKQQYQQRQSVIFHKRAPEQAL	"chr1:239,386,565-239,915,452[+]"	"The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover."	PDB: 2CSA	.	ACM3_HUMAN	reviewed	ENSG00000133019	.	.	.	.	.
Mol01857	Protein	C-C motif chemokine receptor 4 (CCR4)	CCR4; CMKBR4	CCR4	1233	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000330953.6,CCR4-201,3025"	MNPTDIADTTLDESIYSNYYLYESIPKPCTKEGIKAFGELFLPPLYSLVFVFGLLGNSVVVLVLFKYKRLRSMTDVYLLNLAISDLLFVFSLPFWGYYAADQWVFGLGLCKMISWMYLVGFYSGIFFVMLMSIDRYLAIVHAVFSLRARTLTYGVITSLATWSVAVFASLPGFLFSTCYTERNHTYCKTKYSLNSTTWKVLSSLEINILGLVIPLGIMLFCYSMIIRTLQHCKNEKKNKAVKMIFAVVVLFLGFWTPYNIVLFLETLVELEVLQDCTFERYLDYAIQATETLAFVHCCLNPIIYFFLGEKFRKYILQLFKTCRGLFVLCQYCGLLQIYSADTPSSSYTQSTMDHDLHDAL	"chr3:32,951,644-32,956,349[+]"	"High affinity receptor for the C-C type chemokines CCL17/TARC, CCL22/MDC and CKLF isoform 1/CKLF1. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Can function as a chemoattractant homing receptor on circulating memory lymphocytes and as a coreceptor for some primary HIV-2 isolates. In the CNS, could mediate hippocampal-neuron survival."	.	HGNC:1605	CCR4_HUMAN	reviewed	ENSG00000183813	.	.	.	.	.
Mol01858	Protein	Catechol-O-methyltransferase (COMT)	COMT	COMT	1312	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000207636.9,COMT-201,1319; ENST00000361682.11,COMT-202,2272; ENST00000403184.5,COMT-203,2217; ENST00000403710.5,COMT-204,1548; ENST00000406520.7,COMT-205,1339; ENST00000407537.5,COMT-206,1457; ENST00000412786.5,COMT-207,871; ENST00000428707.2,COMT-208,2492; ENST00000449653.5,COMT-209,1035; ENST00000467943.5,COMT-210,546; ENST00000493893.1,COMT-211,354; ENST00000676678.1,COMT-212,1405; ENST00000677397.1,COMT-213,1363; ENST00000677470.1,COMT-214,959; ENST00000677564.1,COMT-215,1818; ENST00000677675.1,COMT-216,909; ENST00000678240.1,COMT-217,617; ENST00000678255.1,COMT-218,3119; ENST00000678769.1,COMT-219,2202; ENST00000678868.1,COMT-220,2405; ENST00000678945.1,COMT-221,1903"	MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP	"chr22:19,941,371-19,969,975[+]"	"Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol."	PDB: 3A7E; PDB: 3BWM; PDB: 3BWY; PDB: 4PYI; PDB: 4PYJ; PDB: 4PYK; PDB: 4XUC; PDB: 4XUD; PDB: 4XUE; PDB: 5LSA; PDB: 6I3C; PDB: 6I3D	HGNC:2228	COMT_HUMAN	reviewed	ENSG00000093010	.	.	.	.	.
Mol01859	Protein	Cytochrome P450 family 1 subfamily A member 1 (CYP1A1)	CYP1A1	CYP1A1	1543	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000379727.8,CYP1A1-201,2603; ENST00000395048.6,CYP1A1-202,2608; ENST00000395049.8,CYP1A1-203,1594; ENST00000562201.5,CYP1A1-204,1192; ENST00000564596.5,CYP1A1-205,988; ENST00000566503.1,CYP1A1-206,796; ENST00000567032.5,CYP1A1-207,2107; ENST00000569630.5,CYP1A1-208,1544; ENST00000617691.4,CYP1A1-209,2521"	MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPHLALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQSMSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAGPGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPILRYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANVQLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLSDRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKLWVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEFSVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS	"chr15:74,719,542-74,725,536[-]"	"A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent)."	PDB: 4I8V; PDB: 6DWM; PDB: 6DWN; PDB: 6O5Y; PDB: 6UDL; PDB: 6UDM	HGNC:2595	CP1A1_HUMAN	reviewed	ENSG00000140465	.	.	.	.	.
Mol01860	Protein	Cytochrome P450 family 2 subfamily C member 19 (CYP2C19)	CYP2C19	CYP2C19	1557	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371321.9,CYP2C19-201,4131; ENST00000480405.2,CYP2C19-202,1417; ENST00000645461.1,CYP2C19-203,2634"	MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKIYGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFMESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRGHMPYTDAVVHEVQRYIDLIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFKKSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVPPFYQLCFIPV	"chr10:94,762,681-94,855,547[+]"	"A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates PUFA specifically at the omega-1 position. Catalyzes the epoxidation of double bonds of PUFA. Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol. Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine. Hydroxylates fenbendazole at the 4' position."	PDB: 4GQS	HGNC:2621	CP2CJ_HUMAN	reviewed	ENSG00000165841	.	.	.	.	.
Mol01861	Protein	Cytochrome P450 family 2 subfamily C member 9 (CYP2C9)	CYP2C9; CYP2C10	CYP2C9	1559	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000260682.8,CYP2C9-201,2561; ENST00000461906.1,CYP2C9-202,1431; ENST00000473496.1,CYP2C9-203,841; ENST00000643112.1,CYP2C9-204,1697; ENST00000645207.1,CYP2C9-205,747"	MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV	"chr10:94,938,658-94,990,091[+]"	"A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. Exhibits low catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2. Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol. Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan."	PDB: 1OG2; PDB: 1OG5; PDB: 1R9O; PDB: 4NZ2; PDB: 5A5I; PDB: 5A5J; PDB: 5K7K; PDB: 5W0C; PDB: 5X23; PDB: 5X24; PDB: 5XXI; PDB: 6VLT; PDB: 7RL2	HGNC:2623	CP2C9_HUMAN	reviewed	ENSG00000138109	.	.	.	.	.
Mol01862	Protein	Cytochrome P450 family 2 subfamily D member 6 (CYP2D6)	CYP2D6; CYP2DL1	CYP2D6	1565	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359033.4,CYP2D6-201,1433; ENST00000360124.9,CYP2D6-202,1187; ENST00000488442.1,CYP2D6-203,2257; ENST00000645361.2,CYP2D6-204,1588"	MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYELCAVPR	"chr22:42,126,499-42,130,865[-]"	"A cytochrome P450 monooxygenase involved in the metabolism of fatty acids, steroids and retinoids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 20-hydroxyeicosatetraenoic acid ethanolamide (20-HETE-EA) and 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling. Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. Catalyzes the oxidative transformations of all-trans retinol to all-trans retinal, a precursor for the active form all-trans-retinoic acid. Also involved in the oxidative metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants."	PDB: 2F9Q; PDB: 3QM4; PDB: 3TBG; PDB: 3TDA; PDB: 4WNT; PDB: 4WNU; PDB: 4WNV; PDB: 4WNW; PDB: 4XRY; PDB: 4XRZ; PDB: 5TFT; PDB: 5TFU; PDB: 6CSB; PDB: 6CSD	HGNC:2625	CP2D6_HUMAN	reviewed	ENSG00000100197	.	.	.	.	.
Mol01863	Protein	Cytochrome P450 family 3 subfamily A member 5 (CYP3A5)	CYP3A5	CYP3A5	1577	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000222982.8,CYP3A5-201,1720; ENST00000339843.6,CYP3A5-202,3320; ENST00000439761.3,CYP3A5-203,4473; ENST00000456417.5,CYP3A5-204,594; ENST00000461920.5,CYP3A5-205,2208; ENST00000463364.5,CYP3A5-206,1625; ENST00000463907.5,CYP3A5-207,1623; ENST00000466061.5,CYP3A5-208,1564; ENST00000469622.5,CYP3A5-209,556; ENST00000469887.5,CYP3A5-210,3149; ENST00000473347.1,CYP3A5-211,2594; ENST00000480723.5,CYP3A5-212,584; ENST00000481825.5,CYP3A5-213,2857; ENST00000488187.1,CYP3A5-214,593; ENST00000489231.1,CYP3A5-215,622; ENST00000646887.1,CYP3A5-216,1824"	MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKFDTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISLAEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYSMDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSLFPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSIIFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVVNETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFSKKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQGLLQPEKPIVLKVDSRDGTLSGE	"chr7:99,648,194-99,679,998[-]"	"A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2. Catalyzes 6beta-hydroxylation of the steroid hormones testosterone, progesterone, and androstenedione. Catalyzes the oxidative conversion of all-trans-retinol to all-trans-retinal, a rate-limiting step for the biosynthesis of all-trans-retinoic acid (atRA). Further metabolizes all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in hepatic atRA clearance. Also involved in the oxidative metabolism of xenobiotics, including calcium channel blocking drug nifedipine and immunosuppressive drug cyclosporine."	PDB: 5VEU	HGNC:2638	CP3A5_HUMAN	reviewed	ENSG00000106258	.	.	.	.	.
Mol01864	Protein	Cytochrome P450 family 51 subfamily A member 1 (CYP51A1)	CYP51A1; CYP51	CYP51A1	1595	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000003100.13,CYP51A1-201,3155; ENST00000422867.1,CYP51A1-202,747; ENST00000450723.5,CYP51A1-203,1729; ENST00000482924.1,CYP51A1-204,555; ENST00000691309.1,CYP51A1-205,2106"	MAAAAGMLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDLNLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFPTVNYTTMIHTPENPVIRYKRRSK	"chr7:92,084,987-92,134,803[-]"	"A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-dihydrolanosterol likely through sequential oxidative conversion of 14-alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase)."	PDB: 3JUS; PDB: 3JUV; PDB: 3LD6; PDB: 4UHI; PDB: 4UHL; PDB: 6Q2T; PDB: 6UEZ	HGNC:2649	CP51A_HUMAN	reviewed	ENSG00000001630	.	.	.	.	.
Mol01865	Protein	24-dehydrocholesterol reductase (DHCR24)	DHCR24; KIAA0018	DHCR24	1718	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000371269.9,DHCR24-201,4233; ENST00000436604.2,DHCR24-202,2027; ENST00000535035.6,DHCR24-203,4225; ENST00000647585.1,DHCR24-204,1221; ENST00000647912.1,DHCR24-205,4314; ENST00000648182.1,DHCR24-206,584; ENST00000648494.1,DHCR24-207,582; ENST00000648641.1,DHCR24-208,577; ENST00000648712.1,DHCR24-209,4238; ENST00000648728.1,DHCR24-210,3575; ENST00000649769.1,DHCR24-211,5311; ENST00000650362.1,DHCR24-212,569"	MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKLSSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMDILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKYGLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKLRFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYYKPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVPPKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQPGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREEFWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH	"chr1:54,849,627-54,887,195[-]"	"Catalyzes the reduction of the delta-24 double bond of sterol intermediates during cholesterol biosynthesis. In addition to its cholesterol-synthesizing activity, can protect cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis."	.	HGNC:2859	DHC24_HUMAN	reviewed	ENSG00000116133	.	.	.	.	.
Mol01866	Protein	Diphthamide biosynthesis 1 (DPH1)	DPH1; DPH2L; DPH2L1; OVCA1	DPH1	1801	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263083.12,DPH1-201,2646; ENST00000263084.7,DPH1-202,1827; ENST00000570477.6,DPH1-203,2680; ENST00000570833.5,DPH1-204,558; ENST00000570867.6,DPH1-205,2739; ENST00000571418.7,DPH1-206,2607; ENST00000571710.6,DPH1-207,2487; ENST00000572214.6,DPH1-208,2141; ENST00000572248.2,DPH1-209,1743; ENST00000572684.2,DPH1-210,3081; ENST00000572819.6,DPH1-211,1345; ENST00000575162.2,DPH1-212,1636; ENST00000575667.6,DPH1-213,2518; ENST00000575998.1,DPH1-214,535; ENST00000576129.5,DPH1-215,991; ENST00000576891.2,DPH1-216,537; ENST00000607788.2,DPH1-217,1252; ENST00000674200.2,DPH1-218,2662"	MRRQVMAALVVSGAAEQGGRDGPGRGRAPRGRVANQIPPEILKNPQLQAAIRVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGADFLVHYGHSCLIPMDTSAQDFRVLYVFVDIRIDTTHLLDSLRLTFPPATALALVSTIQFVSTLQAAAQELKAEYRVSVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQAARQEAIATARSAKSWGLILGTLGRQGSPKILEHLESRLRALGLSFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGTAFPKPLLTPYEAAVALRDISWQQPYPMDFYAGSSLGPWTVNHGQDRRPHAPGRPARGKVQEGSARPPSAVACEDCSCRDEKVAPLAP	"chr17:2,030,137-2,043,898[+]"	"Required for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2). When overexpressed, suppresses colony formation ability and growth rate of ovarian cancer cells. Acts also as a tumor suppressor in lung and breast cancers (By similarity). Plays a role in embryonic growth, organogenesis and postnatal survival (By similarity)."	.	HGNC:3003	DPH1_HUMAN	reviewed	ENSG00000108963	.	.	.	.	.
Mol01867	Protein	Dipeptidyl peptidase 4 (DPP4)	DPP4; ADCP2; CD26	DPP4	1803	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000360534.8,DPP4-201,3573; ENST00000413651.3,DPP4-202,578; ENST00000416189.6,DPP4-203,2737; ENST00000434918.6,DPP4-204,2674; ENST00000461836.6,DPP4-205,1464; ENST00000468903.1,DPP4-206,582; ENST00000490286.5,DPP4-207,2241; ENST00000491591.5,DPP4-208,969; ENST00000494507.2,DPP4-209,3045; ENST00000497461.5,DPP4-210,781; ENST00000676479.1,DPP4-211,3551; ENST00000676624.1,DPP4-212,3433; ENST00000676768.1,DPP4-213,3623; ENST00000676810.1,DPP4-214,3749; ENST00000676996.1,DPP4-215,3433; ENST00000677015.1,DPP4-216,4574; ENST00000677212.1,DPP4-217,4977; ENST00000678522.1,DPP4-218,4796; ENST00000678566.1,DPP4-219,3804; ENST00000678583.1,DPP4-220,8539; ENST00000678668.1,DPP4-221,3339; ENST00000678740.1,DPP4-222,3391; ENST00000679104.1,DPP4-223,3375"	MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP	"chr2:161,992,245-162,074,394[-]"	"Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones such as brain natriuretic peptide 32. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline."	PDB: 1J2E; PDB: 1N1M; PDB: 1NU6; PDB: 1NU8; PDB: 1PFQ; PDB: 1R9M; PDB: 1R9N; PDB: 1RWQ; PDB: 1TK3; PDB: 1TKR; PDB: 1U8E; PDB: 1W1I; PDB: 1WCY; PDB: 1X70; PDB: 2AJL; PDB: 2BGN; PDB: 2BGR; PDB: 2BUB; PDB: 2FJP; PDB: 2G5P; PDB: 2G5T; PDB: 2G63; PDB: 2HHA; PDB: 2I03; PDB: 2I78; PDB: 2IIT; PDB: 2IIV; PDB: 2JID; PDB: 2OAG; PDB: 2OGZ; PDB: 2OLE; PDB: 2ONC; PDB: 2OPH; PDB: 2OQI; PDB: 2OQV; PDB: 2P8S; PDB: 2QJR; PDB: 2QKY; PDB: 2QOE; PDB: 2QT9; PDB: 2QTB; PDB: 2RGU; PDB: 2RIP; PDB: 3BJM; PDB: 3C43; PDB: 3C45; PDB: 3CCB; PDB: 3CCC; PDB: 3D4L; PDB: 3EIO; PDB: 3F8S; PDB: 3G0B; PDB: 3G0C; PDB: 3G0D; PDB: 3G0G; PDB: 3H0C; PDB: 3HAB; PDB: 3HAC; PDB: 3KWF; PDB: 3KWJ; PDB: 3NOX; PDB: 3O95; PDB: 3O9V; PDB: 3OC0; PDB: 3OPM; PDB: 3Q0T; PDB: 3Q8W; PDB: 3QBJ; PDB: 3SWW; PDB: 3SX4; PDB: 3VJK; PDB: 3VJL; PDB: 3VJM; PDB: 3W2T; PDB: 3WQH; PDB: 4A5S; PDB: 4DSA; PDB: 4DSZ; PDB: 4DTC; PDB: 4G1F; PDB: 4J3J; PDB: 4JH0; PDB: 4KR0; PDB: 4L72; PDB: 4LKO; PDB: 4N8D; PDB: 4N8E; PDB: 4PNZ; PDB: 4PV7; PDB: 4QZV; PDB: 5I7U; PDB: 5ISM; PDB: 5J3J; PDB: 5KBY; PDB: 5T4B; PDB: 5T4E; PDB: 5T4F; PDB: 5T4H; PDB: 5Y7H; PDB: 5Y7J; PDB: 5Y7K; PDB: 5ZID; PDB: 6B1E; PDB: 6B1O	.	DPP4_HUMAN	reviewed	ENSG00000197635	.	.	.	.	.
Mol01868	Protein	Dopamine receptor D2 (DRD2)	DRD2	DRD2	1813	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000346454.7,DRD2-201,2433; ENST00000362072.8,DRD2-202,2808; ENST00000535984.1,DRD2-203,529; ENST00000538967.5,DRD2-204,1493; ENST00000539420.1,DRD2-205,546; ENST00000540600.5,DRD2-206,1386; ENST00000542616.1,DRD2-207,443; ENST00000542968.5,DRD2-208,2467; ENST00000543292.1,DRD2-209,714; ENST00000544518.5,DRD2-210,2473"	MDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYNYYATLLTLLIAVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISIVWVLSFTISCPLLFGLNNADQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIVLRRRRKRVNTKRSSRAFRAHLRAPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARRAQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHPKIAKIFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFLKILHC	"chr11:113,409,605-113,475,691[-]"	"Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5."	PDB: 5AER; PDB: 6CM4; PDB: 6LUQ; PDB: 6VMS; PDB: 7DFP; PDB: 7JVR	HGNC:3023	DRD2_HUMAN	reviewed	ENSG00000149295	.	.	.	.	.
Mol01870	Protein	Dual specificity phosphatase 9 (DUSP9)	DUSP9; MKP4	DUSP9	1852	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000342782.4,DUSP9-201,2434; ENST00000370167.8,DUSP9-202,2289; ENST00000477033.1,DUSP9-203,430"	MEGLGRSCLWLRRELSPPRPRLLLLDCRSRELYESARIGGALSVALPALLLRRLRRGSLSVRALLPGPPLQPPPPAPVLLYDQGGGRRRRGEAEAEAEEWEAESVLGTLLQKLREEGYLAYYLQGGFSRFQAECPHLCETSLAGRAGSSMAPVPGPVPVVGLGSLCLGSDCSDAESEADRDSMSCGLDSEGATPPPVGLRASFPVQILPNLYLGSARDSANLESLAKLGIRYILNVTPNLPNFFEKNGDFHYKQIPISDHWSQNLSRFFPEAIEFIDEALSQNCGVLVHCLAGVSRSVTVTVAYLMQKLHLSLNDAYDLVKRKKSNISPNFNFMGQLLDFERSLRLEERHSQEQGSGGQASAASNPPSFFTTPTSDGAFELAPT	"chrX:153,642,492-153,651,326[+]"	Inactivates MAP kinases. Has a specificity for the ERK family.	PDB: 2HXP; PDB: 3LJ8	HGNC:3076	DUS9_HUMAN	reviewed	ENSG00000130829	.	.	.	.	.
Mol01871	Protein	Eukaryotic translation initiation factor 4E binding protein 1 (EIF4EBP1)	EIF4EBP1	EIF4EBP1	1978	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000338825.5,EIF4EBP1-201,827; ENST00000520657.1,EIF4EBP1-202,695"	MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI	"chr8:38,030,534-38,060,365[+]"	"Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways."	PDB: 1EJ4; PDB: 1EJH; PDB: 1WKW; PDB: 2JGB; PDB: 2JGC; PDB: 2V8W; PDB: 2V8X; PDB: 2V8Y; PDB: 3HXG; PDB: 3HXI; PDB: 3M93; PDB: 3M94; PDB: 3U7X; PDB: 4UED; PDB: 5BXV; PDB: 5EKV; PDB: 5NVN; PDB: 5WBJ; PDB: 6BCU; PDB: 6BCX	HGNC:3288	4EBP1_HUMAN	reviewed	ENSG00000187840	.	.	.	.	.
Mol01872	Protein	EPH receptor B4 (EPHB4)	EPHB4; HTK; MYK1; TYRO11	EPHB4	2050	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000358173.8,EPHB4-201,4353; ENST00000360620.7,EPHB4-202,3789; ENST00000467515.1,EPHB4-203,709; ENST00000477446.5,EPHB4-204,1551; ENST00000478459.5,EPHB4-205,965; ENST00000487222.5,EPHB4-206,5058; ENST00000489808.1,EPHB4-207,921; ENST00000492403.1,EPHB4-208,812; ENST00000492878.1,EPHB4-209,769; ENST00000616502.4,EPHB4-210,3737"	MELRVLLCWASLAAALEETLLNTKLETADLKWVTFPQVDGQWEELSGLDEEQHSVRTYEVCDVQRAPGQAHWLRTGWVPRRGAVHVYATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATALTPAWMENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYLAFQDQGACMALLSLHLFYKKCAQLTVNLTRFPETVPRELVVPVAGSCVVDAVPAPGPSPSLYCREDGQWAEQPVTGCSCAPGFEAAEGNTKCRACAQGTFKPLSGEGSCQPCPANSHSNTIGSAVCQCRVGYFRARTDPRGAPCTTPPSAPRSVVSRLNGSSLHLEWSAPLESGGREDLTYALRCRECRPGGSCAPCGGDLTFDPGPRDLVEPWVVVRGLRPDFTYTFEVTALNGVSSLATGPVPFEPVNVTTDREVPPAVSDIRVTRSSPSSLSLAWAVPRAPSGAVLDYEVKYHEKGAEGPSSVRFLKTSENRAELRGLKRGASYLVQVRARSEAGYGPFGQEHHSQTQLDESEGWREQLALIAGTAVVGVVLVLVVIVVAVLCLRKQSNGREAEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFELVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGTPGGTGGPAPQY	"chr7:100,802,565-100,827,523[-]"	"Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 it is involved in the regulation of cell adhesion and migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells."	PDB: 2BBA; PDB: 2E7H; PDB: 2HLE; PDB: 2QKQ; PDB: 2VWU; PDB: 2VWV; PDB: 2VWW; PDB: 2VWX; PDB: 2VWY; PDB: 2VWZ; PDB: 2VX0; PDB: 2VX1; PDB: 2X9F; PDB: 2XVD; PDB: 2YN8; PDB: 3ZEW; PDB: 4AW5; PDB: 4BB4; PDB: 6FNI; PDB: 6FNJ; PDB: 6FNK; PDB: 6FNL; PDB: 6FNM	HGNC:3395	EPHB4_HUMAN	reviewed	ENSG00000196411	.	.	.	.	.
Mol01873	Protein	Fructose-bisphosphatase 1 (FBP1)	FBP1; FBP	FBP1	2203	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375326.9,FBP1-201,1473; ENST00000414122.1,FBP1-202,629; ENST00000415431.5,FBP1-203,1487; ENST00000648117.1,FBP1-204,1073; ENST00000682520.1,FBP1-205,1424"	MADQAPFDTDVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHSAQ	"chr9:94,603,133-94,640,249[-]"	"Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain."	PDB: 1FTA; PDB: 2FHY; PDB: 2FIE; PDB: 2FIX; PDB: 2JJK; PDB: 2VT5; PDB: 2WBB; PDB: 2WBD; PDB: 2Y5K; PDB: 2Y5L; PDB: 3A29; PDB: 3KBZ; PDB: 3KC0; PDB: 3KC1; PDB: 4MJO; PDB: 5LDZ; PDB: 5PZQ; PDB: 5PZR; PDB: 5PZS; PDB: 5PZT; PDB: 5PZU; PDB: 5PZV; PDB: 5PZW; PDB: 5PZX; PDB: 5PZY; PDB: 5PZZ; PDB: 5Q00; PDB: 5Q01; PDB: 5Q02; PDB: 5Q03; PDB: 5Q04; PDB: 5Q05; PDB: 5Q06; PDB: 5Q07; PDB: 5Q08; PDB: 5Q09; PDB: 5Q0A; PDB: 5Q0B; PDB: 6LS5; PDB: 6LW2; PDB: 7C9Q; PDB: 7CVH; PDB: 7CVN; PDB: 7CWE	HGNC:3606	F16P1_HUMAN	reviewed	ENSG00000165140	.	.	.	.	.
Mol01874	Protein	Gamma-aminobutyric acid receptor subunit alpha-1 (GABAARs)	GABRA1	GABAARs	2554	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000023897.10,GABRA1-201,2083; ENST00000393943.10,GABRA1-202,4238; ENST00000428797.7,GABRA1-203,4285; ENST00000437025.6,GABRA1-204,4087; ENST00000519542.1,GABRA1-205,572; ENST00000519621.2,GABRA1-206,566; ENST00000521339.5,GABRA1-207,414; ENST00000522651.6,GABRA1-208,591; ENST00000634335.1,GABRA1-209,1070; ENST00000635096.1,GABRA1-210,411; ENST00000635880.1,GABRA1-211,1739; ENST00000635916.2,GABRA1-212,4878; ENST00000636340.1,GABRA1-213,2239; ENST00000636408.1,GABRA1-214,3677; ENST00000636573.1,GABRA1-215,2262; ENST00000637044.1,GABRA1-216,4108; ENST00000637620.1,GABRA1-217,100; ENST00000637827.1,GABRA1-218,1838; ENST00000638112.1,GABRA1-219,2818; ENST00000638159.1,GABRA1-220,4088"	MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDPLIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKIDRLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ	"chr5:161,847,063-161,899,981[+]"	"Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel. The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer. The alpha1/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor exhibit synaptogenic activity. GABRA1-mediated plasticity in the orbitofrontal cortex regulates context-dependent action selection. Functions also as histamine receptor and mediates cellular responses to histamine."	PDB: 6CDU; PDB: 6D1S; PDB: 6D6T; PDB: 6D6U; PDB: 6HUG; PDB: 6HUJ; PDB: 6HUK; PDB: 6HUO; PDB: 6HUP; PDB: 6I53; PDB: 6X3S; PDB: 6X3T; PDB: 6X3U; PDB: 6X3V; PDB: 6X3W; PDB: 6X3X; PDB: 6X3Z; PDB: 6X40	HGNC:4067	GBRA1_HUMAN	reviewed	ENSG00000022355	.	.	.	.	.
Mol01875	Protein	Glutamine--fructose-6-phosphate aminotransferase 1 (GFPT1)	GFPT1; GFAT; GFPT	GFPT1	2673	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357308.9,GFPT1-201,8665; ENST00000361060.5,GFPT1-202,8632; ENST00000494201.1,GFPT1-203,625; ENST00000674438.1,GFPT1-204,2655; ENST00000674507.1,GFPT1-205,5906"	MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSKFTRWGSQGERGKDKKGSCNLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE	"chr2:69,319,780-69,387,250[-]"	Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1. Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its effects on hyaluronan synthesis that occur during tissue remodeling.	PDB: 2V4M; PDB: 2ZJ3; PDB: 2ZJ4; PDB: 6R4E; PDB: 6R4F; PDB: 6R4G; PDB: 6R4H; PDB: 6R4I; PDB: 6R4J; PDB: 6SVM; PDB: 6SVO; PDB: 6SVP; PDB: 6SVQ; PDB: 6ZMJ; PDB: 6ZMK; PDB: 7NDL	.	GFPT1_HUMAN	reviewed	ENSG00000198380	.	.	.	.	.
Mol01876	Protein	HIC ZBTB transcriptional repressor 1 (HIC1)	HIC1; ZBTB29	HIC1	3090	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000322941.3,HIC1-201,3053; ENST00000399849.4,HIC1-202,3156; ENST00000571875.2,HIC1-203,812; ENST00000571990.1,HIC1-204,654; ENST00000574370.1,HIC1-205,1134; ENST00000576444.1,HIC1-206,725; ENST00000619757.5,HIC1-207,6707"	MTFPEADILLKSGECAGQTMLDTMEAPGHSRQLLLQLNNQRTKGFLCDVIIVVQNALFRAHKNVLAASSAYLKSLVVHDNLLNLDHDMVSPAVFRLVLDFIYTGRLADGAEAAAAAAVAPGAEPSLGAVLAAASYLQIPDLVALCKKRLKRHGKYCHLRGGGGGGGGYAPYGRPGRGLRAATPVIQACYPSPVGPPPPPAAEPPSGPEAAVNTHCAELYASGPGPAAALCASERRCSPLCGLDLSKKSPPGSAAPERPLAERELPPRPDSPPSAGPAAYKEPPLALPSLPPLPFQKLEEAAPPSDPFRGGSGSPGPEPPGRPDGPSLLYRWMKHEPGLGSYGDELGRERGSPSERCEERGGDAAVSPGGPPLGLAPPPRYPGSLDGPGAGGDGDDYKSSSEETGSSEDPSPPGGHLEGYPCPHLAYGEPESFGDNLYVCIPCGKGFPSSEQLNAHVEAHVEEEEALYGRAEAAEVAAGAAGLGPPFGGGGDKVAGAPGGLGELLRPYRCASCDKSYKDPATLRQHEKTHWLTRPYPCTICGKKFTQRGTMTRHMRSHLGLKPFACDACGMRFTRQYRLTEHMRIHSGEKPYECQVCGGKFAQQRNLISHMKMHAVGGAAGAAGALAGLGGLPGVPGPDGKGKLDFPEGVFAVARLTAEQLSLKQQDKAAAAELLAQTTHFLHDPKVALESLYPLAKFTAELGLSPDKAAEVLSQGAHLAAGPDGRTIDRFSPT	"chr17:2,054,154-2,063,241[+]"	"Transcriptional repressor. Recognizes and binds to the consensus sequence '5-[CG]NG[CG]GGGCA[CA]CC-3'. May act as a tumor suppressor. Involved in development of head, face, limbs and ventral body wall. Involved in down-regulation of SIRT1 and thereby is involved in regulation of p53/TP53-dependent apoptotic DNA-damage responses. The specific target gene promoter association seems to be depend on corepressors, such as CTBP1 or CTBP2 and MTA1. In cooperation with MTA1 (indicative for an association with the NuRD complex) represses transcription from CCND1/cyclin-D1 and CDKN1C/p57Kip2 specifically in quiescent cells. Involved in regulation of the Wnt signaling pathway probably by association with TCF7L2 and preventing TCF7L2 and CTNNB1 association with promoters of TCF-responsive genes. Seems to repress transcription from E2F1 and ATOH1 which involves ARID1A, indicative for the participation of a distinct SWI/SNF-type chromatin-remodeling complex. Probably represses transcription of ACKR3, FGFBP1 and EFNA1."	.	HGNC:4909	HIC1_HUMAN	reviewed	ENSG00000177374	.	.	.	.	.
Mol01877	Protein	3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)	HMGCR	HMGCR	3156	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000287936.9,HMGCR-201,4530; ENST00000343975.9,HMGCR-202,3681; ENST00000442032.2,HMGCR-203,268; ENST00000504466.1,HMGCR-204,1107; ENST00000508070.1,HMGCR-205,450; ENST00000509085.5,HMGCR-206,637; ENST00000509431.1,HMGCR-207,421; ENST00000511206.5,HMGCR-208,3395; ENST00000511986.1,HMGCR-209,487; ENST00000512053.1,HMGCR-210,465; ENST00000514315.2,HMGCR-211,603; ENST00000515776.1,HMGCR-212,501; ENST00000679456.1,HMGCR-213,7163; ENST00000680160.1,HMGCR-214,4493; ENST00000680940.1,HMGCR-215,6621; ENST00000681271.1,HMGCR-216,6777; ENST00000681410.1,HMGCR-217,6520; ENST00000681567.1,HMGCR-218,7379"	MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA	"chr5:75,336,329-75,364,001[+]"	"Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis. HMGCR is the main target of statins, a class of cholesterol-lowering drugs."	PDB: 1DQ8; PDB: 1DQ9; PDB: 1DQA; PDB: 1HW8; PDB: 1HW9; PDB: 1HWI; PDB: 1HWJ; PDB: 1HWK; PDB: 1HWL; PDB: 2Q1L; PDB: 2Q6B; PDB: 2Q6C; PDB: 2R4F; PDB: 3BGL; PDB: 3CCT; PDB: 3CCW; PDB: 3CCZ; PDB: 3CD0; PDB: 3CD5; PDB: 3CD7; PDB: 3CDA; PDB: 3CDB	HGNC:5006	HMDH_HUMAN	reviewed	ENSG00000113161	.	.	.	.	.
Mol01878	Protein	3-hydroxy-3-methylglutaryl-CoA synthase 1 (HMGCS1)	HMGCS1; HMGCS	HMGCS1	3157	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000325110.11,HMGCS1-201,5350; ENST00000433297.2,HMGCS1-202,3466; ENST00000507004.1,HMGCS1-203,950; ENST00000507293.1,HMGCS1-204,708; ENST00000508319.1,HMGCS1-205,591; ENST00000511774.1,HMGCS1-206,500; ENST00000514610.1,HMGCS1-207,555"	MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCTDREDINSLCMTVVQNLMERNNLSYDCIGRLEVGTETIIDKSKSVKTNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAVYATGNARPTGGVGAVALLIGPNAPLIFERGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYCKKIHAQWQKEGNDKDFTLNDFGFMIFHSPYCKLVQKSLARMLLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFMKASSELFSQKTKASLLVSNQNGNMYTSSVYGSLASVLAQYSPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTGVAPDVFAENMKLREDTHHLVNYIPQGSIDSLFEGTWYLVRVDEKHRRTYARRPTPNDDTLDEGVGLVHSNIATEHIPSPAKKVPRLPATAAEPEAAVISNGEH	"chr5:43,287,470-43,313,512[-]"	"Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate, a precursor for cholesterol synthesis."	PDB: 2P8U	HGNC:5007	HMCS1_HUMAN	reviewed	ENSG00000112972	.	.	.	.	.
Mol01879	Protein	Histamine receptor H1 (HRH1)	HRH1	HRH1	3269	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000397056.1,HRH1-201,4711; ENST00000413416.1,HRH1-202,574; ENST00000431010.3,HRH1-203,4617; ENST00000438284.2,HRH1-204,2080"	MSLPNSSCLLEDKMCEGNKTTMASPQLMPLVVVLSTICLVTVGLNLLVLYAVRSERKLHTVGNLYIVSLSVADLIVGAVVMPMNILYLLMSKWSLGRPLCLFWLSMDYVASTASIFSVFILCIDRYRSVQQPLRYLKYRTKTRASATILGAWFLSFLWVIPILGWNHFMQQTSVRREDKCETDFYDVTWFKVMTAIINFYLPTLLMLWFYAKIYKAVRQHCQHRELINRSLPSFSEIKLRPENPKGDAKKPGKESPWEVLKRKPKDAGGGSVLKSPSQTPKEMKSPVVFSQEDDREVDKLYCFPLDIVHMQAAAEGSSRDYVAVNRSHGQLKTDEQGLNTHGASEISEDQMLGDSQSFSRTDSDTTTETAPGKGKLRSGSNTGLDYIKFTWKRLRSHSRQYVSGLHMNRERKAAKQLGFIMAAFILCWIPYFIFFMVIAFCKNCCNEHLHMFTIWLGYINSTLNPLIYPLCNENFKKTFKRILHIRS	"chr3:11,137,093-11,263,557[+]"	"In peripheral tissues, the H1 subclass of histamine receptors mediates the contraction of smooth muscles, increase in capillary permeability due to contraction of terminal venules, and catecholamine release from adrenal medulla, as well as mediating neurotransmission in the central nervous system."	PDB: 3RZE; PDB: 7DFL	HGNC:5182	HRH1_HUMAN	reviewed	ENSG00000196639	.	.	.	.	.
Mol01880	Protein	5-hydroxytryptamine receptor 1F (HTR1F)	HTR1F; HTR1EL	HTR1F	3355	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000319595.7,HTR1F-201,3386"	MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC	"chr3:87,792,706-87,993,839[+]"	"G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity."	PDB: 7EXD	HGNC:5292	5HT1F_HUMAN	reviewed	ENSG00000179097	.	.	.	.	.
Mol01881	Protein	5-hydroxytryptamine receptor 4 (HTR4)	HTR4	HTR4	3360	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000360693.7,HTR4-201,3082; ENST00000362016.6,HTR4-202,2979; ENST00000377888.8,HTR4-203,3336; ENST00000517929.5,HTR4-204,1201; ENST00000519495.1,HTR4-205,869; ENST00000520086.1,HTR4-206,2272; ENST00000520514.5,HTR4-207,1236; ENST00000521124.5,HTR4-208,1221; ENST00000521530.5,HTR4-209,1323; ENST00000521735.5,HTR4-210,1242; ENST00000522588.5,HTR4-211,1326; ENST00000524063.3,HTR4-212,2274; ENST00000631296.1,HTR4-213,1224"	MDKLDANVSSEEGFGSVEKVVLLTFLSTVILMAILGNLLVMVAVCWDRQLRKIKTNYFIVSLAFADLLVSVLVMPFGAIELVQDIWIYGEVFCLVRTSLDVLLTTASIFHLCCISLDRYYAICCQPLVYRNKMTPLRIALMLGGCWVIPTFISFLPIMQGWNNIGIIDLIEKRKFNQNSNSTYCVFMVNKPYAITCSVVAFYIPFLLMVLAYYRIYVTAKEHAHQIQMLQRAGASSESRPQSADQHSTHRMRTETKAAKTLCIIMGCFCLCWAPFFVTNIVDPFIDYTVPGQVWTAFLWLGYINSGLNPFLYAFLNKSFRRAFLIILCCDDERYRRPSILGQTVPCSTTTINGSTHVLRDAVECGGQWESQCHPPATSPLVAAQPSDT	"chr5:148,451,032-148,677,235[-]"	"This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase."	PDB: 5EM9	HGNC:5299	5HT4R_HUMAN	reviewed	ENSG00000164270	.	.	.	.	.
Mol01882	Protein	Isopentenyl-diphosphate delta isomerase 1 (IDI1)	IDI1	IDI1	3422	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000381344.8,IDI1-201,2739; ENST00000427898.5,IDI1-202,441; ENST00000429642.2,IDI1-203,3370; ENST00000482091.1,IDI1-204,1029; ENST00000491735.1,IDI1-205,1066; ENST00000695775.1,IDI1-206,2506"	MPEINTNHLDKQQVQLLAEMCILIDENDNKIGAETKKNCHLNENIEKGLLHRAFSVFLFNTENKLLLQQRSDAKITFPGCFTNTCCSHPLSNPAELEESDALGVRRAAQRRLKAELGIPLEEVPPEEINYLTRIHYKAQSDGIWGEHEIDYILLVRKNVTLNPDPNEIKSYCYVSKEELKELLKKAASGEIKITPWFKIIAATFLFKWWDNLNHLNQFVDHEKIYRM	"chr10:1,039,152-1,049,119[-]"	"Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)."	PDB: 2DHO; PDB: 2I6K; PDB: 2ICJ; PDB: 2ICK	HGNC:5387	IDI1_HUMAN	reviewed	ENSG00000067064	.	.	.	.	.
Mol01883	Protein	Interleukin 2 receptor subunit alpha (IL2RA)	IL2RA	IL2RA	3559	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256876.10,IL2RA-201,1006; ENST00000379954.5,IL2RA-202,1562; ENST00000379959.8,IL2RA-203,3218; ENST00000447847.1,IL2RA-204,326; ENST00000644262.1,IL2RA-205,622; ENST00000649218.1,IL2RA-206,2791"	MDSYLLMWGLLTFIMVPGCQAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKSGSLYMLCTGNSSHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQASLPGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQPQLICTGEMETSQFPGEEKPQASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEYQVAVAGCVFLLISVLLLSGLTWQRRQRKSRRTI	"chr10:6,010,689-6,062,370[-]"	Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells.	PDB: 1Z92; PDB: 2B5I; PDB: 2ERJ; PDB: 3IU3; PDB: 3NFP; PDB: 6VWU; PDB: 6YIO; PDB: 7F9W	HGNC:6008	IL2RA_HUMAN	reviewed	ENSG00000134460	.	.	.	.	.
Mol01884	Protein	Interleukin 6 receptor (IL6R)	IL6R	IL6R	3570	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000344086.8,IL6R-201,3217; ENST00000368485.8,IL6R-202,5764; ENST00000476006.5,IL6R-203,881; ENST00000502679.1,IL6R-204,588; ENST00000507256.1,IL6R-205,539; ENST00000512471.1,IL6R-206,527; ENST00000515190.1,IL6R-207,570; ENST00000622330.4,IL6R-208,1496"	MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRSPPAENEVSTPMQALTTNKDDDNILFRDSANATSLPVQDSSSVPLPTFLVAGGSLAFGTLLCIAIVLRFKKTWKLRALKEGKTSMHPPYSLGQLVPERPRPTPVLVPLISPPVSPSSLGSDNTSSHNRPDARDPRSPYDISNTDYFFPR	"chr1:154,405,193-154,469,450[+]"	"Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable)."	PDB: 1N26; PDB: 1P9M; PDB: 2ARW; PDB: 5FUC; PDB: 7DC8	HGNC:6019	IL6RA_HUMAN	reviewed	ENSG00000160712	.	.	.	.	.
Mol01885	Protein	Forkhead box K2 (FOXK2)	FOXK2; ILF; ILF1	FOXK2	3607	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000335255.10,FOXK2-201,5243; ENST00000473637.6,FOXK2-202,3462; ENST00000526383.2,FOXK2-203,786; ENST00000527313.6,FOXK2-204,779; ENST00000529652.1,FOXK2-205,2199; ENST00000531030.5,FOXK2-206,805; ENST00000570585.1,FOXK2-207,756; ENST00000571160.1,FOXK2-208,496; ENST00000571989.1,FOXK2-209,573; ENST00000574694.1,FOXK2-210,731; ENST00000575578.1,FOXK2-211,571; ENST00000624186.1,FOXK2-212,4244"	MAAAAAALSGAGTPPAGGGAGGGGAGGGGSPPGGWAVARLEGREFEYLMKKRSVTIGRNSSQGSVDVSMGHSSFISRRHLEIFTPPGGGGHGGAAPELPPAQPRPDAGGDFYLRCLGKNGVFVDGVFQRRGAPPLQLPRVCTFRFPSTNIKITFTALSSEKREKQEASESPVKAVQPHISPLTINIPDTMAHLISPLPSPTGTISAANSCPSSPRGAGSSGYKVGRVMPSDLNLMADNSQPENEKEASGGDSPKDDSKPPYSYAQLIVQAITMAPDKQLTLNGIYTHITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASESKLIEQAFRKRRPRGVPCFRTPLGPLSSRSAPASPNHAGVLSAHSSGAQTPESLSREGSPAPLEPEPGAAQPKLAVIQEARFAQSAPGSPLSSQPVLITVQRQLPQAIKPVTYTVATPVTTSTSQPPVVQTVHVVHQIPAVSVTSVAGLAPANTYTVSGQAVVTPAAVLAPPKAEAQENGDHREVKVKVEPIPAIGHATLGTASRIIQTAQTTPVQTVTIVQQAPLGQHQLPIKTVTQNGTHVASVPTAVHGQVNNAAASPLHMLATHASASASLPTKRHNGDQPEQPELKRIKTEDGEGIVIALSVDTPPAAVREKGVQN	"chr17:82,519,713-82,644,662[+]"	"Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy. Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context. Together with FOXK1, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen. Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4. Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate. Together with FOXK1, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins. In addition to the 5'-GTAAACA-3' DNA motif, also binds the 5'-TGANTCA-3' palindromic DNA motif, and co-associates with JUN/AP-1 to activate transcription. Also able to bind to a minimal DNA heteroduplex containing a G/T-mismatch with 5'-TRT[G/T]NB-3' sequence. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus. Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements."	PDB: 1JXS; PDB: 2C6Y	HGNC:6036	FOXK2_HUMAN	reviewed	ENSG00000141568	.	.	.	.	.
Mol01886	Protein	Insulin induced gene 1 (INSIG1)	INSIG1	INSIG1	3638	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000340368.9,INSIG1-201,2908; ENST00000342407.5,INSIG1-202,1127; ENST00000344756.8,INSIG1-203,2623; ENST00000425172.1,INSIG1-204,596; ENST00000468307.1,INSIG1-205,852; ENST00000476756.1,INSIG1-206,1320"	MPRLHDHFWSCSCAHSARRRGPPRASAAGLAAKVGEMINVSVSGPSLLAAHGAPDADPAPRGRSAAMSGPEPGSPYPNTWHHRLLQRSLVLFSVGVVLALVLNLLQIQRNVTLFPEEVIATIFSSAWWVPPCCGTAAAVVGLLYPCIDSHLGEPHKFKREWASVMRCIAVFVGINHASAKLDFANNVQLSLTLAALSLGLWWTFDRSRSGLGLGITIAFLATLITQFLVYNGVYQYTSPDFLYIRSWLPCIFFSGGVTVGNIGRQLAMGVPEKPHSD	"chr7:155,297,776-155,310,235[+]"	"Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 25-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi. Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG1 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2. Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligases AMFR/gp78 and/or RNF139. Also regulates degradation of SOAT2/ACAT2 when the lipid levels are low: initiates the ubiquitin-mediated degradation of SOAT2/ACAT2 via recruitment of the ubiquitin ligases AMFR/gp78."	PDB: 4J81	HGNC:6083	INSI1_HUMAN	reviewed	ENSG00000186480	.	.	.	.	.
Mol01887	Protein	Integrin alpha-3 (ITA3)	ITGA3; MSK18	ITA3	3675	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000007722.11,ITGA3-201,3665; ENST00000320031.13,ITGA3-202,4889; ENST00000504417.1,ITGA3-203,227; ENST00000505306.5,ITGA3-204,5479; ENST00000505552.1,ITGA3-205,600; ENST00000505612.1,ITGA3-206,576; ENST00000506401.6,ITGA3-207,1817; ENST00000506437.1,ITGA3-208,3055; ENST00000506827.1,ITGA3-209,827; ENST00000507771.5,ITGA3-210,399; ENST00000508100.1,ITGA3-211,549; ENST00000510809.1,ITGA3-212,518; ENST00000512553.5,ITGA3-213,351; ENST00000514834.1,ITGA3-214,860; ENST00000515147.1,ITGA3-215,535; ENST00000570989.1,ITGA3-216,2495"	MGPGPSRAPRAPRLMLCALALMVAAGGCVVSAFNLDTRFLVVKEAGNPGSLFGYSVALHRQTERQQRYLLLAGAPRELAVPDGYTNRTGAVYLCPLTAHKDDCERMNITVKNDPGHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGSEDQRRMVGKCYVRGNDLELDSSDDWQTYHNEMCNSNTDYLETGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKEWDLSEYSYKDPEDQGNLYIGYTMQVGSFILHPKNITIVTGAPRHRHMGAVFLLSQEAGGDLRRRQVLEGSQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAIYVFMNQAGTSFPAHPSLLLHGPSGSAFGLSVASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSKGLLRQPQQVIHGEKLGLPGLATFGYSLSGQMDVDENFYPDLLVGSLSDHIVLLRARPVINIVHKTLVPRPAVLDPALCTATSCVQVELCFAYNQSAGNPNYRRNITLAYTLEADRDRRPPRLRFAGSESAVFHGFFSMPEMRCQKLELLLMDNLRDKLRPIIISMNYSLPLRMPDRPRLGLRSLDAYPILNQAQALENHTEVQFQKECGPDNKCESNLQMRAAFVSEQQQKLSRLQYSRDVRKLLLSINVTNTRTSERSGEDAHEALLTLVVPPALLLSSVRPPGACQANETIFCELGNPFKRNQRMELLIAFEVIGVTLHTRDLQVQLQLSTSSHQDNLWPMILTLLVDYTLQTSLSMVNHRLQSFFGGTVMGESGMKTVEDVGSPLKYEFQVGPMGEGLVGLGTLVLGLEWPYEVSNGKWLLYPTEITVHGNGSWPCRPPGDLINPLNLTLSDPGDRPSSPQRRRRQLDPGGGQGPPPVTLAAAKKAKSETVLTCATGRAHCVWLECPIPDAPVVTNVTVKARVWNSTFIEDYRDFDRVRVNGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVGAGLLLLGLIILLLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY	"chr17:50,055,968-50,090,481[+]"	"Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration."	.	.	ITA3_HUMAN	reviewed	ENSG00000005884	.	.	.	.	.
Mol01888	Protein	Integrin subunit beta 3 (ITGB3)	ITGB3; GP3A	ITGB3	3690	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000559488.7,ITGB3-201,5941; ENST00000571680.1,ITGB3-202,1668; ENST00000573377.1,ITGB3-203,408"	MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT	"chr17:47,253,827-47,313,743[+]"	"Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling. ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling. ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling. ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1. ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1. In brain, plays a role in synaptic transmission and plasticity. Involved in the regulation of the serotonin neurotransmission, is required to localize to specific compartments within the synapse the serotonin receptor SLC6A4 and for an appropriate reuptake of serotonin. Controls excitatory synaptic strength by regulating GRIA2-containing AMPAR endocytosis, which affects AMPAR abundance and composition. ITGAV:ITGB3 act as a receptor for CD40LG."	PDB: 1JV2; PDB: 1KUP; PDB: 1KUZ; PDB: 1L5G; PDB: 1M1X; PDB: 1M8O; PDB: 1MIZ; PDB: 1MK7; PDB: 1MK9; PDB: 1S4X; PDB: 1TYE; PDB: 1U8C; PDB: 2K9J; PDB: 2KNC; PDB: 2KV9; PDB: 2L1C; PDB: 2L91; PDB: 2LJD; PDB: 2LJE; PDB: 2LJF; PDB: 2MTP; PDB: 2N9Y; PDB: 2Q6W; PDB: 2RMZ; PDB: 2RN0; PDB: 2VC2; PDB: 2VDK; PDB: 2VDL; PDB: 2VDM; PDB: 2VDN; PDB: 2VDO; PDB: 2VDP; PDB: 2VDQ; PDB: 2VDR; PDB: 3FCS; PDB: 3FCU; PDB: 3IJE; PDB: 3NID; PDB: 3NIF; PDB: 3NIG; PDB: 3T3M; PDB: 3T3P; PDB: 3ZDX; PDB: 3ZDY; PDB: 3ZDZ; PDB: 3ZE0; PDB: 3ZE1; PDB: 3ZE2; PDB: 4CAK; PDB: 4G1E; PDB: 4G1M; PDB: 4MMX; PDB: 4MMY; PDB: 4MMZ; PDB: 4O02; PDB: 4Z7N; PDB: 4Z7O; PDB: 4Z7Q; PDB: 5HDB; PDB: 6AVQ; PDB: 6AVR; PDB: 6AVU; PDB: 6BXB; PDB: 6BXF; PDB: 6BXJ; PDB: 6CKB; PDB: 6MK0; PDB: 6MSL; PDB: 6MSU; PDB: 6NAJ; PDB: 6V4P; PDB: 7KN0; PDB: 7LA4	HGNC:6156	ITB3_HUMAN	reviewed	ENSG00000259207	.	.	.	.	.
Mol01889	Protein	Potassium inwardly rectifying channel subfamily J member 10 (KCNJ10)	KCNJ10	KCNJ10	3766	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000509700.2,KCNJ10-201,870; ENST00000636689.1,KCNJ10-202,1184; ENST00000637644.1,KCNJ10-203,1239; ENST00000638728.1,KCNJ10-204,4351; ENST00000638840.1,KCNJ10-205,3260; ENST00000638868.1,KCNJ10-206,3883; ENST00000639408.1,KCNJ10-207,1546; ENST00000640017.1,KCNJ10-208,2968; ENST00000640914.1,KCNJ10-209,565; ENST00000644903.1,KCNJ10-210,5205"	MTSVAKVYYSQTTQTESRPLMGPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELDPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV	"chr1:159,998,651-160,070,160[-]"	"May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules."	.	HGNC:6256	KCJ10_HUMAN	reviewed	ENSG00000177807	.	.	.	.	.
Mol01890	Protein	L1 cell adhesion molecule (L1CAM)	L1CAM; CAML1; MIC5	L1CAM	3897	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000361699.8,L1CAM-201,3888; ENST00000361981.7,L1CAM-202,5004; ENST00000370055.5,L1CAM-203,4655; ENST00000370058.7,L1CAM-204,692; ENST00000370060.7,L1CAM-205,5138; ENST00000407935.6,L1CAM-206,576; ENST00000420165.5,L1CAM-207,569; ENST00000439496.5,L1CAM-208,655; ENST00000455590.1,L1CAM-209,570; ENST00000458029.1,L1CAM-210,637; ENST00000460553.1,L1CAM-211,556; ENST00000474853.1,L1CAM-212,568; ENST00000484652.1,L1CAM-213,551; ENST00000491983.1,L1CAM-214,608; ENST00000496122.1,L1CAM-215,561; ENST00000616195.1,L1CAM-216,740"	MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSVVSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKERMFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE	"chrX:153,861,514-153,886,173[-]"	"Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity."	.	HGNC:6470	L1CAM_HUMAN	reviewed	ENSG00000198910	.	.	.	.	.
Mol01891	Protein	Lymphocyte activating 3 (LAG3)	LAG3; FDC	LAG3	3902	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000203629.3,LAG3-201,1976; ENST00000441671.6,LAG3-202,1576; ENST00000538079.1,LAG3-203,2587; ENST00000541049.1,LAG3-204,684"	MWEAQFLGLLFLQPLWVAPVKPLQPGAEVPVVWAQEGAPAQLPCSPTIPLQDLSLLRRAGVTWQHQPDSGPPAAAPGHPLAPGPHPAAPSSWGPRPRRYTVLSVGPGGLRSGRLPLQPRVQLDERGRQRGDFSLWLRPARRADAGEYRAAVHLRDRALSCRLRLRLGQASMTASPPGSLRASDWVILNCSFSRPDRPASVHWFRNRGQGRVPVRESPHHHLAESFLFLPQVSPMDSGPWGCILTYRDGFNVSIMYNLTVLGLEPPTPLTVYAGAGSRVGLPCRLPAGVGTRSFLTAKWTPPGGGPDLLVTGDNGDFTLRLEDVSQAQAGTYTCHIHLQEQQLNATVTLAIITVTPKSFGSPGSLGKLLCEVTPVSGQERFVWSSLDTPSQRSFSGPWLEAQEAQLLSQPWQCQLYQGERLLGAAVYFTELSSPGAQRSGRAPGALPAGHLLLFLILGVLSLLLLVTGAFGFHLWRRQWRPRRFSALEQGIHPPQAQSKIEELEQEPEPEPEPEPEPEPEPEPEQL	"chr12:6,772,512-6,778,455[+]"	"Lymphocyte activation gene 3 protein: Inhibitory receptor on antigen activated T-cells. Delivers inhibitory signals upon binding to ligands, such as FGL1. FGL1 constitutes a major ligand of LAG3 and is responsible for LAG3 T-cell inhibitory function. Following TCR engagement, LAG3 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation. May inhibit antigen-specific T-cell activation in synergy with PDCD1/PD-1, possibly by acting as a coreceptor for PDCD1/PD-1. Negatively regulates the proliferation, activation, effector function and homeostasis of both CD8(+) and CD4(+) T-cells. Also mediates immune tolerance: constitutively expressed on a subset of regulatory T-cells (Tregs) and contributes to their suppressive function. Also acts as a negative regulator of plasmacytoid dendritic cell (pDCs) activation. Binds MHC class II (MHC-II); the precise role of MHC-II-binding is however unclear."	.	HGNC:6476	LAG3_HUMAN	reviewed	ENSG00000089692	.	.	.	.	.
Mol01892	Protein	Lipoprotein lipase (LPL)	LPL; LIPD	LPL	4023	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000519773.1,LPL-201,554; ENST00000520959.5,LPL-202,560; ENST00000521994.1,LPL-203,566; ENST00000522701.5,LPL-204,559; ENST00000523696.1,LPL-205,463; ENST00000524029.5,LPL-206,629; ENST00000650287.1,LPL-207,3565; ENST00000650478.1,LPL-208,2254"	MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGVAESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEHYPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDWWSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG	"chr8:19,901,717-19,967,259[+]"	"Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans."	PDB: 6E7K; PDB: 6OAU; PDB: 6OAZ; PDB: 6OB0; PDB: 6WN4	HGNC:6677	LIPL_HUMAN	reviewed	ENSG00000175445	.	.	.	.	.
Mol01893	Protein	Lanosterol synthase (LSS)	LSS; OSC	LSS	4047	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356396.8,LSS-201,2995; ENST00000397728.8,LSS-202,4886; ENST00000419093.5,LSS-203,517; ENST00000450351.1,LSS-204,853; ENST00000457828.6,LSS-205,4390; ENST00000464357.1,LSS-206,1041; ENST00000472272.1,LSS-207,581; ENST00000474319.1,LSS-208,3601; ENST00000484808.1,LSS-209,251; ENST00000491729.1,LSS-210,2143; ENST00000522411.5,LSS-211,2523"	MTEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDTKNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLPAGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNILHKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPMSYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALLNLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPASTAFQEHVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRLSQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPRERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMGQTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYLQSAQSQIHNTCWAMMGLMAVRHPDIEAQERGVRCLLEKQLPNGDWPQENIAGVFNKSCAISYTSYRNIFPIWALGRFSQLYPERALAGHP	"chr21:46,188,141-46,228,824[-]"	"Key enzyme in the cholesterol biosynthesis pathway. Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. Through the production of lanosterol may regulate lens protein aggregation and increase transparency."	PDB: 1W6J; PDB: 1W6K	HGNC:6708	LSS_HUMAN	reviewed	ENSG00000160285	.	.	.	.	.
Mol01894	Protein	Monoamine oxidase A (MAOA)	MAOA	MAOA	4128	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000338702.4,MAOA-201,3931; ENST00000490604.1,MAOA-202,557; ENST00000497485.2,MAOA-203,3420; ENST00000542639.6,MAOA-204,5431; ENST00000686683.1,MAOA-205,3914; ENST00000686980.1,MAOA-206,8408; ENST00000688006.1,MAOA-207,4066; ENST00000688859.1,MAOA-208,1843; ENST00000689087.1,MAOA-209,3963; ENST00000693128.1,MAOA-210,3815"	MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS	"chrX:43,654,907-43,746,817[+]"	"Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially oxidizes serotonin. Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline."	PDB: 2BXR; PDB: 2BXS; PDB: 2Z5X; PDB: 2Z5Y	HGNC:6833	AOFA_HUMAN	reviewed	ENSG00000189221	.	.	.	.	.
Mol01895	Protein	Midkine (MDK)	MDK; MK1; NEGF2	MDK	4192	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359803.7,MDK-201,985; ENST00000395565.5,MDK-202,951; ENST00000395566.9,MDK-203,830; ENST00000395569.8,MDK-204,686; ENST00000405308.6,MDK-205,1166; ENST00000407067.1,MDK-206,1026; ENST00000441869.5,MDK-207,540; ENST00000481047.1,MDK-208,775; ENST00000489525.5,MDK-209,1339; ENST00000490240.5,MDK-210,603; ENST00000533283.5,MDK-211,498; ENST00000533952.5,MDK-212,477"	MQHRGFLLLTLLALLALTSAVAKKKDKVKKGGPGSECAEWAWGPCTPSSKDCGVGFREGTCGAQTQRIRCRVPCNWKKEFGADCKYKFENWGACDGGTGTKVRQGTLKKARYNAQCQETIRVTKPCTPKTKAKAKAKKGKGKD	"chr11:46,380,756-46,383,837[+]"	"Secreted protein that functions as cytokine and growth factor and mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors. Binds cell-surface proteoglycan receptors via their chondroitin sulfate (CS) groups. Thereby regulates many processes like inflammatory response, cell proliferation, cell adhesion, cell growth, cell survival, tissue regeneration, cell differentiation and cell migration. Participates in inflammatory processes by exerting two different activities. Firstly, mediates neutrophils and macrophages recruitment to the sites of inflammation both by direct action by cooperating namely with ITGB2 via LRP1 and by inducing chemokine expression. This inflammation can be accompanied by epithelial cell survival and smooth muscle cell migration after renal and vessel damage, respectively. Secondly, suppresses the development of tolerogenic dendric cells thereby inhibiting the differentiation of regulatory T cells and also promote T cell expansion through NFAT signaling and Th1 cell differentiation. Promotes tissue regeneration after injury or trauma. After heart damage negatively regulates the recruitment of inflammatory cells and mediates cell survival through activation of anti-apoptotic signaling pathways via MAPKs and AKT pathways through the activation of angiogenesis. Also facilitates liver regeneration as well as bone repair by recruiting macrophage at trauma site and by promoting cartilage development by facilitating chondrocyte differentiation. Plays a role in brain by promoting neural precursor cells survival and growth through interaction with heparan sulfate proteoglycans. Binds PTPRZ1 and promotes neuronal migration and embryonic neurons survival. Binds SDC3 or GPC2 and mediates neurite outgrowth and cell adhesion. Binds chondroitin sulfate E and heparin leading to inhibition of neuronal cell adhesion induced by binding with GPC2. Binds CSPG5 and promotes elongation of oligodendroglial precursor-like cells. Also binds ITGA6:ITGB1 complex; this interaction mediates MDK-induced neurite outgrowth. Binds LRP1; promotes neuronal survival. Binds ITGA4:ITGB1 complex; this interaction mediates MDK-induced osteoblast cells migration through PXN phosphorylation. Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation. Promotes epithelial to mesenchymal transition through interaction with NOTCH2. During arteriogenesis, plays a role in vascular endothelial cell proliferation by inducing VEGFA expression and release which in turn induces nitric oxide synthase expression. Moreover activates vasodilation through nitric oxide synthase activation. Negatively regulates bone formation in response to mechanical load by inhibiting Wnt/beta-catenin signaling in osteoblasts. In addition plays a role in hippocampal development, working memory, auditory response, early fetal adrenal gland development and the female reproductive system."	PDB: 1MKC; PDB: 1MKN	HGNC:6972	MK_HUMAN	reviewed	ENSG00000110492	.	.	.	.	.
Mol01896	Protein	Prostaglandin-endoperoxide synthase 1 (PTGS1)	MT-CO1; COI; COXI; MTCO1	PTGS1	4512	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MFADRWLFSTNHKDIGTLYLLFGAWAGVLGTALSLLIRAELGQPGNLLGNDHIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASAMVEAGAGTGWTVYPPLAGNYSHPGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGSNMKWSAAVLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFSGYTLDQTYAKIHFTIMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYTTWNILSSVGSFISLTAVMLMIFMIWEAFASKRKVLMVEEPSMNLEWLYGCPPPYHTFEEPVYMKS	.	"Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix."	PDB: 5Z62	HGNC:9604	COX1_HUMAN	reviewed	.	.	.	.	.	.
Mol01898	Protein	"Mucin 4, cell surface associated (MUC4)"	MUC4	MUC4	4585	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000308466.12,MUC4-201,3806; ENST00000339251.9,MUC4-202,3777; ENST00000346145.8,MUC4-203,3982; ENST00000349607.8,MUC4-204,3829; ENST00000392407.6,MUC4-205,3645; ENST00000415455.5,MUC4-206,3716; ENST00000448861.5,MUC4-207,3944; ENST00000462323.5,MUC4-208,16197; ENST00000463781.8,MUC4-209,16756; ENST00000464234.5,MUC4-210,1678; ENST00000466475.5,MUC4-211,16443; ENST00000467235.1,MUC4-212,2571; ENST00000469992.1,MUC4-213,698; ENST00000470451.5,MUC4-214,16169; ENST00000475231.5,MUC4-215,16273; ENST00000477086.5,MUC4-216,16353; ENST00000477756.5,MUC4-217,16401; ENST00000478156.5,MUC4-218,16562; ENST00000478685.1,MUC4-219,925; ENST00000479406.5,MUC4-220,16075; ENST00000480843.5,MUC4-221,16245; ENST00000486425.1,MUC4-222,553"	MKGARWRRVPWVSLSCLCLCLLPHVVPGTTEDTLITGSKTAAPVTSTGSTTATLEGQSTAASSRTSNQDISASSQNHQTKSTETTSKAQTDTLTQMMTSTLFSSPSVHNVMETAPPDEMTTSFPSSVTNTLMMTSKTITMTTSTDSTLGNTEETSTAGTESSTPVTSAVSITAGQEGQSRTTSWRTSIQDTSASSQNHWTRSTQTTRESQTSTLTHRTTSTPSFSPSVHNVTGTVSQKTSPSGETATSSLCSVTNTSMMTSEKITVTTSTGSTLGNPGETSSVPVTGSLMPVTSAALVTFDPEGQSPATFSRTSTQDTTAFSKNHQTQSVETTRVSQINTLNTLTPVTTSTVLSSPSGFNPSGTVSQETFPSGETTTSSPSSVSNTFLVTSKVFRMPTSRDSTLGNTEETSLSVSGTISAITSKVSTIWWSDTLSTALSPSSLPPKISTAFHTQQSEGAETTGRPHERSSFSPGVSQEIFTLHETTTWPSSFSSKGHTTWSQTELPSTSTGAATRLVTGNPSTGTAGTIPRVPSKVSAIGEPGEPTTYSSHSTTLPKTTGAGAQTQWTQETGTTGEALLSSPSYSVTQMIKTATSPSSSPMLDRHTSQQITTAPSTNHSTIHSTSTSPQESPAVSQRGHTQAPQTTQESQTTRSVSPMTDTKTVTTPGSSFTASGHSPSEIVPQDAPTISAATTFAPAPTGDGHTTQAPTTALQAAPSSHDATLGPSGGTSLSKTGALTLANSVVSTPGGPEGQWTSASASTSPDTAAAMTHTHQAESTEASGQTQTSEPASSGSRTTSAGTATPSSSGASGTTPSGSEGISTSGETTRFSSNPSRDSHTTQSTTELLSASASHGAIPVSTGMASSIVPGTFHPTLSEASTAGRPTGQSSPTSPSASPQETAAISRMAQTQRTRTSRGSDTISLASQATDTFSTVPPTPPSITSTGLTSPQTETHTLSPSGSGKTFTTALISNATPLPVTYASSASTGHTTPLHVTDASSVSTGHATPLPVTSPSSVSTGHTTPLPVTDTSSESTGHVTPLPVTSFSSASTGDSTPLPVTDTSSASTGHVTPLPVTSLSSASTGDTTPLPVTDTSSASTGHATSLPVTDTSSVSTGHTTPLPVTDTSSASTGHATSLPVTDTSSVSTGHTTPLHVTDASSASTGQATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHATPLLVTDTSSASTGHATPLPVTDASSVSTDHATSLPVTIPSAASTGHTTPLPVTDTSSASTGQATSLLVTDTSSVSTGDTTPLPVTSTSSASTGHVTPLHVTSPSSASTGHATPLPVTSLSSASTGDTMPLPVTSPSSASTGDTTPLPVTDASSVSTGHTTPLHVTDASSASTGQATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHATPLLVTDTSSASTGHATPLPVTDASSVSTDHATSLPVTIPSAASTGHTTPLPVTDTSSASTGQATSLLVTDTSSVSTGDTTPLPVTSTSSASTGHVTPLHVTSPSSASTGHATPLPVTSLSSASTGDTMPLPVTSPSSASTGDTTPLPVTDASSVSTGHTTPLPVTSPSSASTGHTTPLPVTDTSSASKGDTTPLPVTSPSSASTGHTTPLPVTDTSSASTGDTTPLPVTNASSLSTGHATPLHVTSPSSASTGHATPLPVTSTSSASTGHATPLPVTGLSSATTDDTTRLPVTDVSSASTGQATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHASPLLVTDASSASTGQATPLPVTDTSSVSTAHATPLPVTGLSSASTDDTTRLPVTDVSSASTGQAIPLPVTSPSSASTGDTTPLPVTDASSASTGDTTSLPVTIPSSASSGHTTSLPVTDASSVSTGHATSLLVTDASSVSTGDTTPLPVTDTNSASTGDTTPLHVTDASSVSTGHATSLPVTSLSSASTGDTTPLPVTSPSSASSGHTTPLPVTDASSVPTGHATSLPVTDASSVSTGHATPLPVTDASSVSTGHATPLPVTDTSSVSTGQATPLPVTSLSSASTGDTTPLPVTDTSSASTGQDTPLPVTSLSSVSTGDTTPLPVTNPSSASTGHATPLLVTDASSISTGHATSLLVTDASSVSTGHATALHDTDASSLSTGDTTPLPVTSPSSTSTGDTTPLPVTETSSVSTGHATSLPVTDTSSASTGHATSLPVTDTSSASTGHATPLPVTDTSSASTGQATPLPVTSPSSASTGHAIPLLVTDTSSASTGQATPLPVTSLSSASTGDTTPLPVTDASSVSTGHATSLPVTSLSSVSTGDTTPLPVTSPSSASTGHATPLHVTDASSASTGHATPLPVTSLSSASTGDTTPLPVTSPSSASTGHATPLHVTDASSVSTGDTTPLPVTSSSSASSGHTTPLPVTDASSASTGDTTPLPVTDTSSASTGHATHLPVTGLSSASTGDTTRLPVTNVSSASTGHATPLPVTSTSSASTGDTTPLPGTDTSSVSTGHTTPLLVTDASSVSTGDTTRLPVTSPSSASTGHTTPLPVTDTPSASTGDTTPLPVTNASSLSTRHATSLHVTSPSSASTGHATSLPVTDTSAASTGHATPLPVTSTSSASTGDTTPLPVTDTYSASTGQATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHATPLLVTDASSASTGQATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHATSLPVTDTSSASTGDTTSLPVTDTSSAYTGDTTSLPVTDTSSSSTGDTTPLLVTETSSVSTGDTTPLPVTDTSSASTGHATPLPVTNTSSVSTGHATPLHVTSPSSASTGHTTPLPVTDASSVSTGHATSLPVTDASSVFTGHATSLPVTIPSSASSGHTTPLPVTDASSVSTGHATSLPVTDASSVSTGHATPLPVTDASSVSTGHATPLPLTSLSSVSTGDTTPLPVTDTSSASTGQATPLPVTSLSSVSTGDTTPLPVTDTSSASTGHATSLPVTDTSSASTGHATPLPDTDTSSASTGHATLLPVTDTSSASIGHATSLPVTDTSSISTGHATPLHVTSPSSASTGHATPLPVTDTSSASTGHANPLHVTSPSSASTGHATPLPVTDTSSASTGHATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHTTPLPVTDTSSASTGQATALPVTSTSSASTGDTTPLPVTDTSSASTGQATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHATPLLVTDASSASTGQATPLPVTSLSSVSTGDTTPLPVTSPSSASTGHATSLPVTDTSSASTGDTTSLPVTDTSSAYTGDTTSLPVTDTSSSSTGDTTPLLVTETSSVSTGHATPLLVTDASSASTGHATPLHVTSPSSASTGDTTPVPVTDTSSVSTGHATPLPVTGLSSASTGDTTRLPVTDISSASTGQATPLPVTNTSSVSTGDTMPLPVTSPSSASTGHATPLPVTSTSSASTGHATPVPVTSTSSASTGHTTPLPVTDTSSASTGDTTPLPVTSPSSASTGHTTPLHVTIPSSASTGDTSTLPVTGASSASTGHATPLPVTDTSSVSTGHATPLPVTSLSSVSTGDTTPLPVTDASSASTGQATPLPVTSLSSVSTGDTTPLLVTDASSVSTGHATPLPVTDTSSASTGDTTRLPVTDTSSASTGQATPLPVTSLSSVSTGDTTPLLVTDASSVSTGHATPLPVTDTSSASTGDTTRLPVTDTSSASTGQATPLPVTIPSSSSSGHTTPLPVTSTSSVSTGHVTPLHVTSPSSASTGHVTPLPVTSTSSASTGHATPLLVTDASSVSTGHATPLPVTDASSASTGDTTPLPVTDTSSASTGQATPLPVTSLSSVSTGDTTPLPVTDASSASTGHATPLPVTIPSSVSTGDTMPLPVTSPSSASTGHATPLPVTGLSSASTGDTTPLPVTDTSSASTRHATPLPVTDTSSASTDDTTRLPVTDVSSASTGHATPLPVTSTSSASTGDTTPLPVTDTSSVSTGHATSLPVTSRSSASTGHATPLPVTDTSSVSTGHATPLPVTSTSSVSTGHATPLPVTSPSSASTGHATPVPVTSTSSASTGDTTPLPVTNASSLSTGHATPLHVTSPSSASRGDTSTLPVTDASSASTGHATPLPLTSLSSVSTGDTTPLPVTDTSSASTGQATPLPVTSLSSVSTGDTTPLPVTIPSSASSGHTTSLPVTDASSVSTGHGTPLPVTSTSSASTGDTTPLPVTDTSSASTGHATPLPVTDTSSASTGHATPLPVTSLSSVSTGHATPLAVSSATSASTVSSDSPLKMETPGMTTPSLKTDGGRRTATSPPPTTSQTIISTIPSTAMHTRSTAAPIPILPERGVSLFPYGAGAGDLEFVRRTVDFTSPLFKPATGFPLGSSLRDSLYFTDNGQIIFPESDYQIFSYPNPLPTGFTGRDPVALVAPFWDDADFSTGRGTTFYQEYETFYGEHSLLVQQAESWIRKMTNNGGYKARWALKVTWVNAHAYPAQWTLGSNTYQAILSTDGSRSYALFLYQSGGMQWDVAQRSGNPVLMGFSSGDGYFENSPLMSQPVWERYRPDRFLNSNSGLQGLQFYRLHREERPNYRLECLQWLKSQPRWPSWGWNQVSCPCSWQQGRRDLRFQPVSIGRWGLGSRQLCSFTSWRGGVCCSYGPWGEFREGWHVQRPWQLAQELEPQSWCCRWNDKPYLCALYQQRRPHVGCATYRPPQPAWMFGDPHITTLDGVSYTFNGLGDFLLVGAQDGNSSFLLQGRTAQTGSAQATNFIAFAAQYRSSSLGPVTVQWLLEPHDAIRVLLDNQTVTFQPDHEDGGGQETFNATGVLLSRNGSEVSASFDGWATVSVIALSNILHASASLPPEYQNRTEGLLGVWNNNPEDDFRMPNGSTIPPGSPEEMLFHFGMTWQINGTGLLGKRNDQLPSNFTPVFYSQLQKNSSWAEHLISNCDGDSSCIYDTLALRNASIGLHTREVSKNYEQANATLNQYPPSINGGRVIEAYKGQTTLIQYTSNAEDANFTLRDSCTDLELFENGTLLWTPKSLEPFTLEILARSAKIGLASALQPRTVVCHCNAESQCLYNQTSRVGNSSLEVAGCKCDGGTFGRYCEGSEDACEEPCFPSVHCVPGKGCEACPPNLTGDGRHCAALGSSFLCQNQSCPVNYCYNQGHCYISQTLGCQPMCTCPPAFTDSRCFLAGNNFSPTVNLELPLRVIQLLLSEEENASMAEVNASVAYRLGTLDMRAFLRNSQVERIDSAAPASGSPIQHWMVISEFQYRPRGPVIDFLNNQLLAAVVEAFLYHVPRRSEEPRNDVVFQPISGEDVRDVTALNVSTLKAYFRCDGYKGYDLVYSPQSGFTCVSPCSRGYCDHGGQCQHLPSGPRCSCVSFSIYTAWGEHCEHLSMKLDAFFGIFFGALGGLLLLGVGTFVVLRFWGCSGARFSYFLNSAEALP	"chr3:195,746,765-195,811,973[-]"	"Membrane-bound mucin, a family of highly glycosylated proteins that constitute the major component of the mucus, the slimy and viscous secretion covering epithelial surfaces. These glycoproteins play important roles in the protection of the epithelium and are implicated in epithelial renewal and differentiation. Regulates cellular behavior through both anti-adhesive effects on cell-cell and cell-extracellular matrix interactions and its ability to act as an intramembrane ligand for ERBB2. Plays an important role in proliferation and differentiation of epithelial cells by inducing specific phosphorylation of ERBB2. In polarized epithelial cells, segregates ERBB2 and other ERBB receptors and prevents ERBB2 from acting as a coreceptor. The interaction with ERBB2 leads to enhanced expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1 complex leads to down-regulation of CDKN1B, resulting in repression of apoptosis and stimulation of proliferation. Its ability to promote tumor growth may be mainly due to repression of apoptosis as opposed to proliferation."	.	HGNC:7514	MUC4_HUMAN	reviewed	ENSG00000145113	.	.	.	.	.
Mol01899	Protein	Tripartite motif containing 37 (TRIM37)	TRIM37; KIAA0898; MUL; POB1	TRIM37	4591	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262294.12,TRIM37-201,4489; ENST00000393065.6,TRIM37-202,3548; ENST00000393066.7,TRIM37-203,3622; ENST00000577554.5,TRIM37-204,4310; ENST00000580122.5,TRIM37-205,482; ENST00000580620.5,TRIM37-206,872; ENST00000580973.5,TRIM37-207,573; ENST00000581468.1,TRIM37-208,584; ENST00000582852.1,TRIM37-209,501; ENST00000583387.1,TRIM37-210,842; ENST00000583945.5,TRIM37-211,430; ENST00000584889.3,TRIM37-212,353; ENST00000585287.5,TRIM37-213,634; ENST00000625984.1,TRIM37-214,204"	MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDMLLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPRPPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAALAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGSSQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSETGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDENSGR	"chr17:58,982,638-59,106,921[-]"	"E3 ubiquitin-protein ligase required to prevent centriole reduplication. Probably acts by ubiquitinating positive regulators of centriole reduplication. Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes. Has anti-HIV activity."	PDB: 3LRQ	HGNC:7523	TRI37_HUMAN	reviewed	ENSG00000108395	.	.	.	.	.
Mol01900	Protein	Mevalonate kinase (MVK)	MVK	MVK	4598	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000228510.8,MVK-201,2833; ENST00000392727.7,MVK-202,1770; ENST00000447878.6,MVK-203,1644; ENST00000535044.1,MVK-204,548; ENST00000537237.5,MVK-205,1296; ENST00000539335.5,MVK-206,834; ENST00000539575.4,MVK-207,2747; ENST00000539696.5,MVK-208,608; ENST00000540353.1,MVK-209,4109; ENST00000545516.1,MVK-210,522; ENST00000545774.5,MVK-211,702; ENST00000546277.5,MVK-212,886; ENST00000625889.2,MVK-213,2591; ENST00000629016.2,MVK-214,1591; ENST00000636529.1,MVK-215,1509; ENST00000636996.1,MVK-216,1725; ENST00000639206.1,MVK-217,367"	MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL	"chr12:109,573,255-109,598,125[+]"	"Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis."	PDB: 2R3V	HGNC:7530	KIME_HUMAN	reviewed	ENSG00000110921	.	.	.	.	.
Mol01901	Protein	"MYB proto-oncogene, transcription factor (MYB)"	MYB	MYB	4602	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000316528.12,MYB-201,3571; ENST00000339290.9,MYB-202,3365; ENST00000341911.10,MYB-203,3684; ENST00000367812.6,MYB-204,3565; ENST00000367814.8,MYB-205,3302; ENST00000420123.6,MYB-206,1051; ENST00000430686.2,MYB-207,1036; ENST00000438901.6,MYB-208,3481; ENST00000442647.7,MYB-209,3312; ENST00000463282.6,MYB-210,3422; ENST00000524588.5,MYB-211,1630; ENST00000525002.5,MYB-212,2182; ENST00000525369.5,MYB-213,2866; ENST00000525477.5,MYB-214,3431; ENST00000525514.5,MYB-215,3288; ENST00000525940.5,MYB-216,1838; ENST00000526187.5,MYB-217,2192; ENST00000526320.5,MYB-218,3081; ENST00000526565.5,MYB-219,2399; ENST00000526889.5,MYB-220,3157; ENST00000527615.5,MYB-221,2381; ENST00000528015.5,MYB-222,2201; ENST00000528140.5,MYB-223,2021; ENST00000528343.5,MYB-224,2091; ENST00000528345.5,MYB-225,1973; ENST00000528774.5,MYB-226,2277; ENST00000529262.5,MYB-227,2427; ENST00000529297.1,MYB-228,343; ENST00000529586.5,MYB-229,3203; ENST00000531519.5,MYB-230,2911; ENST00000531634.5,MYB-231,1824; ENST00000531737.5,MYB-232,2436; ENST00000531845.5,MYB-233,3230; ENST00000533384.5,MYB-234,2521; ENST00000533624.5,MYB-235,1818; ENST00000533808.5,MYB-236,3349; ENST00000533837.5,MYB-237,3492; ENST00000534044.5,MYB-238,1812; ENST00000534121.5,MYB-239,2238; ENST00000534736.1,MYB-240,801; ENST00000616088.4,MYB-241,3573"	MARRPRHSIYSSDEDDEDFEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQESSKASQPAVATSFQKNSHLMGFAQAPPTAQLPATGQPTVNNDYSYYHISEAQNVSSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQVLPTQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGEHHSTPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSDLEMPSLTSTPLIGHKLTVTTPFHRDQTVKTQKENTVFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHLVEDLQDVIKQESDESGIVAEFQENGPPLLKKIKQEVESPTDKSGNFFCSHHWEGDSLNTQLFTQTSPVADAPNILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQPCSSTWEPASCGKMEEQMTSSSQARKYVNAFSARTLVM	"chr6:135,181,308-135,219,173[+]"	Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.	.	HGNC:7545	MYB_HUMAN	reviewed	ENSG00000118513	.	.	.	.	.
Mol01902	Protein	Pyruvate dehydrogenase kinase 2 (PDK2)	PDK2; PDHK2	PDK2	5164	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000007708.7,PDK2-201,2384; ENST00000503076.1,PDK2-202,560; ENST00000503176.6,PDK2-203,3364; ENST00000503614.5,PDK2-204,947; ENST00000505440.5,PDK2-205,615; ENST00000505897.5,PDK2-206,865; ENST00000506242.5,PDK2-207,517; ENST00000506647.1,PDK2-208,660; ENST00000508030.5,PDK2-209,578; ENST00000508960.1,PDK2-210,553; ENST00000510219.2,PDK2-211,576; ENST00000511026.1,PDK2-212,577; ENST00000512204.5,PDK2-213,806; ENST00000512238.1,PDK2-214,590; ENST00000515040.5,PDK2-215,567; ENST00000614357.4,PDK2-216,2493"	MRWVWALLKNASLAGAPKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKHIGSIDPNCNVSEVVKDAYDMAKLLCDKYYMASPDLEIQEINAANSKQPIHMVYVPSHLYHMLFELFKNAMRATVESHESSLILPPIKVMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVPSTEPKNTSTYRVS	"chr17:50,094,737-50,112,152[+]"	"Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis."	PDB: 2BTZ; PDB: 2BU2; PDB: 2BU5; PDB: 2BU6; PDB: 2BU7; PDB: 2BU8; PDB: 4MP2; PDB: 4MP7; PDB: 4MPC; PDB: 4MPE; PDB: 4MPN; PDB: 4V25; PDB: 4V26; PDB: 5J6A; PDB: 5J71; PDB: 5M4K; PDB: 5M4M; PDB: 5M4N; PDB: 5M4P; PDB: 6LIL; PDB: 6LIN; PDB: 6LIO; PDB: 6TMP; PDB: 6TMQ; PDB: 6TMZ; PDB: 6TN0; PDB: 6TN2; PDB: 7EA0; PDB: 7EAS; PDB: 7EBH	HGNC:8810	PDK2_HUMAN	reviewed	ENSG00000005882	.	.	.	.	.
Mol01903	Protein	Progesterone receptor (PGR)	PGR; NR3C3	PGR	5241	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263463.9,PGR-201,2496; ENST00000325455.10,PGR-202,13037; ENST00000526300.5,PGR-203,2365; ENST00000528960.5,PGR-204,2633; ENST00000530764.1,PGR-205,620; ENST00000533207.5,PGR-206,2224; ENST00000534013.5,PGR-207,1901; ENST00000534780.5,PGR-208,2750; ENST00000619228.2,PGR-209,3038; ENST00000632634.1,PGR-210,551"	MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGVPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK	"chr11:101,029,624-101,129,813[-]"	"The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as transcriptional activator or repressor."	PDB: 1A28; PDB: 1E3K; PDB: 1SQN; PDB: 1SR7; PDB: 1ZUC; PDB: 2C7A; PDB: 2OVH; PDB: 2OVM; PDB: 2W8Y; PDB: 3D90; PDB: 3G8O; PDB: 3HQ5; PDB: 3KBA; PDB: 3ZR7; PDB: 3ZRA; PDB: 3ZRB; PDB: 4A2J; PDB: 4APU; PDB: 4OAR; PDB: 5CC0	HGNC:8910	PRGR_HUMAN	reviewed	ENSG00000082175	.	.	.	.	.
Mol01904	Protein	Paraoxonase 1 (PON1)	PON1; PON	PON1	5444	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000222381.8,PON1-201,2393; ENST00000433729.1,PON1-202,1058; ENST00000462594.1,PON1-203,553; ENST00000470502.1,PON1-204,578"	MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL	"chr7:95,297,676-95,324,532[-]"	"Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation."	PDB: 1V04	HGNC:9204	PON1_HUMAN	reviewed	ENSG00000005421	.	.	.	.	.
Mol01905	Protein	Protein phosphatase 3 catalytic subunit alpha (PPP3CA)	PPP3R1; CNA2; CNB	PPP3CA	5534	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000234310.8,PPP3R1-201,3024; ENST00000409377.1,PPP3R1-202,684; ENST00000409752.5,PPP3R1-203,851"	MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV	"chr2:68,178,857-68,256,237[-]"	"Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity."	PDB: 1AUI; PDB: 1M63; PDB: 1MF8; PDB: 2P6B; PDB: 3LL8; PDB: 4F0Z; PDB: 4OR9; PDB: 4ORA; PDB: 4ORC; PDB: 5SVE; PDB: 6NUC; PDB: 6NUF; PDB: 6NUU	HGNC:9314	CANB1_HUMAN	reviewed	ENSG00000221823	.	.	.	.	.
Mol01906	Protein	Protein kinase C alpha (PRKCA)	PRKCA; PKCA; PRKACA	PRKCA	5578	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000284384.6,PRKCA-201,2718; ENST00000413366.8,PRKCA-202,8964; ENST00000578063.5,PRKCA-203,1733; ENST00000583361.1,PRKCA-204,519; ENST00000583775.1,PRKCA-205,321"	MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV	"chr17:66,302,613-66,810,743[+]"	"Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteosomal degradation."	PDB: 2ELI; PDB: 3IW4; PDB: 4DNL; PDB: 4RA4	HGNC:9393	KPCA_HUMAN	Reviewed	ENSG00000154229	.	.	.	.	.
Mol01907	Protein	Protein kinase C theta (PRKCT)	PRKCQ; PRKCT	PRKCT	5588	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000539722.5,PRKCQ-203,3224; ENST00000397176.6,PRKCQ-202,3096; ENST00000263125.10,PRKCQ-201,3255"	MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS	"chr10:6,427,143-6,580,301[-]"	"Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylates CCDC88A/GIV and inhibits its guanine nucleotide exchange factor activity."	.	HGNC:9410	KPCT_HUMAN	Reviewed	ENSG00000065675	.	.	.	.	.
Mol01908	Protein	Prostaglandin E2 receptor EP3 subtype (PE2R3)	PTGER3	PE2R3	5733	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000306666.10,PTGER3-201,2360; ENST00000356595.8,PTGER3-202,1943; ENST00000361210.6,PTGER3-203,1922; ENST00000370924.4,PTGER3-204,6982; ENST00000370931.7,PTGER3-205,1914; ENST00000460330.5,PTGER3-206,1447; ENST00000479353.5,PTGER3-207,1895; ENST00000497146.5,PTGER3-208,1971; ENST00000628037.2,PTGER3-209,1815"	MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLLTGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRWEHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLGVWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLLALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLIMMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQIRYHTNNYASSSTSLPCQCSSTLMWSDHLER	"chr1:70,852,353-71,047,816[-]"	"Receptor for prostaglandin E2 (PGE2). The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G(i) proteins, and to an elevation of intracellular calcium. Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation. Required for increased HCO3(-) secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid-induced ulceration. Not required for normal kidney function, normal urine volume and osmolality."	PDB: 6AK3; PDB: 6M9T	.	PE2R3_HUMAN	reviewed	ENSG00000050628	.	.	.	.	.
Mol01909	Protein	Retinoblastoma-like protein 1 (RBL1)	RBL1	RBL1	5933	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000344359.7,RBL1-201,3225; ENST00000373664.8,RBL1-202,5686; ENST00000525052.1,RBL1-203,763; ENST00000527999.1,RBL1-204,599"	MFEDKPHAEGAAVVAAAGEALQALCQELNLDEGSAAEALDDFTAIRGNYSLEGEVTHWLACSLYVACRKSIIPTVGKGIMEGNCVSLTRILRSAKLSLIQFFSKMKKWMDMSNLPQEFRERIERLERNFEVSTVIFKKYEPIFLDIFQNPYEEPPKLPRSRKQRRIPCSVKDLFNFCWTLFVYTKGNFRMIGDDLVNSYHLLLCCLDLIFANAIMCPNRQDLLNPSFKGLPSDFHTADFTASEEPPCIIAVLCELHDGLLVEAKGIKEHYFKPYISKLFDRKILKGECLLDLSSFTDNSKAVNKEYEEYVLTVGDFDERIFLGADAEEEIGTPRKFTRDTPLGKLTAQANVEYNLQQHFEKKRSFAPSTPLTGRRYLREKEAVITPVASATQSVSRLQSIVAGLKNAPSDQLINIFESCVRNPVENIMKILKGIGETFCQHYTQSTDEQPGSHIDFAVNRLKLAEILYYKILETVMVQETRRLHGMDMSVLLEQDIFHRSLMACCLEIVLFAYSSPRTFPWIIEVLNLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLAWSHDSALWEALQVSANKVPTCEEVIFPNNFETGNGGNVQGHLPLMPMSPLMHPRVKEVRTDSGSLRRDMQPLSPISVHERYSSPTAGSAKRRLFGEDPPKEMLMDKIITEGTKLKIAPSSSITAENVSILPGQTLLTMATAPVTGTTGHKVTIPLHGVANDAGEITLIPLSMNTNQESKVKSPVSLTAHSLIGASPKQTNLTKAQEVHSTGINRPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIMKSYRNQPQANSHVYRSVLLKSIPREVVAYNKNINDDFEMIDCDLEDATKTPDCSSGPVKEERGDLIKFYNTIYVGRVKSFALKYDLANQDHMMDAPPLSPFPHIKQQPGSPRRISQQHSIYISPHKNGSGLTPRSALLYKFNGSPSKSLKDINNMIRQGEQRTKKRVIAIDSDAESPAKRVCQENDDVLLKRLQDVVSERANH	"chr20:36,996,349-37,095,997[-]"	"Key regulator of entry into cell division. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Probably acts as a transcription repressor by recruiting chromatin-modifying enzymes to promoters. Potent inhibitor of E2F-mediated trans-activation. May act as a tumor suppressor."	PDB: 1H28; PDB: 4YOO; PDB: 4YOS; PDB: 4YOZ; PDB: 5TUV	.	RBL1_HUMAN	reviewed	ENSG00000080839	.	.	.	.	.
Mol01910	Protein	Reticulocalbin 1 (RCN1)	RCN1; RCN	RCN1	5954	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000054950.4,RCN1-201,2369; ENST00000527337.1,RCN1-202,737; ENST00000528630.1,RCN1-203,549; ENST00000531345.1,RCN1-204,2653; ENST00000532474.5,RCN1-205,714; ENST00000532721.1,RCN1-206,494; ENST00000533898.5,RCN1-207,2416"	MARGGRGRRLGLALGLLLALVLAPRVLRAKPTVRKERVVRPDSELGERPPEDNQSFQYDHEAFLGKEDSKTFDQLTPDESKERLGKIVDRIDNDGDGFVTTEELKTWIKRVQKRYIFDNVAKVWKDYDRDKDDKISWEEYKQATYGYYLGNPAEFHDSSDHHTFKKMLPRDERRFKAADLNGDLTATREEFTAFLHPEEFEHMKEIVVLETLEDIDKNGDGFVDQDEYIADMFSHEENGPEPDWVLSEREQFNEFRDLNKDGKLDKDEIRHWILPQDYDHAQAEARHLVYESDKNKDEKLTKEEILENWNMFVGSQATNYGEDLTKNHDEL	"chr11:32,091,074-32,105,722[+]"	May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment.	.	HGNC:9934	RCN1_HUMAN	reviewed	ENSG00000049449	.	.	.	.	.
Mol01911	Protein	"REL proto-oncogene, NF-kB subunit (REL)"	REL	REL	5966	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000295025.12,REL-201,11255; ENST00000394479.4,REL-202,11108; ENST00000642725.1,REL-203,2156"	MASGAYNPYIEIIEQPRQRGMRFRYKCEGRSAGSIPGEHSTDNNRTYPSIQIMNYYGKGKVRITLVTKNDPYKPHPHDLVGKDCRDGYYEAEFGQERRPLFFQNLGIRCVKKKEVKEAIITRIKAGINPFNVPEKQLNDIEDCDLNVVRLCFQVFLPDEHGNLTTALPPVVSNPIYDNRAPNTAELRICRVNKNCGSVRGGDEIFLLCDKVQKDDIEVRFVLNDWEAKGIFSQADVHRQVAIVFKTPPYCKAITEPVTVKMQLRRPSDQEVSESMDFRYLPDEKDTYGNKAKKQKTTLLFQKLCQDHVETGFRHVDQDGLELLTSGDPPTLASQSAGITVNFPERPRPGLLGSIGEGRYFKKEPNLFSHDAVVREMPTGVSSQAESYYPSPGPISSGLSHHASMAPLPSSSWSSVAHPTPRSGNTNPLSSFSTRTLPSNSQGIPPFLRIPVGNDLNASNACIYNNADDIVGMEASSMPSADLYGISDPNMLSNCSVNMMTTSSDSMGETDNPRLLSMNLENPSCNSVLDPRDLRQLHQMSSSSMSAGANSNTTVFVSQSDAFEGSDFSCADNSMINESGPSNSTNPNSHGFVQDSQYSGIGSMQNEQLSDSFPYEFFQV	"chr2:60,881,521-60,931,612[+]"	"Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator."	.	HGNC:9954	REL_HUMAN	reviewed	ENSG00000162924	.	.	.	.	.
Mol01912	Protein	"RELB proto-oncogene, NF-kB subunit (RELB)"	RELB	RELB	5971	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000221452.13,RELB-201,2258; ENST00000505236.1,RELB-202,2219; ENST00000509229.1,RELB-203,775; ENST00000509480.5,RELB-204,840; ENST00000510184.1,RELB-205,546; ENST00000589972.1,RELB-206,760; ENST00000625761.2,RELB-207,2279"	MLRSGPASGPSVPTGRAMPSRRVARPPAAPELGALGSPDLSSLSLAVSRSTDELEIIDEYIKENGFGLDGGQPGPGEGLPRLVSRGAASLSTVTLGPVAPPATPPPWGCPLGRLVSPAPGPGPQPHLVITEQPKQRGMRFRYECEGRSAGSILGESSTEASKTLPAIELRDCGGLREVEVTACLVWKDWPHRVHPHSLVGKDCTDGICRVRLRPHVSPRHSFNNLGIQCVRKKEIEAAIERKIQLGIDPYNAGSLKNHQEVDMNVVRICFQASYRDQQGQMRRMDPVLSEPVYDKKSTNTSELRICRINKESGPCTGGEELYLLCDKVQKEDISVVFSRASWEGRADFSQADVHRQIAIVFKTPPYEDLEIVEPVTVNVFLQRLTDGVCSEPLPFTYLPRDHDSYGVDKKRKRGMPDVLGELNSSDPHGIESKRRKKKPAILDHFLPNHGSGPFLPPSALLPDPDFFSGTVSLPGLEPPGGPDLLDDGFAYDPTAPTLFTMLDLLPPAPPHASAVVCSGGAGAVVGETPGPEPLTLDSYQAPGPGDGGTASLVGSNMFPNHYREAAFGGGLLSPGPEAT	"chr19:45,001,449-45,038,198[+]"	"NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function."	.	HGNC:9956	RELB_HUMAN	reviewed	ENSG00000104856	.	.	.	.	.
Mol01913	Protein	Bromodomain containing 2 (BRD2)	BRD2; KIAA9001; RING3	BRD2	6046	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374825.9,BRD2-201,4956; ENST00000374831.8,BRD2-202,4807; ENST00000395287.5,BRD2-203,3467; ENST00000449025.5,BRD2-204,3210; ENST00000449085.4,BRD2-205,4579; ENST00000456339.5,BRD2-206,887; ENST00000463639.2,BRD2-207,3045; ENST00000464592.6,BRD2-208,4520; ENST00000469132.2,BRD2-209,6084; ENST00000481259.1,BRD2-210,667; ENST00000482838.1,BRD2-211,759; ENST00000482914.5,BRD2-212,4834; ENST00000495733.5,BRD2-213,3404; ENST00000496118.2,BRD2-214,735; ENST00000580234.1,BRD2-215,718; ENST00000581002.1,BRD2-216,550; ENST00000584808.1,BRD2-217,547; ENST00000606059.1,BRD2-218,565; ENST00000607833.5,BRD2-219,2338; ENST00000677085.1,BRD2-220,4312; ENST00000677331.1,BRD2-221,4144; ENST00000678250.1,BRD2-222,4798; ENST00000678778.1,BRD2-223,4064; ENST00000679099.1,BRD2-224,4737; ENST00000679179.1,BRD2-225,4282"	MLQNVTPHNKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLTPANPPPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPMDMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMPQEEQELVVTIPKNSHKKGAKLAALQGSVTSAHQVPAVSSVSHTALYTPPPEIPTTVLNIPHPSVISSPLLKSLHSAGPPLLAVTAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPASPPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELLSKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLMFSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTAMPPGLAKSSSESSSEESSSESSSEEEEEEDEEDEEEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPISKPKRKREKKEKKKKRKAEKHRGRAGADEDDKGPRAPRPPQPKKSKKASGSGGGSAALGPSGFGPSGGSGTKLPKKATKTAPPALPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKLGRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIKKPVGKTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKANEKTESSSAQQVAVSRLSASSSSSDSSSSSSSSSSSDTSDSDSG	"chr6:32,968,594-32,981,505[+]"	"May play a role in spermatogenesis or folliculogenesis (By similarity). Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly."	PDB: 1X0J; PDB: 2DVQ; PDB: 2DVR; PDB: 2DVS; PDB: 2DVV; PDB: 2E3K; PDB: 2G4A; PDB: 2YDW; PDB: 2YEK; PDB: 3AQA; PDB: 3ONI; PDB: 4A9E; PDB: 4A9F; PDB: 4A9H; PDB: 4A9I; PDB: 4A9J; PDB: 4A9M; PDB: 4A9N; PDB: 4A9O; PDB: 4AKN; PDB: 4ALG; PDB: 4ALH; PDB: 4J1P; PDB: 4MR5; PDB: 4MR6; PDB: 4QEU; PDB: 4QEV; PDB: 4QEW; PDB: 4UYF; PDB: 4UYG; PDB: 4UYH; PDB: 5BT5; PDB: 5DFB; PDB: 5DFC; PDB: 5DFD; PDB: 5DW1; PDB: 5EK9; PDB: 5HEL; PDB: 5HEM; PDB: 5HEN; PDB: 5HFQ; PDB: 5IBN; PDB: 5IG6; PDB: 5N2L; PDB: 5O38; PDB: 5O39; PDB: 5O3A; PDB: 5O3B; PDB: 5O3C; PDB: 5O3D; PDB: 5O3E; PDB: 5O3F; PDB: 5O3G; PDB: 5O3H; PDB: 5O3I; PDB: 5U5S; PDB: 5U6V; PDB: 5UEW; PDB: 5XHE; PDB: 5XHK; PDB: 6CUI; PDB: 6DB0; PDB: 6DBC; PDB: 6DDI; PDB: 6DDJ; PDB: 6E6J; PDB: 6FFE; PDB: 6FFF; PDB: 6FFG; PDB: 6I80; PDB: 6I81; PDB: 6JKE; PDB: 6K04; PDB: 6K05; PDB: 6MO7; PDB: 6MO8; PDB: 6MO9; PDB: 6MOA; PDB: 6ONY; PDB: 6SWO; PDB: 6SWP; PDB: 6TQ1; PDB: 6TQ2; PDB: 6U61; PDB: 6U71; PDB: 6U8H; PDB: 6ULQ; PDB: 6ULT; PDB: 6VIY; PDB: 6WWB; PDB: 6YTM; PDB: 6Z7F; PDB: 6Z8P; PDB: 6ZB0; PDB: 6ZB1; PDB: 6ZB2; PDB: 7DPN; PDB: 7DPO; PDB: 7JX7; PDB: 7L6D; PDB: 7L9G; PDB: 7L9J; PDB: 7L9K; PDB: 7NPY; PDB: 7NPZ; PDB: 7NQ0; PDB: 7NQ1; PDB: 7NQ2; PDB: 7NQ3; PDB: 7NQ5; PDB: 7NQ7; PDB: 7NQ8; PDB: 7NQ9; PDB: 7NQI; PDB: 7NQJ; PDB: 7OE4; PDB: 7OE5; PDB: 7OE6; PDB: 7OE8; PDB: 7OE9; PDB: 7OEP; PDB: 7OER; PDB: 7OES; PDB: 7OET; PDB: 7OGY	HGNC:1103	BRD2_HUMAN	reviewed	ENSG00000204256	.	.	.	.	.
Mol01914	Protein	C-X-C motif chemokine ligand 12 (CXCL12)	CXCL12; SDF1; SDF1A; SDF1B	CXCL12	6387	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000343575.11,CXCL12-201,1928; ENST00000374426.6,CXCL12-202,470; ENST00000374429.6,CXCL12-203,3532; ENST00000395793.7,CXCL12-204,665; ENST00000395794.2,CXCL12-205,1052; ENST00000395795.5,CXCL12-206,404; ENST00000488591.1,CXCL12-207,596; ENST00000496375.1,CXCL12-208,803"	MNAKVVVVLVLVLTALCLSDGKPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNKRFKM	"chr10:44,370,165-44,386,493[-]"	"Chemoattractant active on T-lymphocytes and monocytes but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Stimulates the proliferation of bone marrow-derived B-cell progenitors in the presence of IL7 as well as growth of stromal cell-dependent pre-B-cells."	PDB: 1A15; PDB: 1QG7; PDB: 1SDF; PDB: 1VMC; PDB: 2J7Z; PDB: 2K01; PDB: 2K03; PDB: 2K04; PDB: 2K05; PDB: 2KEC; PDB: 2KED; PDB: 2KEE; PDB: 2KOL; PDB: 2N55; PDB: 2NWG; PDB: 2SDF; PDB: 3GV3; PDB: 3HP3; PDB: 4LMQ; PDB: 4UAI; PDB: 6SHR	HGNC:10672	SDF1_HUMAN	reviewed	ENSG00000107562	.	.	.	.	.
Mol01915	Protein	Synaptic vesicular amine transporter (VMAT2)	SLC18A2; SVMT; VMAT2	VMAT2	6571	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000497497.1,SLC18A2-201,4125; ENST00000644641.2,SLC18A2-202,3831"	MALSELALVRWLQESRRSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNATEIQTARPVHTASISDSFQSIFSYYDNSTMVTGNATRDLTLHQTATQHMVTNASAVPSDCPSEDKDLLNENVQVGLLFASKATVQLITNPFIGLLTNRIGYPIPIFAGFCIMFVSTIMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNVMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMIIVGVSILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDILFAPLCFFLRSPPAKEEKMAILMDHNCPIKTKMYTQNNIQSYPIGEDEESESD	"chr10:117,241,093-117,279,430[+]"	"Involved in the ATP-dependent vesicular transport of biogenic amine neurotransmitters. Pumps cytosolic monoamines including dopamine, norepinephrine, serotonin, and histamine into synaptic vesicles. Requisite for vesicular amine storage prior to secretion via exocytosis."	.	.	VMAT2_HUMAN	reviewed	ENSG00000165646	.	.	.	.	.
Mol01916	Protein	Sterol O-acyltransferase 1 (SOAT1)	SOAT1; ACACT; ACACT1; ACAT; ACAT1; SOAT; STAT	SOAT1	6646	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367619.8,SOAT1-201,6840; ENST00000426956.1,SOAT1-202,870; ENST00000539888.5,SOAT1-203,6794; ENST00000540564.5,SOAT1-204,6861"	MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAEELKPFFMKEVGSHFDDFVTNLIEKSASLDNGGCALTTFSVLEGEKNNHRAKDLRAPPEQGKIFIARRSLLDELLEVDHIRTIYHMFIALLILFILSTLVVDYIDEGRLVLEFSLLSYAFGKFPTVVWTWWIMFLSTFSVPYFLFQHWATGYSKSSHPLIRSLFHGFLFMIFQIGVLGFGPTYVVLAYTLPPASRFIIIFEQIRFVMKAHSFVRENVPRVLNSAKEKSSTVPIPTVNQYLYFLFAPTLIYRDSYPRNPTVRWGYVAMKFAQVFGCFFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLILFLTFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYAYKDFLWFFSKRFKSAAMLAVFAVSAVVHEYALAVCLSFFYPVLFVLFMFFGMAFNFIVNDSRKKPIWNVLMWTSLFLGNGVLLCFYSQEWYARQHCPLKNPTFLDYVRPRSWTCRYVF	"chr1:179,293,714-179,358,680[+]"	"Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions."	PDB: 6L47; PDB: 6L48; PDB: 6P2J; PDB: 6P2P; PDB: 6VUM	HGNC:11177	SOAT1_HUMAN	reviewed	ENSG00000057252	.	.	.	.	.
Mol01917	Protein	Squalene epoxidase (SQLE)	SQLE; ERG1	SQLE	6713	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000265896.10,SQLE-201,2962; ENST00000518604.1,SQLE-202,743; ENST00000518931.1,SQLE-203,554; ENST00000520493.1,SQLE-204,737; ENST00000521232.1,SQLE-205,711; ENST00000523430.5,SQLE-206,1879"	MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSGSQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH	"chr8:124,998,497-125,022,283[+]"	"Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis."	PDB: 6C6N; PDB: 6C6P; PDB: 6C6R	HGNC:11279	ERG1_HUMAN	reviewed	ENSG00000104549	.	.	.	.	.
Mol01918	Protein	Thromboxane A2 receptor (TBXA2R)	TBXA2R	TBXA2R	6915	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375190.10,TBXA2R-201,2642; ENST00000411851.3,TBXA2R-202,1494; ENST00000587717.1,TBXA2R-203,470; ENST00000589966.1,TBXA2R-204,1814"	MWPNGSSLGPCFRPTNITLEERRLIASPWFAASFCVVGLASNLLALSVLAGARQGGSHTRSSFLTFLCGLVLTDFLGLLVTGTIVVSQHAALFEWHAVDPGCRLCRFMGVVMIFFGLSPLLLGAAMASERYLGITRPFSRPAVASQRRAWATVGLVWAAALALGLLPLLGVGRYTVQYPGSWCFLTLGAESGDVAFGLLFSMLGGLSVGLSFLLNTVSVATLCHVYHGQEAAQQRPRDSEVEMMAQLLGIMVVASVCWLPLLVFIAQTVLRNPPAMSPAGQLSRTTEKELLIYLRVATWNQILDPWVYILFRRAVLRRLQPRLSTRPRSLSLQPQLTQRSGLQ	"chr19:3,594,507-3,606,875[-]"	"Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C."	.	HGNC:11608	TA2R_HUMAN	reviewed	ENSG00000006638	.	.	.	.	.
Mol01919	Protein	Tyrosine kinase with immunoglobulin like and EGF like domains 1 (TIE1)	TIE1; TIE	TIE1	7075	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000372476.8,TIE1-201,3893; ENST00000461061.1,TIE1-202,656; ENST00000471187.1,TIE1-203,625; ENST00000473014.1,TIE1-204,3087; ENST00000480269.1,TIE1-205,333; ENST00000485125.1,TIE1-206,557; ENST00000488437.1,TIE1-207,651; ENST00000492599.1,TIE1-208,391; ENST00000492874.1,TIE1-209,617; ENST00000538015.1,TIE1-210,1140"	MVWRVPPFLLPILFLASHVGAAVDLTLLANLRLTDPQRFFLTCVSGEAGAGRGSDAWGPPLLLEKDDRIVRTPPGPPLRLARNGSHQVTLRGFSKPSDLVGVFSCVGGAGARRTRVIYVHNSPGAHLLPDKVTHTVNKGDTAVLSARVHKEKQTDVIWKSNGSYFYTLDWHEAQDGRFLLQLPNVQPPSSGIYSATYLEASPLGSAFFRLIVRGCGAGRWGPGCTKECPGCLHGGVCHDHDGECVCPPGFTGTRCEQACREGRFGQSCQEQCPGISGCRGLTFCLPDPYGCSCGSGWRGSQCQEACAPGHFGADCRLQCQCQNGGTCDRFSGCVCPSGWHGVHCEKSDRIPQILNMASELEFNLETMPRINCAAAGNPFPVRGSIELRKPDGTVLLSTKAIVEPEKTTAEFEVPRLVLADSGFWECRVSTSGGQDSRRFKVNVKVPPVPLAAPRLLTKQSRQLVVSPLVSFSGDGPISTVRLHYRPQDSTMDWSTIVVDPSENVTLMNLRPKTGYSVRVQLSRPGEGGEGAWGPPTLMTTDCPEPLLQPWLEGWHVEGTDRLRVSWSLPLVPGPLVGDGFLLRLWDGTRGQERRENVSSPQARTALLTGLTPGTHYQLDVQLYHCTLLGPASPPAHVLLPPSGPPAPRHLHAQALSDSEIQLTWKHPEALPGPISKYVVEVQVAGGAGDPLWIDVDRPEETSTIIRGLNASTRYLFRMRASIQGLGDWSNTVEESTLGNGLQAEGPVQESRAAEEGLDQQLILAVVGSVSATCLTILAALLTLVCIRRSCLHRRRTFTYQSGSGEETILQFSSGTLTLTRRPKLQPEPLSYPVLEWEDITFEDLIGEGNFGQVIRAMIKKDGLKMNAAIKMLKEYASENDHRDFAGELEVLCKLGHHPNIINLLGACKNRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFAREHGTASTLSSRQLLRFASDAANGMQYLSEKQFIHRDLAARNVLVGENLASKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEQPRNCDDEVYELMRQCWRDRPYERPPFAQIALQLGRMLEARKAYVNMSLFENFTYAGIDATAEEA	"chr1:43,300,982-43,323,108[+]"	Transmembrane tyrosine-protein kinase that may modulate TEK/TIE2 activity and contribute to the regulation of angiogenesis.	PDB: 5N06	HGNC:11809	TIE1_HUMAN	reviewed	ENSG00000066056	.	.	.	.	.
Mol01920	Protein	TIMP metallopeptidase inhibitor 2 (TIMP2)	TIMP2	TIMP2	7077	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000262768.11,TIMP2-201,3652; ENST00000536189.6,TIMP2-202,3415; ENST00000585421.5,TIMP2-203,3345; ENST00000586057.5,TIMP2-204,3389; ENST00000592761.2,TIMP2-205,2433"	MGAAARTLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP	"chr17:78,852,977-78,925,387[-]"	"Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19."	PDB: 1BR9; PDB: 1GXD; PDB: 2TMP; PDB: 4ILW	HGNC:11821	TIMP2_HUMAN	reviewed	ENSG00000035862	.	.	.	.	.
Mol01921	Protein	NK2 homeobox 1 (NKX2-1)	NKX2-1; NKX2A; TITF1; TTF1	NKX2-1	7080	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000354822.7,NKX2-1-201,2190; ENST00000498187.6,NKX2-1-202,2338; ENST00000518149.5,NKX2-1-203,2583; ENST00000522719.4,NKX2-1-204,1962"	MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPPTAAMQQHAVGHHGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPAISRFMGPASGMNMSGMGGLGSLGDVSKNMAPLPSAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQQLQQDSGGGGGGGGTGCPQQQQAQQQSPRRVAVPVLVKDGKPCQAGAPAPGAASLQGHAQQQAQHQAQAAQAAAAAISVGSGGAGLGAHPGHQPGSAGQSPDLAHHAASPAALQGQVSSLSHLNSSGSDYGTMSCSTLLYGRTW	"chr14:36,516,392-36,521,149[-]"	"Transcription factor that binds and activates the promoter of thyroid specific genes such as thyroglobulin, thyroperoxidase, and thyrotropin receptor. Crucial in the maintenance of the thyroid differentiation phenotype. May play a role in lung development and surfactant homeostasis. Forms a regulatory loop with GRHL2 that coordinates lung epithelial cell morphogenesis and differentiation. Activates the transcription of GNRHR and plays a role in enhancing the circadian oscillation of its gene expression. Represses the transcription of the circadian transcriptional repressor NR1D1 (By similarity)."	.	HGNC:11825	NKX21_HUMAN	reviewed	ENSG00000136352	.	.	.	.	.
Mol01922	Protein	Toll like receptor 4 (TLR4)	TLR4	TLR4	7099	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000355622.8,TLR4-201,12677; ENST00000394487.5,TLR4-202,4048; ENST00000472304.2,TLR4-203,2955; ENST00000490685.1,TLR4-204,539"	MMSASRLAGTLIPAMAFLSCVRPESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTIIGVSVLSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI	"chr9:117,704,175-117,724,735[+]"	"Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (9237750835637022195,21393102). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+). Responses triggered by Ni(2+) require non-conserved histidines and are, therefore, species-specific. Both M.tuberculosis HSP70 (dnaK) and HSP65 (groEL-2) act via this protein to stimulate NF-kappa-B expression. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-). Stimulation of monocytes in vitro with M.tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via TLR2, but also partially via this receptor. Activated by the signaling pathway regulator NMI which acts as damage-associated molecular patterns (DAMPs) in response to cell injury or pathogen invasion, therefore promoting nuclear factor NF-kappa-B activation."	PDB: 2Z62; PDB: 2Z63; PDB: 2Z65; PDB: 2Z66; PDB: 3FXI; PDB: 3UL7; PDB: 3UL8; PDB: 3UL9; PDB: 3ULA; PDB: 4G8A; PDB: 5NAM; PDB: 5NAO	HGNC:11850	TLR4_HUMAN	reviewed	ENSG00000136869	.	.	.	.	.
Mol01923	Protein	Transmembrane 7 superfamily member 2 (TM7SF2)	TM7SF2; ANG1	TM7SF2	7108	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000279263.14,TM7SF2-201,1578; ENST00000345348.9,TM7SF2-202,1490; ENST00000524690.5,TM7SF2-203,843; ENST00000524986.5,TM7SF2-204,729; ENST00000525385.5,TM7SF2-205,1014; ENST00000526048.1,TM7SF2-206,1168; ENST00000526085.5,TM7SF2-207,570; ENST00000526809.5,TM7SF2-208,829; ENST00000527851.5,TM7SF2-209,976; ENST00000527968.5,TM7SF2-210,544; ENST00000528026.5,TM7SF2-211,582; ENST00000528802.1,TM7SF2-212,692; ENST00000529233.5,TM7SF2-213,756; ENST00000529292.5,TM7SF2-214,1305; ENST00000529414.5,TM7SF2-215,749; ENST00000529601.5,TM7SF2-216,1671; ENST00000530650.5,TM7SF2-217,2094; ENST00000530750.5,TM7SF2-218,365; ENST00000530892.5,TM7SF2-219,691; ENST00000531029.5,TM7SF2-220,530; ENST00000531321.5,TM7SF2-221,945; ENST00000532328.5,TM7SF2-222,560; ENST00000533646.1,TM7SF2-223,486; ENST00000533766.5,TM7SF2-224,1547; ENST00000534371.5,TM7SF2-225,913; ENST00000534667.1,TM7SF2-226,493"	MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSPRALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAGLPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELNPRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWHEEAVLTTMDITHDGFGFMLAFGDMAWVPFTYSLQAQFLLHHPQPLGLPMASVICLINATGYYIFRGANSQKNTFRKNPSDPRVAGLETISTATGRKLLVSGWWGMVRHPNYLGDLIMALAWSLPCGVSHLLPYFYLLYFTALLVHREARDERQCLQKYGLAWQEYCRRVPYRIMPYIY	"chr11:65,111,845-65,116,384[+]"	"Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis."	.	HGNC:11863	ERG24_HUMAN	reviewed	ENSG00000149809	.	.	.	.	.
Mol01924	Protein	Wnt family member 7B (WNT7B)	WNT7B	WNT7B	7477	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000339464.9,WNT7B-201,3948; ENST00000409496.7,WNT7B-202,2285; ENST00000410058.1,WNT7B-203,714; ENST00000410089.5,WNT7B-204,2202; ENST00000428540.1,WNT7B-205,521"	MHRNFRKWIFYVFLCFGVLYVKLGALSSVVALGANIICNKIPGLAPRQRAICQSRPDAIIVIGEGAQMGINECQYQFRFGRWNCSALGEKTVFGQELRVGSREAAFTYAITAAGVAHAVTAACSQGNLSNCGCDREKQGYYNQAEGWKWGGCSADVRYGIDFSRRFVDAREIKKNARRLMNLHNNEAGRKVLEDRMQLECKCHGVSGSCTTKTCWTTLPKFREVGHLLKEKYNAAVQVEVVRASRLRQPTFLRIKQLRSYQKPMETDLVYIEKSPNYCEEDAATGSVGTQGRLCNRTSPGADGCDTMCCGRGYNTHQYTKVWQCNCKFHWCCFVKCNTCSERTEVFTCK	"chr22:45,920,366-45,977,162[-]"	Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway. Required for normal fusion of the chorion and the allantois during placenta development. Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation.	.	HGNC:12787	WNT7B_HUMAN	reviewed	ENSG00000188064	.	.	.	.	.
Mol01925	Protein	Xanthine oxidase (XDH)	XDH; XDHA	XDH	7498	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000379416.4,XDH-201,5715; ENST00000476043.1,XDH-202,475; ENST00000491727.5,XDH-203,581"	MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRLQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCCMNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQASTLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFGAACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISDLNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSAFKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKEELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLDPTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDKVTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDLKKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKMLGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGRHPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGRLCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKLEGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAASVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAVGEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVTGVPENCKPWSVRV	"chr2:31,334,321-31,414,742[-]"	Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).	PDB: 2CKJ; PDB: 2E1Q	HGNC:12805	XDH_HUMAN	reviewed	ENSG00000158125	.	.	.	.	.
Mol01926	Protein	Paired box 8 (PAX8)	PAX8	PAX8	7849	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263334.9,PAX8-201,4152; ENST00000263335.11,PAX8-202,3735; ENST00000348715.9,PAX8-203,3966; ENST00000397647.7,PAX8-204,3633; ENST00000429538.8,PAX8-205,4055; ENST00000465084.1,PAX8-206,656; ENST00000467778.5,PAX8-207,1414; ENST00000468980.3,PAX8-208,525; ENST00000480684.1,PAX8-209,527; ENST00000485840.1,PAX8-210,2757; ENST00000497038.6,PAX8-211,816; ENST00000554352.1,PAX8-212,567; ENST00000554830.2,PAX8-213,556; ENST00000681162.1,PAX8-214,4036"	MPHNSIRSGHGGLNQLGGAFVNGRPLPEVVRQRIVDLAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIRPGVIGGSKPKVATPKVVEKIGDYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIRTKVQQPFNLPMDSCVATKSLSPGHTLIPSSAVTPPESPQSDSLGSTYSINGLLGIAQPGSDKRKMDDSDQDSCRLSIDSQSSSSGPRKHLRTDAFSQHHLEPLECPFERQHYPEAYASPSHTKGEQGLYPLPLLNSTLDDGKATLTPSNTPLGRNLSTHQTYPVVADPHSPFAIKQETPEVSSSSSTPSSLSSSAFLDLQQVGSGVPPFNAFPHAASVYGQFTGQALLSGREMVGPTLPGYPPHIPTSGQGSYASSAIAGMVAGSEYSGNAYGHTPYSSYSEAWRFPNSSLLSSPYYYSSTSRPSAPPTTATAFDHL	"chr2:113,215,997-113,278,921[-]"	"Transcription factor for the thyroid-specific expression of the genes exclusively expressed in the thyroid cell type, maintaining the functional differentiation of such cells."	PDB: 2K27	HGNC:8622	PAX8_HUMAN	reviewed	ENSG00000125618	.	.	.	.	.
Mol01927	Protein	Frizzled class receptor 7 (FZD7)	FZD7	FZD7	8324	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFSDDGYRTVAQGTKKEGCTILFMVLYFFGMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQVDGDLLSGVCYVGLSSVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVLACYFYEQAFREHWERTWLLQTCKSYAVPCPPGHFPPMSPDFTVFMIKYLMTMIVGITTGFWIWSGKTLQSWRRFYHRLSHSSKGETAV	.	"Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by WNT8 induces expression of beta-catenin target genes. Following ligand activation, binds to CCDC88C/DAPLE which displaces DVL1 from FZD7 and leads to inhibition of canonical Wnt signaling, activation of G-proteins by CCDC88C and triggering of non-canonical Wnt responses. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues."	PDB: 4Z33; PDB: 5T44; PDB: 5URV; PDB: 5WBS; PDB: 6NE2; PDB: 6NE4; PDB: 6O3A; PDB: 6O3B; PDB: 7EVW	HGNC:4045	FZD7_HUMAN	reviewed	.	.	.	.	.	.
Mol01928	Protein	O-linked N-acetylglucosamine (GlcNAc) transferase (OGT)	OGT	OGT	8473	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000373701.7,OGT-201,3310; ENST00000373719.8,OGT-202,5435; ENST00000444774.3,OGT-203,556; ENST00000455587.3,OGT-204,632; ENST00000459760.1,OGT-205,541; ENST00000462638.1,OGT-206,400; ENST00000466181.1,OGT-207,421; ENST00000472270.1,OGT-208,689; ENST00000474633.1,OGT-209,564; ENST00000488174.5,OGT-210,7243; ENST00000498566.3,OGT-211,601"	MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA	"chrX:71,533,104-71,575,892[+]"	"Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, ATG4B, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex. Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity. Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1. Glycosylates HOXA1. O-glycosylates FNIP1. Promotes autophagy by mediating O-glycosylation of ATG4B."	PDB: 1W3B; PDB: 3PE3; PDB: 3PE4; PDB: 3TAX; PDB: 4AY5; PDB: 4AY6; PDB: 4CDR; PDB: 4GYW; PDB: 4GYY; PDB: 4GZ3; PDB: 4GZ5; PDB: 4GZ6; PDB: 4N39; PDB: 4N3A; PDB: 4N3B; PDB: 4N3C; PDB: 4XI9; PDB: 4XIF; PDB: 5BNW; PDB: 5C1D; PDB: 5HGV; PDB: 5LVV; PDB: 5LWV; PDB: 5NPR; PDB: 5NPS; PDB: 5VIE; PDB: 5VIF; PDB: 6E37; PDB: 6EOU; PDB: 6IBO; PDB: 6MA1; PDB: 6MA2; PDB: 6MA3; PDB: 6MA4; PDB: 6MA5; PDB: 6Q4M; PDB: 6TKA; PDB: 7NTF	HGNC:8127	OGT1_HUMAN	reviewed	ENSG00000147162	.	.	.	.	.
Mol01929	Protein	Transmembrane protein (TMEFF1)	TMEFF1; C9orf2	TMEFF1	8577	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000374879.5,TMEFF1-201,2575"	MGAAAAEAPLRLPAAPPLAFCCYTSVLLLFAFSLPGSRASNQPPGGGGGSGGDCPGGKGKSINCSELNVRESDVRVCDESSCKYGGVCKEDGDGLKCACQFQCHTNYIPVCGSNGDTYQNECFLRRAACKHQKEITVIARGPCYSDNGSGSGEGEEEGSGAEVHRKHSKCGPCKYKAECDEDAENVGCVCNIDCSGYSFNPVCASDGSSYNNPCFVREASCIKQEQIDIRHLGHCTDTDDTSLLGKKDDGLQYRPDVKDASDQREDVYIGNHMPCPENLNGYCIHGKCEFIYSTQKASCRCESGYTGQHCEKTDFSILYVVPSRQKLTHVLIAAIIGAVQIAIIVAIVMCITRKCPKNNRGRRQKQNLGHFTSDTSSRMV	"chr9:100,473,149-100,577,636[+]"	May inhibit NODAL and BMP signaling during neural patterning (By similarity). May be a tumor suppressor in brain cancers.	.	HGNC:11866	TEFF1_HUMAN	reviewed	ENSG00000241697	.	.	.	.	.
Mol01930	Protein	TNF superfamily member 11 (TNFSF11)	TNFSF11; OPGL; RANKL; TRANCE	TNFSF11	8600	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000239849.8,TNFSF11-201,911; ENST00000358545.6,TNFSF11-202,1520; ENST00000398795.7,TNFSF11-203,2201; ENST00000405262.6,TNFSF11-204,2135; ENST00000544862.5,TNFSF11-205,818"	MRRASRDYTKYLRGSEEMGGGPGAPHEGPLHAPPPPAPHQPPAASRSMFVALLGLGLGQVVCSVALFFYFRAQMDPNRISEDGTHCIYRILRLHENADFQDTTLESQDTKLIPDSCRRIKQAFQGAVQKELQHIVGSQHIRAEKAMVDGSWLDLAKRSKLEAQPFAHLTINATDIPSGSHKVSLSSWYHDRGWAKISNMTFSNGKLIVNQDGFYYLYANICFRHHETSGDLATEYLQLMVYVTKTSIKIPSSHTLMKGGSTKYWSGNSEFHFYSINVGGFFKLRSGEEISIEVSNPSLLDPDQDATYFGAFKVRDID	"chr13:42,562,736-42,608,013[+]"	"Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy. Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation."	PDB: 3URF; PDB: 5BNQ	HGNC:11926	TNF11_HUMAN	reviewed	ENSG00000120659	.	.	.	.	.
Mol01931	Protein	Sphingosine kinase 1 (SPHK1)	SPHK1; SK1; SPHK; SPK	SPHK1	8877	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000323374.8,SPHK1-201,2138; ENST00000392496.3,SPHK1-202,1779; ENST00000545180.5,SPHK1-203,2238; ENST00000587167.1,SPHK1-204,456; ENST00000588682.5,SPHK1-205,858; ENST00000590379.5,SPHK1-206,588; ENST00000590959.5,SPHK1-207,1851; ENST00000591651.5,SPHK1-208,541; ENST00000591762.1,SPHK1-209,2502; ENST00000592299.6,SPHK1-210,1816"	MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMVSEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL	"chr17:76,376,584-76,387,860[+]"	"Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol. In contrast to proapoptotic SPHK2, has a negative effect on intracellular ceramide levels, enhances cell growth and inhibits apoptosis. Involved in the regulation of inflammatory response and neuroinflammation. Via the product sphingosine 1-phosphate, stimulates TRAF2 E3 ubiquitin ligase activity, and promotes activation of NF-kappa-B in response to TNF signaling leading to IL17 secretion. In response to TNF and in parallel to NF-kappa-B activation, negatively regulates RANTES induction through p38 MAPK signaling pathway. Involved in endocytic membrane trafficking induced by sphingosine, recruited to dilate endosomes, also plays a role on later stages of endosomal maturation and membrane fusion independently of its kinase activity. In Purkinje cells, seems to be also involved in the regulation of autophagosome-lysosome fusion upon VEGFA."	PDB: 3VZB; PDB: 3VZC; PDB: 3VZD; PDB: 4L02; PDB: 4V24	HGNC:11240	SPHK1_HUMAN	reviewed	ENSG00000176170	.	.	.	.	.
Mol01932	Protein	Sphingosine-1-phosphate lyase 1 (SGPL1)	SGPL1; KIAA1252	SGPL1	8879	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000299297.8,SGPL1-201,658; ENST00000373202.8,SGPL1-202,5778; ENST00000409118.2,SGPL1-203,462; ENST00000486993.1,SGPL1-204,537; ENST00000611290.4,SGPL1-205,670; ENST00000613857.4,SGPL1-206,541; ENST00000618021.1,SGPL1-207,562; ENST00000620724.4,SGPL1-208,868"	MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFPPSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAELSSVFLDSLYSTDTVTQGSQMNGSPKPH	"chr10:70,815,948-70,881,184[+]"	"Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP. Seems to play a role in establishing neuronal contact sites and axonal maintenance."	PDB: 4Q6R	HGNC:10817	SGPL1_HUMAN	reviewed	ENSG00000166224	.	.	.	.	.
Mol01933	Protein	ATPase H+ transporting V0 subunit d1 (ATP6V0D1)	ATP6V0D1; ATP6D; VPATPD	ATP6V0D1	9114	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000290949.8,ATP6V0D1-201,1636; ENST00000426604.7,ATP6V0D1-202,1257; ENST00000540149.5,ATP6V0D1-203,1262; ENST00000561658.5,ATP6V0D1-204,556; ENST00000561852.5,ATP6V0D1-205,768; ENST00000563064.5,ATP6V0D1-206,1048; ENST00000563305.1,ATP6V0D1-207,1656; ENST00000564191.5,ATP6V0D1-208,853; ENST00000564615.5,ATP6V0D1-209,680; ENST00000564788.1,ATP6V0D1-210,582; ENST00000565835.5,ATP6V0D1-211,905; ENST00000566322.6,ATP6V0D1-212,821; ENST00000567170.5,ATP6V0D1-213,590; ENST00000567694.5,ATP6V0D1-214,582; ENST00000568101.5,ATP6V0D1-215,552; ENST00000568298.1,ATP6V0D1-216,3274; ENST00000568620.5,ATP6V0D1-217,3390"	MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDRLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF	"chr16:67,438,014-67,481,181[-]"	"Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. May play a role in coupling of proton transport and ATP hydrolysis. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium."	PDB: 6WLW; PDB: 6WM2; PDB: 6WM3; PDB: 6WM4	HGNC:13724	VA0D1_HUMAN	reviewed	ENSG00000159720	.	.	.	.	.
Mol01934	Protein	Solute carrier family 28 member 1 (SLC28A1)	SLC28A1; CNT1	SLC28A1	9154	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000286749.3,SLC28A1-201,2636; ENST00000338602.6,SLC28A1-202,1360; ENST00000394573.6,SLC28A1-203,2770; ENST00000538177.5,SLC28A1-204,2155"	MENDPSRRRESISLTPVAKGLENMGADFLESLEEGQLPRSDLSPAEIRSSWSEAAPKPFSRWRNLQPALRARSFCREHMQLFRWIGTGLLCTGLSAFLLVACLLDFQRALALFVLTCVVLTFLGHRLLKRLLGPKLRRFLKPQGHPRLLLWFKRGLALAAFLGLVLWLSLDTSQRPEQLVSFAGICVFVALLFACSKHHCAVSWRAVSWGLGLQFVLGLLVIRTEPGFIAFEWLGEQIRIFLSYTKAGSSFVFGEALVKDVFAFQVLPIIVFFSCVISVLYHVGLMQWVILKIAWLMQVTMGTTATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEVHVVMTGGYATIAGSLLGAYISFGIDATSLIAASVMAAPCALALSKLVYPEVEESKFRREEGVKLTYGDAQNLIEAASTGAAISVKVVANIAANLIAFLAVLDFINAALSWLGDMVDIQGLSFQLICSYILRPVAFLMGVAWEDCPVVAELLGIKLFLNEFVAYQDLSKYKQRRLAGAEEWVGDRKQWISVRAEVLTTFALCGFANFSSIGIMLGGLTSMVPQRKSDFSQIVLRALFTGACVSLVNACMAGILYMPRGAEVDCMSLLNTTLSSSSFEIYQCCREAFQSVNPEFSPEALDNCCRFYNHTICAQ	"chr15:84,884,654-84,945,798[+]"	"Sodium-dependent and pyrimidine-selective transporter. Exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit) (selective for pyrimidine nucleosides and adenosine). Transports uridine, cytidine, thymidine, and nucleoside-derived drugs. Transports the antiviral pyrimidine nucleoside analogs 3'-azido-3'-deoxythymidine (AZT) and 2',3'-dideoxycytidine (ddC). It may be involved in the intestinal absorption and renal handling of pyrimidine nucleoside analogs used to treat acquired immunodeficiency syndrome (AIDS). It has the following selective inhibition: adenosine, thymidine, cytidine, uridine >> guanosine, inosine."	.	HGNC:11001	S28A1_HUMAN	reviewed	ENSG00000156222	.	.	.	.	.
Mol01935	Protein	Diacylglycerol kinase iota (DGKI)	DGKI	DGKI	9162	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000288490.9,DGKI-201,3895; ENST00000424189.6,DGKI-202,4163; ENST00000446122.5,DGKI-203,4070; ENST00000453654.6,DGKI-204,12928; ENST00000460662.2,DGKI-205,1127; ENST00000470895.5,DGKI-206,922; ENST00000475388.1,DGKI-207,650; ENST00000477835.5,DGKI-208,582; ENST00000483619.1,DGKI-209,551; ENST00000486153.1,DGKI-210,628; ENST00000494390.5,DGKI-211,3223; ENST00000497321.5,DGKI-212,632; ENST00000614521.2,DGKI-213,13469"	MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAGEEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEEKLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENKGRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALELYRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQELKFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGERLHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSVPDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDCDLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLHFVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGMIAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHCSLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGASLRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV	"chr7:137,381,037-137,847,092[-]"	"Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Has probably no preference for any of the diacylglycerols in terms of the acyl chain composition, especially for the acyl chain at the sn-2 position. By controlling the diacylglycerol/DAG-mediated activation of RASGRP3, negatively regulates the Rap1 signaling pathway. May play a role in presynaptic diacylglycerol/DAG signaling and control neurotransmitter release during metabotropic glutamate receptor-dependent long-term depression."	.	HGNC:2855	DGKI_HUMAN	reviewed	ENSG00000157680	.	.	.	.	.
Mol01936	Protein	Zinc finger FYVE-type containing 9 (ZFYVE9)	ZFYVE9; MADHIP; SARA; SMADIP	ZFYVE9	9372	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000287727.8,ZFYVE9-201,5148; ENST00000357206.6,ZFYVE9-202,4567; ENST00000361625.5,ZFYVE9-203,2625; ENST00000371591.2,ZFYVE9-204,7243; ENST00000469134.1,ZFYVE9-205,859"	MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV	"chr1:52,142,089-52,348,671[+]"	Early endosomal protein that functions to recruit SMAD2/SMAD3 to intracellular membranes and to the TGF-beta receptor. Plays a significant role in TGF-mediated signaling by regulating the subcellular location of SMAD2 and SMAD3 and modulating the transcriptional activity of the SMAD3/SMAD4 complex. Possibly associated with TGF-beta receptor internalization.	PDB: 1DEV; PDB: 1MK2; PDB: 4BKW; PDB: 5MJY	HGNC:6775	ZFYV9_HUMAN	reviewed	ENSG00000157077	.	.	.	.	.
Mol01937	Protein	Geranylgeranyl diphosphate synthase 1 (GGPS1)	GGPS1	GGPS1	9453	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000282841.9,GGPS1-201,2895; ENST00000358966.6,GGPS1-202,2740; ENST00000391855.2,GGPS1-203,1407; ENST00000471812.5,GGPS1-204,850; ENST00000482013.1,GGPS1-205,470; ENST00000488594.5,GGPS1-206,1396; ENST00000489692.1,GGPS1-207,506; ENST00000497327.1,GGPS1-208,868"	MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE	"chr1:235,327,350-235,344,532[+]"	"Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins."	PDB: 2Q80; PDB: 6C56; PDB: 6C57; PDB: 6G31; PDB: 6G32; PDB: 6R4V	HGNC:4249	GGPPS_HUMAN	reviewed	ENSG00000152904	.	.	.	.	.
Mol01938	Protein	Serine palmitoyltransferase long chain base subunit 2 (SPTLC2)	SPTLC2; KIAA0526; LCB2	SPTLC2	9517	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000216484.7,SPTLC2-201,8034; ENST00000554365.1,SPTLC2-202,604; ENST00000554901.1,SPTLC2-203,1518; ENST00000556607.1,SPTLC2-204,460; ENST00000557566.1,SPTLC2-205,510; ENST00000686627.1,SPTLC2-206,7002; ENST00000686959.1,SPTLC2-207,2887; ENST00000687688.1,SPTLC2-208,7733; ENST00000691887.1,SPTLC2-209,933; ENST00000692906.1,SPTLC2-210,7702"	MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFNEAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRHRLVPLLDRPFDETTYEETED	"chr14:77,505,997-77,616,637[-]"	"Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate. Plays an important role in de novo sphyngolipid biosynthesis which is crucial for adipogenesis (By similarity)."	PDB: 6M4N; PDB: 6M4O; PDB: 7CQI; PDB: 7CQK; PDB: 7K0I; PDB: 7K0J; PDB: 7K0K; PDB: 7K0L; PDB: 7K0M; PDB: 7K0N; PDB: 7K0O; PDB: 7K0P; PDB: 7K0Q	HGNC:11278	SPTC2_HUMAN	reviewed	ENSG00000100596	.	.	.	.	.
Mol01939	Protein	Scaffold attachment factor B2 (SAFB2)	SAFB2; KIAA0138	SAFB2	9667	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000252542.9,SAFB2-201,3167; ENST00000585449.1,SAFB2-202,443; ENST00000587802.5,SAFB2-203,583; ENST00000589925.1,SAFB2-204,506; ENST00000590000.1,SAFB2-205,633; ENST00000590262.1,SAFB2-206,564; ENST00000591101.5,SAFB2-207,551; ENST00000591120.1,SAFB2-208,1298; ENST00000591123.5,SAFB2-209,836; ENST00000591310.1,SAFB2-210,722; ENST00000592599.5,SAFB2-211,2260"	MAETLPGSGDSGPGTASLGPGVAETGTRRLSELRVIDLRAELKKRNLDTGGNKSVLMERLKKAVKEEGQDPDEIGIELEATSKKSAKRCVKGLKMEEEGTEDNGLEDDSRDGQEDMEASLENLQNMGMMDMSVLDETEVANSSAPDFGEDGTDGLLDSFCDSKEYVAAQLRQLPAQPPEHAVDGEGFKNTLETSSLNFKVTPDIEESLLEPENEKILDILGETCKSEPVKEESSELEQPFAQDTSSVGPDRKLAEEEDLFDSAHPEEGDLDLASESTAHAQSSKADSLLAVVKREPAEQPGDGERTDCEPVGLEPAVEQSSAASELAEASSEELAEAPTEAPSPEARDSKEDGRKFDFDACNEVPPAPKESSTSEGADQKMSSFKEEKDIKPIIKDEKGRVGSGSGRNLWVSGLSSTTRATDLKNLFSKYGKVVGAKVVTNARSPGARCYGFVTMSTSDEATKCISHLHRTELHGRMISVEKAKNEPAGKKLSDRKECEVKKEKLSSVDRHHSVEIKIEKTVIKKEEKIEKKEEKKPEDIKKEEKDQDELKPGPTNRSRVTKSGSRGMERTVVMDKSKGEPVISVKTTSRSKERSSKSQDRKSESKEKRDILSFDKIKEQRERERQRQREREIRETERRREREQREREQRLEAFHERKEKARLQRERLQLECQRQRLERERMERERLERERMRVERERRKEQERIHREREELRRQQEQLRYEQERRPGRRPYDLDRRDDAYWPEGKRVAMEDRYRADFPRPDHRFHDFDHRDRGQYQDHAIDRREGSRPMMGDHRDGQHYGDDRHGHGGPPERHGRDSRDGWGGYGSDKRLSEGRGLPPPPRGGRDWGEHNQRLEEHQARAWQGAMDAGAASREHARWQGGERGLSGPSGPGHMASRGGVAGRGGFAQGGHSQGHVVPGGGLEGGGVASQDRGSRVPHPHPHPPPYPHFTRRY	"chr19:5,586,999-5,624,046[-]"	Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.	.	HGNC:21605	SAFB2_HUMAN	reviewed	ENSG00000130254	.	.	.	.	.
Mol01940	Protein	G3BP stress granule assembly factor 1 (G3BP1)	G3BP1; G3BP	G3BP1	10146	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000356245.8,G3BP1-201,10227; ENST00000394123.7,G3BP1-202,10240; ENST00000507878.7,G3BP1-203,581; ENST00000517947.5,G3BP1-204,558; ENST00000518726.5,G3BP1-205,869; ENST00000519832.1,G3BP1-206,1173; ENST00000520006.2,G3BP1-207,229; ENST00000520177.6,G3BP1-208,2654; ENST00000520578.6,G3BP1-209,529; ENST00000522367.6,G3BP1-210,782; ENST00000522666.1,G3BP1-211,783; ENST00000522761.6,G3BP1-212,1691; ENST00000523519.5,G3BP1-213,535; ENST00000627077.2,G3BP1-214,173; ENST00000676507.1,G3BP1-215,386; ENST00000676590.1,G3BP1-216,345; ENST00000676634.1,G3BP1-217,1000; ENST00000676644.1,G3BP1-218,10372; ENST00000676715.1,G3BP1-219,8602; ENST00000676734.1,G3BP1-220,590; ENST00000676813.1,G3BP1-221,1046; ENST00000676827.1,G3BP1-222,1768; ENST00000676878.1,G3BP1-223,593; ENST00000676894.1,G3BP1-224,1207; ENST00000676899.1,G3BP1-225,1054; ENST00000676911.1,G3BP1-226,998; ENST00000676978.1,G3BP1-227,9997; ENST00000677105.1,G3BP1-228,1532; ENST00000677126.1,G3BP1-229,125; ENST00000677146.1,G3BP1-230,503; ENST00000677211.1,G3BP1-231,520; ENST00000677241.1,G3BP1-232,378; ENST00000677252.1,G3BP1-233,148; ENST00000677284.1,G3BP1-234,299; ENST00000677323.1,G3BP1-235,10540; ENST00000677369.1,G3BP1-236,284; ENST00000677381.1,G3BP1-237,10136; ENST00000677408.1,G3BP1-238,194; ENST00000677433.1,G3BP1-239,583; ENST00000677493.1,G3BP1-240,10243; ENST00000677602.1,G3BP1-241,3216; ENST00000677608.1,G3BP1-242,222; ENST00000677658.1,G3BP1-243,390; ENST00000677687.1,G3BP1-244,222; ENST00000677757.1,G3BP1-245,11945; ENST00000677854.1,G3BP1-246,341; ENST00000677909.1,G3BP1-247,177; ENST00000677923.1,G3BP1-248,10583; ENST00000678027.1,G3BP1-249,125; ENST00000678070.1,G3BP1-250,1565; ENST00000678086.1,G3BP1-251,114; ENST00000678101.1,G3BP1-252,1794; ENST00000678153.1,G3BP1-253,125; ENST00000678194.1,G3BP1-254,311; ENST00000678209.1,G3BP1-255,125; ENST00000678295.1,G3BP1-256,1233; ENST00000678369.1,G3BP1-257,3086; ENST00000678372.1,G3BP1-258,448; ENST00000678500.1,G3BP1-259,531; ENST00000678564.1,G3BP1-260,1737; ENST00000678612.1,G3BP1-261,411; ENST00000678646.1,G3BP1-262,10257; ENST00000678657.1,G3BP1-263,1187; ENST00000678726.1,G3BP1-264,339; ENST00000678750.1,G3BP1-265,1898; ENST00000678825.1,G3BP1-266,436; ENST00000678854.1,G3BP1-267,1326; ENST00000678904.1,G3BP1-268,10474; ENST00000678910.1,G3BP1-269,1737; ENST00000678925.1,G3BP1-270,10011; ENST00000678964.1,G3BP1-271,10622; ENST00000678976.1,G3BP1-272,206; ENST00000679004.1,G3BP1-273,354; ENST00000679057.1,G3BP1-274,192; ENST00000679135.1,G3BP1-275,329; ENST00000679193.1,G3BP1-276,2304; ENST00000679207.1,G3BP1-277,782; ENST00000679289.1,G3BP1-278,10323"	MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ	"chr5:151,771,045-151,812,911[+]"	"ATP- and magnesium-dependent helicase that plays an essential role in innate immunity. Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS. Enhances also DDX58-induced type I interferon production probably by helping DDX58 at sensing pathogenic RNA. In addition, plays an essential role in stress granule formation. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR."	PDB: 3Q90; PDB: 4FCJ; PDB: 4FCM; PDB: 4IIA; PDB: 5FW5; PDB: 6TA7	HGNC:30292	G3BP1_HUMAN	reviewed	ENSG00000145907	.	.	.	.	.
Mol01941	Protein	"NPR2 like, GATOR1 complex subunit (NPRL2)"	NPRL2; TUSC4	NPRL2	10641	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000232501.8,NPRL2-201,1542; ENST00000418825.5,NPRL2-202,1030; ENST00000429366.5,NPRL2-203,1364; ENST00000433381.5,NPRL2-204,1573; ENST00000433999.5,NPRL2-205,1006; ENST00000448302.1,NPRL2-206,939; ENST00000451194.5,NPRL2-207,1747; ENST00000461020.5,NPRL2-208,2229; ENST00000467294.1,NPRL2-209,3113; ENST00000469839.1,NPRL2-210,971; ENST00000476064.5,NPRL2-211,1643; ENST00000479512.5,NPRL2-212,1905; ENST00000480296.5,NPRL2-213,2512; ENST00000487632.5,NPRL2-214,2015; ENST00000492805.1,NPRL2-215,786; ENST00000493465.5,NPRL2-216,462; ENST00000493907.1,NPRL2-217,835; ENST00000667046.1,NPRL2-218,1371; ENST00000667631.1,NPRL2-219,2005; ENST00000671487.1,NPRL2-220,1754"	MGSGCRIECIFFSEFHPTLGPKITYQVPEDFISRELFDTVQVYIITKPELQNKLITVTAMEKKLIGCPVCIEHKKYSRNALLFNLGFVCDAQAKTCALEPIVKKLAGYLTTLELESSFVSMEESKQKLVPIMTILLEELNASGRCTLPIDESNTIHLKVIEQRPDPPVAQEYDVPVFTKDKEDFFNSQWDLTTQQILPYIDGFRHIQKISAEADVELNLVRIAIQNLLYYGVVTLVSILQYSNVYCPTPKVQDLVDDKSLQEACLSYVTKQGHKRASLRDVFQLYCSLSPGTTVRDLIGRHPQQLQHVDERKLIQFGLMKNLIRRLQKYPVRVTREEQSHPARLYTGCHSYDEICCKTGMSYHELDERLENDPNIIICWK	"chr3:50,347,330-50,350,826[-]"	"As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway."	PDB: 6CES; PDB: 6CET	HGNC:24969	NPRL2_HUMAN	reviewed	ENSG00000114388	.	.	.	.	.
Mol01942	Protein	Phosphomevalonate kinase (PMVK)	PMVK; PMKI	PMVK	10654	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368467.4,PMVK-201,1002"	MAPLGGAPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQRLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFREAYGAVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQLENLIEFIRSRL	"chr1:154,924,740-154,936,719[-]"	"Catalyzes the reversible ATP-dependent phosphorylation of mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key step in the mevalonic acid mediated biosynthesis of isopentenyl diphosphate and other polyisoprenoid metabolites."	PDB: 3CH4	HGNC:9141	PMVK_HUMAN	reviewed	ENSG00000163344	.	.	.	.	.
Mol01943	Protein	EBP cholestenol delta-isomerase (EBP)	EBP	EBP	10682	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000276096.10,EBP-201,904; ENST00000414061.1,EBP-202,609; ENST00000446158.5,EBP-203,714; ENST00000466461.1,EBP-204,694; ENST00000495186.6,EBP-205,1125; ENST00000498425.1,EBP-206,796"	MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN	"chrX:48,521,799-48,528,716[+]"	Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.	PDB: 6OHT; PDB: 6OHU	HGNC:3133	EBP_HUMAN	reviewed	ENSG00000147155	.	.	.	.	.
Mol01944	Protein	O-GlcNAcase (OGA)	OGA; HEXC; KIAA0679; MEA5; MGEA5	OGA	10724	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000357797.9,OGA-201,3263; ENST00000361464.8,OGA-202,5174; ENST00000370094.7,OGA-203,3314; ENST00000429860.1,OGA-204,769; ENST00000439817.5,OGA-205,5043; ENST00000461645.1,OGA-206,743; ENST00000462994.1,OGA-207,1088; ENST00000479811.5,OGA-208,695; ENST00000482611.5,OGA-209,1664; ENST00000492204.1,OGA-210,519; ENST00000494347.5,OGA-211,712"	MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL	"chr10:101,784,443-101,818,465[-]"	[Isoform 1]: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro). Does not bind acetyl-CoA and does not have histone acetyltransferase activity.	PDB: 2YDQ; PDB: 5M7R; PDB: 5M7S; PDB: 5M7T; PDB: 5M7U; PDB: 5TKE; PDB: 5UHK; PDB: 5UHL; PDB: 5UHO; PDB: 5UHP; PDB: 5UN8; PDB: 5UN9; PDB: 5VVO; PDB: 5VVT; PDB: 5VVU; PDB: 5VVV; PDB: 5VVX; PDB: 6HKI; PDB: 6PM9	HGNC:7056	OGA_HUMAN	reviewed	ENSG00000198408	.	.	.	.	.
Mol01945	Protein	Bile acyl-CoA synthetase (S27A5)	SLC27A5; ACSB; ACSVL6; FACVL3; FATP5	S27A5	10998	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000263093.7,SLC27A5-201,2292; ENST00000593745.1,SLC27A5-202,5032; ENST00000594683.1,SLC27A5-203,564; ENST00000594786.1,SLC27A5-204,643; ENST00000595851.5,SLC27A5-205,2003; ENST00000599700.1,SLC27A5-206,474; ENST00000601355.1,SLC27A5-207,1987; ENST00000601997.1,SLC27A5-208,575"	MGVRQQLALLLLLLLLLWGLGQPVWPVAVALTLRWLLGDPTCCVLLGLAMLARPWLGPWVPHGLSLAAAALALTLLPARLPPGLRWLPADVIFLAKILHLGLKIRGCLSRQPPDTFVDAFERRARAQPGRALLVWTGPGAGSVTFGELDARACQAAWALKAELGDPASLCAGEPTALLVLASQAVPALCMWLGLAKLGCPTAWINPHGRGMPLAHSVLSSGARVLVVDPDLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL	"chr19:58,479,512-58,512,413[-]"	"Acyl-CoA synthetase that catalyzes the activation of bile acids via formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine. Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates. Also exhibits acyl CoA synthetase activity that activates very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA. In vitro, also activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Exhibits long-chain fatty acids (LCFA) transport activity. Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids."	.	.	S27A5_HUMAN	reviewed	ENSG00000083807	.	.	.	.	.
Mol01946	Protein	Very long-chain acyl-CoA synthetase (S27A2)	SLC27A2; ACSVL1; FACVL1; FATP2; VLACS	S27A2	11001	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000267842.10,SLC27A2-201,2384; ENST00000380902.8,SLC27A2-202,2181; ENST00000544960.1,SLC27A2-203,2025; ENST00000559938.1,SLC27A2-204,353"	MLSAIYTVLAGLLFLPLLVNLCCPYFFQDIGYFLKVAAVGRRVRSYGKRRPARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAKMYVPMTEDIYNAISAKTLKL	"chr15:50,182,196-50,236,385[+]"	"Acyl CoA synthetase that activates long-chain and very long-chain fatty acids (VLCFAs) by catalyzing the formation of fatty acyl-CoA. Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid. Does not activate C24 bile acids, cholate and chenodeoxycholate. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Exhibits long-chain fatty acids (LCFA) transport activity and plays an important role in hepatic fatty acid uptake."	.	.	S27A2_HUMAN	reviewed	ENSG00000140284	.	.	.	.	.
Mol01947	Protein	ADP/ATP translocase 2 (ADT2)	Slc25a5; Aac2; Ant2	ADT2	11740	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000016463.4,Slc25a5-201,1240; ENSMUST00000126608.2,Slc25a5-202,989; ENSMUST00000156672.2,Slc25a5-203,765"	MTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQITADKQYKGIIDCVVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKRTQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKAGAEREFKGLGDCLVKIYKSDGIKGLYQGFNVSVQGIIIYRAAYFGIYDTAKGMLPDPKNTHIFISWMIAQSVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGSKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT	"chrX:36,059,304-36,062,460[+]"	"ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane. In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity. Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis. Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A5/ANT2 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it. Probably mediates mitochondrial uncoupling in tissues that do not express UCP1. Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death. It is however unclear if SLC25A5/ANT2 constitutes a pore-forming component of mPTP or regulates it. Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation."	.	.	ADT2_MOUSE	reviewed	ENSMUSG00000016319	.	.	.	.	.
Mol01948	Protein	Dishevelled binding antagonist of beta catenin 1 (DACT1)	Ctnnb1; Catnb	DACT1	12387	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000007130.15,Ctnnb1-201,3623; ENSMUST00000126633.2,Ctnnb1-202,494; ENSMUST00000130466.8,Ctnnb1-203,364; ENSMUST00000130845.9,Ctnnb1-204,795; ENSMUST00000133689.2,Ctnnb1-205,886; ENSMUST00000139138.2,Ctnnb1-206,577; ENSMUST00000145093.2,Ctnnb1-207,714; ENSMUST00000154356.8,Ctnnb1-208,3548; ENSMUST00000154687.8,Ctnnb1-209,2359; ENSMUST00000156911.2,Ctnnb1-210,773; ENSMUST00000163844.8,Ctnnb1-211,2222; ENSMUST00000169931.8,Ctnnb1-212,505; ENSMUST00000170729.2,Ctnnb1-213,692; ENSMUST00000178812.9,Ctnnb1-214,2702; ENSMUST00000215573.2,Ctnnb1-215,1292"	MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL	"chr9:120,758,282-120,789,573[+]"	"Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle. Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling."	PDB: 1DOW; PDB: 1I7W; PDB: 1I7X; PDB: 1JPP; PDB: 1M1E; PDB: 1V18; PDB: 2BCT; PDB: 3BCT; PDB: 3OUW; PDB: 3OUX; PDB: 4EV8; PDB: 4EV9; PDB: 4EVA; PDB: 4EVP; PDB: 4EVT; PDB: 4ONS	HGNC:17748	CTNB1_MOUSE	reviewed	ENSMUSG00000006932	.	.	.	.	.
Mol01949	Protein	C-C motif chemokine receptor 5 (CCR5)	Ccr5; Cmkbr5	CCR5	12774	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000097855.4,Ccr5-201,449; ENSMUST00000111442.3,Ccr5-202,8227; ENSMUST00000168179.8,Ccr5-203,663; ENSMUST00000169553.8,Ccr5-204,349; ENSMUST00000171499.3,Ccr5-205,403; ENSMUST00000171579.3,Ccr5-206,745"	MDFQGSVPTYSYDIDYGMSAPCQKINVKQIAAQLLPPLYSLVFIFGFVGNMMVFLILISCKKLKSVTDIYLLNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKVFTGLYHIGYFGGIFFIILLTIDRYLAIVHAVFALKVRTVNFGVITSVVTWAVAVFASLPEIIFTRSQKEGFHYTCSPHFPHTQYHFWKSFQTLKMVILSLILPLLVMVICYSGILHTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLLLTTFQEFFGLNNCSSSNRLDQAMQATETLGMTHCCLNPVIYAFVGEKFRSYLSVFFRKHMVKRFCKRCSIFQQDNPDRASSVYTRSTGEHEVSTGL	"chr9:123,921,580-123,947,736[+]"	"Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor."	.	HGNC:1606	CCR5_MOUSE	reviewed	ENSMUSG00000079227	.	.	.	.	.
Mol01950	Protein	Glial fibrillary acidic protein (GFAP)	Gfap	GFAP	14580	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000067444.10,Gfap-201,2648; ENSMUST00000077902.5,Gfap-202,2600; ENSMUST00000127909.2,Gfap-203,356"	MERRRITSARRSYASETVVRGLGPSRQLGTMPRFSLSRMTPPLPARVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESASYQEALARLEEEGQSLKEEMARHLQEYQDLLNVKLALDIEIATYRKLLEGEENRITIPVQTFSNLQIRETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKDSKQEHKDVVM	"chr11:102,778,162-102,791,738[-]"	"GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells."	.	HGNC:4235	GFAP_MOUSE	reviewed	ENSMUSG00000020932	.	.	.	.	.
Mol01951	Protein	Ras-specific guanine nucleotide-releasing factor 2 (RGRF2)	Rasgrf2; Grf2	RGRF2	19418	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000151408.9,Rasgrf2-201,7764; ENSMUST00000216219.2,Rasgrf2-202,2115"	MQKSVRYNEGHALYLAMLARKEGTKRGFLSKKAAEASRWHEKWFALYQNVLFYFEGEQSGRPAGMYLLEGCSCERTPAPPRTNAGPAGARDALDKQYYFTVLFGHDGQKPLELRCEEEQAGKEWMEAIHQASYADILIEREVLMQKYIHLVQIVETEKIATNQLRHQLEDQDTEIERLKSEIVALNKTKERMRPYHVHQEEEDPDIKKIKKVQSFMRGWLCRRKWKTIVQDYICSPHAESMRKRNQIVFTMVEAETEYVHQLYILVNGFLRPLRMAASSKKPPINHDDVSSIFLNSETIMFLHEIFHQGLKARLANWPTLVLADLFDILLPMLNIYQEFVRNHQYSLQVLANCKQNRDFDKLLKQYEANPACEGRMLETFLTYPMFQIPRYIITLHELLAHTPHEHVERKSLEFAKSKLEELSRVMHDEVSDTENIRKNLAIERMIVEGCDILLDTSQTFIRQGSLIQVPSVERGKLSKVRLGSLSLKKEGERQCFLFTKHFLICTRSSGGKLHLLKTGGVLSLIQCTLIEEPDGSDDDPKGSGHMFGHLDFKIVVEPPDAASFTVVLLAPSRQEKAAWMSDISQCVDNIRCNGLMTIVFEENSKVTVPHMIKSDARLHKDDTDICFSKTLNSCKVPQIRYASVERLLERLTDLRFLSIDFLNTFLHTYRIFTTATVVLAKLSDIYKRPFTSIPVRSLELFFATSQNNREHLVDGKSPRLCRKFSSPPPLAVSRTSSPVRARKLSLTSSLNSRIGALDLTNSSSSSSPTTTTHSPAASPPPHTAVLESAPADKAGDSADMSPCRSPTTPRHLRYRQPGGQVADSAHCSVSPASAFAIATAAAGHGSPPGFNNERTCDKEFIIRRTATNRVLNVLRHWVSKHAQDFELNNELKMNVLNLLEEVLRDPDLLPQERKATANILRALSQDDQDDIHLKLEDIIQMTDCPKAECFETLSAMELAEQITLLDHIVFRSIPYEEFLGQGWMKLDKNERTPYIMKTSQHFNEMSNLVASQIMNYADISSRANAIEKWVAVADICRCLHNYNGVLEITSALNRSAIYRLKKTWAKVSKQTKALMDKLQKTVSSEGRFKNLRETLKNCNPPAVPYLGMYLTDLAFIEEGTPNFTEEGLVNFSKMRMISHIIREIRQFQQTAYRIDQQPKVIQYLLDKALVIDEDSLYELSLKIEPRLPA	"chr13:92,028,519-92,268,164[-]"	Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation.	.	.	RGRF2_MOUSE	reviewed	ENSMUSG00000021708	.	.	.	.	.
Mol01952	Protein	Facilitated glucose transporter member 4 (GLUT4)	Slc2a4; Glut4	GLUT4	20528	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000018710.13,Slc2a4-201,2524; ENSMUST00000135437.3,Slc2a4-202,626; ENSMUST00000141837.9,Slc2a4-203,1776; ENSMUST00000142500.8,Slc2a4-204,408; ENSMUST00000152487.8,Slc2a4-205,735; ENSMUST00000178363.8,Slc2a4-206,679; ENSMUST00000178809.8,Slc2a4-207,3193; ENSMUST00000179298.3,Slc2a4-208,787"	MPSGFQQIGSDDGEPPRQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNATWLGRQGPGGPDSIPQGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLANNVLAVLGGALMGLANAAASYEILILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILVAQVLGLESMLGTATLWPLLLALTVLPALLQLILLPFCPESPRYLYIIRNLEGPARKSLKRLTGWADVSDALAELKDEKRKLERERPMSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFESAGVGQPAYATIGAGVVNTVFTLVSVLLVERAGRRTLHLLGLAGMCGCAILMTVALLLLERVPAMSYVSIVAIFGFVAFFEIGPGPIPWFIVAELFSQGPRPAAMAVAGFSNWTCNFIVGMGFQYVADAMGPYVFLLFAVLLLGFFIFTFLKVPETRGRTFDQISAAFRRTPSLLEQEVKPSTELEYLGPDEND	"chr11:69,833,365-69,839,014[-]"	"Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell."	.	.	GLUT4_MOUSE	reviewed	ENSMUSG00000018566	.	.	.	.	.
Mol01953	Protein	Katanin interacting protein (KATNIP)	KATNIP; KIAA0556	KATNIP	23247	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000261588.10,KATNIP-201,6599; ENST00000562207.1,KATNIP-202,321; ENST00000564749.5,KATNIP-203,564; ENST00000565672.5,KATNIP-204,767; ENST00000566023.1,KATNIP-205,440; ENST00000567894.5,KATNIP-206,2262; ENST00000568258.5,KATNIP-207,746; ENST00000568622.1,KATNIP-208,570; ENST00000573850.1,KATNIP-209,3237; ENST00000618117.1,KATNIP-210,392"	MDGQTLRKAERSWSCSREKKEGYAKDMVTDFDEKHDEYLILLQQRNRILKHLKSKDPVQLRLEHLEQGFSVYVNGANSELKSSPRKAIHSDFSRSASHTEGTHDYGRRTLFREAEEALRRSSRTAPSKVQRRGWHQKSVQIRTEAGPRLHIEPPVDYSDDFELCGDVTLQANNTSEDRPQELRRSLELSVNLQRKQKDCSSDEYDSIEEDILSEPEPEDPALVGHPRHDRPPSSGDWTQKDVHGEQETEGRSSPGPDTLVVLEFNPASKSHKRERNLSAKRKDNAEVFVPTKPEPNLTPQAPAVFPDQERMCSRPGSRRERPLSATRKTLCEAEYPEEDASAVLQAIQVENAALQRALLSRKAEQPASPLQDAEGPPAKPWTSLLEEKEETLELLPITTATTTQEPAGAAGGARAINQAMDRIGLLGSRQQQKLLKVLQAVESDSAHLGRVVSPTKEQVSDTEDKQRMRADEIKDAIYVTMEILSNWGNSWWVGLTEVEFFDLNDTKLYVSPHDVDIRNTATPGELGRLVNRNLAGKKDSSPWTCPFHPPLQLFFVIRNTRQLGDFHLAKIKVRNYWTADGDLDIGAKNVKLYVNRNLIFNGKLDKGDREAPADHSILVDQKNEKSEQLEEAMNAHSEESKGTHEMAGASGDKELGLGCSPPAETLADAKLSSQGNVSGKRKNSTNCRKDSLSQLEEYLRLSAVPTSMGDMPSAPATSPPVKCPPVHEEPSLIQQLENLMGRKICEPPGKTPSWLQPSPTGKDRKQGGRKPKPLWLSPEKPLAWKGRLPSDDVIGEGPGETEARDKGLRHEPGWGTSRSVNTKERPQRATTKVHSDDSDIFNQPPNRERPASGRRGSRKDAGSSSHGDDQPASREDTWSSRTPSRSRWRSEQEHTLHESWSSLSAFDRSHRGRISNTELPGDILDELLQQKSSRHSDLPPSKKGEQPGLSRGQDGYSGETDAGGDFKIPVLPYGQRLVIDIKSTWGDRHYVGLNGIEIFSSKGEPVQISNIKADPPDINILPAYGKDPRVVTNLIDGVNRTQDDMHVWLAPFTRGRSHSITIDFTHPCHVALIRIWNYNKSRIHSFRGVKDITMLLDTQCIFEGEIAKASGTLAGAPEHFGDTILFTTDDDILEAIFYSDEMFDLDVGSLDSLQDEEAMRRPSTADGEGDERPFTQAGLGADERIPELELPSSSPVPQVTTPEPGIYHGICLQLNFTASWGDLHYLGLTGLEVVGKEGQALPIHLHQISASPRDLNELPEYSDDSRALDKLIDGTNITMEDEHMWLIPFSPGLDHVVTIRLDRAESIAGLRFWNYNKSPEDTYRGAKIVHVSLDGLCVSPPEGFLIRKGPGNCHFDFAQEILFVDYLRAQLLPQPARRLDMRSLECASMDYEAPLMPCGFIFQFQLLTSWGDPYYIGLTGLELYDERGEKIPLSENNIAAFPDSVNSLEGVGGDVRTPDKLIDQVNDTSDGRHMWLAPILPGLVNRVYVIFDLPTTVSMIKLWNYAKTPHRGVKEFGLLVDDLLVYNGILAMVSHLVGGILPTCEPTVPYHTILFTEDRDIRHQEKHTTISNQAEDQDVQMMNENQIITNAKRKQSVVDPALRPKTCISEKETRRRRC	"chr16:27,550,133-27,780,344[+]"	"May influence the stability of microtubules (MT), possibly through interaction with the MT-severing katanin complex."	.	HGNC:29068	KATIP_HUMAN	reviewed	ENSG00000047578	.	.	.	.	.
Mol01954	Protein	Quinolinate phosphoribosyltransferase (QPRT)	QPRT	QPRT	23475	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000219771.7,QPRT-201,913; ENST00000395384.9,QPRT-202,2200; ENST00000449759.2,QPRT-203,1237; ENST00000562473.1,QPRT-204,579; ENST00000564967.1,QPRT-205,2199"	MDAEGLALLLPPVTLAALVDSWLREDCPGLNYAALVSGAGPSQAALWAKSPGVLAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGLLVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFTLKVEVECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKLFAKEVAPVPKIH	"chr16:29,663,279-29,698,699[+]"	Involved in the catabolism of quinolinic acid (QA).	PDB: 2JBM; PDB: 4KWV; PDB: 4KWW; PDB: 5AYX; PDB: 5AYY; PDB: 5AYZ	HGNC:9755	NADC_HUMAN	reviewed	ENSG00000103485	.	.	.	.	.
Mol01955	Protein	"ArfGAP with coiled-coil, ankyrin repeat and PH domains 2 (ACAP2)"	ACAP2; CENTB2; KIAA0041	ACAP2	23527	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000326793.11,ACAP2-201,7093; ENST00000423531.3,ACAP2-202,475; ENST00000439666.1,ACAP2-203,235; ENST00000439758.3,ACAP2-204,766; ENST00000447662.1,ACAP2-205,700; ENST00000450200.1,ACAP2-206,684; ENST00000466876.2,ACAP2-207,1030; ENST00000471593.1,ACAP2-208,758; ENST00000472860.1,ACAP2-209,573; ENST00000475905.5,ACAP2-210,759; ENST00000480906.5,ACAP2-211,1802; ENST00000481463.5,ACAP2-212,561; ENST00000484296.1,ACAP2-213,692; ENST00000490224.1,ACAP2-214,578; ENST00000635383.1,ACAP2-215,1647"	MKMTVDFEECLKDSPRFRAALEEVEGDVAELELKLDKLVKLCIAMIDTGKAFCVANKQFMNGIRDLAQYSSNDAVVETSLTKFSDSLQEMINFHTILFDQTQRSIKAQLQNFVKEDLRKFKDAKKQFEKVSEEKENALVKNAQVQRNKQHEVEEATNILTATRKCFRHIALDYVLQINVLQSKRRSEILKSMLSFMYAHLAFFHQGYDLFSELGPYMKDLGAQLDRLVVDAAKEKREMEQKHSTIQQKDFSSDDSKLEYNVDAANGIVMEGYLFKRASNAFKTWNRRWFSIQNNQLVYQKKFKDNPTVVVEDLRLCTVKHCEDIERRFCFEVVSPTKSCMLQADSEKLRQAWIKAVQTSIATAYREKGDESEKLDKKSSPSTGSLDSGNESKEKLLKGESALQRVQCIPGNASCCDCGLADPRWASINLGITLCIECSGIHRSLGVHFSKVRSLTLDTWEPELLKLMCELGNDVINRVYEANVEKMGIKKPQPGQRQEKEAYIRAKYVERKFVDKYSISLSPPEQQKKFVSKSSEEKRLSISKFGPGDQVRASAQSSVRSNDSGIQQSSDDGRESLPSTVSANSLYEPEGERQDSSMFLDSKHLNPGLQLYRASYEKNLPKMAEALAHGADVNWANSEENKATPLIQAVLGGSLVTCEFLLQNGANVNQRDVQGRGPLHHATVLGHTGQVCLFLKRGANQHATDEEGKDPLSIAVEAANADIVTLLRLARMNEEMRESEGLYGQPGDETYQDIFRDFSQMASNNPEKLNRFQQDSQKF	"chr3:195,274,745-195,443,044[-]"	GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6).	PDB: 6IF3	HGNC:16469	ACAP2_HUMAN	reviewed	ENSG00000114331	.	.	.	.	.
Mol01956	Protein	Decaprenyl diphosphate synthase subunit 1 (PDSS1)	PDSS1; DPS1; TPRT	PDSS1	23590	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000376215.10,PDSS1-201,1584; ENST00000470978.1,PDSS1-202,799; ENST00000473224.1,PDSS1-203,561; ENST00000491711.5,PDSS1-204,897"	MASRWWRWRRGCSWKPAARSPGPGSPGRAGPLGPSAAAEVRAQVHRRKGLDLSQIPYINLVKHLTSACPNVCRISRFHHTTPDSKTHSGEKYTDPFKLGWRDLKGLYEDIRKELLISTSELKEMSEYYFDGKGKAFRPIIVALMARACNIHHNNSRHVQASQRAIALIAEMIHTASLVHDDVIDDASSRRGKHTVNKIWGEKKAVLAGDLILSAASIALARIGNTTVISILTQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGLATGPVLFACQQFPEMNAMIMRRFSLPGDVDRARQYVLQSDGVQQTTYLAQQYCHEAIREISKLRPSPERDALIQLSEIVLTRDK	"chr10:26,697,701-26,746,798[+]"	"Heterotetrameric enzyme that catalyzes the condensation of farnesyl diphosphate (FPP), which acts as a primer, and isopentenyl diphosphate (IPP) to produce prenyl diphosphates of varying chain lengths and participates in the determination of the side chain of ubiquinone. Supplies nona and decaprenyl diphosphate, the precursors for the side chain of the isoprenoid quinones ubiquinone-9 (Q9)and ubiquinone-10 (Q10) respectively. The enzyme adds isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry."	.	HGNC:17759	DPS1_HUMAN	reviewed	ENSG00000148459	.	.	.	.	.
Mol01957	Protein	Natriuretic peptides A (ANF)	Nppa	ANF	24602	Rattus norvegicus	10116	Rattus norvegicus	Rattus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSRNOT00000011005.6,Nppa-202,814; ENSRNOT00000117878.1,Nppa-201,1183"	MGSFSITKGFFLFLAFWLPGHIGANPVYSAVSNTDLMDFKNLLDHLEEKMPVEDEVMPPQALSEQTDEAGAALSSLSEVPPWTGEVNPSQRDGGALGRGPWDPSDRSALLKSKLRALLAGPRSLRRSSCFGGRIDRIGAQSGLGCNSFRYRR	"5:158,429,042-158,430,351[+]"	"[Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism. Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses. Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance. Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts. Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension. In adipose tissue, acts in various cGMP- and PKG-dependent pathways to regulate lipid metabolism and energy homeostasis. This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue. Binds the clearance receptor NPR3 which removes the hormone from circulation."	PDB: 1T34; PDB: 7BRG; PDB: 7BRL	.	ANF_RAT	reviewed	ENSRNOG00000008176	.	.	.	.	.
Mol01958	Protein	TNF alpha induced protein 8 (TNFAIP8)	TNFAIP8	TNFAIP8	25816	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000274456.6,TNFAIP8-201,795; ENST00000388882.5,TNFAIP8-202,541; ENST00000415806.2,TNFAIP8-203,1990; ENST00000503646.1,TNFAIP8-204,2502; ENST00000504642.1,TNFAIP8-205,711; ENST00000504771.3,TNFAIP8-206,6976; ENST00000513374.1,TNFAIP8-207,1385"	MHSEAEESKEVATDVFNSKNLAVQAQKKILGKMVSKSIATTLIDDTSSEVLDELYRVTREYTQNKKEAEKIIKNLIKTVIKLAILYRNNQFNQDELALMEKFKKKVHQLAMTVVSFHQVDYTFDRNVLSRLLNECREMLHQIIQRHLTAKSHGRVNNVFDHFSDCEFLAALYNPFGNFKPHLQKLCDGINKMLDEENI	"chr5:119,268,692-119,399,688[+]"	"Acts as a negative mediator of apoptosis and may play a role in tumor progression. Suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, subsequently resulting in inhibition of BID cleavage and caspase-3 activation."	.	HGNC:17260	TFIP8_HUMAN	reviewed	ENSG00000145779	.	.	.	.	.
Mol01959	Protein	F-box and leucine rich repeat protein 2 (FBXL2)	FBXL2; FBL2; FBL3	FBXL2	25827	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000283627.10,FBXL2-201,2152; ENST00000421391.5,FBXL2-202,1581; ENST00000422741.5,FBXL2-203,2223; ENST00000425973.5,FBXL2-204,511; ENST00000432809.5,FBXL2-205,1618; ENST00000435207.5,FBXL2-206,1584; ENST00000451636.5,FBXL2-207,1859; ENST00000460186.5,FBXL2-208,550; ENST00000461094.5,FBXL2-209,609; ENST00000463698.5,FBXL2-210,562; ENST00000463736.5,FBXL2-211,1643; ENST00000464164.5,FBXL2-212,527; ENST00000464990.1,FBXL2-213,2775; ENST00000471208.1,FBXL2-214,507; ENST00000483037.5,FBXL2-215,558; ENST00000484457.6,FBXL2-216,3827; ENST00000492662.1,FBXL2-217,554; ENST00000493778.5,FBXL2-218,648; ENST00000497411.5,FBXL2-219,625; ENST00000498807.5,FBXL2-220,558; ENST00000538892.5,FBXL2-221,2793"	MVFSNNDEGLINKKLPKELLLRIFSFLDIVTLCRCAQISKAWNILALDGSNWQRIDLFNFQTDVEGRVVENISKRCGGFLRKLSLRGCIGVGDSSLKTFAQNCRNIEHLNLNGCTKITDSTCYSLSRFCSKLKHLDLTSCVSITNSSLKGISEGCRNLEYLNLSWCDQITKDGIEALVRGCRGLKALLLRGCTQLEDEALKHIQNYCHELVSLNLQSCSRITDEGVVQICRGCHRLQALCLSGCSNLTDASLTALGLNCPRLQILEAARCSHLTDAGFTLLARNCHELEKMDLEECILITDSTLIQLSIHCPKLQALSLSHCELITDDGILHLSNSTCGHERLRVLELDNCLLITDVALEHLENCRGLERLELYDCQQVTRAGIKRMRAQLPHVKVHAYFAPVTPPTAVAGSGQRLCRCCVIL	"chr3:33,277,025-33,403,662[+]"	"Calcium-activated substrate recognition component of the SCF (SKP1-cullin-F-box protein) E3 ubiquitin-protein ligase complex, SCF(FBXL2), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Unlike many F-box proteins, FBXL2 does not seem to target phosphodegron within its substrates but rather calmodulin-binding motifs and is thereby antagonized by calmodulin. This is the case for the cyclins CCND2 and CCND3 which polyubiquitination and subsequent degradation are inhibited by calmodulin. Through CCND2 and CCND3 degradation induces cell-cycle arrest in G(0). SCF(FBXL2) also mediates PIK3R2 ubiquitination and proteasomal degradation thereby regulating phosphatidylinositol 3-kinase signaling and autophagy. PCYT1A monoubiquitination by SCF(FBXL2) and subsequent degradation regulates synthesis of phosphatidylcholine, which is utilized for formation of membranes and of pulmonary surfactant."	PDB: 6O60	HGNC:13598	FBXL2_HUMAN	reviewed	ENSG00000153558	.	.	.	.	.
Mol01960	Protein	"Nuclear protein 1, transcriptional regulator (NUPR1)"	NUPR1; COM1	NUPR1	26471	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000324873.8,NUPR1-201,5291; ENST00000395641.2,NUPR1-202,550; ENST00000567646.1,NUPR1-203,598"	MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR	"chr16:28,532,708-28,539,008[-]"	"Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses. Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A. Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation. Negatively regulates apoptosis through interaction with PTMA. Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter. Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53. Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway. Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac). Coactivator of PAX2 transcription factor activity, both by recruiting EP300 to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2. Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation. Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion. Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities. Also required for LHB expression and ovarian maturation. Exacerbates CNS inflammation and demyelination upon cuprizone treatment."	.	HGNC:29990	NUPR1_HUMAN	reviewed	ENSG00000176046	.	.	.	.	.
Mol01961	Protein	Caspase recruitment domain family member 10 (CARD10)	CARD10; CARMA3	CARD10	29775	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000251973.10,CARD10-201,4111; ENST00000403299.5,CARD10-202,4113; ENST00000406271.7,CARD10-203,3127; ENST00000433485.1,CARD10-204,578; ENST00000437756.5,CARD10-205,2140; ENST00000467812.1,CARD10-206,1910; ENST00000476871.5,CARD10-207,583; ENST00000486118.1,CARD10-208,546; ENST00000488141.5,CARD10-209,2169; ENST00000494166.1,CARD10-210,560"	MPGRAEAGEAEEEAGAGSGSEAEEDALWERIEGVRHRLARALNPAKLTPYLRQCRVIDEQDEEEVLSTYRFPCRVNRTGRLMDILRCRGKRGYEAFLEALEFYYPEHFTLLTGQEPAQRCSMILDEEGPEGLTQFLMTEVRRLREARKSQLQREQQLQARGRVLEEERAGLEQRLRDQQQAQERCQRLREDWEAGSLELLRLKDENYMIAMRLAQLSEEKNSAVLRSRDLQLAVDQLKLKVSRLEEECALLRRARGPPPGAEEKEKEKEKEKEPDNVDLVSELRAENQRLTASLRELQEGLQQEASRPGAPGSERILLDILEHDWREAQDSRQELCQKLHAVQGELQWAEELRDQYLQEMEDLRLKHRTLQKDCDLYKHRMATVLAQLEEIEKERDQAIQSRDRIQLQYSQSLIEKDQYRKQVRGLEAERDELLTTLTSLEGTKALLEVQLQRAQGGTCLKACASSHSLCSNLSSTWSLSEFPSPLGGPEATGEAAVMGGPEPHNSEEATDSEKEINRLSILPFPPSAGSILRRQREEDPAPPKRSFSSMSDITGSVTLKPWSPGLSSSSSSDSVWPLGKPEGLLARGCGLDFLNRSLAIRVSGRSPPGGPEPQDKGPDGLSFYGDRWSGAVVRRVLSGPGSARMEPREQRVEAAGLEGACLEAEAQQRTLLWNQGSTLPSLMDSKACQSFHEALEAWAKGPGAEPFYIRANLTLPERADPHALCVKAQEILRLVDSAYKRRQEWFCTRVDPLTLRDLDRGTVPNYQRAQQLLEVQEKCLPSSRHRGPRSNLKKRALDQLRLVRPKPVGAPAGDSPDQLLLEPCAEPERSLRPYSLVRPLLVSALRPVVLLPECLAPRLIRNLLDLPSSRLDFQVCPAESLSGEELCPSSAPGAPKAQPATPGLGSRIRAIQESVGKKHCLLELGARGVRELVQNEIYPIVIHVEVTEKNVREVRGLLGRPGWRDSELLRQCRGSEQVLWGLPCSWVQVPAHEWGHAEELAKVVRGRILQEQARLVWVECGSSRGCPSSSEA	"chr22:37,490,362-37,519,542[-]"	Scaffold protein that plays an important role in mediating the activation of NF-kappa-B via BCL10 or EGFR.	.	HGNC:16422	CAR10_HUMAN	reviewed	ENSG00000100065	.	.	.	.	.
Mol01962	Protein	SRY-box transcription factor 8 (SOX8)	SOX8	SOX8	30812	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000293894.4,SOX8-201,3087; ENST00000566034.1,SOX8-202,4153"	MLDMSEARSQPPCSPSGTASSMSHVEDSDSDAPPSPAGSEGLGRAGVAVGGARGDPAEAADERFPACIRDAVSQVLKGYDWSLVPMPVRGGGGGALKAKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLSESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSAKAGHSDSDSGAELGPHPGGGAVYKAEAGLGDGHHHGDHTGQTHGPPTPPTTPKTELQQAGAKPELKLEGRRPVDSGRQNIDFSNVDISELSSEVMGTMDAFDVHEFDQYLPLGGPAPPEPGQAYGGAYFHAGASPVWAHKSAPSASASPTETGPPRPHIKTEQPSPGHYGDQPRGSPDYGSCSGQSSATPAAPAGPFAGSQGDYGDLQASSYYGAYPGYAPGLYQYPCFHSPRRPYASPLLNGLALPPAHSPTSHWDQPVYTTLTRP	"chr16:981,770-986,979[+]"	"Transcription factor that may play a role in central nervous system, limb and facial development. May be involved in male sex determination. Binds the consensus motif 5'-[AT][AT]CAA[AT]G-3' (By similarity)."	.	HGNC:11203	SOX8_HUMAN	reviewed	ENSG00000005513	.	.	.	.	.
Mol01963	Protein	Sclerostin (SOST)	SOST; UNQ2976/PRO7455/PRO7476	SOST	50964	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000301691.3,SOST-201,2296"	MQLPLALCLVCLLVHTAFRVVEGQGWQAFKNDATEIIPELGEYPEPPPELENNKTMNRAENGGRPPHHPFETKDVSEYSCRELHFTRYVTDGPCRSAKPVTELVCSGQCGPARLLPNAIGRGKWWRPSGPDFRCIPDRYRAQRVQLLCPGGEAPRARKVRLVASCKCKRLTRFHNQSELKDFGTEAARPQKGRKPRPRARSAKANQAELENAY	"chr17:43,753,738-43,758,791[-]"	Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.	PDB: 2K8P; PDB: 3SOV; PDB: 6L6R	HGNC:13771	SOST_HUMAN	reviewed	ENSG00000167941	.	.	.	.	.
Mol01964	Protein	Fizzy and cell division cycle 20 related 1 (FZR1)	FZR1; CDH1; FYR; FZR; KIAA1242	FZR1	51343	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000313639.8,FZR1-201,1215; ENST00000395095.7,FZR1-202,1491; ENST00000441788.7,FZR1-203,5178; ENST00000586212.1,FZR1-204,623; ENST00000588084.1,FZR1-205,671; ENST00000588327.1,FZR1-206,675; ENST00000591290.5,FZR1-207,1331; ENST00000592214.1,FZR1-208,598; ENST00000652521.1,FZR1-209,3503"	MDQDYERRLLRQIVIQNENTMPRVTEMRRTLTPASSPVSSPSKHGDRFIPSRAGANWSVNFHRINENEKSPSQNRKAKDATSDNGKDGLAYSALLKNELLGAGIEKVQDPQTEDRRLQPSTPEKKGLFTYSLSTKRSSPDDGNDVSPYSLSPVSNKSQKLLRSPRKPTRKISKIPFKVLDAPELQDDFYLNLVDWSSLNVLSVGLGTCVYLWSACTSQVTRLCDLSVEGDSVTSVGWSERGNLVAVGTHKGFVQIWDAAAGKKLSMLEGHTARVGALAWNAEQLSSGSRDRMILQRDIRTPPLQSERRLQGHRQEVCGLKWSTDHQLLASGGNDNKLLVWNHSSLSPVQQYTEHLAAVKAIAWSPHQHGLLASGGGTADRCIRFWNTLTGQPLQCIDTGSQVCNLAWSKHANELVSTHGYSQNQILVWKYPSLTQVAKLTGHSYRVLYLAMSPDGEAIVTGAGDETLRFWNVFSKTRSTKVKWESVSVLNLFTRIR	"chr19:3,506,311-3,538,334[+]"	"Substrate-specific adapter for the anaphase promoting complex/cyclosome (APC/C) E3 ubiquitin-protein ligase complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulators of the cell cycle do not accumulate prematurely. At the G1/S transition FZR1 is phosphorylated, leading to its dissociation from the APC/C. Following DNA damage, it is required for the G2 DNA damage checkpoint: its dephosphorylation and reassociation with the APC/C leads to the ubiquitination of PLK1, preventing entry into mitosis. Acts as an adapter for APC/C to target the DNA-end resection factor RBBP8/CtIP for ubiquitination and subsequent proteasomal degradation. Through the regulation of RBBP8/CtIP protein turnover, may play a role in DNA damage response, favoring DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR)."	PDB: 4UI9; PDB: 5L9T; PDB: 5L9U; PDB: 7QE7	HGNC:24824	FZR1_HUMAN	reviewed	ENSG00000105325	.	.	.	.	.
Mol01965	Protein	Ubiquitin protein ligase E3 component n-recognin 5 (UBR5)	UBR5; EDD; EDD1; HYD; KIAA0896	UBR5	51366	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000220959.8,UBR5-201,9418; ENST00000517465.1,UBR5-202,1095; ENST00000518145.1,UBR5-203,598; ENST00000518205.5,UBR5-204,1931; ENST00000519365.1,UBR5-205,602; ENST00000519528.1,UBR5-206,325; ENST00000520539.6,UBR5-207,10895; ENST00000520898.5,UBR5-208,582; ENST00000521312.1,UBR5-209,560; ENST00000521566.1,UBR5-210,563; ENST00000521767.1,UBR5-211,1763; ENST00000521922.5,UBR5-212,9008; ENST00000522327.1,UBR5-213,701"	MTSIHFVVHPLPGTEDQLNDRLREVSEKLNKYNLNSHPPLNVLEQATIKQCVVGPNHAAFLLEDGRVCRIGFSVQPDRLELGKPDNNDGSKLNSNSGAGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGARDSRRQTRVIRTGRDRGSGLLGSQPQPVIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDEDGDDGDDTASESYLPGEDLMSLLDADIHSAHPSVIIDADAMFSEDISYFGYPSFRRSSLSRLGSSRVLLLPLERDSELLRERESVLRLRERRWLDGASFDNERGSTSKEGEPNLDKKNTPVQSPVSLGEDLQWWPDKDGTKFICIGALYSELLAVSSKGELYQWKWSESEPYRNAQNPSLHHPRATFLGLTNEKIVLLSANSIRATVATENNKVATWVDETLSSVASKLEHTAQTYSELQGERIVSLHCCALYTCAQLENSLYWWGVVPFSQRKKMLEKARAKNKKPKSSAGISSMPNITVGTQVCLRNNPLYHAGAVAFSISAGIPKVGVLMESVWNMNDSCRFQLRSPESLKNMEKASKTTEAKPESKQEPVKTEMGPPPSPASTCSDASSIASSASMPYKRRRSTPAPKEEEKVNEEQWSLREVVFVEDVKNVPVGKVLKVDGAYVAVKFPGTSSNTNCQNSSGPDADPSSLLQDCRLLRIDELQVVKTGGTPKVPDCFQRTPKKLCIPEKTEILAVNVDSKGVHAVLKTGNWVRYCIFDLATGKAEQENNFPTSSIAFLGQNERNVAIFTAGQESPIILRDGNGTIYPMAKDCMGGIRDPDWLDLPPISSLGMGVHSLINLPANSTIKKKAAVIIMAVEKQTLMQHILRCDYEACRQYLMNLEQAVVLEQNLQMLQTFISHRCDGNRNILHACVSVCFPTSNKETKEEEEAERSERNTFAERLSAVEAIANAISVVSSNGPGNRAGSSSSRSLRLREMMRRSLRAAGLGRHEAGASSSDHQDPVSPPIAPPSWVPDPPAMDPDGDIDFILAPAVGSLTTAATGTGQGPSTSTIPGPSTEPSVVESKDRKANAHFILKLLCDSVVLQPYLRELLSAKDARGMTPFMSAVSGRAYPAAITILETAQKIAKAEISSSEKEEDVFMGMVCPSGTNPDDSPLYVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAGQKSARLDLLYRLLTATNLVTLPNSRGEHLLLFLVQTVARQTVEHCQYRPPRIREDRNRKTASPEDSDMPDHDLEPPRFAQLALERVLQDWNALKSMIMFGSQENKDPLSASSRIGHLLPEEQVYLNQQSGTIRLDCFTHCLIVKCTADILLLDTLLGTLVKELQNKYTPGRREEAIAVTMRFLRSVARVFVILSVEMASSKKKNNFIPQPIGKCKRVFQALLPYAVEELCNVAESLIVPVRMGIARPTAPFTLASTSIDAMQGSEELFSVEPLPPRPSSDQSSSSSQSQSSYIIRNPQQRRISQSQPVRGRDEEQDDIVSADVEEVEVVEGVAGEEDHHDEQEEHGEENAEAEGQHDEHDEDGSDMELDLLAAAETESDSESNHSNQDNASGRRSVVTAATAGSEAGASSVPAFFSEDDSQSNDSSDSDSSSSQSDDIEQETFMLDEPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAASSAGLIYIDPSNLRRSGTISTSAAAAAAALEASNASSYLTSASSLARAYSIVIRQISDLMGLIPKYNHLVYSQIPAAVKLTYQDAVNLQNYVEEKLIPTWNWMVSIMDSTEAQLRYGSALASAGDPGHPNHPLHASQNSARRERMTAREEASLRTLEGRRRATLLSARQGMMSARGDFLNYALSLMRSHNDEHSDVLPVLDVCSLKHVAYVFQALIYWIKAMNQQTTLDTPQLERKRTRELLELGIDNEDSEHENDDDTNQSATLNDKDDDSLPAETGQNHPFFRRSDSMTFLGCIPPNPFEVPLAEAIPLADQPHLLQPNARKEDLFGRPSQGLYSSSASSGKCLMEVTVDRNCLEVLPTKMSYAANLKNVMNMQNRQKKEGEEQPVLPEETESSKPGPSAHDLAAQLKSSLLAEIGLTESEGPPLTSFRPQCSFMGMVISHDMLLGRWRLSLELFGRVFMEDVGAEPGSILTELGGFEVKESKFRREMEKLRNQQSRDLSLEVDRDRDLLIQQTMRQLNNHFGRRCATTPMAVHRVKVTFKDEPGEGSGVARSFYTAIAQAFLSNEKLPNLECIQNANKGTHTSLMQRLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSIDTRPFRPASEGNPSDDPEPLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAHGRENGADSILDLGLVDSSEKVQQENRKRHGSSRSVVDMDLDDTDDGDDNAPLFYQPGKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLLQFKRWFWSIVEKMSMTERQDLVYFWTSSPSLPASEEGFQPMPSITIRPPDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIKTKNFGFV	"chr8:102,252,273-102,412,759[-]"	"E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). Involved in maturation and/or transcriptional regulation of mRNA by activating CDK9 by polyubiquitination. May play a role in control of cell cycle progression. May have tumor suppressor function. Regulates DNA topoisomerase II binding protein (TopBP1) in the DNA damage response. Plays an essential role in extraembryonic development. Ubiquitinates acetylated PCK1. Also acts as a regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes."	PDB: 1I2T; PDB: 2QHO; PDB: 3PT3	HGNC:16806	UBR5_HUMAN	reviewed	ENSG00000104517	.	.	.	.	.
Mol01966	Protein	GSK3B interacting protein (GSKIP)	GSKIP; C14orf129; HSPC210	GSKIP	51527	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000438650.5,GSKIP-201,2140; ENST00000553699.5,GSKIP-202,501; ENST00000554182.5,GSKIP-203,760; ENST00000555088.5,GSKIP-204,648; ENST00000555181.6,GSKIP-205,2169; ENST00000555757.1,GSKIP-206,361; ENST00000556095.5,GSKIP-207,3834"	METDCNPMELSSMSGFEEGSELNGFEGTDMKDMRLEAEAVVNDVLFAVNNMFVSKSLRCADDVAYINVETKERNRYCLELTEAGLKVVGYAFDQVDDHLQTPYHETVYSLLDTLSPAYREAFGNALLQRLEALKRDGQS	"chr14:96,363,452-96,387,288[+]"	"A-kinase anchoring protein for GSK3B and PKA that regulates or facilitates their kinase activity towards their targets. The ternary complex enhances Wnt-induced signaling by facilitating the GSK3B- and PKA-induced phosphorylation of beta-catenin leading to beta-catenin degradation and stabilization respectively. Upon cAMP activation, the ternary complex contributes to neuroprotection against oxidative stress-induced apoptosis by facilitating the PKA-induced phosphorylation of DML1 and PKA-induced inactivation of GSK3B. During neurite outgrowth promotes neuron proliferation; while increases beta-catenin-induced transcriptional activity through GSK3B kinase activity inhibition, reduces N-cadherin level to promote cell cycle progression."	PDB: 1SGO	HGNC:20343	GSKIP_HUMAN	reviewed	ENSG00000100744	.	.	.	.	.
Mol01967	Protein	Zinc finger C3HC-type containing 1 (ZC3HC1)	ZC3HC1; NIPA; HSPC216	ZC3HC1	51530	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000311873.9,ZC3HC1-201,2017; ENST00000358303.9,ZC3HC1-202,1889; ENST00000360708.9,ZC3HC1-203,1676; ENST00000467642.5,ZC3HC1-204,1934; ENST00000470651.1,ZC3HC1-205,567; ENST00000471022.5,ZC3HC1-206,978; ENST00000477578.5,ZC3HC1-207,850; ENST00000480193.5,ZC3HC1-208,563; ENST00000481503.5,ZC3HC1-209,1741; ENST00000483827.1,ZC3HC1-210,760; ENST00000484432.1,ZC3HC1-211,559; ENST00000648450.1,ZC3HC1-212,2164"	MAAPCEGQAFAVGVEKNWGAVVRSPEGTPQKIRQLIDEGIAPEEGGVDAKDTSATSQSVNGSPQAEQPSLESTSKEAFFSRVETFSSLKWAGKPFELSPLVCAKYGWVTVECDMLKCSSCQAFLCASLQPAFDFDRYKQRCAELKKALCTAHEKFCFWPDSPSPDRFGMLPLDEPAILVSEFLDRFQSLCHLDLQLPSLRPEDLKTMCLTEDKISLLLHLLEDELDHRTDERKTTIKLGSDIQVHVTACILSVCGWACSSSLESMQLSLITCSQCMRKVGLWGFQQIESSMTDLDASFGLTSSPIPGLEGRPERLPLVPESPRRMMTRSQDATFSPGSEQAEKSPGPIVSRTRSWDSSSPVDRPEPEAASPTTRTRPVTRSMGTGDTPGLEVPSSPLRKAKRARLCSSSSSDTSSRSFFDPTSQHRDWCPWVNITLGKESRENGGTEPDASAPAEPGWKAVLTILLAHKQSSQPAETDSMSLSEKSRKVFRIFRQWESLCSC	"chr7:130,018,287-130,051,451[-]"	"Essential component of a SCF-type E3 ligase complex, SCF(NIPA), a complex that controls mitotic entry by mediating ubiquitination and subsequent degradation of cyclin B1 (CCNB1). Its cell-cycle-dependent phosphorylation regulates the assembly of the SCF(NIPA) complex, restricting CCNB1 ubiquitination activity to interphase. Its inactivation results in nuclear accumulation of CCNB1 in interphase and premature mitotic entry. May have an antiapoptotic role in NPM-ALK-mediated signaling events."	.	HGNC:29913	ZC3C1_HUMAN	reviewed	ENSG00000091732	.	.	.	.	.
Mol01968	Protein	Sirtuin 6 (SIRT6)	SIRT6; SIR2L6	SIRT6	51548	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305232.10,SIRT6-201,1506; ENST00000337491.7,SIRT6-202,1600; ENST00000594279.5,SIRT6-203,1507; ENST00000594341.1,SIRT6-204,371; ENST00000595670.5,SIRT6-205,1057; ENST00000596119.5,SIRT6-206,1537; ENST00000596298.5,SIRT6-207,717; ENST00000597896.5,SIRT6-208,827; ENST00000599365.5,SIRT6-209,1372; ENST00000599394.1,SIRT6-210,607; ENST00000600540.5,SIRT6-211,1407; ENST00000600938.5,SIRT6-212,1473; ENST00000601069.5,SIRT6-213,1260; ENST00000601488.5,SIRT6-214,1361; ENST00000601571.1,SIRT6-215,716"	MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSSVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGPKQEPCAQHNGSEPASPKRERPTSPAPHRPPKRVKAKAVPS	"chr19:4,174,109-4,182,566[-]"	"NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging. Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context. Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B. Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing. Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and deacetylation of histone H3K9ac and H3K56ac. SIRT6 participation to DSB repair is probably involved in extension of life span. Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53. Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence. Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage. Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac. Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism. Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes. Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect. Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2). Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5. Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA. Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1. Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2. The defatty-acylase activity is specifically involved in regulation of protein secretion. Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion. Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170. Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription."	PDB: 3K35; PDB: 3PKI; PDB: 3PKJ; PDB: 3ZG6; PDB: 5MF6; PDB: 5MFP; PDB: 5MFZ; PDB: 5MGN; PDB: 5X16; PDB: 5Y2F; PDB: 6HOY; PDB: 6QCD; PDB: 6QCE; PDB: 6QCH; PDB: 6QCJ; PDB: 6XUY; PDB: 6XV1; PDB: 6XV6; PDB: 6XVG; PDB: 6ZU4; PDB: 7CL0; PDB: 7CL1	HGNC:14934	SIR6_HUMAN	reviewed	ENSG00000077463	.	.	.	.	.
Mol01972	Protein	SET and MYND domain containing 2 (SMYD2)	SMYD2; KMT3C	SMYD2	56950	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000366957.10,SMYD2-201,1745; ENST00000416415.2,SMYD2-202,702; ENST00000460580.5,SMYD2-203,1618; ENST00000471645.5,SMYD2-204,4732; ENST00000484459.1,SMYD2-205,463; ENST00000491455.5,SMYD2-206,3809"	MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH	"chr1:214,281,102-214,337,131[+]"	"Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'."	PDB: 3RIB; PDB: 3S7B; PDB: 3S7D; PDB: 3S7F; PDB: 3S7J; PDB: 3TG4; PDB: 3TG5; PDB: 4O6F; PDB: 4WUY; PDB: 4YND; PDB: 5ARF; PDB: 5ARG; PDB: 5KJK; PDB: 5KJL; PDB: 5KJM; PDB: 5KJN; PDB: 5V3H; PDB: 5WCG; PDB: 6CBX; PDB: 6CBY; PDB: 6MON; PDB: 6N3G	HGNC:20982	SMYD2_HUMAN	reviewed	ENSG00000143499	.	.	.	.	.
Mol01973	Protein	Catenin beta interacting protein 1 (CTNNBIP1)	CTNNBIP1; ICAT	CTNNBIP1	56998	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000377256.1,CTNNBIP1-201,451; ENST00000377258.5,CTNNBIP1-202,852; ENST00000377263.6,CTNNBIP1-203,3006; ENST00000400904.7,CTNNBIP1-204,1206"	MNREGAPGKSPEEMYIQQKVRVLLMLRKMGSNLTASEEEFLRTYAGVVNSQLSQLPPHSIDQGAEDVVMAFSRSETEDRRQ	"chr1:9,848,276-9,910,336[-]"	"Prevents the interaction between CTNNB1 and TCF family members, and acts as negative regulator of the Wnt signaling pathway."	PDB: 1LUJ; PDB: 1M1E; PDB: 1T08	HGNC:16913	CNBP1_HUMAN	reviewed	ENSG00000178585	.	.	.	.	.
Mol01974	Protein	Activation induced cytidine deaminase (AICDA)	AICDA; AID	AICDA	57379	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000229335.11,AICDA-201,2803; ENST00000537228.6,AICDA-202,2796; ENST00000543081.6,AICDA-203,2538; ENST00000544516.6,AICDA-204,210; ENST00000545576.2,AICDA-205,3008; ENST00000696246.1,AICDA-206,2587; ENST00000696271.1,AICDA-207,2988; ENST00000696272.1,AICDA-208,2653; ENST00000696273.1,AICDA-209,2699"	MDSLLMNRRKFLYQFKNVRWAKGRRETYLCYVVKRRDSATSFSLDFGYLRNKNGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVADFLRGNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIAIMTFKDYFYCWNTFVENHERTFKAWEGLHENSVRLSRQLRRILLPLYEVDDLRDAFRTLGL	"chr12:8,602,155-8,613,242[-]"	"Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation."	PDB: 5JJ4; PDB: 5W0R; PDB: 5W0U; PDB: 5W0Z; PDB: 5W1C	HGNC:13203	AICDA_HUMAN	reviewed	ENSG00000111732	.	.	.	.	.
Mol01975	Protein	StAR related lipid transfer domain containing 9 (STARD9)	STARD9; KIAA1300	STARD9	57519	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000290607.12,STARD9-201,15637; ENST00000562139.1,STARD9-202,656; ENST00000562619.1,STARD9-203,7237; ENST00000563872.5,STARD9-204,553; ENST00000564158.5,STARD9-205,6049; ENST00000568493.1,STARD9-206,2469; ENST00000569419.1,STARD9-207,666"	MANVQVAVRVRPLSKRETKEGGRIIVEVDGKVAKIRNLKVDNRPDGFGDSREKVMAFGFDYCYWSVNPEDPQYASQDVVFQDLGMEVLSGVAKGYNICLFAYGQTGSGKTYTMLGTPASVGLTPRICEGLFVREKDCASLPSSCRIKVSFLEIYNERVRDLLKQSGQKKSYTLRVREHPEMGPYVQGLSQHVVTNYKQVIQLLEEGIANRITAATHVHEASSRSHAIFTIHYTQAILENNLPSEMASKINLVDLAGSERADPSYCKDRIAEGANINKSLVTLGIVISTLAQNSQVFSSCQSLNSSVSNGGDSGILSSPSGTSSGGAPSRRQSYIPYRDSVLTWLLKDSLGGNSKTIMVATVSPAHTSYSETMSTLRYASSAKNIINKPRVNEDANLKLIRELREEIERLKALLLSFELRNFSSLSDENLKELVLQNELKIDQLTKDWTQKWNDWQALMEHYSVDINRRRAGVVIDSSLPHLMALEDDVLSTGVVLYHLKEGTTKIGRIDSDQEQDIVLQGQWIERDHCTITSACGVVVLRPARGARCTVNGREVTASCRLTQGAVITLGKAQKFRFNHPAEAAVLRQRRQVGEAAAGRGSLEWLDLDGDLAASRLGLSPLLWKERRALEEQCDEDHQTPRDGETSHRAQIQQQQSYVEDLRHQILAEEIRAAKELEFDQAWISQQIKENQQCLLREETWLASLQQQQQEDQVAEKELEASVALDAWLQTDPEIQPSPFVQSQKRVVHLQLLRRHTLRAAERNVRRKKVSFQLERIIKKQRLLEAQKRLEKLTTLCWLQDDSTQEPPYQVLSPDATVPRPPCRSKLTSCSSLSPQRLCSKHMPQLHSIFLSWDPSTTLPPRPDPTHQTSEKTSSEEHLPQAASYPARTGCLRKNGLHSSGHGQPCTARAALARKGASAPDACLTMSPNSVGIQEMEMGVKQPHQMVSQGLASLRKSANKLKPRHEPKIFTSTTQTRGAKGLADPSHTQAGWRKEGNLGTHKAAKGASCNSLYPHGPRQTAGHGKAVKTFWTEYKPPSPSRASKRHQRVLATRVRNITKKSSHLPLGSPLKRQQNTRDPDTMVPLTDFSPVMDHSREKDNDLSDTDSNYSLDSLSCVYAKALIEPLKPEERKWDFPEPENSESDDSQLSEDSLAEKRYQSPKNRLGGNRPTNNRGQPRTRTRASVRGFTAASDSDLLAQTHRSFSLDSLIDAEEELGEDQQEEPFPGSADEIPTETFWHLEDSSLPVMDQEAICRLGPINYRTAARLDAVLPMSSSFYLDPQFQPHCELQPHCELQPHCELQPHCEQAESQVEPSYSEQADSLQGMQLSRESPLMSMDSWFSCDSKINPSSPPGIVGSLCPSPDMQEFHSCKGERPGYWPNTEELKPSDAETVLPYSSKLHQGSTELLCSARDEHTASAADTSRLSLWGIQRLIQPGADGTFQGRCIPDMTQQGSSEASHNSSVSNVLAASATTLTHVGSTHERDWSALQQKYLLELSCPVLEAIGAPKPAYPYLEEDSGSLAQASSKGGDTLLPVGPRVSSNLNLNNFPVHLSRIRRLRAEKEQDSLNAKLEGVSDFFSTSEKEASYDETYSADLESLSASRSTNAQVFATENAIPDSMTEACEVKQNNLEECLQSCRKPGLMTSSDEDFFQKNACHSNVTTATKADHWSQGWAPLRKNSAVQPGQLSPDSHYPLEEEKTDCQESSKEAVRRHINVSFALPSGPELYLHSAPWNPLSSSLQPPLLETFYVTKSRDALTETALEIPACREVRVPSPPPREAWGFGHNHQALQGAYLKNNLPVLLQNQNSKIASSQQVTAEIPVDLNTREVIRESGKCPGNITEESHDSVYSSVTQNRHFLPSTSTKVCEFENQVVILNKKHSFPALEGGEVTAQSCCGASSDSTESGKSLLFRESEAREEEELDQNTVLRQTINVSLEKDMPGESAVSLKSRSVDRRVSSPVMVAQGGGPTPKWEGKNETGLLEKGLRPKDSSEEFKLPGTKPAYERFQLVACPQERNPSECKSQEMLNPNREPSGKKQNKRVNNTDEMARLIRSVMQLENGILEIESKQNKQVHASHTPGTDKELVFQDQKEQEKTDHAFRPDSSGNPLPSKDQPSSPRQTDDTVFRDSEAGAMEVNSIGNHPQVQKITPNPFRSREGVRESEPVREHTHPAGSDRPARDICDSLGKHTTCREFTNTSLHPQRMKALARALPLQPRLERSSKNNGQFVKASASLKGQPWGLGSLEELETVKGFQESQVAEHVSSSNQEEPKAQGKVEEMPMQRGGSLQEENKVTQKFPSLSQLCRDTFFRQETVSPLLSRTEFCTAPLHQDLSNTLPLNSPRWPRRCLHVPVALGISSLDCVLDLTMLKIHNSPLVTGVEHQDQSTETRSHSPEGNVRGRSSEAHTAWCGSVRSMAMGSHSQSGVPESIPLGTEDRISASTSPQDHGKDLRITLLGFSTSEDFASEAEVAVQKEIRVSSLNKVSSQPEKRVSFSLEEDSDQASKPRQKAEKETEDVGLTSGVSLAPVSLPRVPSPEPRLLEPSDHASMCLAILEEIRQAKAQRKQLHDFVARGTVLSYCETLLEPECSSRVAGRPQCKQIDQSSSDQTRNEGEAPGFHVASLSAEAGQIDLLPDERKVQATSLSADSFESLPNTETDREPWDPVQAFSHAAPAQDRKRRTGELRQFAGASEPFICHSSSSEIIEKKKDATRTPSSADPLAPDSPRSSAPVEEVRRVVSKKVVAALPSQAPYDDPRVTLHELSQSVPQETAEGIPPGSQDSSPEHQEPRTLDTTYGEVSDNLLVTAQGEKTAHFESQSVTCDVQNSTSASGPKQDHVQCPEASTGFEEGRASPKQDTILPGALTRVALEAPTQQCVQCKESVGSGLTEVCRAGSKHSRPIPLPDQRPSANPGGIGEEAPCRHPREALDGPVFSRNPEGSRTLSPSRGKESRTLPCRQPCSSQPVATHAYSSHSSTLLCFRDGDLGKEPFKAAPHTIHPPCVVPSRAYEMDETGEISRGPDVHLTHGLEPKDVNREFRLTESSTCEPSTVAAVLSRAQGCRSPSAPDVRTGSFSHSATDGSVGLIGVPEKKVAEKQASTELEAASFPAGMYSEPLRQFRDSSVGDQNAQVCQTNPEPPATTQGPHTLDLSEGSAESKLVVEPQHECLENTTRCFLEKPQFSTELRDHNRLDSQAKFVARLKHTCSPQEDSPWQEEEQHRDQASGGGEGFAQGVNPLPDEDGLDGCQILDAGREEVAVAKPPVSKILSQGFKDPATVSLRQNETPQPAAQRSGHLYTGREQPAPNHRGSLPVTTIFSGPKHSRSSPTPQFSVVGSSRSLQELNLSVEPPSPTDEDTQGPNRLWNPHLRGYSSGKSVARTSLQAEDSNQKASSRLDDGTTDHRHLKPATPPYPMPSTLSHMPTPDFTTSWMSGTLEQAQQGKREKLGVQVRPENWCSQMDKGMLHFGSSDISPYALPWRPEEPARISWKQYMSGSAVDVSCSQKPQGLTLSNVARCSSMDNGLEDQNSPFHSHLSTYANICDLSTTHSSTENAQGSNEAWEVFRGSSSIALGDPHIPTSPEGVAPTSGHDRRPQFRGPSGEADCLRSKPPLAKGSAAGPVDEIMLLYPSEAGCPVGQTRTNTFEQGTQTLGSRRHWSSTDISFAQPEASAVSAFDLASWTSMHNLSLHLSQLLHSTSELLGSLSQPDVARREQNTKRDIPDKAPQALMMDGSTQTTVDEGSQTDLTLPTLCLQTSEAEPQGANVILEGLGSDTSTVSQEEGDVPGVPQKREAEETAQKMAQLLYLQEESTPYKPQSPSIPSSHLRFQKAPVGQHLPSVSPSVSDAFLPPSSQPEESYCLVVSSPSPSSPHSPGLFPSTSEYPGDSRVQKKLGPTSALFVDRASSPILTLSASTQEPGLSPGSLTLSAPSTHPVEGHQKLDSSPDPVDAPRTPMDNYSQTTDELGGSQRGRSSLQRSNGRSFLELHSPHSPQQSPKLQFSFLGQHPQQLQPRTTIGVQSRLLPPPLRHRSQRLGNSFVPEKVASPEHCPLSGREPSQWQSRTENGGESSASPGEPQRTLDRPSSWGGLQHLSPCPVSELTDTAGLRGSALGLPQACQPEELLCFSCQMCMAPEHQHHSLRDLPVHNKFSNWCGVQKGSPGGLDMTEEELGASGDLSSEKQEQSPPQPPNDHSQDSEWSKREQIPLQVGAQNLSLSVELTEAKLHHGFGEADALLQVLQSGTGEALAADEPVTSTWKELYARQKKAIETLRRERAERLGNFCRTRSLSPQKQLSLLPNKDLFIWDLDLPSRRREYLQQLRKDVVETTRSPESVSRSAHTPSDIELMLQDYQQAHEEAKVEIARARDQLRERTEQEKLRIHQKIISQLLKEEDKLHTLANSSSLCTSSNGSLSSGMTSGYNSSPALSGQLQFPENMGHTNLPDSRDVWIGDERGGHSAVRKNSAYSHRASLGSCCCSPSSLSSLGTCFSSSYQDLAKHVVDTSMADVMAACSDNLHNLFSCQATAGWNYQGEEQAVQLYYKVFSPTRHGFLGAGVVSQPLSRVWAAVSDPTVWPLYYKPIQTARLHQRVTNSISLVYLVCNTTLCALKQPRDFCCVCVEAKEGHLSVMAAQSVYDTSMPRPSRKMVRGEILPSAWILQPITVEGKEVTRVIYLAQVELGAPGFPPQLLSSFIKRQPLVIARLASFLGR	"chr15:42,575,606-42,720,998[+]"	Microtubule-dependent motor protein required for spindle pole assembly during mitosis. Required to stabilize the pericentriolar material (PCM).	.	HGNC:19162	STAR9_HUMAN	reviewed	ENSG00000159433	.	.	.	.	.
Mol01976	Protein	TSPY like 2 (TSPYL2)	TSPYL2; CDA1; DENTT; TSPX; HRIHFB2216	TSPYL2	64061	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000375442.8,TSPYL2-201,2815; ENST00000463525.1,TSPYL2-202,722; ENST00000553557.5,TSPYL2-203,2607; ENST00000556808.1,TSPYL2-204,4178; ENST00000578306.5,TSPYL2-205,966; ENST00000579390.1,TSPYL2-206,869"	MDRPDEGPPAKTRRLSSSESPQRDPPPPPPPPPLLRLPLPPPQQRPRLQEETEAAQVLADMRGVGLGPALPPPPPYVILEEGGIRAYFTLGAECPGWDSTIESGYGEAPPPTESLEALPTPEASGGSLEIDFQVVQSSSFGGEGALETCSAVGWAPQRLVDPKSKEEAIIIVEDEDEDERESMRSSRRRRRRRRRKQRKVKRESRERNAERMESILQALEDIQLDLEAVNIKAGKAFLRLKRKFIQMRRPFLERRDLIIQHIPGFWVKAFLNHPRISILINRRDEDIFRYLTNLQVQDLRHISMGYKMKLYFQTNPYFTNMVIVKEFQRNRSGRLVSHSTPIRWHRGQEPQARRHGNQDASHSFFSWFSNHSLPEADRIAEIIKNDLWVNPLRYYLRERGSRIKRKKQEMKKRKTRGRCEVVIMEDAPDYYAVEDIFSEISDIDETIHDIKISDFMETTDYFETTDNEITDINENICDSENPDHNEVPNNETTDNNESADDHETTDNNESADDNNENPEDNNKNTDDNEENPNNNENTYGNNFFKGGFWGSHGNNQDSSDSDNEADEASDDEDNDGNEGDNEGSDDDGNEGDNEGSDDDDRDIEYYEKVIEDFDKDQADYEDVIEIISDESVEEEGIEEGIQQDEDIYEEGNYEEEGSEDVWEEGEDSDDSDLEDVLQVPNGWANPGKRGKTG	"chrX:53,082,367-53,088,540[+]"	"Part of the CASK/TBR1/TSPYL2 transcriptional complex which modulates gene expression in response to neuronal synaptic activity, probably by facilitating nucleosome assembly. May inhibit cell proliferation by inducing p53-dependent CDKN1A expression."	.	HGNC:24358	TSYL2_HUMAN	reviewed	ENSG00000184205	.	.	.	.	.
Mol01977	Protein	Solute carrier family 28 member 3 (SLC28A3)	SLC28A3; CNT3	SLC28A3	64078	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000376238.5,SLC28A3-201,4962; ENST00000495823.1,SLC28A3-202,514"	MELRSTAAPRAEGYSNVGFQNEENFLENENTSGNNSIRSRAVQSREHTNTKQDEEQVTVEQDSPRNREHMEDDDEEMQQKGCLERRYDTVCGFCRKHKTTLRHIIWGILLAGYLVMVISACVLNFHRALPLFVITVAAIFFVVWDHLMAKYEHRIDEMLSPGRRLLNSHWFWLKWVIWSSLVLAVIFWLAFDTAKLGQQQLVSFGGLIMYIVLLFLFSKYPTRVYWRPVLWGIGLQFLLGLLILRTDPGFIAFDWLGRQVQTFLEYTDAGASFVFGEKYKDHFFAFKVLPIVVFFSTVMSMLYYLGLMQWIIRKVGWIMLVTTGSSPIESVVASGNIFVGQTESPLLVRPYLPYITKSELHAIMTAGFSTIAGSVLGAYISFGVPSSHLLTASVMSAPASLAAAKLFWPETEKPKITLKNAMKMESGDSGNLLEAATQGASSSISLVANIAVNLIAFLALLSFMNSALSWFGNMFDYPQLSFELICSYIFMPFSFMMGVEWQDSFMVARLIGYKTFFNEFVAYEHLSKWIHLRKEGGPKFVNGVQQYISIRSEIIATYALCGFANIGSLGIVIGGLTSMAPSRKRDIASGAVRALIAGTVACFMTACIAGILSSTPVDINCHHVLENAFNSTFPGNTTKVIACCQSLLSSTVAKGPGEVIPGGNHSLYSLKGCCTLLNPSTFNCNGISNTF	"chr9:84,275,457-84,340,758[-]"	"Sodium-dependent, pyrimidine- and purine-selective. Involved in the homeostasis of endogenous nucleosides. Exhibits the transport characteristics of the nucleoside transport system cib or N3 subtype (N3/cib) (with marked transport of both thymidine and inosine). Employs a 2:1 sodium/nucleoside ratio. Also able to transport gemcitabine, 3'-azido-3'-deoxythymidine (AZT), ribavirin and 3-deazauridine."	PDB: 6KSW	HGNC:16484	S28A3_HUMAN	reviewed	ENSG00000197506	.	.	.	.	.
Mol01978	Protein	Purinergic receptor P2Y12 (P2RY12)	P2RY12; HORK3	P2RY12	64805	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000302632.4,P2RY12-201,2244; ENST00000468596.1,P2RY12-202,960"	MQAVDNLTSAPGNTSLCTRDYKITQVLFPLLYTVLFFVGLITNGLAMRIFFQIRSKSNFIIFLKNTVISDLLMILTFPFKILSDAKLGTGPLRTFVCQVTSVIFYFTMYISISFLGLITIDRYQKTTRPFKTSNPKNLLGAKILSVVIWAFMFLLSLPNMILTNRQPRDKNVKKCSFLKSEFGLVWHEIVNYICQVIFWINFLIVIVCYTLITKELYRSYVRTRGVGKVPRKKVNVKVFIIIAVFFICFVPFHFARIPYTLSQTRDVFDCTAENTLFYVKESTLWLTSLNACLDPFIYFFLCKSFRNSLISMLKCPNSATSLSQDNRKKEQDGGDPNEETPM	"chr3:151,336,843-151,384,753[-]"	Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Required for normal platelet aggregation and blood coagulation.	PDB: 4NTJ; PDB: 4PXZ; PDB: 4PY0	HGNC:18124	P2Y12_HUMAN	reviewed	ENSG00000169313	.	.	.	.	.
Mol01979	Protein	Nanog homeobox (NANOG)	NANOG	NANOG	79923	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000229307.9,NANOG-201,5182; ENST00000526286.1,NANOG-202,870; ENST00000526434.2,NANOG-203,558; ENST00000541267.5,NANOG-204,836"	MSVDPACPQSLPCFEASDCKESSPMPVICGPEENYPSLQMSSAEMPHTETVSPLPSSMDLLIQDSPDSSTSPKGKQPTSAEKSVAKKEDKVPVKKQKTRTVFSSTQLCVLNDRFQRQKYLSLQQMQELSNILNLSYKQVKTWFQNQRMKSKRWQKNNWPKNSNGVTQKASAPTYPSLYSSYHQGCLVNPTGNLPMWSNQTWNNSTWSNQTQNIQSWSNHSWNTQTWCTQSWNNQAWNSPFYNCGEESLQSCMQFQPNSPASDLEAALEAAGEGLNVIQQTTRYFSTPQTMDLFLNYSMNMQPEDV	"chr12:7,787,794-7,799,146[+]"	"Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3'. Binds to the POU5F1/OCT4 promoter. Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation."	PDB: 2KT0; PDB: 4RBO	HGNC:20857	NANOG_HUMAN	reviewed	ENSG00000111704	.	.	.	.	.
Mol01980	Protein	Dehydrodolichyl diphosphate synthase subunit (DHDDS)	DHDDS; HDS	DHDDS	79947	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000236342.12,DHDDS-201,3288; ENST00000360009.6,DHDDS-202,3245; ENST00000374185.7,DHDDS-203,1148; ENST00000374186.7,DHDDS-204,656; ENST00000416052.1,DHDDS-205,629; ENST00000427245.6,DHDDS-206,868; ENST00000430232.5,DHDDS-207,703; ENST00000431933.5,DHDDS-208,2673; ENST00000434391.6,DHDDS-209,3338; ENST00000436153.6,DHDDS-210,705; ENST00000487944.5,DHDDS-211,717; ENST00000525165.5,DHDDS-212,573; ENST00000525326.5,DHDDS-213,492; ENST00000525410.1,DHDDS-214,595; ENST00000525546.5,DHDDS-215,581; ENST00000525682.6,DHDDS-216,1235; ENST00000526219.5,DHDDS-217,1072; ENST00000526278.5,DHDDS-218,548; ENST00000527611.1,DHDDS-219,297; ENST00000528557.5,DHDDS-220,516; ENST00000529688.5,DHDDS-221,589; ENST00000530781.5,DHDDS-222,556; ENST00000531312.5,DHDDS-223,496; ENST00000531955.5,DHDDS-224,559; ENST00000533087.5,DHDDS-225,582"	MSWIKEGELSLWERFCANIIKAGPMPKHIAFIMDGNRRYAKKCQVERQEGHSQGFNKLAETLRWCLNLGILEVTVYAFSIENFKRSKSEVDGLMDLARQKFSRLMEEKEKLQKHGVCIRVLGDLHLLPLDLQELIAQAVQATKNYNKCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPSDISESLLDKCLYTNRSPHPDILIRTSGEVRLSDFLLWQTSHSCLVFQPVLWPEYTFWNLFEAILQFQMNHSVLQKARDMYAEERKRQQLERDQATVTEQLLREGLQASGDAQLRRTRLHKLSARREERVQGFLQALELKRADWLARLGTASA	"chr1:26,432,282-26,471,306[+]"	"With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length. Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol."	PDB: 6W2L; PDB: 6Z1N	HGNC:20603	DHDDS_HUMAN	reviewed	ENSG00000117682	.	.	.	.	.
Mol01981	Protein	Nectin cell adhesion molecule 4 (NECTIN4)	NECTIN4; LNIR; PRR4; PVRL4	NECTIN4	81607	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000368012.4,NECTIN4-201,3458; ENST00000486694.1,NECTIN4-202,864"	MPLSLGAEMWGPEAWLLLLLLLASFTGRCPAGELETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQADEGEYECRVSTFPAGSFQARLRLRVLVPPLPSLNPGPALEEGQGLTLAASCTAEGSPAPSVTWDTEVKGTTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQDQRITHILHVSFLAEASVRGLEDQNLWHIGREGAMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVDVLDPQEDSGKQVDLVSASVVVVGVIAALLFCLLVVVVVLMSRYHRRKAQQMTQKYEEELTLTRENSIRRLHSHHTDPRSQPEESVGLRAEGHPDSLKDNSSCSVMSEEPEGRSYSTLTTVREIETQTELLSPGSGRAEEEEDQDEGIKQAMNHFVQENGTLRAKPTGNGIYINGRGHLV	"chr1:161,070,998-161,089,558[-]"	"Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells.; (Microbial infection) Acts as a receptor for measles virus."	PDB: 4FRW; PDB: 4GJT; PDB: 4JJH	HGNC:19688	NECT4_HUMAN	reviewed	ENSG00000143217	.	.	.	.	.
Mol01982	Protein	Hematopoietic SH2 domain containing (HSH2D)	HSH2D; ALX	HSH2D	84941	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000535834.1,HSH2D-201,982; ENST00000586872.5,HSH2D-202,1364; ENST00000591154.1,HSH2D-203,507; ENST00000593031.1,HSH2D-204,585; ENST00000613195.4,HSH2D-205,1508; ENST00000613986.4,HSH2D-206,1957; ENST00000616070.4,HSH2D-207,2473; ENST00000616645.4,HSH2D-208,2366"	MTEAGKLPLPLPPRLDWFVHTQMGQLAQDGVPEWFHGAISREDAENLLESQPLGSFLIRVSHSHVGYTLSYKAQSSCCHFMVKLLDDGTFMIPGEKVAHTSLDALVTFHQQKPIEPRRELLTQPCRQKDPANVDYEDLFLYSNAVAEEAACPVSAPEEASPKPVLCHQSKERKPSAEMNRITTKEATSSCPPKSPLGETRQKLWRSLKMLPERGQRVRQQLKSHLATVNLSSLLDVRRSTVISGPGTGKGSQDHSGDPTSGDRGYTDPCVATSLKSPSQPQAPKDRKVPTRKAERSVSCIEVTPGDRSWHQMVVRALSSQESKPEHQGLAEPENDQLPEEYQQPPPFAPGYC	"chr19:16,134,028-16,158,575[+]"	May be a modulator of the apoptotic response through its ability to affect mitochondrial stability (By similarity). Adapter protein involved in tyrosine kinase and CD28 signaling. Seems to affect CD28-mediated activation of the RE/AP element of the interleukin-2 promoter.	PDB: 2CS0	HGNC:24920	HSH2D_HUMAN	reviewed	ENSG00000196684	.	.	.	.	.
Mol01983	Protein	Leucine rich repeat kinase 2 (LRRK2)	LRRK2; PARK8	LRRK2	120892	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000298910.12,LRRK2-201,9239; ENST00000343742.6,LRRK2-202,4740; ENST00000416796.5,LRRK2-203,1655; ENST00000430804.5,LRRK2-204,6400; ENST00000474202.1,LRRK2-205,556; ENST00000479187.5,LRRK2-206,8306; ENST00000481256.1,LRRK2-207,561; ENST00000636518.1,LRRK2-208,2477; ENST00000644108.1,LRRK2-209,1151; ENST00000679360.1,LRRK2-210,7718; ENST00000679532.1,LRRK2-211,4852; ENST00000679683.1,LRRK2-212,2855; ENST00000680018.1,LRRK2-213,4523; ENST00000680235.1,LRRK2-214,2344; ENST00000680422.1,LRRK2-215,8598; ENST00000680425.1,LRRK2-216,3968; ENST00000680453.1,LRRK2-217,4515; ENST00000680790.1,LRRK2-218,8875; ENST00000681136.1,LRRK2-219,4081; ENST00000681696.1,LRRK2-220,3828; ENST00000681773.1,LRRK2-221,4718"	MASGSCQGCEEDEETLKKLIVRLNNVQEGKQIETLVQILEDLLVFTYSERASKLFQGKNIHVPLLIVLDSYMRVASVQQVGWSLLCKLIEVCPGTMQSLMGPQDVGNDWEVLGVHQLILKMLTVHNASVNLSVIGLKTLDLLLTSGKITLLILDEESDIFMLIFDAMHSFPANDEVQKLGCKALHVLFERVSEEQLTEFVENKDYMILLSALTNFKDEEEIVLHVLHCLHSLAIPCNNVEVLMSGNVRCYNIVVEAMKAFPMSERIQEVSCCLLHRLTLGNFFNILVLNEVHEFVVKAVQQYPENAALQISALSCLALLTETIFLNQDLEEKNENQENDDEGEEDKLFWLEACYKALTWHRKNKHVQEAACWALNNLLMYQNSLHEKIGDEDGHFPAHREVMLSMLMHSSSKEVFQASANALSTLLEQNVNFRKILLSKGIHLNVLELMQKHIHSPEVAESGCKMLNHLFEGSNTSLDIMAAVVPKILTVMKRHETSLPVQLEALRAILHFIVPGMPEESREDTEFHHKLNMVKKQCFKNDIHKLVLAALNRFIGNPGIQKCGLKVISSIVHFPDALEMLSLEGAMDSVLHTLQMYPDDQEIQCLGLSLIGYLITKKNVFIGTGHLLAKILVSSLYRFKDVAEIQTKGFQTILAILKLSASFSKLLVHHSFDLVIFHQMSSNIMEQKDQQFLNLCCKCFAKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADANQAKEGSSLICQVCEKESSPKLVELLLNSGSREQDVRKALTISIGKGDSQIISLLLRRLALDVANNSICLGGFCIGKVEPSWLGPLFPDKTSNLRKQTNIASTLARMVIRYQMKSAVEEGTASGSDGNFSEDVLSKFDEWTFIPDSSMDSVFAQSDDLDSEGSEGSFLVKKKSNSISVGEFYRDAVLQRCSPNLQRHSNSLGPIFDHEDLLKRKRKILSSDDSLRSSKLQSHMRHSDSISSLASEREYITSLDLSANELRDIDALSQKCCISVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTVKCPTLKQFNLSYNQLSFVPENLTDVVEKLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLNFDFKHIGCKAKDIIRFLQQRLKKAVPYNRMKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFVNATEESDALAKLRKTIINESLNFKIRDQLVVGQLIPDCYVELEKIILSERKNVPIEFPVIDRKRLLQLVRENQLQLDENELPHAVHFLNESGVLLHFQDPALQLSDLYFVEPKWLCKIMAQILTVKVEGCPKHPKGIISRRDVEKFLSKKRKFPKNYMSQYFKLLEKFQIALPIGEEYLLVPSSLSDHRPVIELPHCENSEIIIRLYEMPYFPMGFWSRLINRLLEISPYMLSGRERALRPNRMYWRQGIYLNWSPEAYCLVGSEVLDNHPESFLKITVPSCRKGCILLGQVVDHIDSLMEEWFPGLLEIDICGEGETLLKKWALYSFNDGEEHQKILLDDLMKKAEEGDLLVNPDQPRLTIPISQIAPDLILADLPRNIMLNNDELEFEQAPEFLLGDGSFGSVYRAAYEGEEVAVKIFNKHTSLRLLRQELVVLCHLHHPSLISLLAAGIRPRMLVMELASKGSLDRLLQQDKASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNAAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTTGGRIVEGLKFPNEFDELEIQGKLPDPVKEYGCAPWPMVEKLIKQCLKENPQERPTSAQVFDILNSAELVCLTRRILLPKNVIVECMVATHHNSRNASIWLGCGHTDRGQLSFLDLNTEGYTSEEVADSRILCLALVHLPVEKESWIVSGTQSGTLLVINTEDGKKRHTLEKMTDSVTCLYCNSFSKQSKQKNFLLVGTADGKLAIFEDKTVKLKGAAPLKILNIGNVSTPLMCLSESTNSTERNVMWGGCGTKIFSFSNDFTIQKLIETRTSQLFSYAAFSDSNIITVVVDTALYIAKQNSPVVEVWDKKTEKLCGLIDCVHFLREVMVKENKESKHKMSYSGRVKTLCLQKNTALWIGTGGGHILLLDLSTRRLIRVIYNFCNSVRVMMTAQLGSLKNVMLVLGYNRKNTEGTQKQKEIQSCLTVWDINLPHEVQNLEKHIEVRKELAEKMRRTSVE	"chr12:40,196,744-40,369,285[+]"	"Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, autophagy, and vesicle trafficking. Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation. Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB35, and RAB43. Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A. Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A. Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain. Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization. Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. Phosphorylates PRDX3. By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis. Independent of its kinase activity, inhibits the proteosomal degradation of MAPT, thus promoting MAPT oligomerization and secretion. In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity."	PDB: 2ZEJ; PDB: 3D6T; PDB: 5MY9; PDB: 5MYC; PDB: 6DLO; PDB: 6DLP; PDB: 6OJE; PDB: 6OJF; PDB: 6VNO; PDB: 6VP6; PDB: 6VP7; PDB: 6XAF; PDB: 6XR4; PDB: 7LHT; PDB: 7LHW; PDB: 7LI3; PDB: 7LI4	HGNC:18618	LRRK2_HUMAN	reviewed	ENSG00000188906	.	.	.	.	.
Mol01984	Protein	Interleukin 23 receptor (IL23R)	IL23R	IL23R	149233	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000347310.10,IL23R-201,2858; ENST00000395227.2,IL23R-202,1459; ENST00000425614.3,IL23R-203,1295; ENST00000473881.2,IL23R-204,1507; ENST00000637002.1,IL23R-205,2208"	MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYKNFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYINISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGHLTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQNILESHFNRISLLEK	"chr1:67,138,907-67,259,979[+]"	"Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis."	PDB: 5MZV; PDB: 6WDQ	HGNC:19100	IL23R_HUMAN	reviewed	ENSG00000162594	.	.	.	.	.
Mol01985	Protein	SH3 domain containing ring finger 2 (SH3RF2)	SH3RF2; POSH3; POSHER; PPP1R39; RNF158	SH3RF2	153769	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359120.9,SH3RF2-201,3004; ENST00000503848.5,SH3RF2-202,671; ENST00000504522.1,SH3RF2-203,678; ENST00000506591.1,SH3RF2-204,555; ENST00000509286.1,SH3RF2-205,437; ENST00000511217.1,SH3RF2-206,5607; ENST00000511705.1,SH3RF2-207,1008"	MDDLTLLDLLECPVCFEKLDVTAKVLPCQHTFCKPCLQRVFKAHKELRCPECRTPVFSNIEALPANLLLVRLLDGVRSGQSSGRGGSFRRPGTMTLQDGRKSRTNPRRLQASPFRLVPNVRIHMDGVPRAKALCNYRGQNPGDLRFNKGDIILLRRQLDENWYQGEINGISGNFPASSVEVIKQLPQPPPLCRALYNFDLRGKDKSENQDCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFVEPNLTARHLLEKNKGRQSSRTKNLSLVSSSSRGNTSTLRRGPGSRRKVPGQFSITTALNTLNRMVHSPSGRHMVEISTPVLISSSNPSVITQPMEKADVPSSCVGQVSTYHPAPVSPGHSTAVVSLPGSQQHLSANMFVALHSYSAHGPDELDLQKGEGVRVLGKCQDGWLRGVSLVTGRVGIFPNNYVIPIFRKTSSFPDSRSPGLYTTWTLSTSSVSSQGSISEGDPRQSRPFKSVFVPTAIVNPVRSTAGPGTLGQGSLRKGRSSMRKNGSLQRPLQSGIPTLVVGSLRRSPTMVLRPQQFQFYQPQGIPSSPSAVVVEMGSKPALTGEPALTCISRGSEAWIHSAASSLIMEDKEIPIKSEPLPKPPASAPPSILVKPENSRNGIEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPATLKASQPEAASLGPEMTVLFAHRSGCHSGQQTDLRRKSALGKATTLVSTASGTQTVFPSK	"chr5:145,936,578-146,081,791[+]"	"Has E3 ubiquitin-protein ligase activity. Acts as an anti-apoptotic regulator of the JNK pathway by ubiquitinating and promoting the degradation of SH3RF1, a scaffold protein that is required for pro-apoptotic JNK activation. Facilitates TNF-alpha-mediated recruitment of adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein stability via inhibition of its ubiquitin-mediated proteasomal degradation. Inhibits PPP1CA phosphatase activity."	.	HGNC:26299	SH3R2_HUMAN	reviewed	ENSG00000156463	.	.	.	.	.
Mol01986	Protein	Serine palmitoyltransferase small subunit B (SPTSB)	SPTSSB; ADMP; C3orf57; SSSPTB	SPTSB	165679	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000359175.9,SPTSSB-201,3094; ENST00000497137.1,SPTSSB-202,880; ENST00000497374.1,SPTSSB-203,679; ENST00000620149.2,SPTSSB-204,1734"	MDLRRVKEYFSWLYYQYQIISCCAVLEPWERSMFNTILLTIIAMVVYTAYVFIPIHIRLAWEFFSKICGYHSTISN	"chr3:161,344,798-161,372,880[-]"	"Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference, complexes with this subunit showing a clear preference for longer acyl-CoAs. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. May play a role in signal transduction."	.	.	SPTSB_HUMAN	reviewed	ENSG00000196542	.	.	.	.	.
Mol01988	Protein	Tribbles homolog 3 (TRIB3)	Trib3; Nipk; Trb3	TRIB3	228775	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000040312.7,Trib3-201,2026; ENSMUST00000123145.2,Trib3-202,639; ENSMUST00000124995.2,Trib3-203,504"	MRATPLAASADVSCRKKPLEFDDNIDAKCPVLKRVRDEPEPGPLPSLLPPSPPPASDLSPAVAPATRLGPYILLEREQGSCSYRALHCPTGTEYTCKVYPASEAQAVLAPYARLPTHQHVARPTEVLLGSRLLYIFFTKTHGDLHSLVRSRRGIPESEAAGLFRQMASAVAHCHKHGLVLRDLKLRRFVFSNCERTKLVLENLEDACVMTGSDDSLWDKHACPAYVGPEILSSRPSYSGKAADVWSLGVALFTMLAGRYPFHDSEPVLLFGKIRRGTFALPEGLSAPARCLIRCLLRKEPSERLVALGILLHPWLREDHGRVSPPQSDRREMDQVVPDGPQLEEAEEGEVGLYG	"chr2:152,179,342-152,185,952[-]"	"Inactive protein kinase which acts as a regulator of the integrated stress response (ISR), a process for adaptation to various stress. Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress. May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells. Acts as a negative feedback regulator of the ATF4-dependent transcription during the ISR: while TRIB3 expression is promoted by ATF4, TRIB3 protein interacts with ATF4 and inhibits ATF4 transcription activity. Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation. May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1. Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity. Interacts with MAPK kinases and regulates activation of MAP kinases. Can inhibit APOBEC3A editing of nuclear DNA."	.	.	TRIB3_MOUSE	reviewed	ENSMUSG00000032715	.	.	.	.	.
Mol01989	Protein	Ceramide synthase 6 (CERS6)	CERS6; LASS6	CERS6	253782	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000305747.11,CERS6-201,6804; ENST00000392687.4,CERS6-202,6851"	MAGILAWFWNERFWLPHNVTWADLKNTEEATFPQAEDLYLAFPLAFCIFMVRLIFERFVAKPCAIALNIQANGPQIAPPNAILEKVFTAITKHPDEKRLEGLSKQLDWDVRSIQRWFRQRRNQEKPSTLTRFCESMWRFSFYLYVFTYGVRFLKKTPWLWNTRHCWYNYPYQPLTTDLHYYYILELSFYWSLMFSQFTDIKRKDFGIMFLHHLVSIFLITFSYVNNMARVGTLVLCLHDSADALLEAAKMANYAKFQKMCDLLFVMFAVVFITTRLGIFPLWVLNTTLFESWEIVGPYPSWWVFNLLLLLVQGLNCFWSYLIVKIACKAVSRGKVSKDDRSDIESSSDEEDSEPPGKNPHTATTTNGTSGTNGYLLTGSCSMDD	"chr2:168,456,249-168,775,134[+]"	"Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA). Can use other acyl donors, but with less efficiency. N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively. Ceramides generated by CERS6 play a role in inflammatory response. Acts as a regulator of metabolism and hepatic lipid accumulation. Under high fat diet, palmitoyl- (C16:0-) ceramides generated by CERS6 specifically bind the mitochondrial fission factor MFF, thereby promoting mitochondrial fragmentation and contributing to the development of obesity."	.	HGNC:23826	CERS6_HUMAN	reviewed	ENSG00000172292	.	.	.	.	.
Mol01990	Protein	Long-chain fatty acid transport protein 1 (S27A1)	SLC27A1; ACSVL5; FATP1	S27A1	376497	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000252595.12,SLC27A1-201,3514; ENST00000593701.5,SLC27A1-202,688; ENST00000594962.5,SLC27A1-203,4343; ENST00000598424.5,SLC27A1-204,2681; ENST00000598848.1,SLC27A1-205,497; ENST00000599380.5,SLC27A1-206,2596; ENST00000599965.1,SLC27A1-207,788; ENST00000600277.5,SLC27A1-208,1423; ENST00000600297.1,SLC27A1-209,1163"	MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSVLIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLFRQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALIFGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIGVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRLAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIRLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSVFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVYGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAFAL	"chr19:17,468,769-17,506,168[+]"	"Mediates the ATP-dependent import of long-chain fatty acids (LCFA) into the cell by mediating their translocation at the plasma membrane. Has also an acyl-CoA ligase activity for long-chain and very-long-chain fatty acids. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Probably involved in fatty acid transport across the blood barrier."	.	.	S27A1_HUMAN	reviewed	ENSG00000130304	.	.	.	.	.
Mol01991	Protein	Transcription factor PDR3 (PDR3)	PDR3; YBL005W; YBL0323	PDR3	852278	Saccharomyces cerevisiae	4932	Saccharomyces cerevisiae	Saccharomyces	.	Saccharomycetaceae	Saccharomycetales	4892	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MKVKKSTRSKVSTACVNCRKRKIKCTGKYPCTNCISYDCTCVFLKKHLPQKEDSSQSLPTTAVAPPSSHANVEASADVQHLDTAIKLDNQYYFKLMNDLIQTPVSPSATHAPDTSNNPTNDNNILFKDDSKYQNQLVTYQNILTNLYALPPCDDTQLLIDKTKSQLNNLINSWNPEINYPKLSSFSPRPQRSIETYLLTNKYRNKIHMTRFSFWTDQMVKSQSPDSFLATTPLVDEVFGLFSPIQAFSLRGIGYLIKKNIENTGSSMLIDTKETIYLILRLFDLCYEHLIQGCISISNPLENYLQKIKQTPTTTASASLPTSPAPLSNDLVISVIHQLPQPFIQSITGFTTTQLIENLHDSFSMFRIVTQMYAQHRKRFAEFLNQAFSLPHQEKSVLFSSFCSSEYLLSTLCYAYYNVTLYHMLDINTLDYLEILVSLLEIQNEIDERFGFEKMLEVAVTCSTKMGLSRWEYYVGIDENTAERRRKIWWKIYSLEKRFLTDLGDLSLINEHQMNCLLPKDFRDMGFINHKEFLTKIGTSSLSPSSPKLKNLSLSRLIEYGELAIAQIVGDFFSETLYNEKFTSLEVSVKPTIIRQKLLEKVFEDIESFRLKLAKIKLHTSRVFQVAHCKYPEYPKNDLIEAAKFVSYHKNTWFSILGAVNNLIARLSEDPEVITEQSMKYANEMFQEWREINQFLIQVDTDFIVWACLDFYELIFFVMASKFYVEDPHITLEDVINTLKVFKRITNIISFFNNNLDEKDYDCQTFREFSRSSSLVAISIRIIFLKYCYAEQIDRAEFIERLKEVEPGLSDLLREFFDTRSFIYRYMLKSVEKSGFHLIIRKMLESDYKFLYRDKLATGNIPDQGNSSQISQLYDSTAPSYNNASASAANSPLKLSSLLNSGEESYTQDASENVPCNLRHQDRSLQQTKRQHSAPSQISANENNIYNLGTLEEFVSSGDLTDLYHTLWNDNTSYPFL	.	PDR1 and PDR3 jointly control the transcription level of both SNQ2 and PDR5.	.	.	PDR3_YEAST	reviewed	.	.	.	.	.	.
Mol01992	Protein	Transcription factor PDR1 (PDR1)	PDR1; AMY1; ANT1; BOR2; CYH3; NRA2; SMR2; TIL1; TPE1; TPE3; YGL013C	PDR1	852871	Saccharomyces cerevisiae	4932	Saccharomyces cerevisiae	Saccharomyces	.	Saccharomycetaceae	Saccharomycetales	4892	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MRGLTPKNGVHIETGPDTESSADSSNFSTGFSGKIRKPRSKVSKACDNCRKRKIKCNGKFPCASCEIYSCECTFSTRQGGARIKNLHKTSLEGTTVQVKEETDSSSTSFSNPQRCTDGPCAVEQPTKFFENFKLGGRSSGDNSGSDGKNDDDVNRNGFYEDDSESQATLTSLQTTLKNLKEMAHLGTHVTSAIESIELQISDLLKRWEPKVRTKELATTKFYPNKSIETQLMKNKYCDVVHLTRYAAWSNNKKDQDTSSQPLIDEIFGLYSPFQFLSLQGIGKCFQNYRSKSKCEIFPRTAKETIYIMLRFFDVCFHHINQGCVSIANPLENYLQKMNLLPSTPSSISSAGSPNTAHTKSHVALVINHLPQPFVRNITGISNSELLSEMNNDISMFGILLKMLDMHKNSYQNFLMEITSNPSVAKNTQSIDVLQEFIHYCQAGEALIALCYSYYNSTLYNYVDFTCDITHLEQLLYFLDLLFWLSEIYGFEKVLNVAVHFVSRVGLSRWEFYVGLDENFAERRRNLWWKAFYFEKTLASKLGYPSNIDDSKINCLLPKNFRDVGFLDNRDFIENVHLVRRSEAFDNMCISDLKYYGELAVLQIVSHFSSSVLFNEKFTSIRNTSKPSVVREKLLFEVLEIFNETEMKYDAIKEQTGKLFDIAFSKDSTELKVSREDKIMASKFVLFYEHHFCRMVNESDNIVARLCVHRRPSILIENLKIYLHKIYKSWTDMNKILLDFDNDYSVYRSFAHYSISCIILVSQAFSVAEFIKVNDVVNMIRVFKRFLDIKIFSENETNEHVFNSQSFKDYTRAFSFLTIVTRIMLLAYGESSSTNLDVISKYIDENAPDLKGIIELVLDTNSCAYRFLLEPVQKSGFHLTVSQMLKNRKFQEPLMSNEDNKQMKHNSGKNLNPDLPSLKTGTSCLLNGIESPQLPFNGRSAPSPVRNNSLPEFAQLPSFRSLSVSDMINPDYAQPTNGQNNTQVQSNKPINAQQQIPTSVQVPFMNTNEINNNNNNNNNNKNNINNINNNNSNNFSATSFNLGTLDEFVNNGDLEDLYSILWSDVYPDS	.	Positive regulator of proteins involved in permeability. PDR1 and PDR3 jointly control the transcription level of both SNQ2 and PDR5.	.	.	PDR1_YEAST	reviewed	.	.	.	.	.	.
Mol01993	Protein	FO synthase (FBIC)	fbiC; Rv1173	FBIC	886061	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MPQPVGRKSTALPSPVVPPQANASALRRVLRRARDGVTLNVDEAAIAMTARGDELADLCASAARVRDAGLVSAGRHGPSGRLAISYSRKVFIPVTRLCRDNCHYCTFVTVPGKLRAQGSSTYMEPDEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGERGYDSTLSYVRAMAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPSMGMMLETTSRRLFETKGLAHYGSPDKDPAVRLRVLTDAGRLSIPFTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARLVLGPGMRIQAPPNLVSGDECRALVGAGVDDWGGVSPLTPDHVNPERPWPALDELAAVTAEAGYDMVQRLTAQPKYVQAGAAWIDPRVRGHVVALADPATGLARDVNPVGMPWQEPDDVASWGRVDLGAAIDTQGRNTAVRSDLASAFGDWESIREQVHELAVRAPERIDTDVLAALRSAERAPAGCTDGEYLALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSPLYLAGAARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTYALLAA	.	"Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine."	.	.	FBIC_MYCTU	reviewed	.	.	.	.	.	.
Mol01994	Protein	Probable arabinosyltransferase C (EMBC)	embC; Rv3793; MTCY13D12.27	EMBC	886112	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MATEAAPPRIAVRLPSTSVRDAGANYRIARYVAVVAGLLGAVLAIATPLLPVNQTTAQLNWPQNGTFASVEAPLIGYVATDLNITVPCQAAAGLAGSQNTGKTVLLSTVPKQAPKAVDRGLLLQRANDDLVLVVRNVPLVTAPLSQVLGPTCQRLTFTAHADRVAAEFVGLVQGPNAEHPGAPLRGERSGYDFRPQIVGVFTDLAGPAPPGLSFSASVDTRYSSSPTPLKMAAMILGVALTGAALVALHILDTADGMRHRRFLPARWWSTGGLDTLVIAVLVWWHFVGANTSDDGYILTMARVSEHAGYMANYYRWFGTPEAPFGWYYDLLALWAHVSTASIWMRLPTLAMALTCWWVISREVIPRLGHAVKTSRAAAWTAAGMFLAVWLPLDNGLRPEPIIALGILLTWCSVERAVATSRLLPVAIACIIGALTLFSGPTGIASIGALLVAIGPLRTILHRRSRRFGVLPLVAPILAAATVTAIPIFRDQTFAGEIQANLLKRAVGPSLKWFDEHIRYERLFMASPDGSIARRFAVLALVLALAVSVAMSLRKGRIPGTAAGPSRRIIGITIISFLAMMFTPTKWTHHFGVFAGLAGSLGALAAVAVTGAAMRSRRNRTVFAAVVVFVLALSFASVNGWWYVSNFGVPWSNSFPKWRWSLTTALLELTVLVLLLAAWFHFVANGDGRRTARPTRFRARLAGIVQSPLAIATWLLVLFEVVSLTQAMISQYPAWSVGRSNLQALAGKTCGLAEDVLVELDPNAGMLAPVTAPLADALGAGLSEAFTPNGIPADVTADPVMERPGDRSFLNDDGLITGSEPGTEGGTTAAPGINGSRARLPYNLDPARTPVLGSWRAGVQVPAMLRSGWYRLPTNEQRDRAPLLVVTAAGRFDSREVRLQWATDEQAAAGHHGGSMEFADVGAAPAWRNLRAPLSAIPSTATQVRLVADDQDLAPQHWIALTPPRIPRVRTLQNVVGAADPVFLDWLVGLAFPCQRPFGHQYGVDETPKWRILPDRFGAEANSPVMDHNGGGPLGITELLMRATTVASYLKDDWFRDWGALQRLTPYYPDAQPADLNLGTVTRSGLWSPAPLRRG	.	Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.	PDB: 3PTY	.	EMBC_MYCTU	reviewed	.	.	.	.	.	.
Mol01995	Protein	Probable arabinosyltransferase A (EMBA)	embA; Rv3794; MTCY13D12.28	EMBA	886123	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MPHDGNERSHRIARLAAVVSGIAGLLLCGIVPLLPVNQTTATIFWPQGSTADGNITQITAPLVSGAPRALDISIPCSAIATLPANGGLVLSTLPAGGVDTGKAGLFVRANQDTVVVAFRDSVAAVAARSTIAAGGCSALHIWADTGGAGADFMGIPGGAGTLPPEKKPQVGGIFTDLKVGAQPGLSARVDIDTRFITTPGALKKAVMLLGVLAVLVAMVGLAALDRLSRGRTLRDWLTRYRPRVRVGFASRLADAAVIATLLLWHVIGATSSDDGYLLTVARVAPKAGYVANYYRYFGTTEAPFDWYTSVLAQLAAVSTAGVWMRLPATLAGIACWLIVSRFVLRRLGPGPGGLASNRVAVFTAGAVFLSAWLPFNNGLRPEPLIALGVLVTWVLVERSIALGRLAPAAVAIIVATLTATLAPQGLIALAPLLTGARAIAQRIRRRRATDGLLAPLAVLAAALSLITVVVFRDQTLATVAESARIKYKVGPTIAWYQDFLRYYFLTVESNVEGSMSRRFAVLVLLFCLFGVLFVLLRRGRVAGLASGPAWRLIGTTAVGLLLLTFTPTKWAVQFGAFAGLAGVLGAVTAFTFARIGLHSRRNLTLYVTALLFVLAWATSGINGWFYVGNYGVPWYDIQPVIASHPVTSMFLTLSILTGLLAAWYHFRMDYAGHTEVKDNRRNRILASTPLLVVAVIMVAGEVGSMAKAAVFRYPLYTTAKANLTALSTGLSSCAMADDVLAEPDPNAGMLQPVPGQAFGPDGPLGGISPVGFKPEGVGEDLKSDPVVSKPGLVNSDASPNKPNAAITDSAGTAGGKGPVGINGSHAALPFGLDPARTPVMGSYGENNLAATATSAWYQLPPRSPDRPLVVVSAAGAIWSYKEDGDFIYGQSLKLQWGVTGPDGRIQPLGQVFPIDIGPQPAWRNLRFPLAWAPPEADVARIVAYDPNLSPEQWFAFTPPRVPVLESLQRLIGSATPVLMDIATAANFPCQRPFSEHLGIAELPQYRILPDHKQTAASSNLWQSSSTGGPFLFTQALLRTSTIATYLRGDWYRDWGSVEQYHRLVPADQAPDAVVEEGVITVPGWGRPGPIRALP	.	Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.	PDB: 7BVF	.	EMBA_MYCTU	reviewed	.	.	.	.	.	.
Mol01996	Protein	FAD-containing monooxygenase EthA (ETHA)	ethA; etaA; Rv3854c	ETHA	886175	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTEHLDVVIVGAGISGVSAAWHLQDRCPTKSYAILEKRESMGGTWDLFRYPGIRSDSDMYTLGFRFRPWTGRQAIADGKPILEYVKSTAAMYGIDRHIRFHHKVISADWSTAENRWTVHIQSHGTLSALTCEFLFLCSGYYNYDEGYSPRFAGSEDFVGPIIHPQHWPEDLDYDAKNIVVIGSGATAVTLVPALADSGAKHVTMLQRSPTYIVSQPDRDGIAEKLNRWLPETMAYTAVRWKNVLRQAAVYSACQKWPRRMRKMFLSLIQRQLPEGYDVRKHFGPHYNPWDQRLCLVPNGDLFRAIRHGKVEVVTDTIERFTATGIRLNSGRELPADIIITATGLNLQLFGGATATIDGQQVDITTTMAYKGMMLSGIPNMAYTVGYTNASWTLKADLVSEFVCRLLNYMDDNGFDTVVVERPGSDVEERPFMEFTPGYVLRSLDELPKQGSRTPWRLNQNYLRDIRLIRRGKIDDEGLRFAKRPAPVGV	.	"Monooxygenase able to convert a wide range of ketones to the corresponding esters or lactones via a Baeyer-Villiger oxidation reaction. Can act on long-chain aliphatic ketones (2-hexanone to 2-dodecanone) and on aromatic ketones (phenylacetone and benzylacetone). Is also able to catalyze enantioselective sulfoxidation of methyl-p-tolylsulfide. In vivo, likely functions as a BVMO, but the exact nature of the physiological substrate(s) remains to be established."	.	.	ETHA_MYCTU	reviewed	.	.	.	.	.	.
Mol01997	Protein	HTH-type transcriptional regulator EthR (ETHR)	ethR; etaR; Rv3855	ETHR	886189	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTTSAASQASLPRGRRTARPSGDDRELAILATAENLLEDRPLADISVDDLAKGAGISRPTFYFYFPSKEAVLLTLLDRVVNQADMALQTLAENPADTDRENMWRTGINVFFETFGSHKAVTRAGQAARATSVEVAELWSTFMQKWIAYTAAVIDAERDRGAAPRTLPAHELATALNLMNERTLFASFAGEQPSVPEARVLDTLVHIWVTSIYGENR	.	Involved in the repression of the monooxygenase EthA which is responsible of the formation of the active metabolite of ethionamide (ETH).	PDB: 1T56; PDB: 1U9N; PDB: 1U9O; PDB: 3G1L; PDB: 3G1M; PDB: 3G1O; PDB: 3O8G; PDB: 3O8H; PDB: 3Q0U; PDB: 3Q0V; PDB: 3Q0W; PDB: 3Q3S; PDB: 3QPL; PDB: 3SDG; PDB: 3SFI; PDB: 3TP0; PDB: 3TP3; PDB: 4DW6; PDB: 4M3B; PDB: 4M3D; PDB: 4M3E; PDB: 4M3G; PDB: 5EYR; PDB: 5EZG; PDB: 5EZH; PDB: 5F04; PDB: 5F08; PDB: 5F0C; PDB: 5F0F; PDB: 5F0H; PDB: 5F1J; PDB: 5F27; PDB: 5J1R; PDB: 5J1U; PDB: 5J1Y; PDB: 5J3L; PDB: 5MWO; PDB: 5MXK; PDB: 5MXV; PDB: 5MYL; PDB: 5MYM; PDB: 5MYN; PDB: 5MYR; PDB: 5MYS; PDB: 5MYT; PDB: 5MYW; PDB: 5NIM; PDB: 5NIO; PDB: 5NIZ; PDB: 5NJ0; PDB: 5NZ0; PDB: 5NZ1; PDB: 6HO0; PDB: 6HO4; PDB: 6R1P; PDB: 6R1S	.	ETHR_MYCTU	reviewed	.	.	.	.	.	.
Mol01998	Protein	Enoyl-[acyl-carrier-protein] reductase [NADH] (INHA)	inhA; Rv1484; MTCY277.05	INHA	886523	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL	.	"Enoyl-ACP reductase of the type II fatty acid syntase (FAS-II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls. Catalyzes the NADH-dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway. Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates. The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids."	PDB: 1BVR; PDB: 1ENY; PDB: 1ENZ; PDB: 1P44; PDB: 1P45; PDB: 1ZID; PDB: 2AQ8; PDB: 2AQH; PDB: 2AQI; PDB: 2AQK; PDB: 2B35; PDB: 2B36; PDB: 2B37; PDB: 2H9I; PDB: 2IDZ; PDB: 2IE0; PDB: 2IEB; PDB: 2IED; PDB: 2NSD; PDB: 2NTJ; PDB: 2NV6; PDB: 2PR2; PDB: 2X22; PDB: 2X23; PDB: 3FNE; PDB: 3FNF; PDB: 3FNG; PDB: 3FNH; PDB: 3OEW; PDB: 3OEY; PDB: 3OF2; PDB: 4BGE; PDB: 4BGI; PDB: 4BII; PDB: 4BQP; PDB: 4BQR; PDB: 4COD; PDB: 4D0R; PDB: 4D0S; PDB: 4DQU; PDB: 4DRE; PDB: 4DTI; PDB: 4OHU; PDB: 4OIM; PDB: 4OXK; PDB: 4OXN; PDB: 4OXY; PDB: 4OYR; PDB: 4QXM; PDB: 4R9R; PDB: 4R9S; PDB: 4TRJ; PDB: 4TRM; PDB: 4TRN; PDB: 4TRO; PDB: 4TZK; PDB: 4TZT; PDB: 4U0J; PDB: 4U0K; PDB: 4UVD; PDB: 4UVE; PDB: 4UVG; PDB: 4UVH; PDB: 4UVI; PDB: 5COQ; PDB: 5CP8; PDB: 5CPB; PDB: 5CPF; PDB: 5G0S; PDB: 5G0T; PDB: 5G0U; PDB: 5G0V; PDB: 5G0W; PDB: 5JFO; PDB: 5MTP; PDB: 5MTQ; PDB: 5MTR; PDB: 5OIF; PDB: 5OIL; PDB: 5OIM; PDB: 5OIN; PDB: 5OIT; PDB: 5UGS; PDB: 5UGT; PDB: 5UGU; PDB: 6EP8; PDB: 6GGM; PDB: 6GH1; PDB: 6GH4; PDB: 6GHN; PDB: 6R9W; PDB: 6SQ5; PDB: 6SQ7; PDB: 6SQ9; PDB: 6SQB; PDB: 6SQD; PDB: 6SQL; PDB: 6ZKW; PDB: 6ZKX; PDB: 6ZKY; PDB: 6ZKZ; PDB: 7E48	.	INHA_MYCTU	reviewed	.	.	.	.	.	.
Mol02000	Protein	DNA gyrase subunit A (GYRA)	gyrA; Rv0006; MTCY10H4.04	GYRA	887105	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MTDTTLPPDDSLDRIEPVDIEQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMFDSGFRPDRSHAKSARSVAETMGNYHPHGDASIYDSLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLRELADAVFWALENHDADEEETLAAVMGRVKGPDFPTAGLIVGSQGTADAYKTGRGSIRMRGVVEVEEDSRGRTSLVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVIEIKRDAVAKVVINNLYKHTQLQTSFGANMLAIVDGVPRTLRLDQLIRYYVDHQLDVIVRRTTYRLRKANERAHILRGLVKALDALDEVIALIRASETVDIARAGLIELLDIDEIQAQAILDMQLRRLAALERQRIIDDLAKIEAEIADLEDILAKPERQRGIVRDELAEIVDRHGDDRRTRIIAADGDVSDEDLIAREDVVVTITETGYAKRTKTDLYRSQKRGGKGVQGAGLKQDDIVAHFFVCSTHDLILFFTTQGRVYRAKAYDLPEASRTARGQHVANLLAFQPEERIAQVIQIRGYTDAPYLVLATRNGLVKKSKLTDFDSNRSGGIVAVNLRDNDELVGAVLCSAGDDLLLVSANGQSIRFSATDEALRPMGRATSGVQGMRFNIDDRLLSLNVVREGTYLLVATSGGYAKRTAIEEYPVQGRGGKGVLTVMYDRRRGRLVGALIVDDDSELYAVTSGGGVIRTAARQVRKAGRQTKGVRLMNLGEGDTLLAIARNAEESGDDNAVDANGADQTGN	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state, while in the absence of ATP it relaxes supercoiled dsDNA. Also catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes. Gyrase from M.tuberculosis has higher decatenation than supercoiling activity compared to E.coli; as M.tuberculosis only has 1 type II topoisomerase, gyrase has to fulfill the decatenation function of topoisomerase IV as well. At comparable concentrations M.tuberculosis gyrase cannot introduce as many negative supercoils into DNA as the E.coli enzyme, and its ATPase activity is lower, perhaps because it does not couple DNA wrapping and ATP binding as well as E.coli."	PDB: 3IFZ; PDB: 3ILW; PDB: 3UC1; PDB: 4G3N; PDB: 5BS8; PDB: 5BTA; PDB: 5BTC; PDB: 5BTD; PDB: 5BTF; PDB: 5BTG; PDB: 5BTI; PDB: 5BTL; PDB: 5BTN; PDB: 6GAU; PDB: 6GAV	.	GYRA_MYCTU	reviewed	.	.	.	.	.	.
Mol02001	Protein	D-inositol 3-phosphate glycosyltransferase (MSHA)	mshA; Rv0486; MTCY20G9.12	MSHA	887160	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAGVRHDDGSGLIAQRRPVRGEGATRSRGPSGPSNRNVSAADDPRRVALLAVHTSPLAQPGTGDAGGMNVYMLQSALHLARRGIEVEIFTRATASADPPVVRVAPGVLVRNVVAGPFEGLDKYDLPTQLCAFAAGVLRAEAVHEPGYYDIVHSHYWLSGQVGWLARDRWAVPLVHTAHTLAAVKNAALADGDGPEPPLRTVGEQQVVDEADRLIVNTDDEARQVISLHGADPARIDVVHPGVDLDVFRPGDRRAARAALGLPVDERVVAFVGRIQPLKAPDIVLRAAAKLPGVRIIVAGGPSGSGLASPDGLVRLADELGISARVTFLPPQSHTDLATLFRAADLVAVPSYSESFGLVAVEAQACGTPVVAAAVGGLPVAVRDGITGTLVSGHEVGQWADAIDHLLRLCAGPRGRVMSRAAARHAATFSWENTTDALLASYRRAIGEYNAERQRRGGEVISDLVAVGKPRHWTPRRGVGA	.	"Catalyzes the transfer of an N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol (MSH) biosynthesis pathway. MSH and WhiB3 are probably part of a regulatory circuit that mediates gene expression upon acid stress (like that found in host macrophage phagosomes). MSH is one of the major redox buffers which protects bacteria against redox stressors and antibiotics; loss of MSH or ergothioneine (ERG, the other major redox buffer in this bacteria) leads to respiratory alterations and bioenergetic deficiencies that negatively impact virulence."	.	.	MSHA_MYCTU	reviewed	.	.	.	.	.	.
Mol02002	Protein	Alanine racemase (ALR)	alr; Rv3423c; MTCY78.06	ALR	887634	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAMTPISQTPGLLAEAMVDLGAIEHNVRVLREHAGHAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLHPPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAMAEDAVRLRGLMSHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPALGDMGLVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPGPLDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVTSPRGRITRTYREAENR	.	Catalyzes the interconversion of L-alanine and D-alanine. D-alanine plays a key role in peptidoglycan cross-linking.	PDB: 1XFC; PDB: 6SCZ	.	ALR_MYCTU	reviewed	.	.	.	.	.	.
Mol02003	Protein	D-alanine--D-alanine ligase (DDL)	ddl; ddlA; Rv2981c; MTCY349.06	DDL	888415	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSANDRRDRRVRVAVVFGGRSNEHAISCVSAGSILRNLDSRRFDVIAVGITPAGSWVLTDANPDALTITNRELPQVKSGSGTELALPADPRRGGQLVSLPPGAGEVLESVDVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAVGMDKEFTKKLLAADGLPVGAYAVLRPPRSTLHRQECERLGLPVFVKPARGGSSIGVSRVSSWDQLPAAVARARRHDPKVIVEAAISGRELECGVLEMPDGTLEASTLGEIRVAGVRGREDSFYDFATKYLDDAAELDVPAKVDDQVAEAIRQLAIRAFAAIDCRGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLATMIETTLARGVGLH	.	Catalyzes the ATP-driven ligation of two D-alanine molecules to form the D-alanyl-D-alanine dipeptide. This molecule is a key building block in peptidoglycan biosynthesis.	PDB: 3LWB	.	DDL_MYCTU	reviewed	.	.	.	.	.	.
Mol02004	Protein	UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MURA)	murA; murZ; b3189; JW3156	MURA	947703	Escherichia coli	562	Escherichia coli	Escherichia	.	Enterobacteriaceae	Enterobacterales	91347	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MDKFRVQGPTKLQGEVTISGAKNAALPILFAALLAEEPVEIQNVPKLKDVDTSMKLLSQLGAKVERNGSVHIDARDVNVFCAPYDLVKTMRASIWALGPLVARFGQGQVSLPGGCTIGARPVDLHISGLEQLGATIKLEEGYVKASVDGRLKGAHIVMDKVSVGATVTIMCAATLAEGTTIIENAAREPEIVDTANFLITLGAKISGQGTDRIVIEGVERLGGGVYRVLPDRIETGTFLVAAAISRGKIICRNAQPDTLDAVLAKLRDAGADIEVGEDWISLDMHGKRPKAVNVRTAPHPAFPTDMQAQFTLLNLVAEGTGFITETVFENRFMHVPELSRMGAHAEIESNTVICHGVEKLSGAQVMATDLRASASLVLAGCIAEGTTVVDRIYHIDRGYERIEDKLRALGANIERVKGE	.	Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine. Target for the antibiotic fosfomycin.	PDB: 1A2N; PDB: 1UAE; PDB: 2Z2C; PDB: 3ISS; PDB: 3KQJ; PDB: 3KR6; PDB: 3SWD	.	MURA_ECOLI	reviewed	.	.	.	.	.	.
Mol02007	Protein	TBEV RNA-directed RNA polymerase (TBEV NS5)	TBEV NS5	.	1489719	Tick-borne encephalitis virus	11088	Tick-borne encephalitis virus	Flavivirus	11051	Flaviviridae	11050	Amarillovirales	2732545	Flasuviricetes	2732462	Kitrinoviricota	2732406	Orthornavirae	2732396	.	MVKKAILKGKGGGPPRRVSKETATKTRQPRVQMPNGLVLMRMMGILWHAVAGTARNPVLKAFWNSVPLKQATAALRKIKRTVSALMVGLQKRGKRRSATDWMSWLLVITLLGMTLAATVRKERDGSTVIRAEGKDAATQVRVENGTCVILATDMGSWCDDSLSYECVTIDQGEEPVDVDCFCRNVDGVYLEYGRCGKQEGSRTRRSVLIPSHAQGELTGRGHKWLEGDSLRTHLTRVEGWVWKNKLLALAMVTVVWLTLESVVTRVAVLVVLLCLAPVYASRCTHLENRDFVTGTQGTTRVTLVLELGGCVTITAEGKPSMDVWLDAIYQENPAKTREYCLHAKLSDTKVAARCPTMGPATLAEEHQGGTVCKRDQSDRGWGNHCGLFGKGSIVACVKAACEAKKKATGHVYDANKIVYTVKVEPHTGDYVAANETHSGRKTASFTISSEKTILTMGEYGDVSLLCRVASGVDLAQTVILELDKTVEHLPTAWQVHRDWFNDLALPWKHEGAQNWNNAERLVEFGAPHAVKMDVYNLGDQTGVLLKALAGVPVAHIEGTKYHLKSGHVTCEVGLEKLKMKGLTYTMCDKTKFTWKRAPTDSGHDTVVMEVTFSGTKPCRIPVRAVAHGSPDVNVAMLITPNPTIENNGGGFIEMQLPPGDNIIYVGELSHQWFQKGSSIGRVFQKTKKGIERLTVIGEHAWDFGSAGGFLSSIGKAVHTVLGGAFNSIFGGVGFLPKLLLGVALAWLGLNMRNPTMSMSFLLAGGLVLAMTLGVGADVGCAVDTERMELRCGEGLVVWREVSEWYDNYAYYPETPGALASAIKETFEEGSCGVVPQNRLEMAMWRSSVTELNLALAEGEANLTVVVDKFDPTDYRGGVPGLLKKGKDIKVSWKSWGHSMIWSIPEAPRRFMVGTEGQSECPLERRKTGVFTVAEFGVGLRTKVFLDFRQEPTHECDTGVMGAAVKNGMAIHTDQSLWMRSMKNDTGTYIVELLVTDLRNCSWPASHTIDNADVVDSELFLPASLAGPRSWYNRIPGYSEQVKGPWKYTPIRVIREECPGTTVTINAKCDKRGASVRSTTESGKVIPEWCCRACTMPPVTFRTGTDCWYAMEIRPVHDQGGLVRSMVVADNGELLSEGGVPGIVALFVVLEYIIRRRPSTGTTVVWGGIVVLALLVTGMVRIESLVRYVVAVGITFHLELGPEIVALMLLQAVFELRVGLLSAFALRRSLTVREMVTTYFLLLVLELGLPGASLEEFWKWGDALAMGALIFRACTAEGKTGAGLLLMALMTQQDVVTVHHGLVCFLSVASACSVWRLLKGHREQKGLTWVVPLAGLLGGEGSGIRLLAFWELSAHRGRRSFSEPLTVVGVMLTLASGMMRHTSQEALCALAVASFLLLMLVLGTRKMQLVAEWSGCVEWYPELVNEGGEVSLRVRQDAMGNFHLTELEKEERMMAFWLIAGLAASAIHWSGILGVMGLWTLTEMLRSSRRSDLVFSGQGGRERGDRPFEVKDGVYRIFSPGLFWGQNQVGVGYGSKGVLHTMWHVTRGAALSIDDAVAGPYWADVREDVVCYGGAWSLEEKWKGETVQVHAFPPGRAHEVHQCQPGELILDTGRKLGAIPIDLVKGTSGSPILNAQGVVVGLYGNGLKTNETYVSSIAQGEAEKSRPNLPQAVVGTGWTSKGQITVLDMHPGSGKTHRVLPELIRQCIDRRLRTLVLAPTRVVLKEMERALNGKRVRFHSPAVSDQQAGGAIVDVMCHATYVNRRLLPQGRQNWEVAIMDEAHWTDPHSIAARGHLYTLAKENKCALVLMTATPPGKSEPFPESNGAITSEERQIPDGEWRDGFDWITEYEGRTAWFVPSIAKGGAIARTLRQKGKSVICLNSKTFEKDYSRVRDEKPDFVVTTDISEMGANLDVSRVIDGRTNIKPEEVDGKVELTGTRRVTTASAAQRRGRVGRQDGRTDEYIYSGQCDDDDSGLVQWKEAQILLDNITTLRGPVATFYGPEQDKMPEVAGHFRLTEEKRKHFRHLLTHCDFTPWLAWHVAANVSSVTDRSWTWEGPEANAVDEASGDLVTFRSPNGAERTLRPVWKDARMFKEGRDIKEFVAYASGRRSFGDVLTGMSGVPELLRHRCVSALDVFYTLMHEEPGSRAMRMAERDAPEAFLTMVEMMVLGLATLGVIWCFVVRTSISRMMLGTLVLLASLLLLWAGGVGYGNMAGVALIFYTLLTVLQPEAGKQRSSDDNKLAYFLLTLCSLAGLVAANEMGFLEKTKADLSTALWSEREEPRPWSEWTNVDIQPARSWGTYVLVVSLFTPYIIHQLQTKIQQLVNSAVASGAQAMRDLGGGAPFFGVAGHVMTLGVVSLIGATPTSLMVGVGLAALHLAIVVSGLEAELTQRAHKVFFSAMVRNPMVDGDVINPFGEGEAKPALYERKMSLVLATVLCLMSVVMNRTVASITEASAVGLAAAGQLLRPEADTLWTMPVACGMSGVVRGSLWGFLPLGHRLWLRASGGRRGGSEGDTLGDLWKRRLNNCTREEFFVYRRTGILETERDKARELLRRGETNVGLAVSRGTAKLAWLEERGYATLKGEVVDLGCGRGGWSYYAASRPAVMSVRAYTIGGKGHEAPKMVTSLGWNLIKFRSGMDVFSMQPHRADTVMCDIGESSPDAAVEGERTRKVILLMEQWKNRNPTAACVFKVLAPYRPEVIEALHRFQLQWGGGLVRTPFSRNSTHEMYYSTAVTGNIVNSVNVQSRKLLARFGDQRGPTKVPELDLGVGTRCVVLAEDKVKEQDVQERIRALREQYSETWHMDEEHPYRTWQYWGSYRTAPTGSAASLINGVVKLLSWPWNAREDVVRMAMTDTTAFGQQRVFKDKVDTKAQEPQPGTRVIMRAVNDWILERLAQKSKPRMCSREEFIAKVKSNAALGAWSDEQNRWASAREAVEDPAFWRLVDEERERHLMGRCAHCVYNMMGKREKKLGEFGVAKGSRAIWYMWLGSRFLEFEALGFLNEDHWASRESSGAGVEGISLNYLGWHLKKLSTLNGGLFYADDTAGWDTKVTNADLEDEEQILRYMEGEHKQLATTIMQKAYHAKVVKVARPSRDGGCIMDVITRRDQRGSGQVVTYALNTLTNIKVQLIRMMEGEGVIEAADAHNPRLLRVERWLKEHGEERLGRMLVSGDDCVVRPLDDRFGKALYFLNDMAKTRKDIGEWEHSAGFSSWEEVPFCSHHFHELVMKDGRTLVVPCRDQDELVGRARISPGCGWSVRETACLSKAYGQMWLLSYFHRRDLRTLGLAINSAVPADWVPTGRTTWSIHASGAWMTTEDMLDVWNRVWILDNPFMQNKERVMEWRDVPYLPKAQDMLCSSLVGRRERAEWAKNIWGAVEKVRKMIGPEKFKDYLSCMDRHDLHWELRLESSII	.	"Replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in RNA genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway."	PDB: 1N6G; PDB: 1NA4; PDB: 1SVB; PDB: 1URZ; PDB: 6J5G; PDB: 6S8C; PDB: 7LSF; PDB: 7LSG	.	POLG_TBEVW (2512-3414)	reviewed	.	.	.	.	.	.
Mol02008	Protein	Fusion glycoprotein F0 (MV HRB)	FUS	FUS	1489800	Measles morbillivirus	645098	Measles morbillivirus	Morbillivirus	11229	Paramyxoviridae	11158	Mononegavirales	11157	Monjiviricetes	2497574	Negarnaviricota	2497569	Orthornavirae	2732396	.	MGLKVNVSAIFMAVLLTLQTPTGQIHWGNLSKIGVVGIGSASYKVMTRSSHQSLVIKLMPNITLLNNCTRVEIAEYRRLLRTVLEPIRDALNAMTQNIRPVQSVASSRRHKRFAGVVLAGAALGVATAAQITAGIALHQSMLNSQAIDNLRASLETTNQAIEAIRQAGQEMILAVQGVQDYINNELIPSMNQLSCDLIGQKLGLKLLRYYTEILSLFGPSLRDPISAEISIQALSYALGGDINKVLEKLGYSGGDLLGILESRGIKARITHVDTESYFIVLSIAYPTLSEIKGVIVHRLEGVSYNIGSQEWYTTVPKYVATQGYLISNFDESSCTFMPEGTVCSQNALYPMSPLLQECLRGSTKSCARTLVSGSFGNRFILSQGNLIANCASILCKCYTTGTIINQDPDKILTYIAADHCPVVEVNGVTIQVGSRRYPDAVYLHRIDLGPPISLERLDVGTNLGNAIAKLEDAKELLESSDQILRSMKGLSSTSIVYILIAVCLGGLIGIPALICCCRGRCNKKGEQVGMSRPGLKPDLTGTSKSYVRSL	.	"Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity)."	PDB: 5YXW; PDB: 5YZC; PDB: 5YZD	.	FUS_MEASC	reviewed	.	.	.	.	.	.
Mol02009	Protein	C-22 sterol desaturase ERG5 (ERG5)	ERG5; CYP61; orf19.5178; CAALFM_C702840CA	ERG5	3641400	Candida albicans	237561	Candida albicans	Candida	5475	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MNSTEVDNLPFQQQLTSFVELAVAKATGSPITTLFTIIFLILSYDQLSYQINKGSIAGPRFKFYPIIGPFLESLDPKFEEYKAKWDSGELSCVSIFHKFVVIASSRDLARKILSSPKYVKPCVVDVAIKILRPTNWVFLDGKQHTDYRRSLNGLFSSKALEIYIPVQEKYMDIYLERFCKYDGPREFFPEFRELLCALSLRTFCGDYITEDQIALVADNYYRVTAALELVNFPIIIPYTKTWYGKKIADDTMKIFENCAAMAKKHINENNGTPKCVMDEWIHLMKEAREKHSEDPDSKLLVREFSNREISEAIFTFLFASQDASSSLACWLFQIVADRPDIVAKIREEQLRVRNNNPDVRLSLDLINEMTYTNNVVKESLRYRPPVLMVPYVVKKSFPVTESYTAPKGAMIIPTLYPALHDPEVYDEPDSFIPERWENASGDMYKRNWLVFGTGPHVCLGKNYVLMLFTGMLGKFVMNSDMIHHKTDLSEEIKVFATIFPKDDLILEWKKRDPLKSL	.	"C-22 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Probable). ERG5 converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable)."	.	.	ERG5_CANAL	reviewed	.	.	.	.	.	.
Mol02010	Protein	Multidrug resistance regulator 1 (MRR1)	MRR1; HAP1; CAALFM_C305920WA; CaO19.7372	MRR1	3641741	Candida albicans	237561	Candida albicans	Candida	5475	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MSIATTPIETPKSPKSTEPQVRKRKKVSTVCTNCRKRKIRCDRQHPCNNCIKSKKHNACVYDDGQVSPANFSTNGSSHGNTVPESRPYEESARIPIRFDAEAPRKKSKPNTPNNERKNSKKSPDNTVANNQQTASENEVTITLSELNMLKQRLQNIEANINAQSNPQSNPSYVPQTPAYPTQPNILPPPVSFNSWSPKQSNERVMFSPQQRLTTNYNVSHTRGQSPSIQLPPLSFKDTPRASIDSAPLYSEMSPPRSDLIASSLTSPESIQMSVSGDVVGVNPYLNETETINFYDGYTSICVRDFRRVNHGPFAWSSLMRKDKALSSLWNHILKKKEKKNVASQTFVFGQDVHEISQENTQLVASESNESETKFKKKTLETFGFNDVVPYDILKKKLQTQINKTTSPLGLTLYEEQVNMELQLVDRIHQQLPKKKVLWKLIDRFFSLLYPFMPFLDEIDFRESVTKIIGETEYKDEKIKELKVEKRLDLAVIGVLLIILRMSYLSLFCNKESVNEMRLKTTDPSPEAQDMKYLLQNPIGISLIDSAQNCLQYFDIFRKTSMPVLQCAYFLQLYHIFAPEDGDDGDGADTYALNSMVVRMAYSMGLNREPDNFKDVLNDKRQNHLGRKIWHFLVIGDVHNSYAFGTPKLIGDDFYDTKVPFIEEGNENLIDKSLDQYVTKSVFPGYFSIYNSVDQILKLILSVSRRSKVSEICKILNQFEIGIAEQYGTLSDCLKPKENLIHIFARNMPVKMYISLKSFLVSVYFHLFLYYEHKNDSLSFFYLRKILKTGAGDIMPHYFELLGNSEVVCDMVINPKLIQIIHKANQINIALIIRVNMSIYRMKNSQHHAENCKKDDFYYSYYKELCKFSSCLTRCAEVGIAAVSKLSTRYYYAWKITKGHNFLLKTITSMEFYEKESTNAQEITLPKYKLEQIADLENICEVALNKLGKTSVMGDEFCSNVNYKKYKGDQTYSTSSESSSTPNKDSPLDSRKYTNDFGLDLVNNQEIDKIWLQMLSLKSEEAQQQRQQESQPFTSSQSQSQSPLTSANQGYMPRPESRRGSYYGNTPFALENLNFDGFGGQSKSSNNGEADLSSFDFFVDLPFDQLFTN	.	"Transcription factor that acts as the central regulator of the MDR1 efflux pump. Other target genes include those encoding oxidoreductases, whose up-regulation in fluconazole-resistant isolates may help to prevent cell damage resulting from the generation of toxic molecules in the presence of fluconazole and thereby contribute to drug resistance."	.	.	MRR1_CANAL	reviewed	.	.	.	.	.	.
Mol02011	Protein	Delta(7)-sterol 5(6)-desaturase ERG3 (ERG3)	ERG3; orf19.767; CAALFM_C104770CA	ERG3	3644776	Candida albicans	237561	Candida albicans	Candida	5475	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MDIVLEICDYYLFDKVYADVFPKDGAVHEFLKPAIQSFSQIDFPSLPNLDSFDTNSTLISSNNFNISNVNPATIPSYLFSKIASYQDKSEIYGLAPKFFPATDFINTSFLARSNIFRETLSLFIITTIFGWLLYFIVAYLSYVFVFDKKIFNHPRYLKNQMSLEIKRATTAIPVMVLLTIPFFLLELNGYSFLYLDINECTGGYKAILWQIPKFILFTDCGIYFLHRWLHWPSVYKVLHKPHHKWIVCTPFASHAFHPVDGFFQSLPYHLYPLLFPLHKVLYLFLFTFVNFWTVMIHDGSYWSNDPVVNGTACHTVHHLYFNYNYGQFTTLWDRLGNSYRRPDDSLFVKDAKAEEEKKIWKEQTRKMEEIRGEVEGKVDDREYVEQ	.	"C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathwa. ERG3 catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable)."	.	.	ERG3_CANAL	reviewed	.	.	.	.	.	.
Mol02012	Protein	multidrug resistance regulator 2 (MRR2)	MRR2; ZCF34; CAALFM_C307860CA; CaO19.6182	MRR2	3647468	Candida albicans	237561	Candida albicans	Candida	5475	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MTKRDRTIYSCDACRSRKIKCNRQTPCASCHKSKRDCVYTVSRQRDAQITNRKLDKKTYHQISAIEKKISALEGKKGLLQVETINFNKSFTDQTPLVELQSLFPYLLLSKQDPGCVLVRHHCHHLLEKDPRYFEYSQLLADLSLTKRHHLTARAKALLGEAYIPSPQEGHTIDQLKHVLSLNPNFRFAGNFADPLTSFFSLIPPAWANKQLVDTFFQHIYPVIPIIDETDFNTSINRVLGPQIDGHYINSFPSIGSADDLPFLALFLLVLRISYMYTPGACPVSYDTLRAAETIMKEFDITKTHSLTALQAEIMLRFYKIVAPESYTQSNYVQVSVGVLIQNCYSLALHRDPEYIGEHNPKQQHLRRKIWHLLLRMEVIDSAIFQTILSSNPDASDTKLPQLIDQAPPMEQSIVKHIWRSTDLFVSLRKLVEINSKTSEDTPLETVLELLVEVETKLQAFLATIDSEASTVFYNDLVIFSVNFLLVYMYYSLYLFKGPTPLGNKYLLKSAQILFVDLARTRSTSLFLAYFNLNYIHLVLMITNFLRMRVDCIIHRHLRAQDSSVQDLQCCRYFLKIIFFSHVKELGNYSSSHKYAWQMRKVYLTLAKIMERSSDVLISNDPELVKSAAVDIPVKEINKLLEQYINFKGFTPTTLFDPTDNELIDEMQHENLWNAMENIEYSEKVYSGWIDAIKNVPSNWDWDYWDFLKIS	.	"Transcription factor that controls the expression of CDR1, the major multidrug efflux pump. Required for yeast cell adherence to silicone substrate and plays a role in virulence."	.	.	MRR2_CANAL	reviewed	.	.	.	.	.	.
Mol02013	Protein	Aminoacyltransferase FemB (FEMB)	femB; SAOUHSC_01374	FEMB	3920783	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKFTELTVTEFDNFVQNPSLESHYFQVKENIVTRENDGFEVVLLGIKDDNNKVIAASLFSKIPTMGSYVYYSNRGPVMDFSDLGLVDYYLKELDKYLQQHQCLYVKLDPYWLYHLYDKDIVPFEGREKNDALVNLFKSHGYEHHGFTTEYDTSSQVRWMGVLNLEGKTPETLKKTFDSQRKRNINKAINYGVKVRFLERDEFNLFLDLYRETEERAGFVSKTDDYFYNFIDTYGDKVLVPLAYIDLDEYVLKLQQELNDKENRRDQMMAKENKSDKQMKKIAELDKQIDHDQHELLNASELSKTDGPILNLASGVYFANAYEVNYFSGGSSEKYNQFMGPYMMHWFMINYCFDNGYDRYNFYGLSGDFTENSEDYGVYRFKRGFNVQIEELIGDFYKPIHKVKYWLFTTLDKLRKKLKK	.	"Catalyzes the formation of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. Adds glycines 4 and 5 of the pentaglycine bridge, using glycyl-tRNA(Gly) as donor. Involved in resistance to methicillin."	.	.	FEMB_STAA8	reviewed	.	.	.	.	.	.
Mol02014	Protein	Multidrug resistance protein MdtE (MDTE)	TVAG_572140	MDTE	4741312	Trichomonas vaginalis	5722	Trichomonas vaginalis	Trichomonas	5721	Trichomonadidae	181550	Trichomonadida	37104	.	.	Parabasalia	5719	.	.	.	MSNNIKLVVVGDGAVGKTCLLVVYARNEFPSEYVPTVFDNYTAKVKIDDTLYPVQLWDTAGQEELENIRTLSYQNTSVFLLCFSVTTPTTFDNLTTVWIPEIKRYVKNPEILLIGTKADLRNDEQTLKNLEADGKAPITLEQAQQKAKEIGAIAYCECSALKNEGVREAFDKAINHIIEKDNGGCCHLI	.	.	.	.	A2GGN6_TRIVA	unreviewed	.	.	.	.	.	.
Mol02015	Protein	ABC transporter family protein (ABC)	TVAG_605460	ABC	4742937	Trichomonas vaginalis	5722	Trichomonas vaginalis	Trichomonas	5721	Trichomonadidae	181550	Trichomonadida	37104	.	.	Parabasalia	5719	.	.	.	MKASKTRITDVFRVFWNASSWFSTLILGTILIFALGELIVGNYSGLYPSKLMKYITKKDTKQFGHDLYIYAFFLVGSVLILGIKLWLCDRLSIRFRDKLVQQIHKDYMTGNSFYDLLMYDTHIDNPDGRITQDIENYGETSIKVIVAAAQSPLIIAYYSYSTFKDMGLNSLLITLLFTTVSFFATRFAMSPIVRLTYKFEAANADFRTAHVNLKENAETIALSRGQSAEEKLLSDRLASVLSVQKQLSNTSIILNIVVNICQYFGNALVYLCIYICAPATEDPSILAEFTGRVSFEVIMLISGITSLMNVINDFSKLSGYSTRIQELLSILREQAEHVNINKFGNSFVLENATVMRPSGDSLINDLNLTVRPGESLFIVGPSGAGKSSLFRVLGGIWPIKSGKVTIPEEKTMILTQRPYVPRNATLEEAIAFPKELNEVDLFEIQNTLRLLKIEHLKLRDDEDWWVGLSPGEQQRVAIARILVHRPTFALLDEATSAIPSKLEEEIFKVLAQKDITCITIAHNKELRKWHKNVLELTGNGRYSIY	.	.	.	.	A2GC20_TRIVA	unreviewed	.	.	.	.	.	.
Mol02016	Protein	ABC transporter G family member 6 (ABCG6)	ABCG6; LMJF_36_2890	ABCG6	5655579	Mycobacteroides abscessus	38568	Mycobacteroides abscessus	Mycobacteroides	670516	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSSPAPPTDRADAGLLHHLPHSPPESPESSAPPPASSHRTAVLTWEDVSYTVSGADEGDTRILVRHVSGYVQSGEMLAVLGPSGAGKTTLLDILAQRKVKSKGDITGRIMLNGEPVEPAAFQLCSGYVQQEDIMHSYVTVEEVVRFSATLRTSPTISEEVLESRVSQVLRQLGIYHVRHSCIGSALVRGISGGERKRCAVAAEMVTLPSLLFLDEPTTGLDTFTALHLLTLLRSLSRSGVAVVFSIHQPRSRIYEAFDRVLLLNGFGEEAYFGPAADAVQFLAEIGLSSGCSSNPADYLIDAVSVSPVEEAWLSEEAQQSAAVEAATDGNQLRLPSPAPTQGRDIAAAFASLRLADVMRQIDELQRSSRAATAALAETGSPVRAYPRSWTTQVRCIAMRCLRNRRRDPVATYVSVTSAIVFAFLTGTIYYQVGNSQDSIRSRMGVLFFIMMISTFSSLGSLEMFLTDRAIYAREHRNGMYSTSAYYVGKFIQDAPIVVAINFLFNLIVYLLVGLQGTVAKFLIFDSVGALVTLNSYALCLLMSNLSKDYATGNIITSLLLVLYLLPTGGMLVSLNSIPFMWRWIKHISFARFAFSVMVANEFDGLTFVCDPVPSDIAPCITSGTTYAASQGMYAKDIRSHMLVVALSMAVYLVLGYLALRGWRSTEGK	.	.	.	.	Q4Q1D0_LEIMA	unreviewed	.	.	.	.	.	.
Mol02019	Protein	ATP binding cassette subfamily G member 4 (ABCG4)	ABCG4; LPMP_150900	ABCG4	22573510	Mycobacteroides abscessus	38568	Mycobacteroides abscessus	Mycobacteroides	670516	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MGKQVDQVYNPSARTLTPPLRETSEQVALRNTPVDTTDALAMPPLSESDGKDTKVPTCSRAVNFTWENLTYQVPVEDKDGNVTYKTLLFNLSGCAKGGRVLAIMGPSGAGKTTLMGTITGKLYNATARQEGCCFMNNNIYQQRYKRLVSYVCQDDIVMGKDTPREAIFFSARLRLGLDSSTARRRTADVIKRLSLTRCQDTILGIPGILKGVSGGERKRTNIGTELITNPFVMLLDEPTTGLDSVNAVRVGQLLQDLAKNDMRTVIATVHSPSSELFDLFDDLLLLAKGHVIYHGPTADSIEYFASLGYDVPPRTNPTEYFMNLLQLPEDILSQLWLAWEDYVMSDAARYNPCLTPVTGAITLTDDYLEEQLELKGASFCLQFSELFKRSWRMYLRDPGNFYGRSVQTLFFAIFLGLFFFNVQLNQQGVQDRQGALYMTLMNNLFGAAMNGIAAFPPERAVFLQEQANDAYNAYTYFLAKNAAELPWQILFPTLFDLIAYFLIHFHRSADAFFVHWFILVLLANLGYAFGLMFATFFKQSQAAFAMVPLILLPLFIVAGLFASTDRLYPYWVWLNYLSFPRHAYLGVFTNEFERLTVICSPVTPLCTFPDGQSVIEHMGFQNWRYWQSFIALIVYQIGLRFIGATSLFFQGRKRRGKLQFVKNLRHRVASPRAIASARSNDVLSDVQSTLVGSIATPSNAYGAETSLRDHQEPHHSLWGNEIELAALSPLDTPVTFEESPISVREKKHRY	.	.	.	HGNC:13884	A0A088RLA3_9TRYP	unreviewed	.	.	.	.	.	.
Mol02020	Protein	Enoyl-CoA hydratase 2 (HADA)	hadA; NCGM2209_1021	HADA	45424594	Mycobacterium tuberculosis	1773	Mycobacterium tuberculosis	Mycobacterium	.	Mycobacteriaceae	Corynebacteriales	85007	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MALSADIVGMHYRYPDHYEVEREKIREYAVAVQNDDAWYFEEDGAAELGYKGLLAPLTFICVFGYKAQAAFFKHANIATAEAQIVQVDQVLKFEKPIVAGDKLYCDVYVDSVREAHGTQIIVTKNIVTNEEGDLVQETYTTLAGRAGEDGEGFSDGAA	.	.	.	.	A0A7U9PK65_MYCTX	unreviewed	.	.	.	.	.	.
Mol02021	Protein	Short-chain diamines transporter (PACE)	aceI; A1S_2063	PACE	56377069	Acinetobacter baumannii	470	Acinetobacter baumannii	Acinetobacter	.	Moraxellaceae	Moraxellales	2887326	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MLISKRRLIHAISYEGILLVIIAIALSFIFNMPMEVTGTLGVFMAVVSVFWNMIFNHYFEKVEHKYNWERTIPVRILHAIGFEGGLLIATVPMIAYMMQMTVIDAFILDIGLTLCILVYTFIFQWCYDHIEDKFFPNAKAASLH	.	"Mediates the efflux of short-chain diamines when energized by an electrochemical gradient. Recognizes specifically the short-chain diamines cadaverine and putrescine as substrates, and promotes the active transport of these substrates in exchange for a cation. Protons are probably the primary source of energy for transport, however it was not possible to conclude with complete certainty that protons, rather than alternative cations such as Na(+) ions, are exchanged for substrates by AceI. In addition, is involved in resistance to the synthetic biocide chlorhexidine, a widely used antiseptic and disinfectant in both hospital and community settings. Interacts directly with chlorhexidine and mediates its efflux via an energy-dependent mechanism."	.	.	PACE_ACIBT	reviewed	.	.	.	.	.	.
Mol02022	Protein	Beta-lactamase (Q9X4S7)	cfxA2; CLI70_02470; CTI18_10205; CTM44_04660; CTM46_08920; CTM50_00090; CTM53_10840; CTM59_09130; CTM62_10610; CUB95_12895; CUB97_12180	Q9X4S7	57246820	Prevotella intermedia	28131	Prevotella intermedia	Prevotella	838	Prevotellaceae	171552	Bacteroidales	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS	.	.	.	.	Q9X4S7_PREIN	unreviewed	.	.	.	.	.	.
Mol02023	Protein	Beta-lactamase (BLAC)	blaZ	BLAC	58063709	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKKLIFLIVIALVLSACNSNSSHAKELNDLEKKYNAHIGVYALDTKSGKEVKFNSDKRFAYASTSKAINSAILLEQVPYNKLNKKVHINKDDIVAYSPILEKYVGKDITLKALIEASMTYSDNTANNKIIKEIGGIKKVKQRLKELGDKVTNPVRYEIELNYYSPKSKKDTSTPAAFGKTLNKLIANGKLSKENKKFLLDLMLNNKSGDTLIKDGVPKDYKVADKSGQAITYASRNDVAFVYPKGQSEPIVLVIFTNKDNKSDKPNDKLISETAKSVMKEF	.	.	PDB: 1ALQ; PDB: 1BLC; PDB: 1BLH; PDB: 1BLP; PDB: 1DJA; PDB: 1DJB; PDB: 1DJC; PDB: 1GHI; PDB: 1GHM; PDB: 1GHP; PDB: 1KGE; PDB: 1KGF; PDB: 1KGG; PDB: 1OME; PDB: 1PIO; PDB: 3BLM; PDB: 6WGR	.	BLAC_STAAU	reviewed	.	.	.	.	.	.
Mol02024	Protein	Metallo-beta-lactamase type 2 (BLAN1)	blaNDM-1	BLAN1	61419528	Klebsiella pneumoniae	573	Klebsiella pneumoniae	Klebsiella	.	Enterobacteriaceae	Enterobacterales	91347	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR	.	"Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin."	PDB: 3PG4; PDB: 3RKJ; PDB: 3RKK; PDB: 3SBL; PDB: 3SFP; PDB: 3SPU; PDB: 3SRX; PDB: 3ZR9; PDB: 4EXS; PDB: 4EXY; PDB: 4EY2; PDB: 4EYB; PDB: 4EYF; PDB: 4EYL; PDB: 4GYQ; PDB: 4GYU; PDB: 4H0D; PDB: 4HKY; PDB: 4HL1; PDB: 4HL2; PDB: 4RAM; PDB: 4RAW; PDB: 4RBS; PDB: 4RL0; PDB: 4RL2; PDB: 4RM5; PDB: 4U4L; PDB: 5A5Z; PDB: 5JQJ; PDB: 5K4M; PDB: 5N0H; PDB: 5N0I; PDB: 5NBK; PDB: 5O2E; PDB: 5O2F; PDB: 5WIG; PDB: 5XP6; PDB: 5XP9; PDB: 5ZGE; PDB: 5ZGF; PDB: 5ZGI; PDB: 5ZGP; PDB: 5ZGQ; PDB: 5ZGR; PDB: 5ZGT; PDB: 5ZGU; PDB: 5ZGV; PDB: 5ZGW; PDB: 5ZGX; PDB: 5ZGY; PDB: 5ZGZ; PDB: 5ZH1; PDB: 5ZIO; PDB: 5ZJ1; PDB: 5ZJ2; PDB: 5ZJ7; PDB: 5ZJ8; PDB: 5ZJC; PDB: 6C6I; PDB: 6CAC; PDB: 6D1A; PDB: 6D1B; PDB: 6D1C; PDB: 6D1D; PDB: 6D1E; PDB: 6D1F; PDB: 6D1G; PDB: 6D1H; PDB: 6D1I; PDB: 6D1J; PDB: 6D1K; PDB: 6EFJ; PDB: 6EX7; PDB: 6IBS; PDB: 6IBV; PDB: 6JKB; PDB: 6LHE; PDB: 6LIP; PDB: 6LIZ; PDB: 6LJ0; PDB: 6LJ1; PDB: 6LJ2; PDB: 6LJ4; PDB: 6LJ5; PDB: 6LJ6; PDB: 6LJ7; PDB: 6LJ8; PDB: 6MDU; PDB: 6MGY; PDB: 6MGZ; PDB: 6NY7; PDB: 6O3R; PDB: 6Q2Y; PDB: 6Q30; PDB: 6RMF; PDB: 6TWT; PDB: 6V1M; PDB: 6ZYP; PDB: 6ZYQ	.	BLAN1_KLEPN	reviewed	.	.	.	.	.	.
Mol02025	Protein	rRNA adenine N-6-methyltransferase (ErmB)	ermB; erm(B); ermBP; BN1095_710032; BN1096_640001; BN1097_650002; SAMEA1531904_02452; Tn6215_11	ErmB	64019358	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKLNTRVTLIHQDILQFQFPNKQRYKIVGSIPYHLSTQIIKKVVFESHASDIYLIVEEGFYKRTLDIHRTLGLLLHTQVSIQQLLKLPAECFHPKPKVNSVLIKLTRHTTDVPDKYWKLYTYFVSKWVNREYRQLFTKNQFHQAMKHAKVNNLSTVTYEQVLSIFNSYLLFNGRK	.	.	.	.	Q7AYX9_CLODI	unreviewed	.	.	.	.	.	.
Mol02026	Protein	4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ISPH)	ispH; CD630_18180	ISPH	66354236	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MNIKIAKNAGFCFGVKRAMKMAWDEVEKNDSGIYALGPLIHNKQAVAKYEEKGLKTVNEIDTIPNHENMIIRSHGVPENIYKEAKDKKLKIVDTTCPFVKKIHTVVSEYHNKGYEIIVIGDMKHPEVIGINGWCENSAIIIKTLEQMENMEFDNSKRYCLVAQTTINPELYISIVNKLSDKLEEIVFNDTICSATKTRQESAKELAKEVDCMIVIGGKHSSNTQKLVKVCEDLVPTFAIETKDELDVNTLKKYKNLGITAGASTPNWIIEEVVTFLENL	.	Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.	.	.	ISPH_CLOD6	reviewed	.	.	.	.	.	.
Mol02027	Protein	Ribosomal tetracycline resistance protein tet (TET(44))	BGV00_19340; BN1095_620053; BN1096_520088; BN1097_680096; E5F26_13010; E5F27_11275; E5F28_08645; E5F29_03080; E5F30_14860; E5F31_09375; E5F32_08895; E5F33_19320; E5F34_11670; E5F35_02795; E5F36_15070; E5F37_19425; E5F38_19050; E5F39_10665; E5F40_01415; E5F41_11825; E5F42_18275; E5F43_02490; E5F44_06595; E5F45_10465	TET(44)	66355013	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKTNNMKQAILSSATNLIAKNGVQNTSLADIAKDVNISKGTLYYHYASKDDIIYDIADTHLEVITSAILNCVKNVKSKNSQIEMVNLILEKISTIESRGRVHMYLICEAITSNNDLKERIRLKYIEWRTTLKSEIVESLEKYNSSENEQDAESFSFLLMSIVDGLVVQSLLKTEKIPYENIASFLVNHWI	.	.	.	.	A0A031WAZ8_CLODI	unreviewed	.	.	.	.	.	.
Mol02028	Protein	OXA-23 carbapenemase (BLA OXA-23)	ari-1; bla(OXA-23); bla-OXA-23; bla-oxa-23; bla_1; bla_2; bla_3; blaOXA-23; blaOXA23; OXA-23; oxa-23; oxa23; A7M90_19440; ABUW_0563; ACX61_17625; ACX61_20055; AYR68_05160; AYR68_16375; B7L45_15940; B7L45_16275; BAA1790NC_2235; BAA1790NC_2239; BAA1790NC_2243; CBE85_20255; CBL15_02250; CBL15_17480; DLI71_13510; DLI72_20175; DVA69_16975; E2532_00765; E2533_00255; E2534_00245; E2535_00255; E2536_01300; E2538_00225; E2539_00710; E2540_01480; E2541_00230; EA686_06705; EA720_018585; EGM95_08810; F2P40_21140; FDN00_02125; FDN00_19010; FGL68_16065; FJU36_20505; G3N53_19695; GNY86_20740; HB367_12275; HBK86_19320; HBK86_20965; HIN86_20200; IAG11_18825; ITE13_20155; NCTC13421_03368; NCTC13421_03411; NG19_0098; SAMEA104305318_04148; SAMEA104305385_00775	BLA OXA-23	66373343	Acinetobacter baumannii	405416	Acinetobacter baumannii	Acinetobacter	469	Moraxellaceae	468	Moraxellales	2887326	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNKYFTCYVVASLFLSGCTVQHNLINETPSQIVQGHNQVIHQYFDEKNTSGVLVIQTDKKINLYGNALSRANTEYVPASTFKMLNALIGLENQKTDINEIFKWKGEKRSFTAWEKDMTLGEAMKLSAVPVYQELARRIGLDLMQKEVKRIGFGNAEIGQQVDNFWLVGPLKVTPIQEVEFVSQLAHTQLPFSEKVQANVKNMLLLEESNGYKIFGKTGWAMDIKPQVGWLTGWVEQPDGKIVAFALNMEMRSEMPASIRNELLMKSLKQLNII	.	.	PDB: 4JF4; PDB: 4JF5; PDB: 4JF6; PDB: 4K0X; PDB: 6N6T; PDB: 6N6U; PDB: 6N6V; PDB: 6N6W; PDB: 6N6X; PDB: 6N6Y	.	Q9L4P2_ACIBA	unreviewed	.	.	.	.	.	.
Mol02029	Protein	FAD-containing monooxygenase EthA (ETHA)	ethA_2; I3U33_00520; SAMEA2071181_01734	ETHA	66970488	Mycobacteroides abscessus	36809	Mycobacteroides abscessus	Mycobacteroides	670516	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MSEHFDVLIVGAGISGISAAWHIQDRCPTKTYAVLEARDDMGGTWNLFKYPGIRSDSDMYTLGFRFSPWNDSRTLADGPSILDYVHKTAANAGIDGHVRYRQKVVGAAWNTETQQWTVEVDHDGKTIEYTCSFLFCCSGYYDYDQGYSPEFPGVADFKGTVVHPQHWPEDLDYKGKKVVVIGSGATAVTLVPAMAPDTGHITMLQRSPTYIMSLPNENPIINGLRKILPPKVAYPIARWINIGQLIFSYQASRKFPRAARRIIMQQAKLQLPKGFDYKTHFGPKYNPWDERLCVVPNGDLYKAIRKGKADIVTDHIETFDETGIKLKSGKHLDADIIITATGLNLKFFSGVIPTVDGVPVDLPAQTVYKGAMLTGIPNMAFTIGYTNASWTLKADLVSEYVSRLLNYMDENGYVTAVPELADETLEKQPFMDFTPGYVLRALDELPKQGNKHPWRLKQNYAYDIGMMRRSRVTEGMRFGRKKTAAAPASESVAVNS	.	.	.	.	A0A1N2GJY0_9MYCO	unreviewed	.	.	.	.	.	.
Mol02032	Protein	HCV Serine protease/helicase NS3 (HCV NS3)	NS3	NS3	.	Hepacivirus C	11103	Hepacivirus C	Hepacivirus	11102	Flaviviridae	11050	Amarillovirales	2732545	Flasuviricetes	2732462	Kitrinoviricota	2732406	Orthornavirae	2732396	.	APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHSTDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEGVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMRKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVT	.	"Displays three enzymatic activities: serine protease with a chymotrypsin-like fold, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B."	PDB: 1A1R; PDB: 1A1V; PDB: 1CWX; PDB: 1HEI; PDB: 1JR6; PDB: 1N1L; PDB: 1ONB; PDB: 1R7C; PDB: 1R7D; PDB: 1R7E; PDB: 1R7F; PDB: 1R7G; PDB: 1RGQ; PDB: 2A4R; PDB: 2F9V; PDB: 2HD0; PDB: 2JXF; PDB: 2KDR; PDB: 2N1P; PDB: 2O8M; PDB: 2OBO; PDB: 2OBQ; PDB: 2OC0; PDB: 2OC1; PDB: 2OC7; PDB: 2OC8; PDB: 2OIN; PDB: 2P59; PDB: 2QV1; PDB: 2XI2; PDB: 2XI3; PDB: 2XNI; PDB: 3RC4; PDB: 3RC5; PDB: 4CL1; PDB: 4JZN; PDB: 4JZO; PDB: 4MWF; PDB: 4N0Y; PDB: 4Q0X; PDB: 4XVJ; PDB: 4Z0X; PDB: 5EOC; PDB: 5ERW; PDB: 5FGB; PDB: 5FGC; PDB: 5JZI; PDB: 5YXN; PDB: 5YXU; PDB: 6BQJ; PDB: 6BQK; PDB: 6BZU; PDB: 6BZV; PDB: 6BZW; PDB: 6BZY; PDB: 6UYD; PDB: 6WO5; PDB: 6WOQ	.	POLG_HCVJA (1027-1657)	reviewed	.	.	.	.	.	.
Mol02033	Protein	Tyrosine-protein kinase Yes (YES)	YES1; YES	YES	.	Canis lupus	9615	Canis lupus	Canis	9611	Canidae	9608	Carnivora	33554	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MGCIKSKEDKGPAIKYRNTPEPVSVSHYGAEPTQATPWPSSSGWGTAFNFSSLSMTGFGGSSGVTPFGGASSSFSVVPSPYPAGLTGGVTIFVALYDYEARTTEDLSFKGGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIAAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEIRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHSTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKLGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEFMSKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGENLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILQTELTTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHELMNLCWKKDPDERPTFEYIQSFLEDYFTAAEPQYQPGENL	.	"Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGRF, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis (By similarity)."	.	.	YES_CANLF	reviewed	.	.	.	.	.	.
Mol02034	Protein	Vancomycin/teicoplanin A-type resistance protein VanA (VANA)	VANA	VANA	.	Enterococcus faecium	1352	Enterococcus faecium	Enterococcus	.	Enterococcaceae	Lactobacillales	186826	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNRIKVAILFGGCSEEHDVSVKSAIEIAANINKEKYEPLYIGITKSGVWKMCEKPCAEWENDNCYSAVLSPDKKMHGLLVKKNHEYEINHVDVAFSALHGKSGEDGSIQGLFELSGIPFVGCDIQSSAICMDKSLTYIVAKNAGIATPAFWVINKDDRPVAATFTYPVFVKPARSGSSFGVKKVNSADELDYAIESARQYDSKILIEQAVSGCEVGCAVLGNSAALVVGEVDQIRLQYGIFRIHQEVEPEKGSENAVITVPADLSAEERGRIQETAKKIYKALGCRGLARVDMFLQDNGRIVLNEVNTLPGFTSYSRYPRMMAAAGIALPELIDRLIVLALKG	.	"Required for high-level resistance to glycopeptide antibiotics. D-Ala--D-Ala ligase of altered specificity which catalyzes ester bond formation between D-Ala and various D-hydroxy acids; produces a peptidoglycan which does not terminate in D-alanine but in D-lactate, thus preventing vancomycin or teicoplanin binding."	PDB: 1E4E	.	VANA_ENTFC	reviewed	.	.	.	.	.	.
Mol02035	Protein	"Vimentin 2, pseudogene (VIM2P)"	vim2	VIM2P	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	.	Pseudomonadaceae	Pseudomonadales	72274	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MGLPVTRAVSTHFHDDRSPLLGVLRVSGVATYSPPSPRRLAEVEGNEIPTHSLEGLSSSEVQLPFHPL	.	.	.	HGNC:43891	V9W1K1_PSEAI	unreviewed	.	.	.	.	.	.
Mol02036	Protein	Serine/threonine protein kinase UL97 (UL97)	UL97	UL97	.	Human betaherpesvirus 5	10359	Human betaherpesvirus 5	Cytomegalovirus	10358	Herpesviridae	10292	Herpesvirales	548681	Herviviricetes	2731363	Peploviricota	2731361	Heunggongvirae	2731360	.	MSSALRSRARSASLGTTTQGWDPPPLRRPSRARRRQWMREAAQAAAQAAVQAAQAAAAQVAQAHVDENEVVDLMADEAGGGVTTLTTLSSVSTTTVLGHATFSACVRSDVMRDGEKEDAASDKENLRRPVVPSTSSRGSAASGDGYHGLRCRETSAMWSFEYDRDGDVTSVRRALFTGGSDPSDSVSGVRGGRKRPLRPPLVSLARTPLCRRRVGGVDAVLEENDVELRAESQDSAVASGPGRIPQPLSGSSGEESATAVEADSTSHDDVHCTCSNDQIITTSIRGLTCDPRMFLRLTHPELCELSISYLLVYVPKEDDFCHKICYAVDMSDESYRLGQGSFGEVWPLDRYRVVKVARKHSETVLTVWMSGLIRTRAAGEQQQPPSLVGTGVHRGLLTATGCCLLHNVTVHRRFHTDMFHHDQWKLACIDSYRRAFCTLADAIKFLNHQCRVCHFDITPMNVLIDVNPHNPSEIVRAALCDYSLSEPYPDYNERCVAVFQETGTARRIPNCSHRLRECYHPAFRPMPLQKLLICDPHARFPVAGLRRYCMSELSALGNVLGFCLMRLLDRRGLDEVRMGTEALLFKHAGAACRALENGKLTHCSDACLLILAAQMSYGACLLGEHGAALVSHTLRFVEAKMSSCRVRAFRRFYHECSQTMLHEYVRKNVERLLATSDGLYLYNAFRRTTSIICEEDLDGDCRQLFPE	.	"Serine/threonine protein kinase that plays important roles in several processes including nuclear viral egress, viral replication or regulation of host cell cycle progression. Participates in the acquisition of tegument during virion morphogenesis in the nucleus. Phosphorylates the viral nuclear egress complex (NEC) subunits UL50 and UL53. Redistributes the host nuclear lamina by phosphorylating cellular Lamins-A/C. Plays a role in viral DNA synthesis by phosphorylating the DNA polymerase processivity factor UL44. Stimulates host cell cycle to support viral DNA synthesis by phosphorylating host retinoblastoma/RB1 protein. Additional substrates have been identified including host EF1D or H2B. Phosphorylates also host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity."	.	.	UL97_HCMVA	Reviewed	.	.	.	.	.	.
Mol02038	Protein	23S rRNA (cytidine-2'-O)-methyltransferase TlyA (TLYA)	tlyA; CJJ81176_0616	TLYA	.	Campylobacter jejuni	354242	Campylobacter jejuni	Campylobacter	194	Campylobacteraceae	72294	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MRFDFFVSKRLNISRNKALELIENEEVLLNGKSFKASFDVKNFLENLKKTQDLNPEDILLTDGLKLDLLSEIYVSRAALKLKNFLEENGIEIKHKNCLDIGSSTGGFVQILLENQALKITALDVGNNQLHLSLRTNEKIILHENTDLRTFKSEEKFELITCDVSFISLINLLYYIDNLALKEIILLFKPQFEVGKNIKRDKKGVLKDDKAILKARMDFEKACAKLGWLLKNTQKSSIKGKEGNVEYFYYYIKN	.	Catalyzes the 2'-O-methylation at nucleotide C1920 in 23S rRNA. Enhances motility. Enchances biofilm formation. Involved in the assembly of 70S ribosomes. Involved in virulence by promoting adherence and invasion to host cells. Involved in pathogenicity by modulating secretion of host-protective chemokine interleukin 8 (IL-8). Involved in susceptibility to antibiotic capreomycin.	.	.	TLYA_CAMJJ	reviewed	.	.	.	.	.	.
Mol02039	Protein	Tubulin beta-1 chain (TBB1)	TBB1	TBB1	.	Filarial nematodes	6280	.	Brugia	6278	Onchocercidae	6296	Rhabditida	6236	Chromadorea	119089	Nematoda	6231	Metazoa	33208	.	MREIVHVQAGQCGNQIGAKFWEVISDEHGVQPDGTYKGDSDLQIERINVYYNEANGGKYVPRAVLVDLEPGTMDSIRGGEFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDNVLDVIRKEAEGCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMSSFSVVPSPKVSDVVLEPYNATLSVHQLVENTDETFCIDNEALYDICFRTLKLANPTYGDLNHLVSVTMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLSARDAAAYRALNVAELTQQMFDAKNMMAACDPRHGRYLTVAAMFRGRMSMREVDEQMMQVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNTTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEGDLQEGESEYIEQEE	.	"Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain."	.	.	TBB1_BRUPA	reviewed	.	.	.	.	.	.
Mol02040	Protein	Preadipocyte factor (PREF-1)	pref-1	PREF-1	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MTATEALPARPLAPAGFRPQHL	.	.	.	.	Q9NS53_HUMAN	unreviewed	.	.	.	.	.	.
Mol02041	Protein	Cytochrome P450 family 1 subfamily A member 1 (CYP1A1)	cyp6-6	CYP1A1	.	Myzus persicae	13164	Myzus persicae	Myzus	13163	Aphididae	27482	Hemiptera	7524	Insecta	50557	Arthropoda	6656	Metazoa	33208	.	EFETFRKYPIAYSIMRVATKTYTLPDKSFVIEKGQKIFIPMFNIHRDPKYYPDPLSFNPERFSMEQKSQRPNGTYIPFGDGPNS	.	May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.	.	.	Q9BLP7_MYZPE	unreviewed	.	.	.	.	.	.
Mol02042	Protein	Cholinergic receptor muscarinic 1 (CHRM1)	GPM1	CHRM1	.	Guinea-pig	10141	.	Cavia	10140	Caviidae	10139	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MNTSAPPAVSPNITILAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTSSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRTKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGEQTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCALYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPESPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGCLHRTPSR	.	"The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover."	.	HGNC:1950	Q8VH28_CAVPO	unreviewed	.	.	.	.	.	.
Mol02043	Protein	Cytochrome P450 family 1 subfamily A member 1 (CYP1A1)	CYP9G2	CYP1A1	.	Phthiraptera	51655	.	Plutella	51654	Plutellidae	51653	Lepidoptera	7088	Insecta	50557	Arthropoda	6656	Metazoa	33208	.	MIAEILIFILTTLVAFAFYSYYKNQNVFKSKDMKFLPGFPMFGNIIKSSFGKNHMFYDLDRVYRAFPGESYVGYVEGFVPLYLIRDPSIIRLITVKDFDHFVDHRRFATDDLFNESLFMMTGDRWRDMRSTLSPAFTGSKMRQMVPFMNETSQNIVQYLRETEGQDIDASRLIRCYTNDVIASTIFGLQVNSLKDPENDFYKAGQSLVVGNSLTRRPSFFIVMTIPALSKFFPFFPKETTDFFRGIVLKTMQHRENNNIERPDMIRMLMEAAKGTLKMQTHDKLDDIGFATTDEADIKPKGEMRQWTPDTLAAQAFLFFFGGFESSASVIVMAVHELAVNSEAQGKLYEEVKEYHEKHGKMTYEGVQKMTYLDCVANEALRKWSPAVITNRVCVKPYVLPPPREGGKPVQLEVGDGIYNSVSSVHWDEQYYPEPEKFKPERFNDENKHKIQPFTFMPFGTGPRNCIASRFAILELKVLLYHIVLNFEIQKCGKTSDPVQLAPGDFNIRAVGGSWVKFRSRN	.	May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.	.	.	Q8IU14_PLUXY	unreviewed	.	.	.	.	.	.
Mol02044	Protein	Multidrug export protein MepA (cdeA)	eA; cdeA; BN1096_590031; BN1097_570030; E5F35_13510	cdeA	.	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MENLFTRKFTTFEFLKFVSPAIISMIFISLYTIIDGIFVSTLVGSDALASINIVLPIINLVCGFGIMMATGGGAIVSIRMGENRQDEANSTFSFIVLFSLIVGILFTVISYFFIKEISILLGATDKLLPYCITYGKVMILCTPFYILKFIFEYFARTDGNSKFSLFLSVIGGVTNIILDYVFIKYFGMGLLGAAVATAIGIILTCVLGIIYFLSNKSTLKLRKPKTDFRLIRDTMINGSSEMVTELSTGITTFLFNVVALKLAGENGLAALTIVLYAHFLMTSVYLGFAAGVSPLISYNFGAENSDKLKETFKHSLKFIFISSLLVFIIALVFAPFIVRVFVNPDNTVFKLALQGLKIFAFAFLFVGINIFASGFFTAFHNGKISAIISFSRAFVFIIIGIIILPPMLNMTGLWLTVPFAEVITIFISILFIKKYKGRYKY	.	.	.	.	Q7WZ38_CLODI	unreviewed	.	.	.	.	.	.
Mol02045	Protein	Beta-lactamase (Q6QJ55)	blaoxa-10; bla1; blaOXA-10; OXA-10; oxa-10; oxa10; E5D53_33915; GUL26_37150; PA52Ts2_0147	Q6QJ55	.	Pseudomonas aeruginosa	287	Pseudomonas aeruginosa	Pseudomonas	.	Pseudomonadaceae	Pseudomonadales	72274	72274	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MKTFAAYVIIACLSSTALAGSITENTSWNKEFSAEAVNGVFVLCKSSSKSCATNDLARASKEYLPASTFKIPNAIIGLETGVIKNEHQVFKWDGKPRAMKQWERDLTLRGAIQVSAVPVFQQIAREVGEVRMQKYLKKFSYGNQNISGGIDKFWLEGQLRISAVNQVEFLESLYLNKLSASKENQLIVKEALVTEAAPEYLVHSKTGFSGVGTESNPGVAWWVGWVEKETEVYFFAFNMDIDNESKLPLRKSIPTKIMESEGIIGG	.	.	.	.	Q6QJ55_PSEAI	unreviewed	.	.	.	.	.	.
Mol02046	Protein	D-alanine--D-alanine ligase (Q5MPQ2)	vanB; ddl	Q5MPQ2	.	Enterococcus faecium	1352	Enterococcus faecium	Enterococcus	.	Enterococcaceae	Lactobacillales	186826	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MNRIKVAIIFGGCSEEHDVSVKSAIEIAANIDTEKFDPHYIGITKNGVWKLCKKPCTEWEADSLPAILSPDRKTHGLLVMKESEYETRRIDVAFPVLHGKCGEDGAIQGLFVLSGIPYVGCDIQSSAACMDKSLAYILTKNAGIAVPEFQIIDKGDKPEAGALTYPVFVKPARSGSSFGVTKVNGTEELNAAIEAAGQYDGKILIEQAISGCEVGCAVMGNEDDLIVGEVDQIRLSHGIFRIHQENEPEKGSENAMITVPADIPVEERNRVQETAKKVYRVLGCRGLARVDLFLQEDGGIVLNEVNTMPGFTSYSRYPRMVAAAGITLPALIDSLITLALKR	.	Cell wall formation.	.	.	Q5MPQ2_ENTFC	unreviewed	.	.	.	.	.	.
Mol02047	Protein	Thioredoxin (TRX)	cotE; CD630_14330	TRX	.	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MIYMPNLPSLGSKAPDFKANTTNGPIRLSDYKGNWIVLFSHPGDFTPVCTTEFLCFAKYYDEFKKRNTELIGLSVDSNSSHLAWMYNISLLTGVEIPFPIIEDRDMRIAKLYGMISKPMSDTSTVRSVFIIDNNQILRTILYYPLTTGRNIPEILRIVDALQTSDRDNIVTPANWFPGMPVILPYPKNYKELKNRVNSCNKKYSCMDWYLCFVPDNYNDEEVSKKIDNTCSWKKEHTKNIENECNCEHEHHDYLNKALDCKQEHKTDIKDDCNHEKKHTKNTNKVHNSKQDKFKDKSCDEMNFNYDKDESCDKINSSYNKEDSSYEDFYKHNYKNYDYTSEKNTKKIAMKTLKDSKKLVRPQITDPYNPIVENANCPDINPIVAEYVLGNPTNVDAQLLDAVIFAFAEIDQSGNLFIPYPRFLNQLLALKGEKPSLKVIVAIGGWGAEGFSDAALTPTSRYNFARQVNQMINEYALDGIDIDWEYPGSSASGITSRPQDRENFTLLLTAIRDVIGDDKWLSVAGTGDRGYINSSAEIDKIAPIIDYFNLMSYDFTAGETGPNGRKHQANLFDSDLSLPGYSVDAMVRNLENAGMPSEKILLGIPFYGRLGATITRTYDELRRDYINKNGYEYRFDNTAQVPYLVKDGDFAMSYDDALSIFLKTQYVLRNCLGGVFSWTSTYDQANILARTMSIGINDPEVLKEELEGIYGQF	.	"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides."	PDB: 6T9M; PDB: 6TSB	.	Q18BV5_CLOD6	unreviewed	.	.	.	.	.	.
Mol02049	Protein	Bifunctional dihydrofolate reductase-thymidylate synthase (PVDHFR)	dhfr; dfhr	Pvdhfr	.	Plasmodium vivax	126793	Plasmodium vivax	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MEDLSDVFDIYAICACCKVAPTSEGTKNEPFSPRTFRGLGNKGTLPWKCNSVDMKYFRSVTTYVDESKYEKLKWKRERYLRMEASQGGGDNTSGGDNTHGGDNADKLQNVVVMGRSNWESIPKQYKPLPNRINVVLSKTLTKEDVKEKVFIIDSIDDLLLLLKKLKYYKCFIIGGAQVYRECLSRNLIKQIYFTRIN	.	"Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP."	.	.	Q0PW60_PLAVI	unreviewed	.	.	.	.	.	.
Mol02050	Protein	VEEV spike proteins E1 (VEEV E1)	E1	E1	.	Venezuelan equine encephalitis virus	11038	Venezuelan equine encephalitis virus	Alphavirus	11019	Togaviridae	11018	Martellivirales	2732544	Alsuviricetes	2732461	Kitrinoviricota	2732406	Orthornavirae	2732396	.	LVMAGAAAGAYEHATTMPSQAGISYNTIVNRAGYAPLPISITPTKIKLIPTVNLEYVTCHYKTGMDSPAIKCCGSQECTPTYRPDEQCKVFTGVYPFMWGGAYCFCDTENTQVSKAYVMKSDDCLADHAEAYKAHTASVQAFLNITVGEHSIVTTVYVNGETPVNFNGVKLTAGPLSTAWTPFDRKIVQYAGEIYNYDFPEYGAGQPGAFGDIQSRTVSSSDLYANTNLVLQRPKAGAIHVPYTQAPSGFEQWKKDKAPSLKFTAPFGCEIYTNPIRAENCAVGSIPLAFDIPDALFTRVSETPTLSAAECTLNECVYSSDFGGIATVKYSASKSGKCAVHVPSGTATLKEAAVELTEQGSATIHFSTANIHPEFRLQICTSYVTCKGDCHPPKDHIVTHPQYHAQTFTAAVSKTAWTWLTSLLGGSAVIIIIGLVLATIVAMYVLT	.	"Class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to cell receptor LDLRAD3 and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group."	.	.	POLS_EEVVT (813 - 1254)	reviewed	.	.	.	.	.	.
Mol02051	Protein	VEEV RNA-directed RNA polymerase (VEEV nsP4)	nsP4	nsP4	.	Venezuelan equine encephalitis virus	11038	Venezuelan equine encephalitis virus	Alphavirus	11019	Togaviridae	11018	Martellivirales	2732544	Alsuviricetes	2732461	Kitrinoviricota	2732406	Orthornavirae	2732396	.	YIFSSDTGQGHLQQKSVRQTVLSEVVLERTELEISYAPRLDQEKEELLRKKLQLNPTPANRSRYQSRKVENMKAITARRILQGLGHYLKAEGKVECYRTLHPVPLYSSSVNRAFSSPKVAVEACNAMLKENFPTVASYCIIPEYDAYLDMVDGASCCLDTASFCPAKLRSFPKKHSYLEPTIRSAVPSAIQNTLQNVLAAATKRNCNVTQMRELPVLDSAAFNVECFKKYACNNEYWETFKENPIRLTEENVVNYITKLKGPKAAALFAKTHNLNMLQDIPMDRFVMDLKRDVKVTPGTKHTEERPKVQVIQAADPLATAYLCGIHRELVRRLNAVLLPNIHTLFDMSAEDFDAIIAEHFQPGDCVLETDIASFDKSEDDAMALTALMILEDLGVDAELLTLIEAAFGEISSIHLPTKTKFKFGAMMKSGMFLTLFVNTVINIVIASRVLRERLTGSPCAAFIGDDNIVKGVKSDKLMADRCATWLNMEVKIIDAVVGEKAPYFCGGFILCDSVTGTACRVADPLKRLFKLGKPLAADDEHDDDRRRALHEESTRWNRVGILSELCKAVESRYETVGTSIIVMAMTTLASSVKSFSYLRGAPITLYG	.	Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyproteins P123/P123' and nsP4 synthesizes minus-strand RNAs. The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs.	PDB: 2HWK; PDB: 5EZQ; PDB: 5EZS; PDB: 6BCM	.	POLN_EEVVT (1887-2493)	reviewed	.	.	.	.	.	.
Mol02052	Protein	VEEV Protease (VEEV nsP2)	nsP2	nsP2	.	Venezuelan equine encephalitis virus	11038	Venezuelan equine encephalitis virus	Alphavirus	11019	Togaviridae	11018	Martellivirales	2732544	Alsuviricetes	2732461	Kitrinoviricota	2732406	Orthornavirae	2732396	.	GSVETPRGLIKVTSYAGEDKIGSYAVLSPQAVLKSEKLSCIHPLAEQVIVITHSGRKGRYAVEPYHGKVVVPEGHAIPVQDFQALSESATIVYNEREFVNRYLHHIATHGGALNTDEEYYKTVKPSEHDGEYLYDIDRKQCVKKELVTGLGLTGELVDPPFHEFAYESLRTRPAAPYQVPTIGVYGVPGSGKSGIIKSAVTKKDLVVSAKKENCAEIIRDVKKMKGLDVNARTVDSVLLNGCKHPVETLYIDEAFACHAGTLRALIAIIRPKKAVLCGDPKQCGFFNMMCLKVHFNHEICTQVFHKSISRRCTKSVTSVVSTLFYDKKMRTTNPKETKIVIDTTGSTKPKQDDLILTCFRGWVKQLQIDYKGNEIMTAAASQGLTRKGVYAVRYKVNENPLYAPTSEHVNVLLTRTEDRIVWKTLAGDPWIKTLTAKYPGNFTATIEEWQAEHDAIMRHILERPDPTDVFQNKANVCWAKALVPVLKTAGIDMTTEQWNTVDYFETDKAHSAEIVLNQLCVRFFGLDLDSGLFSAPTVPLSIRNNHWDNSPSPNMYGLNKEVVRQLSRRYPQLPRAVATGRVYDMNTGTLRNYDPRINLVPVNRRLPHALVLHHNEHPQSDFSSFVSKLKGRTVLVVGEKLSVPGKMVDWLSDRPEATFRARLDLGIPGDVPKYDIIFVNVRTPYKYHHYQQCEDHAIKLSMLTKKACLHLNPGGTCVSIGYGYADRASESIIGAIARQFKFSRVCKPKSSLEETEVLFVFIGYDRKARTHNPYKLSSTLTNIYTGSRLHEAGC	.	"Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities."	PDB: 2HWK; PDB: 5EZQ; PDB: 5EZS; PDB: 6BCM	.	POLN_EEVVT (536-1329)	reviewed	.	.	.	.	.	.
Mol02053	Protein	VEEV Non-structural protein 3 (VEEV nsP3)	nsP3	nsP3	.	Venezuelan equine encephalitis virus	11038	Venezuelan equine encephalitis virus	Alphavirus	11019	Togaviridae	11018	Martellivirales	2732544	Alsuviricetes	2732461	Kitrinoviricota	2732406	Orthornavirae	2732396	.	APSYHVVRGDIATATEGVIINAANSKGQPGGGVCGALYKKFPESFDLQPIEVGKARLVKGAAKHIIHAVGPNFNKVSEVEGDKQLAEAYESIAKIVNDNNYKSVAIPLLSTGIFSGNKDRLTQSLNHLLTALDTTDADVAIYCRDKKWEMTLKEAVARREAVEEICISDDSSVTEPDAELVRVHPKSSLAGRKGYSTSDGKTFSYLEGTKFHQAAKDIAEINAMWPVATEANEQVCMYILGESMSSIRSKCPVEESEASTPPSTLPCLCIHAMTPERVQRLKASRPEQITVCSSFPLPKYRITGVQKIQCSQPILFSPKVPAYIHPRKYLVETPPVDETPEPSAENQSTEGTPEQPPLITEDETRTRTPEPIIIEEEEEDSISLLSDGPTHQVLQVEADIHGPPSVSSSSWSIPHASDFDVDSLSILDTLEGASVTSGATSAETNSYFAKSMEFLARPVPAPRTVFRNPPHPAPRTRTPSLAPSRACSRTSLVSTPPGVNRVITREELEALTPSRTPSRSVSRTSLVSNPPGVNRVITREEFEAFVAQQQ	.	Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis 	PDB: 2HWK; PDB: 5EZQ; PDB: 5EZS; PDB: 6BCM	.	POLN_EEVVT (1330-1879)	reviewed	.	.	.	.	.	.
Mol02054	Protein	HCV Non-structural protein 5A (HCV NS5A)	NS5A	NS5A	.	Hepacivirus C	356418	Hepacivirus C	Hepacivirus	11102	Flaviviridae	11050	Amarillovirales	2732545	Flasuviricetes	2732462	Kitrinoviricota	2732406	Orthornavirae	2732396	.	AESWLWEVWDWVLHVLSDFKTCLKAKFVPLMPGIPLLSWPRGYKGEWRGDGVMHTTCPCGADLAGHIKNGSMRITGPKTCSNTWHGTFPINAYTTGPGVPIPAPNYKFALWRVSAEDYVEVRRVGDFHYVTGVTQDNIKFPCQVPAPELFTEVDGIRIHRHAPKCKPLLRDEVSFSVGLNSFVVGSQLPCEPEPDVAVLTSMLTDPSHITAESARRRLARGSRPSLASSSASQLSPRLLQATCTAPHDSPGTDLLEANLLWGSTATRVETDEKVIILDSFESCVAEQNDDREVSVAAEILRPTKKFPPALPIWARPDYNPPLTETWKQQDYQAPTVHGCALPPAKQPPVPSPRRKRTVQLTESVVSTALAELAAKTFGQSEPSSDRDTDLTTPTETTDSGPIVVDDASDDGSYSSMPPLEGEPGDPDLTSDSWSTVSGSEDVVCCSM	.	Phosphorylated protein that is indispensable for viral replication and assembly. Both hypo- and hyperphosphorylated states are required for the viral life cycle.	.	.	POLG_HCVJA (1973-2419)	reviewed	.	.	.	.	.	.
Mol02055	Protein	HCV RNA-directed RNA polymerase (HCV NS5B)	NS5A	NS5A	.	Hepacivirus C	356418	Hepacivirus C	Hepacivirus	11102	Flaviviridae	11050	Amarillovirales	2732545	Flasuviricetes	2732462	Kitrinoviricota	2732406	Orthornavirae	2732396	.	SYSWTGALVTPCAAEESKLPISPLSNSLLRHHNMVYATTTRSAVTRQKKVTFDRLQVVDSTYNEVLKEIKARASRVKPRLLTTEEACDLTPPHSARSKFGYGKKDVRSHSRKAINHISSVWKDLLDDNNTPIPTTIMAKNEVFAVNPAKGGRKPARLIVYPDLGSRVCEKRALHDVIKKTALAVMGAAYGFQYSPAQRVEFLLTAWKSKNDPMGFSYDTRCFDSTVTEKDIRVEEEVYQCCDLEPEARKVITALTDRLYVGGPMHNSKGDLCGYRRCRATGVYTTSFGNTLTCYLKATAAIRAAALRDCTMLVCGDDLVVIAESDGVEEDNRALRAFTEAMTRYSAPPGDAPQPAYDLELITSCSSNVSVAHDVTGKKVYYLTRDPETPLARAVWETVRHTPVNSWLGNIIVYAPTIWVRMILMTHFFSILQSQEALEKALDFDMYGVTYSITPLDLPAIIQRLHGLSAFTLHGYSPHELNRVAGALRKLGVPPLRAWRHRARAVRAKLIAQGGRAKICGIYLFNWAVKTKLKLTPLPAAAKLDLSGWFTVGAGGGDIYHSMSHARPRYLLLCLLILTVGVGIFLLPAR	.	RNA-dependent RNA polymerase that performs primer-template recognition and RNA synthesis during viral replication.	.	.	POLG_HCVJA (2420-3010)	reviewed	.	.	.	.	.	.
Mol02056	Protein	SARS-CoV-2 Non-structural protein 6 (SARS-CoV-2 nsp6)	nsp6	rep	43740578	Severe acute respiratory syndrome coronavirus 2 	2697049	Severe acute respiratory syndrome coronavirus	Betacoronavirus	694002	Coronaviridae	11118	Nidovirales	76804	Pisoniviricetes	2732506	Pisuviricota	2732408	Orthornavirae	2732396	.	AKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIV	.	Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.	PDB: 5R7Z; PDB: 5R80; PDB: 5R81; PDB: 5R82; PDB: 5R83; PDB: 5R84; PDB: 5R8T; PDB: 5RE4; PDB: 5RE5; PDB: 5RE6; PDB: 5RE7; PDB: 5RE8; PDB: 5RE9; PDB: 5REA; PDB: 5REB; PDB: 5REC; PDB: 5RED; PDB: 5REE; PDB: 5REF; PDB: 5REG; PDB: 5REH; PDB: 5REI; PDB: 5REJ; PDB: 5REK; PDB: 5REL; PDB: 5REM; PDB: 5REN; PDB: 5REO; PDB: 5REP; PDB: 5RER; PDB: 5RES; PDB: 5RET; PDB: 5REU; PDB: 5REV; PDB: 5REW; PDB: 5REX; PDB: 5REY; PDB: 5REZ; PDB: 5RF0; PDB: 5RF1; PDB: 5RF2; PDB: 5RF3; PDB: 5RF4; PDB: 5RF5; PDB: 5RF6; PDB: 5RF7; PDB: 5RF8; PDB: 5RF9; PDB: 5RFA; PDB: 5RFB; PDB: 5RFC; PDB: 5RFD; PDB: 5RFE; PDB: 5RFF; PDB: 5RFG; PDB: 5RFH; PDB: 5RFI; PDB: 5RFJ; PDB: 5RFK; PDB: 5RFL; PDB: 5RFM; PDB: 5RFN; PDB: 5RFO; PDB: 5RFP; PDB: 5RFQ; PDB: 5RFR; PDB: 5RFS; PDB: 5RFT; PDB: 5RFU; PDB: 5RFV; PDB: 5RFW; PDB: 5RFX; PDB: 5RFY; PDB: 5RFZ; PDB: 5RG0; PDB: 5RG1; PDB: 5RG2; PDB: 5RG3; PDB: 5RGG; PDB: 5RGH; PDB: 5RGI; PDB: 5RGJ; PDB: 5RGK; PDB: 5RGL; PDB: 5RGM; PDB: 5RGN; PDB: 5RGO; PDB: 5RGP; PDB: 5RGQ; PDB: 5RGR; PDB: 5RGS; PDB: 5RGT; PDB: 5RGU; PDB: 5RGV; PDB: 5RGW; PDB: 5RGX; PDB: 5RGY; PDB: 5RGZ; PDB: 5RH0; PDB: 5RH1; PDB: 5RH2; PDB: 5RH3; PDB: 5RH4; PDB: 5RH5; PDB: 5RH6; PDB: 5RH7; PDB: 5RH8; PDB: 5RH9; PDB: 5RHA; PDB: 5RHB; PDB: 5RHC; PDB: 5RHD; PDB: 5RHE; PDB: 5RHF; PDB: 5RL0; PDB: 5RL1; PDB: 5RL2; PDB: 5RL3; PDB: 5RL4; PDB: 5RL5; PDB: 5RL6; PDB: 5RL7; PDB: 5RL8; PDB: 5RL9; PDB: 5RLB; PDB: 5RLC; PDB: 5RLD; PDB: 5RLE; PDB: 5RLF; PDB: 5RLG; PDB: 5RLH; PDB: 5RLI; PDB: 5RLJ; PDB: 5RLK; PDB: 5RLL; PDB: 5RLM; PDB: 5RLN; PDB: 5RLO; PDB: 5RLP; PDB: 5RLQ; PDB: 5RLR; PDB: 5RLS; PDB: 5RLT; PDB: 5RLU; PDB: 5RLV; PDB: 5RLW; PDB: 5RLY; PDB: 5RLZ; PDB: 5RM0; PDB: 5RM1; PDB: 5RM2; PDB: 5RM3; PDB: 5RM4; PDB: 5RM5; PDB: 5RM6; PDB: 5RM7; PDB: 5RM8; PDB: 5RM9; PDB: 5RMA; PDB: 5RMB; PDB: 5RMC; PDB: 5RMD; PDB: 5RME; PDB: 5RMF; PDB: 5RMG; PDB: 5RMH; PDB: 5RMI; PDB: 5RMJ; PDB: 5RMK; PDB: 5RML; PDB: 5RMM; PDB: 5ROB; PDB: 5RS7; PDB: 5RS8; PDB: 5RS9; PDB: 5RSB; PDB: 5RSC; PDB: 5RSD; PDB: 5RSE; PDB: 5RSF; PDB: 5RSG; PDB: 5RSH; PDB: 5RSI; PDB: 5RSJ; PDB: 5RSK; PDB: 5RSL; PDB: 5RSM; PDB: 5RSN; PDB: 5RSO; PDB: 5RSP; PDB: 5RSQ; PDB: 5RSR; PDB: 5RSS; PDB: 5RST; PDB: 5RSU; PDB: 5RSV; PDB: 5RSW; PDB: 5RSX; PDB: 5RSY; PDB: 5RSZ; PDB: 5RT0; PDB: 5RT1; PDB: 5RT2; PDB: 5RT3; PDB: 5RT4; PDB: 5RT5; PDB: 5RT6; PDB: 5RT7; PDB: 5RT8; PDB: 5RT9; PDB: 5RTA; PDB: 5RTB; PDB: 5RTC; PDB: 5RTD; PDB: 5RTE; PDB: 5RTF; PDB: 5RTG; PDB: 5RTH; PDB: 5RTI; PDB: 5RTJ; PDB: 5RTK; PDB: 5RTL; PDB: 5RTM; PDB: 5RTN; PDB: 5RTO; PDB: 5RTP; PDB: 5RTQ; PDB: 5RTR; PDB: 5RTS; PDB: 5RTT; PDB: 5RTU; PDB: 5RTV; PDB: 5RTW; PDB: 5RTX; PDB: 5RTY; PDB: 5RTZ; PDB: 5RU0; PDB: 5RU1; PDB: 5RU2; PDB: 5RU3; PDB: 5RU4; PDB: 5RU5; PDB: 5RU6; PDB: 5RU7; PDB: 5RU8; PDB: 5RU9; PDB: 5RUA; PDB: 5RUC; PDB: 5RUD; PDB: 5RUE; PDB: 5RUF; PDB: 5RUG; PDB: 5RUH; PDB: 5RUI; PDB: 5RUJ; PDB: 5RUK; PDB: 5RUL; PDB: 5RUM; PDB: 5RUN; PDB: 5RUO; PDB: 5RUP; PDB: 5RUQ; PDB: 5RUR; PDB: 5RUS; PDB: 5RUT; PDB: 5RUU; PDB: 5RUV; PDB: 5RUW; PDB: 5RUX; PDB: 5RUY; PDB: 5RUZ; PDB: 5RV0; PDB: 5RV1; PDB: 5RV2; PDB: 5RV3; PDB: 5RV4; PDB: 5RV5; PDB: 5RV6; PDB: 5RV7; PDB: 5RV8; PDB: 5RV9; PDB: 5RVA; PDB: 5RVB; PDB: 5RVC; PDB: 5RVD; PDB: 5RVE; PDB: 5RVF; PDB: 5RVG; PDB: 5RVH; PDB: 5RVI; PDB: 5RVJ; PDB: 5RVK; PDB: 5RVL; PDB: 5RVM; PDB: 5RVN; PDB: 5RVO; PDB: 5RVP; PDB: 5RVQ; PDB: 5RVR; PDB: 5RVS; PDB: 5RVT; PDB: 5RVU; PDB: 5RVV; PDB: 5S18; PDB: 5S1A; PDB: 5S1C; PDB: 5S1E; PDB: 5S1G; PDB: 5S1I; PDB: 5S1K; PDB: 5S1M; PDB: 5S1O; PDB: 5S1Q; PDB: 5S1S; PDB: 5S1U; PDB: 5S1W; PDB: 5S1Y; PDB: 5S20; PDB: 5S22; PDB: 5S24; PDB: 5S26; PDB: 5S27; PDB: 5S28; PDB: 5S29; PDB: 5S2A; PDB: 5S2B; PDB: 5S2C; PDB: 5S2D; PDB: 5S2E; PDB: 5S2F; PDB: 5S2G; PDB: 5S2H; PDB: 5S2I; PDB: 5S2J; PDB: 5S2K; PDB: 5S2L; PDB: 5S2M; PDB: 5S2N; PDB: 5S2O; PDB: 5S2P; PDB: 5S2Q; PDB: 5S2R; PDB: 5S2S; PDB: 5S2T; PDB: 5S2U; PDB: 5S2V; PDB: 5S2W; PDB: 5S2X; PDB: 5S2Y; PDB: 5S2Z; PDB: 5S30; PDB: 5S31; PDB: 5S32; PDB: 5S33; PDB: 5S34; PDB: 5S35; PDB: 5S36; PDB: 5S37; PDB: 5S38; PDB: 5S39; PDB: 5S3A; PDB: 5S3B; PDB: 5S3C; PDB: 5S3D; PDB: 5S3E; PDB: 5S3F; PDB: 5S3G; PDB: 5S3H; PDB: 5S3I; PDB: 5S3J; PDB: 5S3K; PDB: 5S3L; PDB: 5S3M; PDB: 5S3N; PDB: 5S3O; PDB: 5S3P; PDB: 5S3Q; PDB: 5S3R; PDB: 5S3S; PDB: 5S3T; PDB: 5S3U; PDB: 5S3V; PDB: 5S3W; PDB: 5S3X; PDB: 5S3Y; PDB: 5S3Z; PDB: 5S40; PDB: 5S41; PDB: 5S42; PDB: 5S43; PDB: 5S44; PDB: 5S45; PDB: 5S46; PDB: 5S47; PDB: 5S48; PDB: 5S49; PDB: 5S4A; PDB: 5S4B; PDB: 5S4C; PDB: 5S4D; PDB: 5S4E; PDB: 5S4F; PDB: 5S4G; PDB: 5S4H; PDB: 5S4I; PDB: 5S4J; PDB: 5S4K; PDB: 5S6X; PDB: 5S6Y; PDB: 5S6Z; PDB: 5S70; PDB: 5S71; PDB: 5S72; PDB: 5S73; PDB: 5S74; PDB: 5SA4; PDB: 5SA5; PDB: 5SA6; PDB: 5SA7; PDB: 5SA8; PDB: 5SA9; PDB: 5SAA; PDB: 5SAB; PDB: 5SAC; PDB: 5SAD; PDB: 5SAE; PDB: 5SAF; PDB: 5SAG; PDB: 5SAH; PDB: 5SAI; PDB: 6LU7; PDB: 6LZE; PDB: 6M03; PDB: 6M0K; PDB: 6M2N; PDB: 6M2Q; PDB: 6M71; PDB: 6VWW; PDB: 6VXS; PDB: 6W01; PDB: 6W02; PDB: 6W4B; PDB: 6W4H; PDB: 6W61; PDB: 6W63; PDB: 6W6Y; PDB: 6W75; PDB: 6W9C; PDB: 6W9Q; PDB: 6WC1; PDB: 6WCF; PDB: 6WEN; PDB: 6WEY; PDB: 6WIQ; PDB: 6WJT; PDB: 6WKQ; PDB: 6WKS; PDB: 6WLC; PDB: 6WNP; PDB: 6WOJ; PDB: 6WQ3; PDB: 6WQD; PDB: 6WQF; PDB: 6WRH; PDB: 6WRZ; PDB: 6WTC; PDB: 6WTJ; PDB: 6WTK; PDB: 6WTM; PDB: 6WTT; PDB: 6WUU; PDB: 6WVN; PDB: 6WX4; PDB: 6WXC; PDB: 6WXD; PDB: 6WZU; PDB: 6X1B; PDB: 6X4I; PDB: 6XA4; PDB: 6XA9; PDB: 6XAA; PDB: 6XB0; PDB: 6XB1; PDB: 6XB2; PDB: 6XBG; PDB: 6XBH; PDB: 6XBI; PDB: 6XCH; PDB: 6XDH; PDB: 6XFN; PDB: 6XG3; PDB: 6XHM; PDB: 6XHU; PDB: 6XIP; PDB: 6XKF; PDB: 6XKH; PDB: 6XKM; PDB: 6XMK; PDB: 6XOA; PDB: 6XQS; PDB: 6XQT; PDB: 6XQU; PDB: 6XR3; PDB: 6Y2E; PDB: 6Y2F; PDB: 6Y2G; PDB: 6Y84; PDB: 6YB7; PDB: 6YNQ; PDB: 6YVA; PDB: 6YVF; PDB: 6YWK; PDB: 6YWL; PDB: 6YWM; PDB: 6YYT; PDB: 6YZ1; PDB: 6Z2E; PDB: 6Z5T; PDB: 6Z6I; PDB: 6Z72; PDB: 6ZCT; PDB: 6ZLW; PDB: 6ZM7; PDB: 6ZME; PDB: 6ZMI; PDB: 6ZMO; PDB: 6ZMT; PDB: 6ZN5; PDB: 6ZOJ; PDB: 6ZOK; PDB: 6ZON; PDB: 6ZP4; PDB: 6ZPE; PDB: 6ZRT; PDB: 6ZRU; PDB: 6ZSL; PDB: 7A1U; PDB: 7ABU; PDB: 7ADW; PDB: 7AEG; PDB: 7AF0; PDB: 7AGA; PDB: 7AHA; PDB: 7AK4; PDB: 7AKU; PDB: 7ALH; PDB: 7ALI; PDB: 7AMJ; PDB: 7ANS; PDB: 7AOL; PDB: 7AP6; PDB: 7APH; PDB: 7AQE; PDB: 7AQI; PDB: 7AQJ; PDB: 7AR5; PDB: 7AR6; PDB: 7ARF; PDB: 7AVD; PDB: 7AWR; PDB: 7AWS; PDB: 7AWU; PDB: 7AWW; PDB: 7AX6; PDB: 7AXM; PDB: 7AXO; PDB: 7AY7; PDB: 7B3E; PDB: 7B83; PDB: 7BAJ; PDB: 7BAK; PDB: 7BAL; PDB: 7BB2; PDB: 7BE7; PDB: 7BF3; PDB: 7BF4; PDB: 7BF5; PDB: 7BF6; PDB: 7BFB; PDB: 7BGP; PDB: 7BQ7; PDB: 7BQY; PDB: 7BRO; PDB: 7BRP; PDB: 7BTF; PDB: 7BUY; PDB: 7BV1; PDB: 7BV2; PDB: 7BWQ; PDB: 7BZF; PDB: 7C2I; PDB: 7C2J; PDB: 7C2K; PDB: 7C2Q; PDB: 7C2Y; PDB: 7C6S; PDB: 7C6U; PDB: 7C7P; PDB: 7C8B; PDB: 7C8R; PDB: 7C8T; PDB: 7C8U; PDB: 7CA8; PDB: 7CAM; PDB: 7CB7; PDB: 7CBT; PDB: 7CJD; PDB: 7CJM; PDB: 7CMD; PDB: 7COM; PDB: 7CUT; PDB: 7CUU; PDB: 7CWB; PDB: 7CWC; PDB: 7CX9; PDB: 7D1M; PDB: 7D1O; PDB: 7D7K; PDB: 7D7L; PDB: 7DDC; PDB: 7DG6; PDB: 7DIY; PDB: 7DVX; PDB: 7DVY; PDB: 7DW0; PDB: 7DW6; PDB: 7EQ4; PDB: 7JFQ; PDB: 7JHE; PDB: 7JIB; PDB: 7JKV; PDB: 7JME; PDB: 7JOY; PDB: 7JP0; PDB: 7JP1; PDB: 7JPE; PDB: 7JPY; PDB: 7JPZ; PDB: 7JQ0; PDB: 7JQ1; PDB: 7JQ2; PDB: 7JQ3; PDB: 7JQ4; PDB: 7JQ5; PDB: 7JQB; PDB: 7JQC; PDB: 7JR3; PDB: 7JR4; PDB: 7JST; PDB: 7JSU; PDB: 7JT0; PDB: 7JT7; PDB: 7JU7; PDB: 7JVZ; PDB: 7JW8; PDB: 7JYC; PDB: 7JYY; PDB: 7JZ0; PDB: 7K0E; PDB: 7K0F; PDB: 7K0R; PDB: 7K1L; PDB: 7K1O; PDB: 7K3N; PDB: 7K3T; PDB: 7K40; PDB: 7K5I; PDB: 7K6D; PDB: 7K6E; PDB: 7K7P; PDB: 7K9P; PDB: 7KAG; PDB: 7KEG; PDB: 7KEH; PDB: 7KF4; PDB: 7KFI; PDB: 7KG3; PDB: 7KHP; PDB: 7KOA; PDB: 7KPH; PDB: 7KQO; PDB: 7KQP; PDB: 7KQW; PDB: 7KR0; PDB: 7KR1; PDB: 7KRI; PDB: 7KVL; PDB: 7KVR; PDB: 7KX5; PDB: 7KXB; PDB: 7KYU; PDB: 7L0D; PDB: 7L10; PDB: 7L11; PDB: 7L12; PDB: 7L13; PDB: 7L14; PDB: 7L1F; PDB: 7L5D; PDB: 7L6R; PDB: 7L6T; PDB: 7L8I; PDB: 7L8J; PDB: 7LB7; PDB: 7LBN; PDB: 7LBR; PDB: 7LBS; PDB: 7LCO; PDB: 7LCS; PDB: 7LCT; PDB: 7LDL; PDB: 7LDX; PDB: 7LFE; PDB: 7LFP; PDB: 7LFZ; PDB: 7LG2; PDB: 7LG3; PDB: 7LG7; PDB: 7LGO; PDB: 7LKD; PDB: 7LKE; PDB: 7LKR; PDB: 7LKS; PDB: 7LKT; PDB: 7LKU; PDB: 7LKV; PDB: 7LKW; PDB: 7LKX; PDB: 7LLF; PDB: 7LLZ; PDB: 7LMD; PDB: 7LME; PDB: 7LMF; PDB: 7LOS; PDB: 7LTJ; PDB: 7LTN; PDB: 7LW3; PDB: 7LW4; PDB: 7LYH; PDB: 7LYI; PDB: 7LZT; PDB: 7LZU; PDB: 7LZV; PDB: 7LZW; PDB: 7LZX; PDB: 7LZY; PDB: 7LZZ; PDB: 7M00; PDB: 7M01; PDB: 7M02; PDB: 7M03; PDB: 7M04; PDB: 7M2P; PDB: 7M8M; PDB: 7M8N; PDB: 7M8O; PDB: 7M8P; PDB: 7M8X; PDB: 7M8Y; PDB: 7M8Z; PDB: 7M90; PDB: 7M91; PDB: 7MBG; PDB: 7MBI; PDB: 7MC5; PDB: 7MC6; PDB: 7ME0; PDB: 7MGR; PDB: 7MGS; PDB: 7MHF; PDB: 7MHG; PDB: 7MHH; PDB: 7MHI; PDB: 7MHJ; PDB: 7MHK; PDB: 7MHL; PDB: 7MHM; PDB: 7MHN; PDB: 7MHO; PDB: 7MHP; PDB: 7MHQ; PDB: 7MLF; PDB: 7MLG; PDB: 7MNG; PDB: 7MPB; PDB: 7MRR; PDB: 7MSW; PDB: 7MSX; PDB: 7N06; PDB: 7N0B; PDB: 7N0C; PDB: 7N0D; PDB: 7N33; PDB: 7N3K; PDB: 7N44; PDB: 7N5Z; PDB: 7N6N; PDB: 7N7R; PDB: 7N7U; PDB: 7N7W; PDB: 7N7Y; PDB: 7N83; PDB: 7N89; PDB: 7N8C; PDB: 7NBR; PDB: 7NBS; PDB: 7NBY; PDB: 7NEV; PDB: 7NF5; PDB: 7NFV; PDB: 7NG3; PDB: 7NG6; PDB: 7NIO; PDB: 7NN0; PDB: 7NNG; PDB: 7NTS; PDB: 7O7Y; PDB: 7O7Z; PDB: 7O80; PDB: 7O81; PDB: 7ORR; PDB: 7ORU; PDB: 7ORV; PDB: 7ORW; PDB: 7QGI; PDB: 7R7H; PDB: 7RB0; PDB: 7RB2; PDB: 7RBZ; PDB: 7RC0; PDB: 7RFR; PDB: 7RFS; PDB: 7RFU; PDB: 7RFW; PDB: 7RLS; PDB: 7RM2; PDB: 7RMB; PDB: 7RME; PDB: 7RMT; PDB: 7RMZ; PDB: 7RN0; PDB: 7RN1; PDB: 7RN4; PDB: 7RNH; PDB: 7RNK; PDB: 7RQG; PDB: 7S3K; PDB: 7S3S; PDB: 7S4B; PDB: 7SI9; PDB: 7T42; PDB: 7T43; PDB: 7T44; PDB: 7T45; PDB: 7T46; PDB: 7T48; PDB: 7T49; PDB: 7T4A; PDB: 7T4B; PDB: 7T9W; PDB: 7TE0; PDB: 7THH; PDB: 7TI9; 	.	R1AB_SARS2 (3570 - 3859)	Reviewed	.	.	.	.	.	.
Mol02057	Protein	HCV NS3/NS4A complex (HCV NS3/4A)	NS3/4A	NS3/4A	.	Hepacivirus C	11103	Hepacivirus C	Hepacivirus	11102	Flaviviridae	11050	Amarillovirales	2732545	Flasuviricetes	2732462	Kitrinoviricota	2732406	Orthornavirae	2732396	.	APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHSTDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEGVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMRKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPAIIPDREVLYQEFDEMEEC	.	"The NS3/NS4A complex prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state."	PDB: 1A1R; PDB: 1A1V; PDB: 1CWX; PDB: 1HEI; PDB: 1JR6; PDB: 1N1L; PDB: 1ONB; PDB: 1R7C; PDB: 1R7D; PDB: 1R7E; PDB: 1R7F; PDB: 1R7G; PDB: 1RGQ; PDB: 2A4R; PDB: 2F9V; PDB: 2HD0; PDB: 2JXF; PDB: 2KDR; PDB: 2N1P; PDB: 2O8M; PDB: 2OBO; PDB: 2OBQ; PDB: 2OC0; PDB: 2OC1; PDB: 2OC7; PDB: 2OC8; PDB: 2OIN; PDB: 2P59; PDB: 2QV1; PDB: 2XI2; PDB: 2XI3; PDB: 2XNI; PDB: 3RC4; PDB: 3RC5; PDB: 4CL1; PDB: 4JZN; PDB: 4JZO; PDB: 4MWF; PDB: 4N0Y; PDB: 4Q0X; PDB: 4XVJ; PDB: 4Z0X; PDB: 5EOC; PDB: 5ERW; PDB: 5FGB; PDB: 5FGC; PDB: 5JZI; PDB: 5YXN; PDB: 5YXU; PDB: 6BQJ; PDB: 6BQK; PDB: 6BZU; PDB: 6BZV; PDB: 6BZW; PDB: 6BZY; PDB: 6UYD; PDB: 6WO5; PDB: 6WOQ	.	POLG_HCVJA (1027-1711)	reviewed	.	.	.	.	.	.
Mol02058	Protein	Gag-Pol polyprotein (POL)	gag-pol	gag-pol	155348	Human immunodeficiency virus 1	11676	Human immunodeficiency virus 1	Lentivirus	11646	Retroviridae	11632	Ortervirales	2169561	Revtraviricetes	2732514	Artverviricota	2732409	Pararnavirae	2732397	.	MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNTATIMMQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLREDLAFLQGKAREFSSEQTRANSPTISSEQTRANSPTRRELQVWGRDNNSPSEAGADRQGTVSFNFPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMSLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKKKKSVTVLDVGDAYFSVPLDEDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQSSMTKILEPFKKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGLTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYPGIKVRQLCKLLRGTKALTEVIPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMRGAHTNDVKQLTEAVQKITTESIVIWGKTPKFKLPIQKETWETWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIVGAETFYVDGAANRETKLGKAGYVTNKGRQKVVPLTNTTNQKTELQAIYLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVNQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDKLVSAGIRKILFLDGIDKAQDEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTIHTDNGSNFTSATVKAACWWAGIKQEFGIPYNPQSQGVVESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRNPLWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED	.	"[Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation."	PDB: 1A9M; PDB: 1AJV; PDB: 1AJX; PDB: 1AXA; PDB: 1BQM; PDB: 1BQN; PDB: 1D4H; PDB: 1D4I; PDB: 1D4J; PDB: 1DLO; PDB: 1DW6; PDB: 1EBK; PDB: 1EBW; PDB: 1EBY; PDB: 1EBZ; PDB: 1EC0; PDB: 1EC1; PDB: 1EC2; PDB: 1EC3; PDB: 1EET; PDB: 1G35; PDB: 1GNM; PDB: 1GNN; PDB: 1GNO; PDB: 1HAR; PDB: 1HBV; PDB: 1HEF; PDB: 1HEG; PDB: 1HIH; PDB: 1HMV; PDB: 1HNI; PDB: 1HNV; PDB: 1HOS; PDB: 1HPS; PDB: 1HPZ; PDB: 1HQE; PDB: 1HQU; PDB: 1HRH; PDB: 1HTE; PDB: 1HTF; PDB: 1HTG; PDB: 1HVI; PDB: 1HVK; PDB: 1HVU; PDB: 1HYS; PDB: 1IKV; PDB: 1IKW; PDB: 1IKX; PDB: 1IKY; PDB: 1J5O; PDB: 1KJH; PDB: 1MER; PDB: 1MES; PDB: 1MET; PDB: 1MEU; PDB: 1N5Y; PDB: 1N6Q; PDB: 1NPA; PDB: 1NPV; PDB: 1NPW; PDB: 1QE1; PDB: 1QMC; PDB: 1R0A; PDB: 1RDH; PDB: 1RTD; PDB: 1S6P; PDB: 1S6Q; PDB: 1S9E; PDB: 1S9G; PDB: 1SBG; PDB: 1SUQ; PDB: 1SV5; PDB: 1T03; PDB: 1T05; PDB: 1T7K; PDB: 1TV6; PDB: 1TVR; PDB: 1UWB; PDB: 1W5V; PDB: 1W5W; PDB: 1W5X; PDB: 1W5Y; PDB: 1YT9; PDB: 1ZP8; PDB: 1ZPA; PDB: 1ZSF; PDB: 1ZSR; PDB: 2AQU; PDB: 2B5J; PDB: 2B6A; PDB: 2BAN; PDB: 2BBB; PDB: 2BE2; PDB: 2EXF; PDB: 2G69; PDB: 2HB3; PDB: 2HMI; PDB: 2HNZ; PDB: 2HS1; PDB: 2HS2; PDB: 2I4D; PDB: 2I4U; PDB: 2I4V; PDB: 2I4W; PDB: 2I4X; PDB: 2I5J; PDB: 2IAJ; PDB: 2IC3; PDB: 2IDW; PDB: 2IEO; PDB: 2JZW; PDB: 2L45; PDB: 2L46; PDB: 2L4L; PDB: 2UXZ; PDB: 2UY0; PDB: 2VG5; PDB: 2VG6; PDB: 2VG7; PDB: 2X4U; PDB: 2YKM; PDB: 2YKN; PDB: 2ZD1; PDB: 2ZE2; PDB: 3AVI; PDB: 3BGR; PDB: 3DLK; PDB: 3GGA; PDB: 3GGV; PDB: 3GGX; PDB: 3HVT; PDB: 3IG1; PDB: 3IRX; PDB: 3IS9; PDB: 3ISN; PDB: 3ITH; PDB: 3JSM; PDB: 3JYT; PDB: 3K2P; PDB: 3K4V; PDB: 3KLE; PDB: 3KLF; PDB: 3KLG; PDB: 3KLH; PDB: 3KLI; PDB: 3NDT; PDB: 3NU3; PDB: 3NU4; PDB: 3NU5; PDB: 3NU6; PDB: 3NU9; PDB: 3NUJ; PDB: 3NUO; PDB: 3OK9; PDB: 3PSU; PDB: 3QAA; PDB: 3QLH; PDB: 3QO9; PDB: 3TKG; PDB: 3TKW; PDB: 3TL9; PDB: 3TLH; PDB: 3V4I; PDB: 3V6D; PDB: 3V81; PDB: 3ZPS; PDB: 3ZPT; PDB: 3ZPU; PDB: 4COE; PDB: 4CP7; PDB: 4CPQ; PDB: 4CPR; PDB: 4CPS; PDB: 4CPT; PDB: 4CPU; PDB: 4CPW; PDB: 4CPX; PDB: 4DG1; PDB: 4G1Q; PDB: 4G8G; PDB: 4G8I; PDB: 4G9D; PDB: 4G9F; PDB: 4H4M; PDB: 4H4O; PDB: 4I2P; PDB: 4I2Q; PDB: 4ICL; PDB: 4ID5; PDB: 4IDK; PDB: 4IFV; PDB: 4IFY; PDB: 4IG0; PDB: 4IG3; PDB: 4KFB; PDB: 4KKO; PDB: 4KO0; PDB: 4LSL; PDB: 4LSN; PDB: 4MFB; PDB: 4O44; PDB: 4O4G; PDB: 4OJR; PDB: 4PQU; PDB: 4PUO; PDB: 4PWD; PDB: 4Q0B; PDB: 4QAG; PDB: 4R5P; PDB: 4RW4; PDB: 4RW6; PDB: 4RW7; PDB: 4RW8; PDB: 4RW9; PDB: 4U8W; PDB: 4WE1; PDB: 4YE3; PDB: 4YHQ; PDB: 4ZIP; PDB: 4ZLS; PDB: 5AGZ; PDB: 5AH6; PDB: 5AH7; PDB: 5AH8; PDB: 5AH9; PDB: 5AHA; PDB: 5AHB; PDB: 5AHC; PDB: 5BRY; PDB: 5BS4; PDB: 5C24; PDB: 5C25; PDB: 5C42; PDB: 5CYM; PDB: 5CYQ; PDB: 5D3G; PDB: 5FDL; PDB: 5HBM; PDB: 5HLF; PDB: 5HP1; PDB: 5HRO; PDB: 5I3U; PDB: 5I42; PDB: 5J1E; PDB: 5JFP; PDB: 5JFU; PDB: 5JG1; PDB: 5OI2; PDB: 5OI3; PDB: 5OI5; PDB: 5OI8; PDB: 5OIA; PDB: 5T6Z; PDB: 5T70; PDB: 5TER; PDB: 5TUQ; PDB: 5TW3; PDB: 5TXL; PDB: 5TXM; PDB: 5TXN; PDB: 5TXO; PDB: 5TXP; PDB: 5UFZ; PDB: 5ULT; PDB: 5UOV; PDB: 5UPZ; PDB: 5UV5; PDB: 5V5L; PDB: 5V5M; PDB: 5VQQ; PDB: 5VQR; PDB: 5VQS; PDB: 5VQT; PDB: 5VQU; PDB: 5VQV; PDB: 5VQW; PDB: 5VQX; PDB: 5VQY; PDB: 5VQZ; PDB: 5W5W; PDB: 5YOJ; PDB: 6AMO; PDB: 6AN2; PDB: 6AN8; PDB: 6ANQ; PDB: 6AOC; PDB: 6ASW; PDB: 6AVM; PDB: 6AVT; PDB: 6B19; PDB: 6BZ2; PDB: 6C0J; PDB: 6C0K; PDB: 6C0L; PDB: 6C0N; PDB: 6C0O; PDB: 6C0P; PDB: 6C0R; PDB: 6C8X; PDB: 6C8Y; PDB: 6CGF; PDB: 6D0D; PDB: 6D0E; PDB: 6DTW; PDB: 6DTX; PDB: 6DUF; PDB: 6DUG; PDB: 6DUH; PDB: 6ECL; PDB: 6ELI; PDB: 6HAK; PDB: 6KMP; PDB: 6O48; PDB: 6O9E; PDB: 6OE3; PDB: 6OUN; PDB: 6PRF; PDB: 6UL5; PDB: 6VUG; PDB: 6WAZ; PDB: 6WB0; PDB: 6WB1; PDB: 6WB2; PDB: 6X47; PDB: 6X49; PDB: 6X4A; PDB: 6X4B; PDB: 6X4C; PDB: 6X4D; PDB: 6X4E; PDB: 6X4F; PDB: 7AHX; PDB: 7AID; PDB: 7AIF; PDB: 7AIG; PDB: 7AII; PDB: 7AIJ; PDB: 7KJV; PDB: 7KJW; PDB: 7KJX; PDB: 7KRC; PDB: 7KRD; PDB: 7KRE; PDB: 7KRF; PDB: 7KWU; PDB: 7LPW; PDB: 7LPX; PDB: 7LQU; PDB: 7OT6; PDB: 7OTA; PDB: 7OTK; PDB: 7OTN; PDB: 7OTX; PDB: 7OTZ; PDB: 7OUT; PDB: 7OXQ; PDB: 7OZ2; PDB: 7OZ5; PDB: 7OZW; PDB: 7P15	.	POL_HV1B1	reviewed	.	.	.	.	.	.
Mol02060	Protein	Neuraminidase (NRAM)	NRAM	NRAM	.	Influenza A virus	381518	Influenza A virus	Alphainfluenzavirus	197911	Orthomyxoviridae	11308	Articulavirales	2499411	Insthoviricetes	2497577	Negarnaviricota	2497569	Orthornavirae	2732396	.	MNPNQKIITIGSICMVVGIISLILQIGNIISIWISHSIQTGNQNHTGICNQGIITYNVVAGQDSTSVILTGNSSLCPIRGWAIHSKDNGIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPVGEAPSPYNSRFESVAWSASACHDGMGWLTIGISGPDNGAVAVLKYNGIITETIKSWRKKILRTQESECTCVNGSCFTIMTDGPSNGLASYKIFKIEKGKVTKSIELNAPNSHYEECSCYPDTGKVMCVCRDNWHGSNRPWVSFDQNLDYQIGYICSGVFGDNPRPKDGPGSCGPVSADGANGVKGFSYRYGNGVWIGRTKSDSSRHGFEMIWDPNGWTETDSRFSVRQDVVAMTDRSGYSGSFVQHPELTGLDCMRPCFWVELIRGRPEEETIWTSGSIISFCGVNSDTVDWSWPDGAELPFTIDK	.	"Unlike other strains, A/WSN/33 neuraminidase binds and activates plasminogen into plasmin in the vicinity of HA so that activated plasmin cleaves HA rendering the virus infectious."	.	.	NRAM_I33A0	reviewed	.	.	.	.	.	.
Mol02061	Protein	UDP-N-acetylmuramate-L-alanine ligase (MURC)	murC; USA300HOU_1730	MURC	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MTHYHFVGIKGSGMSSLAQIMHDLGHEVQGSDIENYVFTEVALRNKGIKILPFDANNIKEDMVVIQGNAFASSHEEIVRAHQLKLDVVSYNDFLGQIIDQYTSVAVTGAHGKTSTTGLLSHVMNGDKKTSFLIGDGTGMGLPESDYFAFEACEYRRHFLSYKPDYAIMTNIDFDHPDYFKDINDVFDAFQEMAHNVKKGIIAWGDDEHLRKIEADVPIYYYGFKDSDDIYAQNIQITDKGTAFDVYVDGEFYDHFLSPQYGDHTVLNALAVIAISYLEKLDVTNIKEALETFGGVKRRFNETTIANQVIVDDYAHHPREISATIETARKKYPHKEVVAVFQPHTFSRTQAFLNEFAESLSKADRVFLCEIFGSIRENTGALTIQDLIDKIEGASLINEDSINVLEQFDNAVILFMGAGDIQKLQNAYLDKLGMKNAF	.	Cell wall formation.	.	.	MURC_STAAT	reviewed	.	.	.	.	.	.
Mol02062	Protein	UDP-N-acetylglucosamine 1-carboxyvinyltransferase 1 (MURA1)	murA1; murA; MW2024	MURA1	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MDKIVIKGGNKLTGEVKVEGAKNAVLPILTASLLASDKPSKLVNVPALSDVETINNVLTTLNADVTYKKDENAVVVDATKTLNEEAPYEYVSKMRASILVMGPLLARLGHAIVALPGGCAIGSRPIEQHIKGFEALGAEIHLENGNIYANAKDGLKGTSIHLDFPSVGATQNIIMAASLAKGKTLIENAAKEPEIVDLANYINEMGGRITGAGTDTITINGVESLHGVEHAIIPDRIEAGTLLIAGAITRGDIFVRGAIKEHMASLVYKLEEMGVELDYQEDGIRVRAEGELQPVDIKTLPHPGFPTDMQSQMMALLLTANGHKVVTETVFENRFMHVAEFKRMNANINVEGRSAKLEGKSQLQGAQVKATDLRAAAALILAGLVADGKTSVTELTHLDRGYVDLHGKLKQLGADIERIND	.	Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.	.	.	MURA1_STAAW	reviewed	.	.	.	.	.	.
Mol02063	Protein	S-adenosylmethionine synthase (METK)	METK; MAT2	METK	.	Leishmania infantum	5671	Leishmania infantum	Leishmania	5658	Trypanosomatidae	5654	Trypanosomatida	2704949	Kinetoplastea	5653	Euglenozoa	33682	.	.	.	MSVHSILFSSEHVTEGHPDKLCDQVSDAVLDACLAGDPFSKVACESCAKTGMVMVFGEITTKAVLDYQKIVRNTIKDIGFDSADKGLDYESCNVLVAIEQQSPDICQGLGNFDSEDLGAGDQGMMFGYATDETETLMPLTYELARGLAKKYSELRRSGSLEWARPDAKTQVTVEYDYDTREGKQVLTPKRVAVVLISAQHDEHVTNDKISVDLMEKVIKAVIPANMLDAETKYWLNPSGRFVRGGPHGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDPSKVDRSAAYAARWIAKSIVAGGLARRCLVQLAYAIGVAEPLSMHVETYGTGKYDDAKLLEIVKQNFKLRPYDIIQELNLRRPIYYDTSRFGHFGRKDELGTGGFTWEVPKKMVE	.	"Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate."	.	.	METK_LEIIN	reviewed	.	.	.	.	.	.
Mol02064	Protein	Matrix protein 2 (M2)	M	M2	956528	Influenza A virus	211044	Influenza A virus	Alphainfluenzavirus	197911	Orthomyxoviridae	11308	Articulavirales	2499411	Insthoviricetes	2497577	Negarnaviricota	2497569	Orthornavirae	2732396	.	MSLLTEVETPTRNGWECKCSDSSDPLVIAASIIGILHLILWILDRLFFKCIYRRIKYGLKRGPSTEGVPESMREEYRQEQQSAVDVDDGHFVNIELE	.	"Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation."	PDB: 5DLM	.	M2_I66A1	reviewed	.	.	.	.	.	.
Mol02065	Protein	Tetracycline resistance protein TetM (TETM)	tetM; tet; (M)	TETM	.	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKIINIGVLAHVDAGKTTLTESLLYNSGAITELGSVDKGTTRTDNTLLERQRGITIQTGITSFQWENTKVNIIDTPGHMDFLAEVYRSLSVLDGAILLISAKDGVQAQTRILFHALRKMGIPTIFFINKIDQNGIDLSTVYQDIKEKLSAEIVIKQKVELYPNVCVTNFTESEQWDTVIEGNDDLLEKYMSGKSLEALELEQEESIRFQNCSLFPLYHGSAKSNIGIDNLIEVITNKFYSSTHRGPSELCGNVFKIEYTKKRQRLAYIRLYSGVLHLRDSVRVSEKEKIKVTEMYTSINGELCKIDRAYSGEIVILQNEFLKLNSVLGDTKLLPQRKKIENPHPLLQTTVEPSKPEQREMLLDALLEISDSDPLLRYYVDSTTHEIILSFLGKVQMEVISALLQEKYHVEIELKEPTVIYMERPLKNAEYTIHIEVPPNPFWASIGLSVSPLPLGSGMQYESSVSLGYLNQSFQNAVMEGIRYGCEQGLYGWNVTDCKICFKYGLYYSPVSTPADFRMLAPIVLEQVLKKAGTELLEPYLSFKIYAPQEYLSRAYNDAPKYCANIVDTQLKNNEVILSGEIPARCIQEYRSDLTFFTNGRSVCLTELKGYHVTTGEPVCQPRRPNSRIDKVRYMFNKIT	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	H6VNE3_CLODI	unreviewed	.	.	.	.	.	.
Mol02066	Protein	Cuticle protein (TERG_08771 )	TERG_08771	TERG_08771 	.	Trichophyton rubrum	559305	Trichophyton rubrum	Trichophyton	5550	Arthrodermataceae	34384	Onygenales	33183	Eurotiomycetes	147545	Ascomycota	4890	Fungi	4751	.	MKASIGALALLLAQQASAAYIPSGSAKGSTLVRRDWGGLDGSQFVDPGNQPSCPECGGDGGEPQCPDGNCGGGEPQCPNGNCGGGIGGNIGGGIGGGIGGGIGGGIGGGIGGGIGGGIGGGIGGGGGDCWGGDDGLPPPCYPVPGNTPPDCTPEQENGFDFIDLIEGAINFFGGCDFSGFTCVDGIVKGALEVGGKVITALLRAGGDNIPTISKSNGGLAIVSIEAYAEVDVDIVLVFTMPDGSICRQFASCSPAGQTIMNEQCGGATSVGFHLAVHSKVSVCAVVIKKINFGCEPPTIPTWPFPPLPFPTTSLPPPETSGGYTTIPGTSESGSWSSMPSSYSMPTSGYTTVPGTSSPHSTPSGGFPTSSGGIPGQTTVPTSPAPTTWTSQSISTIYTTSTMTITSCPPEVPDCPTGSTTVITSTIPDNPDSQVSQVSQDSPVSLDSLDSQVSQDSQDSQVSLDSQDSQDSQDSQVSLDSQDNQVSLDSQVSLDSQVSQDSQDSQDSQDSQDSQDSQVSLDSQVNPDSQVSLDSQVNPDSQVSQDSLDNQVSQVSLDSQDSQVNQVSLDSQVSLDSQDNQVSLDSQVSLDSQVSLDSQDSQDSQDSQDSLDSQVNPDSQVSLDSQVNPDSQVSQDSQVSLDSQDSQDSQDSQVSLDSQDNQVSLDSQVSLDSQVSLDSQDSQDSQDSQVSLDSQVNPDSQVSLDSQVNPDSQVSQDSLDNQVSQVSLDSQDSQVNQVSQVSLDNPDSQVSQDNPVSQDSLDSQVNQVSQDSQCLIHQSFPDCDSNSHITCLCPSSEFAHKVIECIRAWSDDEKETQAALSFFLGICVTYIPKNPGLTDNLPPGIPIAPTSAPNGPAPPAVTVIITPTATGNHTVPPTTIVIPTVSFTTPTSGASHQAPYPVPAAPTSDGGSAPTPAPGGVPAPTPPYGSTGFMTVSPTGGVPHPTSTTEPYIGAASSVEAFLSQWVMMGITAMVGLIQFAL	.	.	.	.	F2SMI7_TRIRC	unreviewed	.	.	.	.	.	.
Mol02067	Protein	Mitochondrial trans-2-enoyl-CoA reductase (MECR)	mecR; mecR1; R114_08; R92_08	MECR	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MLYIKYTQNIMSHKIWLLVLVSTLIPLIPFYKISNFTFSKDMMNRNVSDTTSSVSHMLDGQQSSVTKDLAINVNQFETSNITYMILLIWVFGSLLCLFYMIKAFRQIDVIKSSSLESSYLNERLKVCQSKMQFYKKHITISYSSNIDNPMVFGLVKSQIVLPTVVVETMNDKEIEYIILHELSHVKSHDLIFNQLYVVFKMIFWFNPALYISKTMMDNDCEKVCDRNVLKILNRHEHIRYGESILKCSILKSQHINNVAAQYLLGFNSNIKERVKYIALYDSMPKPNRNKRIVAYIVCSISSFT	.	.	.	HGNC:19691	E9KNT8_STAAU	unreviewed	.	.	.	.	.	.
Mol02068	Protein	Fusion glycoprotein F0 (F)	F	F	.	Respiratory syncytial virus	12814	.	.	.	Pneumoviridae	11244	Mononegavirales	11157	Monjiviricetes	2497574	Negarnaviricota	2497569	Orthornavirae	2732396	.	MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKNAVTELQLLMQSTPPTNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEINLCNVDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGMDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN	.	[Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.	PDB: 2MDP; PDB: 3IXT; PDB: 3KPE; PDB: 3O41; PDB: 3O45; PDB: 3RKI; PDB: 3RRR; PDB: 3RRT; PDB: 4CCF; PDB: 4JHW; PDB: 4MMQ; PDB: 4MMR; PDB: 4MMS; PDB: 4MMT; PDB: 4MMU; PDB: 4MMV; PDB: 4ZYP; PDB: 5C69; PDB: 5C6B; PDB: 5EA3; PDB: 5EA4; PDB: 5EA5; PDB: 5EA6; PDB: 5EA7; PDB: 5EA8; PDB: 5J3D; PDB: 5K6B; PDB: 5K6C; PDB: 5K6F; PDB: 5K6G; PDB: 5K6H; PDB: 5K6I; PDB: 5KWW; PDB: 5TOJ; PDB: 5TOK; PDB: 5TPN; PDB: 5U68; PDB: 5UDC; PDB: 5W23; PDB: 6APB; PDB: 6APD; PDB: 6CXC; PDB: 6DC3; PDB: 6DC5; PDB: 6EAD; PDB: 6EAE; PDB: 6EAF; PDB: 6EAG; PDB: 6EAH; PDB: 6EAI; PDB: 6EAJ; PDB: 6EAK; PDB: 6EAL; PDB: 6EAM; PDB: 6EAN; PDB: 6NTX; PDB: 6OE4; PDB: 6OE5; PDB: 6OJ7; PDB: 6OUS; PDB: 6VKC; PDB: 6VKD; PDB: 6VKE; PDB: 6W52; PDB: 7LUE; PDB: 7LVW; PDB: 7MMN	.	FUS_HRSVA	reviewed	.	.	.	.	.	.
Mol02069	Protein	Formin binding protein 1 (FNBP1)	fnbP; ebpS; G6Y24_15200; HK402_07100	FNBP1	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MSNNFKDDFEKNRQSIDTNSHQDHTEDVEKDQSELEHQDTIENTEQQFPPRNAQRRKRRRDLATNHNKQVHNESQTSEDNVQNEAGTIDDRQVESSHSTESQEPSHQDSTPQHEEEYYNKNAFAMDKSHPEPIEDNDKHETIKDAENNTEHSTVSDKSKAEQSQQPKPYFATGANQANTSKDKHDDVTVKQDKDESKDHHSGKKGAAIGAGTAGVAGAAGAMGVSKAKKHSNDAQNKSNSDKSNNSTEDKASQDKSKDHHNGKKGAAIGAGTAGLAGGAASKSASAASKPHASNNASQNHDEHDNHDRDKERKKGGMAKVLLPLIAAVLIIGALAIFGGMALNNHNNGTKENKIANTNKNNADESKDKDTSKDASKDKSKSTDSDKSKEDQDKATKDESDNDQNNANQANNQAQNNQNQQQANQNQQQQQQRQGGGQRHTVNGQENLYRIAIQYYGSGSPENVEKIRRANGLSGNNIRNGQQIVIP	.	.	.	HGNC:17069	G0YZL6_STAAU	unreviewed	.	.	.	.	.	.
Mol02070	Protein	Aminoacyltransferase FemA (FEMA)	femA; SACOL1410	FEMA	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	MKFTNLTAKEFGAFTDSMPYSHFTQTVGHYELKLAEGYETHLVGIKNNNNEVIAACLLTAVPVMKVFKYFYSNRGPVIDYENQELVHFFFNELSKYVKKHRCLYLHIDPYLPYQYLNHDGEITGNAGNDWFFDKMSNLGFEHTGFHKGFDPVLQIRYHSVLDLKDKTADDIIKNMDGLRKRNTKKVKKNGVKVRFLSEEELPIFRSFMEDTSESKAFADRDDKFYYNRLKYYKDRVLVPLAYINFDEYIKELNEERDILNKDLNKALKDIEKRPENKKAHNKRDNLQQQLDANEQKIEEGKRLQEEHGNELPISAGFFFINPFEVVYYAGGTSNAFRHFAGSYAVQWEMINYALNHGIDRYNFYGVSGKFTEDAEDAGVVKFKKGYNAEIIEYVGDFIKPINKPVYAAYTALKKVKDRIF	.	"Catalyzes the formation of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. Adds glycines 2 and 3 of the pentaglycine bridge, using glycyl-tRNA(Gly) as donor. Involved in resistance to methicillin (By similarity)."	.	.	FEMA_STAAC	reviewed	.	.	.	.	.	.
Mol02072	Protein	Hydroxymethylpterin pyrophosphokinase-dihydropteroate synthetase (DHPS)	DHPS	DHPS	.	Plasmodium vivax	126793	Plasmodium vivax	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	RMIAIDILFFNNYPIFEKSISLKGEDIYKIITKYIHINHTSDQNRLDIIQNLGDKIEFLCIPHVYTKYRYSILLCLNDIIPEYKHSTFEEAIRSTYNSYVESFEEKYHINIRKNNKRLYVLKDKVSYLKERTHIVGILNVNYDSFSDGGLFVDPVKAVERMFEMASDGASVIDIGGESSGPYVVPNPSVTERDLVMPVLKLFKEEWHKLECEVGGGAVCCAAASDARKNAQSSLQGKLQKVRDAKPIISIDTVNYDLFKECVEGE	.	.	.	.	D5K9Y2_PLAVI	unreviewed	.	.	.	.	.	.
Mol02073	Protein	Cytochrome b (CYB)	MT-CYB; COB; CYTB; MTCYB	CYB	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	.	Plasmodiidae	Haemosporida	5819	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MNFYSINLVKAHLINYPCPLNINFLWNYGFLLGIIFFIQIITGVFLASRYTPDVSYAYYSIQHILRELWSGWCFRYMHATGASLVFLLTYLHILRGLNYSYMYLPLSWISGLILFMIFIVTAFVGYVLPWGQMSYWGATVITNLLSSIPVAVIWICGGYTVSDPTIKRFFVLHFILPFIGLCIVFIHIFFLHLHGSTNPLGYDTALKIPFYPNLLSLDVKGFNNVIILFLIQSLFGIIPLSHPDNAIVVNTYVTPSQIVPEWYFLPFYAMLKTVPSKPAGLVIVLLSLQLLFLLAEQRSLTTIIQFKMIFGARDYSVPIIWFMCAFYALLWIGCQLPQDIFILYGRLFIVLFFCSGLFVLVHYRRTHYDYSSQANI	.	Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.	.	.	CYB_PLAFA	reviewed	.	.	.	.	.	.
Mol02074	Protein	Chloramphenicol acetyltransferase (CAT)	catD	CAT	.	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MVFEKIDKNSWNRKEYFDHYFASVPCTYSMTVKVDITQIKEKGMKLYPAMLYYIAMIVNRHSEFRTAINQDGELGIYDEMIPSYTIFHNDTETFSSLWTECKSDFKSFLADYESDTQRYGNNHRMEGKPNAPENIFNVSMIPWSTFDGFNLNLQKGYDYLIPIFTMGKIIKKDNKIILPLAIQVHHAVCDGFHICRFVNELQELIIVTQVCL	.	This enzyme is an effector of chloramphenicol resistance in bacteria.	.	.	CAT_CLODI	reviewed	.	.	.	.	.	.
Mol02075	Protein	NADH dehydrogenase [ubiquinone] flavoprotein 1 (TbAT1)	Tb927.5.450b	TbAT1	.	Trypanosoma brucei	185431	Trypanosoma brucei	Trypanosoma	5690	Trypanosomatidae	5654	Trypanosomatida	2704949	Kinetoplastea	5653	Euglenozoa	33682	.	.	.	MLRRVGFLSATGSLLQAAASQQPPTQQEQRVHGGLKDQDRIFVNLYQDFGTDIDSAERRGDWYRTRDLLLKGHDWVINEIKASGLRGRGGAGFPSGLKWSFMPKSKPDGRPSYIVVNGDESEPGTCKDREIMRHEPHKLVEGALIAGFAMRARYGYIYIRGEFYNEWRAVDQAIKEAYARGYLGRNACGSGYDFDLYTYCGAGAYICGEETAMISSIEGGPGKPRLKPPFPANVGLYGCPTTVTNVETVSVSPTILRRGPSWFNSFGRRNNAGVKLFCICGHVNRPCTVEEEMSIPLRDLIERHAGGVRGGWDNLLAVIPGGSSCPLIPKSICDNVLMDFDALKEAQTGLGTAAVIVMDKSTDLIAAIHRLSMFYAHESCGQCTPCREGSPWLEKMMQRFVHGNARMEEVGTMLDVSKQLEGRTICALATAAAWPVQGLARHFTPLLQERIEKYWEANPHWGKSGSPWRRWKTHRYYAMQKGEKLNWDGKIVRNWN	.	"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I."	.	.	B2ZWD5_TRYB2	unreviewed	.	.	.	.	.	.
Mol02076	Protein	Tetracycline resistance protein TetW (TETW)	tetW	TET(W)	.	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MKIINIGILAHVDAGKTTLTESLLYASGAISEPGSVEKGTTRTDTMFLERQRGITIQAAVTSFQWHRCKVNIVDTPGHMDFLAEVYRSLAVLDGAILVISAKDGVQAQTRILFHALRKMNIPTVIFINKIDQAGVDLQSVVQSVRDKLSADIIIKQTVSLSPEIVLEENTDIEAWDAVIENNDKLLEKYIAGEPISREKLVREEQRRVQDASLFPVYYGSAKKGLGIQPLMDAVTGLFQPIGEQGSAALCGSVFKVEYTDCGQRRVYLRLYSGTLRLRDTVALAGREKLKITEMRIPSKGEIVRTDTAYPGEIVILPSDSVRLNDVLGDPTRLPRKRWREDPLPMLRTTIAPKTAAQRERLLDALTQLADTDPLLRCEVDSITHEIILSFLGRVQLEVVSALLSEKYKLETVVKEPSVIYMERPLKAASHTIHIEVPPNPFWASIGLSVTPLSLGSGVQYESRVSLGYLNQSFQNAVRDGIRYGLEQGLFGWNVTDCKICFEYGLYYSPVSTPADFRSLAPIVLEQALKESGTQLLEPYLSFILYAPQEYLSRAYHDAPKYCATIETAQVKKDEVVFTGEIPARCIQAYRTDLAFYTNGRSVCLTELKGYQAAVGQPVIQPRRPNSRLDKVRHMFQKVM	.	Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes.	.	.	B0B5F3_CLODI	unreviewed	.	.	.	.	.	.
Mol02077	Protein	DNA polymerase (A6BMM6)	UL54	A6BMM6	.	Human betaherpesvirus 5	10360	Human betaherpesvirus 5	Cytomegalovirus	10358	Herpesviridae	10292	Herpesvirales	548681	Herviviricetes	2731363	Peploviricota	2731361	Heunggongvirae	2731360	.	MFFNPYLSGGLTGGAVAGGRRQRSQPGSAQGSGKRPPQKQFLQIVPRGVMFDGQTGLIKHKTGRLPLMFYREIKHLLSHDMVWPCPWRETLVGRVVGPIRFHTYDQTDAVLFFDSPENVSPRYRQHLVPSGNVLRFFGATEHGYSICVNVFGQRSYFYCEYSDTDRLREVIASVGELVPEPRTPYAVSVTPATKTSIYGYGTRPVPDLQCVSISNWTMARKIGEYLLEQGFPVYEVRVDPLTRLVIDRRITTFGWCSVNRYDWRQQGRASTCDIEVDCDVSDLVAVPDDSSWPRYRCLSFDIECMSGEGGFPCAEKSDDIVIQISCVCYETGGNTAVDQGIPNGNDGRGCTSEGVIFGHSGLHLFTIGTCGQVGPDVDVYEFPSEYELLLGFMLFFQRYAPAFVTGYNINSFDLKYILTRLEYLYKVDSQRFCKLPTAQGGRFFLHSPAVGFKRQYAAAFPSASHNNPASTAATKVYIAGSVVIDMYPVCMAKTNSPNYKLNTMAELYLRQRKDDLSYKDIPRCFVANAEGRAQVGRYCLQDAVLVRDLFNTINFHYEAGAIARLAKIPLRRVIFDGHQIRIYTSLLDECACRDFILPNHYSKGTTVPETNSVAVSPNAAIISTAAVPGDAGSVAAMFQMSPPLQSAPSSQDGVLPGSGSNSSSSVGVFSVGSGSSGGVGVSNDSHGAGGTAAVSYQGATVFEPEVGYYNDPVAVFDFASLYPSIIMAHNLCYSTLLVPGGEYPVDPADVYSVTLENGVTHRFVRASVRVSVLSELLNKWVSQRRAVRECMRECQDPVRRMLLDKEQMALKVTCNAFYGFTGVVNGMMPCLPIAASITRIGRDMLERTARFIKDNFSEPCFLHNFFNQEDYVVRTREGDSEESSTLPEGLETSSGGSDERRVEARVIYGDTDSVFVRFRGLTPQALVARGPSLAHYVTACLFVEPVKLEFEKVFVSLMMICKKRYIGKVEGASGLSMKGVDLVRKTACEFVKGVTRDVLSLLFEDREVSEAAVRLSRLSLDEVKKYGVPRGFWRILRRLVQARDDLYLHRVRVEDLVLSSVLSKDISLYRQSNLPHIAVIKRLAARSEELPSVGDRVFYVLTAPGVRTAPQGSSDNGDSVTAGVVSRSDAIDGTDDDADGGGVEESNRRGGEPAKKRARKPPSAVCNYEVAEDPSYVREHGVPIHADKYFEQVLKAVTNVLSPVFPGGETARKDKFLHMVLPRRLHLEPAFLPYSVKAHECC	.	.	.	.	A6BMM6_HCMV	unreviewed	.	.	.	.	.	.
Mol02078	Protein	D-alanine ligase (vanD5)	vanD; ddl; Tn6712_000090	vanD5	.	Enterococcus faecium	1352	Enterococcus faecium	Enterococcus	.	Enterococcaceae	Lactobacillales	186826	186826	Bacilli	91061	Firmicutes	1239	.	.	.	MFKIKVAVLFGGCSEEHNVSIKSAMEIAANIDTKKYQPYYIGITKSGVWKMCEKPCLEWEQYAGDPVVFSPDRNTHGLLIQKDTGYEIQPVDVVFPMIHGKFGEDGSIQGLLELSGIPYVGCDIQSSVICMDKALAYIVVKNAGIAVPGFRILQEGDRLETEDFVYPVFVKPARSGSSFGVNKVCKAEELQAAIEEARKYDSKILIEEAVTGSEVGCAILGNGNNLMAGEVDQIELRHGFFKIHQEAQPEKGSENAVIRVPAALPDEVRERIQKTAMKIYRILGCRGLARIDLFLREDGYIVLNEVNTMPGFTSYSRYPRMMTAAGFTLSEILDRLIELSLRR	.	Cell wall formation.	.	.	A0A8F5Z8R9_ENTFC	unreviewed	.	.	.	.	.	.
Mol02079	Protein	Siderophore exporter (MMPL5)	mmpL5; SAMEA2071181_04373	MMPL5	.	Mycobacteroides abscessus	36809	Mycobacteroides abscessus	Mycobacteroides	670516	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MNDPTTDAFPAARHAARPWLPRMIRVLAVPIVLGWIAVTIALNTVVPQLEEVGHMRAVSMSPNDAPAMIATKRVGEVFEEFKTSSSVMIVLEGEQSLGADAHRFYDQMVRDLRADTTHVQHVQDFWADALTAAAAQSSDGKAAYVQVYIAGDQGEALANESVEAVRHITAAVPPSPGVRVYVTGPATTSADQEIVANDSMELIELVTFGVIMVMLLLVYRSVITMVIVVAMVMLELASARGLVALLSYHNAFGLTSFATSLVVTLAIAAATDYAIFLIGRYQEARRAGEDRESAYYTMFHGTAHVVLASGLTIAGATFCLHFTRLPYFKTTGIPLSIGMAIVVAMALTLGPALISVASRFGNVLEPKGAGKARGWRRVGAATVRWPGAILVAAVTMALVGLLTLPGYHTTYNDRIYLPGQVPANVGYAAADRHFSKAKMNPDLLLVESDHDLRNPADFLVIDKIAKALARVRGIAQVQTITRPDGKPIKHTSIPFNMSTANTAQTLTNDYSQANFANLLKQADAMQVTIDSMEKMQAITQQMAEVTASMSANMKNTAQDINQLRDNMSNFDDQFRPIRNYFYWEKHCFDIPMCWALRSVFDALDGISLMSDDFDTLVPDIQRMAGLMPQMVVLMPPMIASMKEQKQIMLSQYQVQKAQQDQTMAMQANASAMGQAFDDAKNDDSFYLPPEAFETADFKSGIKLFVSPNGHAVRFTIFHQSDPLTEEGTSRVEPLKTAAEDAIKGTPLEGSSIYVGGSAALYKDMQEGADYDLLIAAVAALILIFLIMVLLTRAVVAAAVIVGTVVLSLGASFGLSVLLWQHIIGTPLHWMVLPMAVIILLAVGADYNLLLVSRMKEELHAGLHTGTIRSMAGTGSVVTSAGLVFAFTMMGMMVSSFTVIGQIGTTIGLGLLFDTLVVRSFMTPSIASLLGRWFWWPMVVRPRPRPQPWPQPLHAGAAEAVRA	.	.	.	.	A0A8B4DZM8_9MYCO	unreviewed	.	.	.	.	.	.
Mol02080	Protein	HTH-type transcriptional activator (RHAR)	rhaR; GAN91_29155	RHAR	.	Bacteroides thetaiotaomicron	818	Bacteroides thetaiotaomicron	Bacteroides	.	Bacteroidaceae	Bacteroidales	171549	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MVFCNNANLLNVFVRHIANNQLRSLAEVATVAHQLKLLKDDFFASDQQAVAVADRYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPERLKLNLDWQRAIPGFSASAGQPHWRLGSMGMAQARQIIGQLEHESSQHVPFANEMAELLFGQLVMLLNRHRYTSDSLPPTSSETLLDKLITRLAASLKSPFALDEFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRHLNSQKD	.	.	.	.	A0A6I0SC50_BACT4	unreviewed	.	.	.	.	.	.
Mol02081	Protein	Cysteine desulfurase (K13)	K13	K13	.	Plasmodium falciparum	5841	Plasmodium falciparum	Plasmodium	5820	Plasmodiidae	1639119	Haemosporida	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	MKFLQIIKHLKLQNKKNALDNFVNCRTYEHISNINKLFLNNFSSTKEHSEHGQVKHENFLNNTLQYGENSQNGSTNNLKNGKYNMYVSEGNVNINEEKYKDNNISSNNTQYNNNSSNSGSLNDEGPLWKEHIDDVVNENKKKKMNRFYLDSQATTMIDPRVLDKMLPYMTYIYGNAHSRNHFFGWESEKAVEDARTNLLNLINGKNNKEIIFTSGATESNNLALIGICTYYNKLNKQKNHIITSQIEHKCILQTCRFLQTKGFEVTYLKPDTNGLVKLDDIKNSIKDNTIMASFIFVNNEIGVIQDIENIGNLCKEKNILFHTDASQAAGKVPIDVQKMNIDLMSMSGHKLYGPKGIGALYIKRKKPNIRLNALIHGGGQERGLRSGTLPTHLIVGFGEAAKVCSLEMNRDEKKVRYFFNYVKDYLTKHLDYIVFNGCQINRYYGNMNISFLFVEGESLLMSLNEIALSSGSACTSSTLEPSYVLRSIGISEDIAHTSIRIGFNRFTTFFEVQQLCINLVKSVERLRSISPLYEME	.	.	.	.	A0A5J6C8W8_PLAFA	unreviewed	.	.	.	.	.	.
Mol02082	Protein	Pyruvate synthase subunit (PORD)	porD; HPYLPMSS1_01051	PORD	.	Helicobacter pylori	210	Helicobacter pylori	Helicobacter	209	Helicobacteraceae	72293	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MKDWNEFEMGAVLFPFEKNAQSEMEKHNDERHYTEQSYFTTSVAHWRVAKPVHNNNICINCFNCWVYCPDAAILSREGKLKGVDYSHCKGCGVCVDVCPTNPKSLWMFEEQIEPATALTQWPQKQEKKKS	.	.	.	.	A0A3S6H3S8_HELPX	unreviewed	.	.	.	.	.	.
Mol02083	Protein	2-Oxoglutarate oxidoreductase OorD subunit (OORD)	oorD; HPYLPMSS1_00793	OORD	.	Helicobacter pylori	210	Helicobacter pylori	Helicobacter	209	Helicobacteraceae	72293	Campylobacterales	213849	Epsilonproteobacteria	29547	Proteobacteria	1224	.	.	.	MAKMSAPDGVAVWVNEDRCKGCDICVSVCPAGVLGMGIEKERVLGKVAKVAYPESCIGCVQCELHCPDFAIYVADRKDFKFAKVSKEAQERSEKVKANKYMLLEETILEGRGK	.	.	.	.	A0A3Q8AJW8_HELPX	unreviewed	.	.	.	.	.	.
Mol02084	Protein	Inferred by orthology to a S. mansoni protein (SMDR2)	SMDR2	SMDR2	.	Schistosoma mansoni	6183	.	Schistosoma	6181	Schistosomatidae	31245	Strigeidida	6180	Trematoda	6178	Platyhelminthes	6157	Metazoa	33208	.	MAKTQSSNTQVSLSQKSEKDHENVKKNNVSFGKLFQYASTCHKFLIIIGNICAILLGISFPASILVFRSMINGLFNRSSSNNIYGLLGWYFLMAILIFVLCMWKCVCVEFASKRIVQQIQLLYYQAVLHKDVLWFDDHPTGDIINNLTENLNSIESGIGTKLSDFNQNMSGFLAGIIIGFIVKWKLALVACSTLPFVVIAFSLFGIAFKYFHGKEIKAYSRACTISNEVLSSIRTVIAFGGEKRESLRYQKELTSAELMGIKKATAFGSVGGCIGLVIFSSAALVFWFGVKLIRDEDADPGSVIAVFINILLGSIFLGNALPNIPYIMGAVTASKDIFATIDHVSEIEKKDRGKILSDFDGSITFRHVNFNYPSRPDVTILVNFCLTVKSGQTIALVGSSGSGKSTLIHMLQRFYDPTQGEILIQGVDLRELNIHNYRNQIGCVQQEPVLFDGTIRENIGLGKLNATDEEIHEAAIKANAHQFIMRLPQGYDTLVGEKGSNLSGGQKQRIAIARVLIRKPKLLLLDEATSALDTQSERIVQGALDKIVGGCTVIIIAHRLSTIINADYIIVLDQGCIREMGKHNELLKLNGLYATMYYGQEGIDKEQEDSTDDEVDHNQNDGSKRHLTNHHPSPFPKDDYSECSNVTTSSLHNKTVIWLTTNINTKISRAHNSLYLRLLSINRPEMIYIIMGCFCSIISGLLQPAFSLLYSEVYQVFDLRKTPDEMTKKINMVSGIMAGLGFIQLFIGATQGYLFGVAAERLTKRLRSNLFDSMLKQEIGWFDRSDNRPGALTAFLSTDASKVAQISGSRLSTAFEAVVLVIASLVIGFIYSWQLTLVMIPFIPVLLLSSRINMKRVSKNEDKIVAKGISIAKESISAHRTVKSLSLEEYFYQRFKLACIECSSTHLQEAIKIGLVQSIALSGPVLSLTACFALGNYLIQQNAISMISLFKVFITFSMCSQALGRITAFTTKTKEAEEAMGRIFTVIDRKPSIETNQGDQPKEKFNGLIEFKHVNFRYPTRPETKVLNNFTYRIQPGSKIALVGQSGCGKSTLIQLLQRFYDPTDHGLHNGIFFDGINLRQLAPYWIRRQIGIVSQEPILFNISLRDNIAYGDNSRIVSMDEIIEAAKLANIHDFILSLPNAYETLAGQDGSHLSGGQKQRIAIARAIIRKPTLLLLDEATSALDNENQRLVQKALDDAMVTRTSIIIAHRLNTIEKVDYIIVLSNGRIIEYGKLNELIHRKGEFFNLYKLDNTK	.	.	.	.	A0A3Q0KG70_SCHMA	unreviewed	.	.	.	.	.	.
Mol02085	Protein	Type I nitroreductase (NTR)	NTR	NTR	.	Trypanosoma cruzi	5693	Trypanosoma cruzi	Trypanosoma	5690	Trypanosomatidae	5654	Trypanosomatida	2704949	Kinetoplastea	5653	Euglenozoa	33682	.	.	.	MRRNDIKRGLWDSLILYWRWNRESLLRNVSAFAENGRHVIGMDGPVETGSEKGVGRGNSSMPPFFSSMPPSLSSSSSLPLDAMKRVVHERRSCKRFDPTKPIDLDVVSDLLAMTVRAPTALNLQLWVAVVIHEEEQRETLSRAALGQPQPRDAAVTVVFAGDMEPESNAPAALEMGLESGYYHSLYGAAYLRHVYYLLHGGPCEAMSHVKAIVSAWYSESTGNAMLSVPRNKQAYAWKQVMIPATTFLYLATAAGFDTAILEGFDEAQVRRVAGLPPRFTVPVIISVGHGAKNGFHSVRSPRFPTKHLVRWGKF	.	.	.	.	A0A2S1JL39_TRYCR	unreviewed	.	.	.	.	.	.
Mol02086	Protein	Glutathione S-transferase kappa (GST)	QR98_0015530	GST	.	H9N2 subtype	52283	H9N2 subtype	Sarcoptes	52282	Sarcoptidae	52281	Sarcoptiformes	83137	Arachnida	6854	Arthropoda	6656	Metazoa	33208	.	MTVVEFFFDIISPYSRLQYELLMRKVPHWKSMQLKLTPVSIRAIFEGSSNPSPALNPVKRAYLLRDLEMVHQYHDIPFAIPNDFMKIAIEIGSLKLQHFLAAIQSEIDDETFKRLVGEKFFDPNNPINVFLEDQFKQVAIDMKIDRNLIEKILSRLDSEEIKAKLEENNRIALNLGGFGLPITLVHCDPPQWVFGSDRMHLLAHLLHESI	.	.	.	.	A0A131ZWQ3_SARSC	unreviewed	.	.	.	.	.	.
Mol02087	Protein	Bifunctional dihydrofolate reductase-thymidylate synthase (PFDHFR)	dhfr	Pfdhfr	.	Plasmodium falciparum	5833	Plasmodium falciparum	Plasmodium	.	Plasmodiidae	Haemosporida	5819	5819	Aconoidasida	422676	Apicomplexa	5794	.	.	.	DIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCNSLDMKYFRAVTTYVNESKYEKLKYKRCKYLNKETVDNVNDMPNSKKLQNVVVMGRTNWESIPKKFKPLSNRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCFIIGGSVVYQEFLEKKLIKKIYFTRINSTYEC	.	"Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP."	.	.	A0A0U2XGD2_PLAFA	unreviewed	.	.	.	.	.	.
Mol02088	Protein	Aquaporin 2/3 (AQP2/3)	AQP2/3	AQP2/3	.	Trypanosoma	5690	Trypanosoma	.	.	Trypanosomatidae	5654	Trypanosomatida	2704949	Kinetoplastea	5653	Euglenozoa	33682	.	.	.	MQSQPDNVAYPMELQAVNKDGTVEVRVQGNDDSSNRKHEVAEAQEEVPGGINFWAPRELRLNYRDYMGELLGTFVLLFMGNGVVATVIIDGKLGFLSITLGWGIAVTMALYVSLGISSGHLNPAVTVGNAVFGDFPWRKVPGYIAAQMLGAFLGAACAYGVFADLLKAHGGGELIAFGEKGIAWVFAMYPAEGNGIFYPIFAELISTAVLLLCVCGIFDPNNSPAKGYETVAIGALVFVMVNNFGLASPLAMNPSLDFGPRVFGAILLGGEVFSHANYYFWVPLVVPFFGAILGLFLYKYFLPH	.	.	.	.	A0A0H4BF23_9TRYP	unreviewed	.	.	.	.	.	.
Mol02089	Protein	Aquaporin 2 (AQP2)	AQP2	AQP2	.	Trypanosoma	5690	Trypanosoma	.	.	Trypanosomatidae	5654	Trypanosomatida	2704949	Kinetoplastea	5653	Euglenozoa	33682	.	.	.	MQSQPDNVAYPMELQAVNKDGTVEVRVQGNDDSSNRKHEVAEAQEEVPGGINFWAPRELRLNYRDYMGELLGTFVLLFMGNGVVATVIIDGKLGFLSITLGWGIAVTMALYVSLGISSGHLNPAVTVGNAVFGDFPWRKVPGYIAAQMLGAFLGAACAYGVFADLLKAHGGGELIAFGEKGIAWVFAMYPAEGNGIFYPIFAELISTAVLLLCVCGIFDPNNSPAKGYETVAIGALVFVMVNNFGLASPLAMNPSLDFGPRVFGAILLGGEVFSHANYYFWVPLVVPFFGAILGLFLYKYFLPH	.	.	.	HGNC:634	A0A0H4BF23_9TRYP	unreviewed	.	.	.	.	.	.
Mol02090	Protein	G2-specific protein kinase (NIMA)	NIMA	NIMA	.	Bacteroides fragilis	817	Bacteroides fragilis	Bacteroides	.	Bacteroidaceae	Bacteroidales	171549	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	MVESLVYLVLHTRLAGRILLCQPKHSGTLLDLIGQNTGFTEDNDTPEIGCKLGRNYPVLLHHTKRDFGMLPDGIHLMPLHGTVKINLPVGIHIAHGDGIRISVIAMKGKRTAGHALQYRQAFFGRQQLAFAPHFSEHHISFI	.	.	.	.	A0A097IY62_BACFG	unreviewed	.	.	.	.	.	.
Mol02091	Protein	mRNA export factor (UL54)	UL54	UL54	.	Human betaherpesvirus 5	10359	Human betaherpesvirus 5	Cytomegalovirus	10358	Herpesviridae	10292	Herpesvirales	548681	Herviviricetes	2731363	Peploviricota	2731361	Heunggongvirae	2731360	.	MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSSGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPEQHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGPRTRGVRQAPPPLMTLAISPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGPSLYRTFAGNPRAASTAKAMRDCVLRQENFIEALASADETLAWCKMCIHHNLPLRPQDPIIGTAAAVLDNLATRLRPFLQCYLKARGLCGLDELCSRRRLADIKDIASFVFVILARLANRVERGVAEIDYATLGVGVGEKMHFYLPGACMAGLIEILDTHRQECSSRVCELTASHIVAPPYVHGKYFYCNSLF	.	.	.	.	A0A076N1M8_HHV1	unreviewed	.	.	.	.	.	.
Mol02092	Protein	Flavodoxin (Fld)	ispG; gcpE; BN1095_330259; BN1096_520594; BN1097_630018; E5F40_00180	Fld	.	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MSYERRKTREVSVGTVKIGGENPISIQSMTNTDTRDADATIAQIKRLEEAGCDIVRVAVPDIKAAKNIAKIKSSVNIPIIADIHFDYKLALEAIEQGVDGIRINPGNIGSIERVKMVVEKCKERNLKIRIGVNGGSLEKELLKKYGSATAEALVESAMGHIKILEDLDFHNIVISLKSSDIYKTVDAYELISKRVDYPLHIGITESGSVHKGTIKSSIGVGALLLKGIGDTVRISLTGDPVEEVIVGKQILRSLGLLNDKIKVISCPTCGRCNIDLISVVNEVEEKIGSMEKNITVAIMGCAVNGPGEAREADIGIAGGKGEGLLFKKGEIVRMIDGNKLVDELLEEIEKL	.	"Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate."	.	.	A0A069A8Y2_CLODI	unreviewed	.	.	.	.	.	.
Mol02093	Protein	Mitogen-activated protein kinase 15 (MAPK15)	Mitogen-activated protein kinase 15 (MAP kinase 15) (MAPK 15) (EC 2.7.11.24) (Extracellular signal-regulated kinase 7) (ERK-7) (Extracellular signal-regulated kinase 8) (ERK-8); MAPK15; ERK7; ERK8	MAPK15	225689	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000533830.1,MAPK15-208,881; ENST00000528175.1,MAPK15-207,507; ENST00000484654.1,MAPK15-206,2240; ENST00000475376.1,MAPK15-205,351; ENST00000461928.1,MAPK15-204,925; ENST00000395108.2,MAPK15-203,765; ENST00000395107.8,MAPK15-202,834; ENST00000338033.9,MAPK15-201,1871"	MCTVVDPRIVRRYLLRRQLGQGAYGIVWKAVDRRTGEVVAIKKIFDAFRDKTDAQRTFREITLLQEFGDHPNIISLLDVIRAENDRDIYLVFEFMDTDLNAVIRKGGLLQDVHVRSIFYQLLRATRFLHSGHVVHRDQKPSNVLLDANCTVKLCDFGLARSLGDLPEGPEDQAVTEYVATRWYRAPEVLLSSHRYTLGVDMWSLGCILGEMLRGRPLFPGTSTLHQLELILETIPPPSEEDLLALGSGCRASVLHQLGSRPRQTLDALLPPDTSPEALDLLRRLLVFAPDKRLSATQALQHPYVQRFHCPSDEWAREADVRPRAHEGVQLSVPEYRSRVYQMILECGGSSGTSREKGPEGVSPSQAHLHKPRADPQLPSRTPVQGPRPRPQSSPGHDPAEHESPRAAKNVPRQNSAPLLQTALLGNGERPPGAKEAPPLTLSLVKPSGRGAAPSLTSQAAAQVANQALIRGDWNRGGGVRVASVQQVPPRLPPEARPGRRMFSTSALQGAQGGARALLGGYSQAYGTVCHSALGHLPLLEGHHV	"Chromosome 8: 143,716,340-143,722,458 forward strand"	"Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner. Controls both, basal and starvation-induced autophagy throught its interaction with GABARAP, MAP1LC3B and GABARAPL1 leading to autophagosome formation, SQSTM1 degradation and reduced MAP1LC3B inhibitory phosphorylation. Regulates primary cilium formation and the localization of ciliary proteins involved in cilium structure, transport, and signaling. Prevents the relocation of the sugar-adding enzymes from the Golgi to the endoplasmic reticulum, thereby restricting the production of sugar-coated proteins. Upon amino-acid starvation, mediates transitional endoplasmic reticulum site disassembly and inhibition of secretion. Binds to chromatin leading to MAPK15 activation and interaction with PCNA, that which protects genomic integrity by inhibiting MDM2-mediated degradation of PCNA. Regulates DA transporter (DAT) activity and protein expression via activation of RhoA. In response to H(2)O(2) treatment phosphorylates ELAVL1, thus preventing it from binding to the PDCD4 3'UTR and rendering the PDCD4 mRNA accessible to miR-21 and leading to its degradation and loss of protein expression. Also functions in a kinase activity-independent manner as a negative regulator of growth. Phosphorylates in vitro FOS and MBP. During oocyte maturation, plays a key role in the microtubule organization and meiotic cell cycle progression in oocytes, fertilized eggs, and early embryos. Interacts with ESRRA promoting its re-localization from the nucleus to the cytoplasm and then prevents its transcriptional activity."	.	HGNC:24667	MK15_HUMAN	reviewed	ENSG00000181085	.	.	.	.	.
Mol02094	Protein	SARS-CoV-2 Papain-like protease (SARS-CoV-2 nsp3)	nsp3	rep	43740578	Severe acute respiratory syndrome coronavirus 2 	2697049	Severe acute respiratory syndrome coronavirus	Betacoronavirus	694002	Coronaviridae	11118	Nidovirales	76804	Pisoniviricetes	2732506	Pisuviricota	2732408	Orthornavirae	2732396	.	APTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGG	.	Responsible for the cleavages located at the N-terminus of the replicase polyprotein. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.	PDB: 5R7Z; PDB: 5R80; PDB: 5R81; PDB: 5R82; PDB: 5R83; PDB: 5R84; PDB: 5R8T; PDB: 5RE4; PDB: 5RE5; PDB: 5RE6; PDB: 5RE7; PDB: 5RE8; PDB: 5RE9; PDB: 5REA; PDB: 5REB; PDB: 5REC; PDB: 5RED; PDB: 5REE; PDB: 5REF; PDB: 5REG; PDB: 5REH; PDB: 5REI; PDB: 5REJ; PDB: 5REK; PDB: 5REL; PDB: 5REM; PDB: 5REN; PDB: 5REO; PDB: 5REP; PDB: 5RER; PDB: 5RES; PDB: 5RET; PDB: 5REU; PDB: 5REV; PDB: 5REW; PDB: 5REX; PDB: 5REY; PDB: 5REZ; PDB: 5RF0; PDB: 5RF1; PDB: 5RF2; PDB: 5RF3; PDB: 5RF4; PDB: 5RF5; PDB: 5RF6; PDB: 5RF7; PDB: 5RF8; PDB: 5RF9; PDB: 5RFA; PDB: 5RFB; PDB: 5RFC; PDB: 5RFD; PDB: 5RFE; PDB: 5RFF; PDB: 5RFG; PDB: 5RFH; PDB: 5RFI; PDB: 5RFJ; PDB: 5RFK; PDB: 5RFL; PDB: 5RFM; PDB: 5RFN; PDB: 5RFO; PDB: 5RFP; PDB: 5RFQ; PDB: 5RFR; PDB: 5RFS; PDB: 5RFT; PDB: 5RFU; PDB: 5RFV; PDB: 5RFW; PDB: 5RFX; PDB: 5RFY; PDB: 5RFZ; PDB: 5RG0; PDB: 5RG1; PDB: 5RG2; PDB: 5RG3; PDB: 5RGG; PDB: 5RGH; PDB: 5RGI; PDB: 5RGJ; PDB: 5RGK; PDB: 5RGL; PDB: 5RGM; PDB: 5RGN; PDB: 5RGO; PDB: 5RGP; PDB: 5RGQ; PDB: 5RGR; PDB: 5RGS; PDB: 5RGT; PDB: 5RGU; PDB: 5RGV; PDB: 5RGW; PDB: 5RGX; PDB: 5RGY; PDB: 5RGZ; PDB: 5RH0; PDB: 5RH1; PDB: 5RH2; PDB: 5RH3; PDB: 5RH4; PDB: 5RH5; PDB: 5RH6; PDB: 5RH7; PDB: 5RH8; PDB: 5RH9; PDB: 5RHA; PDB: 5RHB; PDB: 5RHC; PDB: 5RHD; PDB: 5RHE; PDB: 5RHF; PDB: 5RL0; PDB: 5RL1; PDB: 5RL2; PDB: 5RL3; PDB: 5RL4; PDB: 5RL5; PDB: 5RL6; PDB: 5RL7; PDB: 5RL8; PDB: 5RL9; PDB: 5RLB; PDB: 5RLC; PDB: 5RLD; PDB: 5RLE; PDB: 5RLF; PDB: 5RLG; PDB: 5RLH; PDB: 5RLI; PDB: 5RLJ; PDB: 5RLK; PDB: 5RLL; PDB: 5RLM; PDB: 5RLN; PDB: 5RLO; PDB: 5RLP; PDB: 5RLQ; PDB: 5RLR; PDB: 5RLS; PDB: 5RLT; PDB: 5RLU; PDB: 5RLV; PDB: 5RLW; PDB: 5RLY; PDB: 5RLZ; PDB: 5RM0; PDB: 5RM1; PDB: 5RM2; PDB: 5RM3; PDB: 5RM4; PDB: 5RM5; PDB: 5RM6; PDB: 5RM7; PDB: 5RM8; PDB: 5RM9; PDB: 5RMA; PDB: 5RMB; PDB: 5RMC; PDB: 5RMD; PDB: 5RME; PDB: 5RMF; PDB: 5RMG; PDB: 5RMH; PDB: 5RMI; PDB: 5RMJ; PDB: 5RMK; PDB: 5RML; PDB: 5RMM; PDB: 5ROB; PDB: 5RS7; PDB: 5RS8; PDB: 5RS9; PDB: 5RSB; PDB: 5RSC; PDB: 5RSD; PDB: 5RSE; PDB: 5RSF; PDB: 5RSG; PDB: 5RSH; PDB: 5RSI; PDB: 5RSJ; PDB: 5RSK; PDB: 5RSL; PDB: 5RSM; PDB: 5RSN; PDB: 5RSO; PDB: 5RSP; PDB: 5RSQ; PDB: 5RSR; PDB: 5RSS; PDB: 5RST; PDB: 5RSU; PDB: 5RSV; PDB: 5RSW; PDB: 5RSX; PDB: 5RSY; PDB: 5RSZ; PDB: 5RT0; PDB: 5RT1; PDB: 5RT2; PDB: 5RT3; PDB: 5RT4; PDB: 5RT5; PDB: 5RT6; PDB: 5RT7; PDB: 5RT8; PDB: 5RT9; PDB: 5RTA; PDB: 5RTB; PDB: 5RTC; PDB: 5RTD; PDB: 5RTE; PDB: 5RTF; PDB: 5RTG; PDB: 5RTH; PDB: 5RTI; PDB: 5RTJ; PDB: 5RTK; PDB: 5RTL; PDB: 5RTM; PDB: 5RTN; PDB: 5RTO; PDB: 5RTP; PDB: 5RTQ; PDB: 5RTR; PDB: 5RTS; PDB: 5RTT; PDB: 5RTU; PDB: 5RTV; PDB: 5RTW; PDB: 5RTX; PDB: 5RTY; PDB: 5RTZ; PDB: 5RU0; PDB: 5RU1; PDB: 5RU2; PDB: 5RU3; PDB: 5RU4; PDB: 5RU5; PDB: 5RU6; PDB: 5RU7; PDB: 5RU8; PDB: 5RU9; PDB: 5RUA; PDB: 5RUC; PDB: 5RUD; PDB: 5RUE; PDB: 5RUF; PDB: 5RUG; PDB: 5RUH; PDB: 5RUI; PDB: 5RUJ; PDB: 5RUK; PDB: 5RUL; PDB: 5RUM; PDB: 5RUN; PDB: 5RUO; PDB: 5RUP; PDB: 5RUQ; PDB: 5RUR; PDB: 5RUS; PDB: 5RUT; PDB: 5RUU; PDB: 5RUV; PDB: 5RUW; PDB: 5RUX; PDB: 5RUY; PDB: 5RUZ; PDB: 5RV0; PDB: 5RV1; PDB: 5RV2; PDB: 5RV3; PDB: 5RV4; PDB: 5RV5; PDB: 5RV6; PDB: 5RV7; PDB: 5RV8; PDB: 5RV9; PDB: 5RVA; PDB: 5RVB; PDB: 5RVC; PDB: 5RVD; PDB: 5RVE; PDB: 5RVF; PDB: 5RVG; PDB: 5RVH; PDB: 5RVI; PDB: 5RVJ; PDB: 5RVK; PDB: 5RVL; PDB: 5RVM; PDB: 5RVN; PDB: 5RVO; PDB: 5RVP; PDB: 5RVQ; PDB: 5RVR; PDB: 5RVS; PDB: 5RVT; PDB: 5RVU; PDB: 5RVV; PDB: 5S18; PDB: 5S1A; PDB: 5S1C; PDB: 5S1E; PDB: 5S1G; PDB: 5S1I; PDB: 5S1K; PDB: 5S1M; PDB: 5S1O; PDB: 5S1Q; PDB: 5S1S; PDB: 5S1U; PDB: 5S1W; PDB: 5S1Y; PDB: 5S20; PDB: 5S22; PDB: 5S24; PDB: 5S26; PDB: 5S27; PDB: 5S28; PDB: 5S29; PDB: 5S2A; PDB: 5S2B; PDB: 5S2C; PDB: 5S2D; PDB: 5S2E; PDB: 5S2F; PDB: 5S2G; PDB: 5S2H; PDB: 5S2I; PDB: 5S2J; PDB: 5S2K; PDB: 5S2L; PDB: 5S2M; PDB: 5S2N; PDB: 5S2O; PDB: 5S2P; PDB: 5S2Q; PDB: 5S2R; PDB: 5S2S; PDB: 5S2T; PDB: 5S2U; PDB: 5S2V; PDB: 5S2W; PDB: 5S2X; PDB: 5S2Y; PDB: 5S2Z; PDB: 5S30; PDB: 5S31; PDB: 5S32; PDB: 5S33; PDB: 5S34; PDB: 5S35; PDB: 5S36; PDB: 5S37; PDB: 5S38; PDB: 5S39; PDB: 5S3A; PDB: 5S3B; PDB: 5S3C; PDB: 5S3D; PDB: 5S3E; PDB: 5S3F; PDB: 5S3G; PDB: 5S3H; PDB: 5S3I; PDB: 5S3J; PDB: 5S3K; PDB: 5S3L; PDB: 5S3M; PDB: 5S3N; PDB: 5S3O; PDB: 5S3P; PDB: 5S3Q; PDB: 5S3R; PDB: 5S3S; PDB: 5S3T; PDB: 5S3U; PDB: 5S3V; PDB: 5S3W; PDB: 5S3X; PDB: 5S3Y; PDB: 5S3Z; PDB: 5S40; PDB: 5S41; PDB: 5S42; PDB: 5S43; PDB: 5S44; PDB: 5S45; PDB: 5S46; PDB: 5S47; PDB: 5S48; PDB: 5S49; PDB: 5S4A; PDB: 5S4B; PDB: 5S4C; PDB: 5S4D; PDB: 5S4E; PDB: 5S4F; PDB: 5S4G; PDB: 5S4H; PDB: 5S4I; PDB: 5S4J; PDB: 5S4K; PDB: 5S6X; PDB: 5S6Y; PDB: 5S6Z; PDB: 5S70; PDB: 5S71; PDB: 5S72; PDB: 5S73; PDB: 5S74; PDB: 5SA4; PDB: 5SA5; PDB: 5SA6; PDB: 5SA7; PDB: 5SA8; PDB: 5SA9; PDB: 5SAA; PDB: 5SAB; PDB: 5SAC; PDB: 5SAD; PDB: 5SAE; PDB: 5SAF; PDB: 5SAG; PDB: 5SAH; PDB: 5SAI; PDB: 6LU7; PDB: 6LZE; PDB: 6M03; PDB: 6M0K; PDB: 6M2N; PDB: 6M2Q; PDB: 6M71; PDB: 6VWW; PDB: 6VXS; PDB: 6W01; PDB: 6W02; PDB: 6W4B; PDB: 6W4H; PDB: 6W61; PDB: 6W63; PDB: 6W6Y; PDB: 6W75; PDB: 6W9C; PDB: 6W9Q; PDB: 6WC1; PDB: 6WCF; PDB: 6WEN; PDB: 6WEY; PDB: 6WIQ; PDB: 6WJT; PDB: 6WKQ; PDB: 6WKS; PDB: 6WLC; PDB: 6WNP; PDB: 6WOJ; PDB: 6WQ3; PDB: 6WQD; PDB: 6WQF; PDB: 6WRH; PDB: 6WRZ; PDB: 6WTC; PDB: 6WTJ; PDB: 6WTK; PDB: 6WTM; PDB: 6WTT; PDB: 6WUU; PDB: 6WVN; PDB: 6WX4; PDB: 6WXC; PDB: 6WXD; PDB: 6WZU; PDB: 6X1B; PDB: 6X4I; PDB: 6XA4; PDB: 6XA9; PDB: 6XAA; PDB: 6XB0; PDB: 6XB1; PDB: 6XB2; PDB: 6XBG; PDB: 6XBH; PDB: 6XBI; PDB: 6XCH; PDB: 6XDH; PDB: 6XFN; PDB: 6XG3; PDB: 6XHM; PDB: 6XHU; PDB: 6XIP; PDB: 6XKF; PDB: 6XKH; PDB: 6XKM; PDB: 6XMK; PDB: 6XOA; PDB: 6XQS; PDB: 6XQT; PDB: 6XQU; PDB: 6XR3; PDB: 6Y2E; PDB: 6Y2F; PDB: 6Y2G; PDB: 6Y84; PDB: 6YB7; PDB: 6YNQ; PDB: 6YVA; PDB: 6YVF; PDB: 6YWK; PDB: 6YWL; PDB: 6YWM; PDB: 6YYT; PDB: 6YZ1; PDB: 6Z2E; PDB: 6Z5T; PDB: 6Z6I; PDB: 6Z72; PDB: 6ZCT; PDB: 6ZLW; PDB: 6ZM7; PDB: 6ZME; PDB: 6ZMI; PDB: 6ZMO; PDB: 6ZMT; PDB: 6ZN5; PDB: 6ZOJ; PDB: 6ZOK; PDB: 6ZON; PDB: 6ZP4; PDB: 6ZPE; PDB: 6ZRT; PDB: 6ZRU; PDB: 6ZSL; PDB: 7A1U; PDB: 7ABU; PDB: 7ADW; PDB: 7AEG; PDB: 7AF0; PDB: 7AGA; PDB: 7AHA; PDB: 7AK4; PDB: 7AKU; PDB: 7ALH; PDB: 7ALI; PDB: 7AMJ; PDB: 7ANS; PDB: 7AOL; PDB: 7AP6; PDB: 7APH; PDB: 7AQE; PDB: 7AQI; PDB: 7AQJ; PDB: 7AR5; PDB: 7AR6; PDB: 7ARF; PDB: 7AVD; PDB: 7AWR; PDB: 7AWS; PDB: 7AWU; PDB: 7AWW; PDB: 7AX6; PDB: 7AXM; PDB: 7AXO; PDB: 7AY7; PDB: 7B3E; PDB: 7B83; PDB: 7BAJ; PDB: 7BAK; PDB: 7BAL; PDB: 7BB2; PDB: 7BE7; PDB: 7BF3; PDB: 7BF4; PDB: 7BF5; PDB: 7BF6; PDB: 7BFB; PDB: 7BGP; PDB: 7BQ7; PDB: 7BQY; PDB: 7BRO; PDB: 7BRP; PDB: 7BTF; PDB: 7BUY; PDB: 7BV1; PDB: 7BV2; PDB: 7BWQ; PDB: 7BZF; PDB: 7C2I; PDB: 7C2J; PDB: 7C2K; PDB: 7C2Q; PDB: 7C2Y; PDB: 7C6S; PDB: 7C6U; PDB: 7C7P; PDB: 7C8B; PDB: 7C8R; PDB: 7C8T; PDB: 7C8U; PDB: 7CA8; PDB: 7CAM; PDB: 7CB7; PDB: 7CBT; PDB: 7CJD; PDB: 7CJM; PDB: 7CMD; PDB: 7COM; PDB: 7CUT; PDB: 7CUU; PDB: 7CWB; PDB: 7CWC; PDB: 7CX9; PDB: 7D1M; PDB: 7D1O; PDB: 7D7K; PDB: 7D7L; PDB: 7DDC; PDB: 7DG6; PDB: 7DIY; PDB: 7DVX; PDB: 7DVY; PDB: 7DW0; PDB: 7DW6; PDB: 7EQ4; PDB: 7JFQ; PDB: 7JHE; PDB: 7JIB; PDB: 7JKV; PDB: 7JME; PDB: 7JOY; PDB: 7JP0; PDB: 7JP1; PDB: 7JPE; PDB: 7JPY; PDB: 7JPZ; PDB: 7JQ0; PDB: 7JQ1; PDB: 7JQ2; PDB: 7JQ3; PDB: 7JQ4; PDB: 7JQ5; PDB: 7JQB; PDB: 7JQC; PDB: 7JR3; PDB: 7JR4; PDB: 7JST; PDB: 7JSU; PDB: 7JT0; PDB: 7JT7; PDB: 7JU7; PDB: 7JVZ; PDB: 7JW8; PDB: 7JYC; PDB: 7JYY; PDB: 7JZ0; PDB: 7K0E; PDB: 7K0F; PDB: 7K0R; PDB: 7K1L; PDB: 7K1O; PDB: 7K3N; PDB: 7K3T; PDB: 7K40; PDB: 7K5I; PDB: 7K6D; PDB: 7K6E; PDB: 7K7P; PDB: 7K9P; PDB: 7KAG; PDB: 7KEG; PDB: 7KEH; PDB: 7KF4; PDB: 7KFI; PDB: 7KG3; PDB: 7KHP; PDB: 7KOA; PDB: 7KPH; PDB: 7KQO; PDB: 7KQP; PDB: 7KQW; PDB: 7KR0; PDB: 7KR1; PDB: 7KRI; PDB: 7KVL; PDB: 7KVR; PDB: 7KX5; PDB: 7KXB; PDB: 7KYU; PDB: 7L0D; PDB: 7L10; PDB: 7L11; PDB: 7L12; PDB: 7L13; PDB: 7L14; PDB: 7L1F; PDB: 7L5D; PDB: 7L6R; PDB: 7L6T; PDB: 7L8I; PDB: 7L8J; PDB: 7LB7; PDB: 7LBN; PDB: 7LBR; PDB: 7LBS; PDB: 7LCO; PDB: 7LCS; PDB: 7LCT; PDB: 7LDL; PDB: 7LDX; PDB: 7LFE; PDB: 7LFP; PDB: 7LFZ; PDB: 7LG2; PDB: 7LG3; PDB: 7LG7; PDB: 7LGO; PDB: 7LKD; PDB: 7LKE; PDB: 7LKR; PDB: 7LKS; PDB: 7LKT; PDB: 7LKU; PDB: 7LKV; PDB: 7LKW; PDB: 7LKX; PDB: 7LLF; PDB: 7LLZ; PDB: 7LMD; PDB: 7LME; PDB: 7LMF; PDB: 7LOS; PDB: 7LTJ; PDB: 7LTN; PDB: 7LW3; PDB: 7LW4; PDB: 7LYH; PDB: 7LYI; PDB: 7LZT; PDB: 7LZU; PDB: 7LZV; PDB: 7LZW; PDB: 7LZX; PDB: 7LZY; PDB: 7LZZ; PDB: 7M00; PDB: 7M01; PDB: 7M02; PDB: 7M03; PDB: 7M04; PDB: 7M2P; PDB: 7M8M; PDB: 7M8N; PDB: 7M8O; PDB: 7M8P; PDB: 7M8X; PDB: 7M8Y; PDB: 7M8Z; PDB: 7M90; PDB: 7M91; PDB: 7MBG; PDB: 7MBI; PDB: 7MC5; PDB: 7MC6; PDB: 7ME0; PDB: 7MGR; PDB: 7MGS; PDB: 7MHF; PDB: 7MHG; PDB: 7MHH; PDB: 7MHI; PDB: 7MHJ; PDB: 7MHK; PDB: 7MHL; PDB: 7MHM; PDB: 7MHN; PDB: 7MHO; PDB: 7MHP; PDB: 7MHQ; PDB: 7MLF; PDB: 7MLG; PDB: 7MNG; PDB: 7MPB; PDB: 7MRR; PDB: 7MSW; PDB: 7MSX; PDB: 7N06; PDB: 7N0B; PDB: 7N0C; PDB: 7N0D; PDB: 7N33; PDB: 7N3K; PDB: 7N44; PDB: 7N5Z; PDB: 7N6N; PDB: 7N7R; PDB: 7N7U; PDB: 7N7W; PDB: 7N7Y; PDB: 7N83; PDB: 7N89; PDB: 7N8C; PDB: 7NBR; PDB: 7NBS; PDB: 7NBY; PDB: 7NEV; PDB: 7NF5; PDB: 7NFV; PDB: 7NG3; PDB: 7NG6; PDB: 7NIO; PDB: 7NN0; PDB: 7NNG; PDB: 7NTS; PDB: 7O7Y; PDB: 7O7Z; PDB: 7O80; PDB: 7O81; PDB: 7ORR; PDB: 7ORU; PDB: 7ORV; PDB: 7ORW; PDB: 7QGI; PDB: 7R7H; PDB: 7RB0; PDB: 7RB2; PDB: 7RBZ; PDB: 7RC0; PDB: 7RFR; PDB: 7RFS; PDB: 7RFU; PDB: 7RFW; PDB: 7RLS; PDB: 7RM2; PDB: 7RMB; PDB: 7RME; PDB: 7RMT; PDB: 7RMZ; PDB: 7RN0; PDB: 7RN1; PDB: 7RN4; PDB: 7RNH; PDB: 7RNK; PDB: 7RQG; PDB: 7S3K; PDB: 7S3S; PDB: 7S4B; PDB: 7SI9; PDB: 7T42; PDB: 7T43; PDB: 7T44; PDB: 7T45; PDB: 7T46; PDB: 7T48; PDB: 7T49; PDB: 7T4A; PDB: 7T4B; PDB: 7T9W; PDB: 7TE0; PDB: 7THH; PDB: 7TI9; 	.	R1AB_SARS2 (819-2763)	Reviewed	.	.	.	.	.	.
Mol02095	Protein	SARS-CoV-2 Non-structural protein 4 (SARS-CoV-2 nsp4)	nsp4	rep	43740578	Severe acute respiratory syndrome coronavirus 2 	2697049	Severe acute respiratory syndrome coronavirus	Betacoronavirus	694002	Coronaviridae	11118	Nidovirales	76804	Pisoniviricetes	2732506	Pisuviricota	2732408	Orthornavirae	2732396	.	KIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQ	.	Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.	PDB: 5R7Z; PDB: 5R80; PDB: 5R81; PDB: 5R82; PDB: 5R83; PDB: 5R84; PDB: 5R8T; PDB: 5RE4; PDB: 5RE5; PDB: 5RE6; PDB: 5RE7; PDB: 5RE8; PDB: 5RE9; PDB: 5REA; PDB: 5REB; PDB: 5REC; PDB: 5RED; PDB: 5REE; PDB: 5REF; PDB: 5REG; PDB: 5REH; PDB: 5REI; PDB: 5REJ; PDB: 5REK; PDB: 5REL; PDB: 5REM; PDB: 5REN; PDB: 5REO; PDB: 5REP; PDB: 5RER; PDB: 5RES; PDB: 5RET; PDB: 5REU; PDB: 5REV; PDB: 5REW; PDB: 5REX; PDB: 5REY; PDB: 5REZ; PDB: 5RF0; PDB: 5RF1; PDB: 5RF2; PDB: 5RF3; PDB: 5RF4; PDB: 5RF5; PDB: 5RF6; PDB: 5RF7; PDB: 5RF8; PDB: 5RF9; PDB: 5RFA; PDB: 5RFB; PDB: 5RFC; PDB: 5RFD; PDB: 5RFE; PDB: 5RFF; PDB: 5RFG; PDB: 5RFH; PDB: 5RFI; PDB: 5RFJ; PDB: 5RFK; PDB: 5RFL; PDB: 5RFM; PDB: 5RFN; PDB: 5RFO; PDB: 5RFP; PDB: 5RFQ; PDB: 5RFR; PDB: 5RFS; PDB: 5RFT; PDB: 5RFU; PDB: 5RFV; PDB: 5RFW; PDB: 5RFX; PDB: 5RFY; PDB: 5RFZ; PDB: 5RG0; PDB: 5RG1; PDB: 5RG2; PDB: 5RG3; PDB: 5RGG; PDB: 5RGH; PDB: 5RGI; PDB: 5RGJ; PDB: 5RGK; PDB: 5RGL; PDB: 5RGM; PDB: 5RGN; PDB: 5RGO; PDB: 5RGP; PDB: 5RGQ; PDB: 5RGR; PDB: 5RGS; PDB: 5RGT; PDB: 5RGU; PDB: 5RGV; PDB: 5RGW; PDB: 5RGX; PDB: 5RGY; PDB: 5RGZ; PDB: 5RH0; PDB: 5RH1; PDB: 5RH2; PDB: 5RH3; PDB: 5RH4; PDB: 5RH5; PDB: 5RH6; PDB: 5RH7; PDB: 5RH8; PDB: 5RH9; PDB: 5RHA; PDB: 5RHB; PDB: 5RHC; PDB: 5RHD; PDB: 5RHE; PDB: 5RHF; PDB: 5RL0; PDB: 5RL1; PDB: 5RL2; PDB: 5RL3; PDB: 5RL4; PDB: 5RL5; PDB: 5RL6; PDB: 5RL7; PDB: 5RL8; PDB: 5RL9; PDB: 5RLB; PDB: 5RLC; PDB: 5RLD; PDB: 5RLE; PDB: 5RLF; PDB: 5RLG; PDB: 5RLH; PDB: 5RLI; PDB: 5RLJ; PDB: 5RLK; PDB: 5RLL; PDB: 5RLM; PDB: 5RLN; PDB: 5RLO; PDB: 5RLP; PDB: 5RLQ; PDB: 5RLR; PDB: 5RLS; PDB: 5RLT; PDB: 5RLU; PDB: 5RLV; PDB: 5RLW; PDB: 5RLY; PDB: 5RLZ; PDB: 5RM0; PDB: 5RM1; PDB: 5RM2; PDB: 5RM3; PDB: 5RM4; PDB: 5RM5; PDB: 5RM6; PDB: 5RM7; PDB: 5RM8; PDB: 5RM9; PDB: 5RMA; PDB: 5RMB; PDB: 5RMC; PDB: 5RMD; PDB: 5RME; PDB: 5RMF; PDB: 5RMG; PDB: 5RMH; PDB: 5RMI; PDB: 5RMJ; PDB: 5RMK; PDB: 5RML; PDB: 5RMM; PDB: 5ROB; PDB: 5RS7; PDB: 5RS8; PDB: 5RS9; PDB: 5RSB; PDB: 5RSC; PDB: 5RSD; PDB: 5RSE; PDB: 5RSF; PDB: 5RSG; PDB: 5RSH; PDB: 5RSI; PDB: 5RSJ; PDB: 5RSK; PDB: 5RSL; PDB: 5RSM; PDB: 5RSN; PDB: 5RSO; PDB: 5RSP; PDB: 5RSQ; PDB: 5RSR; PDB: 5RSS; PDB: 5RST; PDB: 5RSU; PDB: 5RSV; PDB: 5RSW; PDB: 5RSX; PDB: 5RSY; PDB: 5RSZ; PDB: 5RT0; PDB: 5RT1; PDB: 5RT2; PDB: 5RT3; PDB: 5RT4; PDB: 5RT5; PDB: 5RT6; PDB: 5RT7; PDB: 5RT8; PDB: 5RT9; PDB: 5RTA; PDB: 5RTB; PDB: 5RTC; PDB: 5RTD; PDB: 5RTE; PDB: 5RTF; PDB: 5RTG; PDB: 5RTH; PDB: 5RTI; PDB: 5RTJ; PDB: 5RTK; PDB: 5RTL; PDB: 5RTM; PDB: 5RTN; PDB: 5RTO; PDB: 5RTP; PDB: 5RTQ; PDB: 5RTR; PDB: 5RTS; PDB: 5RTT; PDB: 5RTU; PDB: 5RTV; PDB: 5RTW; PDB: 5RTX; PDB: 5RTY; PDB: 5RTZ; PDB: 5RU0; PDB: 5RU1; PDB: 5RU2; PDB: 5RU3; PDB: 5RU4; PDB: 5RU5; PDB: 5RU6; PDB: 5RU7; PDB: 5RU8; PDB: 5RU9; PDB: 5RUA; PDB: 5RUC; PDB: 5RUD; PDB: 5RUE; PDB: 5RUF; PDB: 5RUG; PDB: 5RUH; PDB: 5RUI; PDB: 5RUJ; PDB: 5RUK; PDB: 5RUL; PDB: 5RUM; PDB: 5RUN; PDB: 5RUO; PDB: 5RUP; PDB: 5RUQ; PDB: 5RUR; PDB: 5RUS; PDB: 5RUT; PDB: 5RUU; PDB: 5RUV; PDB: 5RUW; PDB: 5RUX; PDB: 5RUY; PDB: 5RUZ; PDB: 5RV0; PDB: 5RV1; PDB: 5RV2; PDB: 5RV3; PDB: 5RV4; PDB: 5RV5; PDB: 5RV6; PDB: 5RV7; PDB: 5RV8; PDB: 5RV9; PDB: 5RVA; PDB: 5RVB; PDB: 5RVC; PDB: 5RVD; PDB: 5RVE; PDB: 5RVF; PDB: 5RVG; PDB: 5RVH; PDB: 5RVI; PDB: 5RVJ; PDB: 5RVK; PDB: 5RVL; PDB: 5RVM; PDB: 5RVN; PDB: 5RVO; PDB: 5RVP; PDB: 5RVQ; PDB: 5RVR; PDB: 5RVS; PDB: 5RVT; PDB: 5RVU; PDB: 5RVV; PDB: 5S18; PDB: 5S1A; PDB: 5S1C; PDB: 5S1E; PDB: 5S1G; PDB: 5S1I; PDB: 5S1K; PDB: 5S1M; PDB: 5S1O; PDB: 5S1Q; PDB: 5S1S; PDB: 5S1U; PDB: 5S1W; PDB: 5S1Y; PDB: 5S20; PDB: 5S22; PDB: 5S24; PDB: 5S26; PDB: 5S27; PDB: 5S28; PDB: 5S29; PDB: 5S2A; PDB: 5S2B; PDB: 5S2C; PDB: 5S2D; PDB: 5S2E; PDB: 5S2F; PDB: 5S2G; PDB: 5S2H; PDB: 5S2I; PDB: 5S2J; PDB: 5S2K; PDB: 5S2L; PDB: 5S2M; PDB: 5S2N; PDB: 5S2O; PDB: 5S2P; PDB: 5S2Q; PDB: 5S2R; PDB: 5S2S; PDB: 5S2T; PDB: 5S2U; PDB: 5S2V; PDB: 5S2W; PDB: 5S2X; PDB: 5S2Y; PDB: 5S2Z; PDB: 5S30; PDB: 5S31; PDB: 5S32; PDB: 5S33; PDB: 5S34; PDB: 5S35; PDB: 5S36; PDB: 5S37; PDB: 5S38; PDB: 5S39; PDB: 5S3A; PDB: 5S3B; PDB: 5S3C; PDB: 5S3D; PDB: 5S3E; PDB: 5S3F; PDB: 5S3G; PDB: 5S3H; PDB: 5S3I; PDB: 5S3J; PDB: 5S3K; PDB: 5S3L; PDB: 5S3M; PDB: 5S3N; PDB: 5S3O; PDB: 5S3P; PDB: 5S3Q; PDB: 5S3R; PDB: 5S3S; PDB: 5S3T; PDB: 5S3U; PDB: 5S3V; PDB: 5S3W; PDB: 5S3X; PDB: 5S3Y; PDB: 5S3Z; PDB: 5S40; PDB: 5S41; PDB: 5S42; PDB: 5S43; PDB: 5S44; PDB: 5S45; PDB: 5S46; PDB: 5S47; PDB: 5S48; PDB: 5S49; PDB: 5S4A; PDB: 5S4B; PDB: 5S4C; PDB: 5S4D; PDB: 5S4E; PDB: 5S4F; PDB: 5S4G; PDB: 5S4H; PDB: 5S4I; PDB: 5S4J; PDB: 5S4K; PDB: 5S6X; PDB: 5S6Y; PDB: 5S6Z; PDB: 5S70; PDB: 5S71; PDB: 5S72; PDB: 5S73; PDB: 5S74; PDB: 5SA4; PDB: 5SA5; PDB: 5SA6; PDB: 5SA7; PDB: 5SA8; PDB: 5SA9; PDB: 5SAA; PDB: 5SAB; PDB: 5SAC; PDB: 5SAD; PDB: 5SAE; PDB: 5SAF; PDB: 5SAG; PDB: 5SAH; PDB: 5SAI; PDB: 6LU7; PDB: 6LZE; PDB: 6M03; PDB: 6M0K; PDB: 6M2N; PDB: 6M2Q; PDB: 6M71; PDB: 6VWW; PDB: 6VXS; PDB: 6W01; PDB: 6W02; PDB: 6W4B; PDB: 6W4H; PDB: 6W61; PDB: 6W63; PDB: 6W6Y; PDB: 6W75; PDB: 6W9C; PDB: 6W9Q; PDB: 6WC1; PDB: 6WCF; PDB: 6WEN; PDB: 6WEY; PDB: 6WIQ; PDB: 6WJT; PDB: 6WKQ; PDB: 6WKS; PDB: 6WLC; PDB: 6WNP; PDB: 6WOJ; PDB: 6WQ3; PDB: 6WQD; PDB: 6WQF; PDB: 6WRH; PDB: 6WRZ; PDB: 6WTC; PDB: 6WTJ; PDB: 6WTK; PDB: 6WTM; PDB: 6WTT; PDB: 6WUU; PDB: 6WVN; PDB: 6WX4; PDB: 6WXC; PDB: 6WXD; PDB: 6WZU; PDB: 6X1B; PDB: 6X4I; PDB: 6XA4; PDB: 6XA9; PDB: 6XAA; PDB: 6XB0; PDB: 6XB1; PDB: 6XB2; PDB: 6XBG; PDB: 6XBH; PDB: 6XBI; PDB: 6XCH; PDB: 6XDH; PDB: 6XFN; PDB: 6XG3; PDB: 6XHM; PDB: 6XHU; PDB: 6XIP; PDB: 6XKF; PDB: 6XKH; PDB: 6XKM; PDB: 6XMK; PDB: 6XOA; PDB: 6XQS; PDB: 6XQT; PDB: 6XQU; PDB: 6XR3; PDB: 6Y2E; PDB: 6Y2F; PDB: 6Y2G; PDB: 6Y84; PDB: 6YB7; PDB: 6YNQ; PDB: 6YVA; PDB: 6YVF; PDB: 6YWK; PDB: 6YWL; PDB: 6YWM; PDB: 6YYT; PDB: 6YZ1; PDB: 6Z2E; PDB: 6Z5T; PDB: 6Z6I; PDB: 6Z72; PDB: 6ZCT; PDB: 6ZLW; PDB: 6ZM7; PDB: 6ZME; PDB: 6ZMI; PDB: 6ZMO; PDB: 6ZMT; PDB: 6ZN5; PDB: 6ZOJ; PDB: 6ZOK; PDB: 6ZON; PDB: 6ZP4; PDB: 6ZPE; PDB: 6ZRT; PDB: 6ZRU; PDB: 6ZSL; PDB: 7A1U; PDB: 7ABU; PDB: 7ADW; PDB: 7AEG; PDB: 7AF0; PDB: 7AGA; PDB: 7AHA; PDB: 7AK4; PDB: 7AKU; PDB: 7ALH; PDB: 7ALI; PDB: 7AMJ; PDB: 7ANS; PDB: 7AOL; PDB: 7AP6; PDB: 7APH; PDB: 7AQE; PDB: 7AQI; PDB: 7AQJ; PDB: 7AR5; PDB: 7AR6; PDB: 7ARF; PDB: 7AVD; PDB: 7AWR; PDB: 7AWS; PDB: 7AWU; PDB: 7AWW; PDB: 7AX6; PDB: 7AXM; PDB: 7AXO; PDB: 7AY7; PDB: 7B3E; PDB: 7B83; PDB: 7BAJ; PDB: 7BAK; PDB: 7BAL; PDB: 7BB2; PDB: 7BE7; PDB: 7BF3; PDB: 7BF4; PDB: 7BF5; PDB: 7BF6; PDB: 7BFB; PDB: 7BGP; PDB: 7BQ7; PDB: 7BQY; PDB: 7BRO; PDB: 7BRP; PDB: 7BTF; PDB: 7BUY; PDB: 7BV1; PDB: 7BV2; PDB: 7BWQ; PDB: 7BZF; PDB: 7C2I; PDB: 7C2J; PDB: 7C2K; PDB: 7C2Q; PDB: 7C2Y; PDB: 7C6S; PDB: 7C6U; PDB: 7C7P; PDB: 7C8B; PDB: 7C8R; PDB: 7C8T; PDB: 7C8U; PDB: 7CA8; PDB: 7CAM; PDB: 7CB7; PDB: 7CBT; PDB: 7CJD; PDB: 7CJM; PDB: 7CMD; PDB: 7COM; PDB: 7CUT; PDB: 7CUU; PDB: 7CWB; PDB: 7CWC; PDB: 7CX9; PDB: 7D1M; PDB: 7D1O; PDB: 7D7K; PDB: 7D7L; PDB: 7DDC; PDB: 7DG6; PDB: 7DIY; PDB: 7DVX; PDB: 7DVY; PDB: 7DW0; PDB: 7DW6; PDB: 7EQ4; PDB: 7JFQ; PDB: 7JHE; PDB: 7JIB; PDB: 7JKV; PDB: 7JME; PDB: 7JOY; PDB: 7JP0; PDB: 7JP1; PDB: 7JPE; PDB: 7JPY; PDB: 7JPZ; PDB: 7JQ0; PDB: 7JQ1; PDB: 7JQ2; PDB: 7JQ3; PDB: 7JQ4; PDB: 7JQ5; PDB: 7JQB; PDB: 7JQC; PDB: 7JR3; PDB: 7JR4; PDB: 7JST; PDB: 7JSU; PDB: 7JT0; PDB: 7JT7; PDB: 7JU7; PDB: 7JVZ; PDB: 7JW8; PDB: 7JYC; PDB: 7JYY; PDB: 7JZ0; PDB: 7K0E; PDB: 7K0F; PDB: 7K0R; PDB: 7K1L; PDB: 7K1O; PDB: 7K3N; PDB: 7K3T; PDB: 7K40; PDB: 7K5I; PDB: 7K6D; PDB: 7K6E; PDB: 7K7P; PDB: 7K9P; PDB: 7KAG; PDB: 7KEG; PDB: 7KEH; PDB: 7KF4; PDB: 7KFI; PDB: 7KG3; PDB: 7KHP; PDB: 7KOA; PDB: 7KPH; PDB: 7KQO; PDB: 7KQP; PDB: 7KQW; PDB: 7KR0; PDB: 7KR1; PDB: 7KRI; PDB: 7KVL; PDB: 7KVR; PDB: 7KX5; PDB: 7KXB; PDB: 7KYU; PDB: 7L0D; PDB: 7L10; PDB: 7L11; PDB: 7L12; PDB: 7L13; PDB: 7L14; PDB: 7L1F; PDB: 7L5D; PDB: 7L6R; PDB: 7L6T; PDB: 7L8I; PDB: 7L8J; PDB: 7LB7; PDB: 7LBN; PDB: 7LBR; PDB: 7LBS; PDB: 7LCO; PDB: 7LCS; PDB: 7LCT; PDB: 7LDL; PDB: 7LDX; PDB: 7LFE; PDB: 7LFP; PDB: 7LFZ; PDB: 7LG2; PDB: 7LG3; PDB: 7LG7; PDB: 7LGO; PDB: 7LKD; PDB: 7LKE; PDB: 7LKR; PDB: 7LKS; PDB: 7LKT; PDB: 7LKU; PDB: 7LKV; PDB: 7LKW; PDB: 7LKX; PDB: 7LLF; PDB: 7LLZ; PDB: 7LMD; PDB: 7LME; PDB: 7LMF; PDB: 7LOS; PDB: 7LTJ; PDB: 7LTN; PDB: 7LW3; PDB: 7LW4; PDB: 7LYH; PDB: 7LYI; PDB: 7LZT; PDB: 7LZU; PDB: 7LZV; PDB: 7LZW; PDB: 7LZX; PDB: 7LZY; PDB: 7LZZ; PDB: 7M00; PDB: 7M01; PDB: 7M02; PDB: 7M03; PDB: 7M04; PDB: 7M2P; PDB: 7M8M; PDB: 7M8N; PDB: 7M8O; PDB: 7M8P; PDB: 7M8X; PDB: 7M8Y; PDB: 7M8Z; PDB: 7M90; PDB: 7M91; PDB: 7MBG; PDB: 7MBI; PDB: 7MC5; PDB: 7MC6; PDB: 7ME0; PDB: 7MGR; PDB: 7MGS; PDB: 7MHF; PDB: 7MHG; PDB: 7MHH; PDB: 7MHI; PDB: 7MHJ; PDB: 7MHK; PDB: 7MHL; PDB: 7MHM; PDB: 7MHN; PDB: 7MHO; PDB: 7MHP; PDB: 7MHQ; PDB: 7MLF; PDB: 7MLG; PDB: 7MNG; PDB: 7MPB; PDB: 7MRR; PDB: 7MSW; PDB: 7MSX; PDB: 7N06; PDB: 7N0B; PDB: 7N0C; PDB: 7N0D; PDB: 7N33; PDB: 7N3K; PDB: 7N44; PDB: 7N5Z; PDB: 7N6N; PDB: 7N7R; PDB: 7N7U; PDB: 7N7W; PDB: 7N7Y; PDB: 7N83; PDB: 7N89; PDB: 7N8C; PDB: 7NBR; PDB: 7NBS; PDB: 7NBY; PDB: 7NEV; PDB: 7NF5; PDB: 7NFV; PDB: 7NG3; PDB: 7NG6; PDB: 7NIO; PDB: 7NN0; PDB: 7NNG; PDB: 7NTS; PDB: 7O7Y; PDB: 7O7Z; PDB: 7O80; PDB: 7O81; PDB: 7ORR; PDB: 7ORU; PDB: 7ORV; PDB: 7ORW; PDB: 7QGI; PDB: 7R7H; PDB: 7RB0; PDB: 7RB2; PDB: 7RBZ; PDB: 7RC0; PDB: 7RFR; PDB: 7RFS; PDB: 7RFU; PDB: 7RFW; PDB: 7RLS; PDB: 7RM2; PDB: 7RMB; PDB: 7RME; PDB: 7RMT; PDB: 7RMZ; PDB: 7RN0; PDB: 7RN1; PDB: 7RN4; PDB: 7RNH; PDB: 7RNK; PDB: 7RQG; PDB: 7S3K; PDB: 7S3S; PDB: 7S4B; PDB: 7SI9; PDB: 7T42; PDB: 7T43; PDB: 7T44; PDB: 7T45; PDB: 7T46; PDB: 7T48; PDB: 7T49; PDB: 7T4A; PDB: 7T4B; PDB: 7T9W; PDB: 7TE0; PDB: 7THH; PDB: 7TI9; 	.	R1AB_SARS2 (2764-3263)	Reviewed	.	.	.	.	.	.
Mol02096	Protein	Protein kinase C (PRKC)	PRKC	PRKC	5578	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000583775.1,PRKCA-205,321; ENST00000583361.1,PRKCA-204,519; ENST00000578063.5,PRKCA-203,1733; ENST00000413366.8,PRKCA-202,8964; ENST00000284384.6,PRKCA-201,2718"	MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV	"chr17:66,302,613-66,810,743[+]"	"Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42. Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteosomal degradation."	PDB: 2ELI; PDB: 3IW4; PDB: 4DNL; PDB: 4RA4	HGNC:9393	KPCA_HUMAN	Reviewed	ENSG00000154229	.	.	.	.	.
Mol02097	Protein	2-Nitroimidazole nitrohydrolase (NNHA)	NNHA	NNHA	.	Escherichia coli	562	Escherichia coli	Escherichia	.	Enterobacteriaceae	Enterobacterales	91347	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02098	Protein	Adipocytic Glutamine Synthetase (GS)	GS	GS	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02099	Protein	CREB/ATF bZIP transcription factor (CREBZF)	CREB/ATF bZIP transcription factor (Host cell factor-binding transcription factor Zhangfei) (HCF-binding transcription factor Zhangfei); CREBZF; ZF	CREBZF	58487	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000682836.1,CREBZF-210,4368; ENST00000534224.1,CREBZF-209,545; ENST00000531515.5,CREBZF-208,724; ENST00000528889.1,CREBZF-207,745; ENST00000528561.5,CREBZF-206,1099; ENST00000527529.6,CREBZF-205,898; ENST00000527447.2,CREBZF-204,7140; ENST00000525639.1,CREBZF-203,2850; ENST00000490820.2,CREBZF-202,4329; ENST00000260058.9,CREBZF-201,1431"	MRHSLTKLLAASGSNSPTRSESPEPAATCSLPSDLTRAAAGEEETAAAGSPGRKQQFGDEGELEAGRGSRGGVAVRAPSPEEMEEEAIASLPGEETEDMDFLSGLELADLLDPRQPDWHLDPGLSSPGPLSSSGGGSDSGGLWRGDDDDEAAAAEMQRFSDLLQRLLNGIGGCSSSSDSGSAEKRRRKSPGGGGGGGSGNDNNQAATKSPRKAAAAAARLNRLKKKEYVMGLESRVRGLAAENQELRAENRELGKRVQALQEESRYLRAVLANETGLARLLSRLSGVGLRLTTSLFRDSPAGDHDYALPVGKQKQDLLEEDDSAGGVCLHVDKDKVSVEFCSACARKASSSLKM	"Chromosome 11: 85,657,742-85,682,908 reverse strand"	Strongly activates transcription when bound to HCFC1. Suppresses the expression of HSV proteins in cells infected with the virus in a HCFC1-dependent manner. Also suppresses the HCFC1-dependent transcriptional activation by CREB3 and reduces the amount of CREB3 in the cell. Able to down-regulate expression of some cellular genes in CREBZF-expressing cells.	.	HGNC:24905	ZHANG_HUMAN	reviewed	ENSG00000137504	.	.	.	.	.
Mol02100	Protein	Prostaglandin G/H synthase 2 (Cox-2)	Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (Glucocorticoid-regulated inflammatory cyclooxygenase) (Gripghs) (Macrophage activation-associated marker protein P71/73) (PES-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2) (TIS10 protein); Ptgs2; Cox-2; Cox2; Pghs-b; Tis10	Cox-2	19225	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000190784.2,Ptgs2-202,358; ENSMUST00000035065.9,Ptgs2-201,4453"	MLFRAVLLCAALGLSQAANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLNHIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIAGRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFNVQDPQPTKTATINASASHSRLDDINPTVLIKRRSTEL	"Chromosome 1: 149,975,782-149,983,978 forward strand"	"Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump. Has a primary role in D-glucose reabsorption from glomerular filtrate across the brush border of the early proximal tubules of the kidney."	PDB: 7VSI	.	PGH2_MOUSE	reviewed	ENSMUSG00000032487	.	.	.	.	.
Mol02101	Protein	Estrogen receptor (ESR)	Erb; ESRB; ODG8; ESTRB; NR3A2; ER-BETA; ESR-BETA	ESR	2100	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000557772.5,ESR2-213,5458; ENST00000556275.5,ESR2-212,2695; ENST00000555783.1,ESR2-211,306; ENST00000555483.5,ESR2-210,1436; ENST00000555278.5,ESR2-209,1883; ENST00000554572.5,ESR2-208,3588; ENST00000554520.1,ESR2-207,1215; ENST00000553796.5,ESR2-206,1634; ENST00000358599.9,ESR2-205,1899; ENST00000353772.7,ESR2-204,2454; ENST00000344288.10,ESR2-203,1427; ENST00000341099.6,ESR2-202,6842; ENST00000267525.10,ESR2-201,1518"	MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ	"chr14:64,084,232-64,338,112[-]"	"Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner."	.	HGNC:3468	ESR2_HUMAN	Reviewed	ENSG00000140009	.	.	.	.	.
Mol02102	Protein	Estrogen receptor beta (ESR2)	Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2); ESR2; ESTRB; NR3A2	ESR2	2100	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000557772.5,ESR2-213,5458; ENST00000556275.5,ESR2-212,2695; ENST00000555783.1,ESR2-211,306; ENST00000555483.5,ESR2-210,1436; ENST00000555278.5,ESR2-209,1883; ENST00000554572.5,ESR2-208,3588; ENST00000554520.1,ESR2-207,1215; ENST00000553796.5,ESR2-206,1634; ENST00000358599.9,ESR2-205,1899; ENST00000353772.7,ESR2-204,2454; ENST00000344288.10,ESR2-203,1427; ENST00000341099.6,ESR2-202,6842; ENST00000267525.10,ESR2-201,1518"	MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ	"Chromosome 14: 64,084,232-64,338,112 reverse strand."	"Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner."	PDB: 1L2J; PDB: 1NDE; PDB: 1QKM; PDB: 1U3Q; PDB: 1U3R; PDB: 1U3S; PDB: 1U9E; PDB: 1X76; PDB: 1X78; PDB: 1X7B; PDB: 1X7J; PDB: 1YY4; PDB: 1YYE; PDB: 1ZAF; PDB: 2FSZ; PDB: 2GIU; PDB: 2I0G; PDB: 2JJ3; PDB: 2NV7; PDB: 2QTU; PDB: 2YJD; PDB: 2YLY; PDB: 2Z4B; PDB: 3OLL; PDB: 3OLS; PDB: 3OMO; PDB: 3OMP; PDB: 3OMQ; PDB: 4J24; PDB: 4J26; PDB: 4ZI1; PDB: 5TOA	HGNC:3468	ESR2_HUMAN	reviewed	ENSG00000140009	.	.	.	.	.
Mol02103	Protein	Cell death activator CIDE-3 (CIDEC)	Cell death activator CIDE-3 (Cell death-inducing DFFA-like effector protein C) (Fat-specific protein FSP27 homolog); CIDEC; FSP27	CIDEC	63924	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000336832.7,CIDEC-201,1305; ENST00000383817.5,CIDEC-202,1199; ENST00000423850.5,CIDEC-203,1036; ENST00000430427.6,CIDEC-204,1214; ENST00000443115.1,CIDEC-205,443; ENST00000455015.6,CIDEC-206,1153; ENST00000487454.1,CIDEC-207,660; ENST00000618572.4,CIDEC-208,1226; ENST00000675828.1,CIDEC-209,1192; ENST00000679265.1,CIDEC-210,1231"	MEYAMKSLSLLYPKSLSRHVSVRTSVVTQQLLSEPSPKAPRARPCRVSTADRSVRKGIMAYSLEDLLLKVRDTLMLADKPFFLVLEEDGTTVETEEYFQALAGDTVFMVLQKGQKWQPPSEQGTRHPLSLSHKPAKKIDVARVTFDLYKLNPQDFIGCLNVKATFYDTYSLSYDLHCCGAKRIMKEAFRWALFSMQATGHVLLGTSCYLQQLLDATEEGQPPKGKASSLIPTCLKILQ	"Chromosome 3: 9,866,711-9,880,255 reverse strand"	"Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression."	.	HGNC:24229	CIDEC_HUMAN	reviewed	ENSG00000187288	.	.	.	.	.
Mol02104	Protein	"Solute carrier family 2, facilitated glucose transporter member 1 (Glucose transporter type 1, erythrocyte/brain) (GLUT-1) (GT1)"	Solute carrier family 2; facilitated glucose transporter member 1 (Glucose transporter type 1; erythrocyte/brain) (GLUT-1) (GT1); Slc2a1; Glut1	Glut1	20525	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000208090.2,Slc2a1-205,434; ENSMUST00000174372.3,Slc2a1-204,2241; ENSMUST00000144329.8,Slc2a1-203,633; ENSMUST00000134105.8,Slc2a1-202,698; ENSMUST00000030398.10,Slc2a1-201,3260"	MDPSSKKVTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWNHRYGEPIPSTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVAAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNADLWPLLLSVIFIPALLQCILLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTRDLQEMKEEGRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAVLMTIALALLERLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV	"Chromosome 4: 118,965,908-118,995,180 forward strand"	"Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake. Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses. Most important energy carrier of the brain: present at the blood-brain barrier and assures the energy-independent, facilitative transport of glucose into the brain. In association with BSG and NXNL1, promotes retinal cone survival by increasing glucose uptake into photoreceptors."	.	.	GTR1_MOUSE	reviewed	ENSMUSG00000028645	.	.	.	.	.
Mol02105	Protein	Glycosyltransferase Bme (BME)	BME	BME	.	Bacteroides fragilis	817	Bacteroides fragilis	Bacteroides	.	Bacteroidaceae	Bacteroidales	171549	171549	Bacteroidia	200643	Bacteroidetes	976	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02106	Protein	High-affinity pentamidine transporter (HAPT1)	HAPT1	HAPT1	.	Trypanosoma	5690	Trypanosoma	.	.	Trypanosomatidae	5654	Trypanosomatida	2704949	Kinetoplastea	5653	Euglenozoa	33682	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02107	Protein	Maltokinase (MAK1)	Maltokinase (MaK) (EC 2.7.1.175) (Maltose-1-phosphate synthase); mak1	mak1	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	MTLPFAEWLPKQRWYAGRSRVLASVKEASATPLGEELDLVLVDVEYTDGSSERYQVMVGWGDGPLPEYSTIASIGTADDGRDGYDALYDPRATRHLLGLVDTSATAGDVTFEKEPGVELPLEAWPRVFDAEQSNTSVIFDEDAILKLFRRVTCGVNPDIELNRVLGRAGNPHVARLLGSLQSADDSGPCSLGMVTEYAANSAEGWAMATASARDLFADAEMRADEVGGDFQGESYRLGEAVASVHRTLAEELGTGPAPFPLDAVLARVRTAAAAVPELQQFVPAITARFEALTGAEVVVQRVHGDLHLGQVLRTPEAWLLIDFEGEPGQPLDERRMPDSPLRDVAGVLRSYEYAAYQLLVDQDDDEHLAARAREWVDRNRAAFCDGYTNVAGADPREQGALLSAYELDKAVYEAAYEARHRPGWLRIPLRSITRLVG	.	"Catalyzes the ATP-dependent phosphorylation of maltose to maltose 1-phosphate. Only maltose acts effectively as phosphoryl-group acceptor, but maltotriose, maltotetraose, maltopentaose, and maltohexaose show a weak potential to replace maltose. ATP is not replaceable as phosphoryl-group donor."	.	.	MAK_ACTMI	reviewed	.	.	.	.	.	.
Mol02109	Protein	(Na+)-NQR maturation NqrM (nqrM)	(Na+)-NQR maturation NqrM; nqrM; AOG25_00280; F0254_11835; HKB35_09295; HUO05_09255	nqrM	61533190	Vibrio alginolyticus	663	Vibrio alginolyticus	Vibrio	662	Vibrionaceae	641	Vibrionales	135623	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MNTFLITFAVFVAVITAMAVGYIFQKKVVKGSCGGLGAVGIEKVCNCPEPCDARKKREAREAARAEKLAAWEKDRIA	.	.	.	.	A0A0H0YCL5_VIBAL	unreviewed	.	.	.	.	.	.
Mol02110	Protein	Oleandomycin glycosyltransferase oleD (OLED)	OLED	OLED	.	Actinomycetia	1760	Actinomycetia	.	.	.	.	.	.	.	.	Actinobacteria	201174	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02111	Protein	Phosphodiesterase III (PDE)	PDE	PDE	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02112	Protein	Ribonucleic Acid Polymerase (RNAP)	RNAP+K265	RNAP	.	Escherichia coli	562	Escherichia coli	Escherichia	.	Enterobacteriaceae	Enterobacterales	91347	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02113	Protein	Sulfotransferase (SULT)	SULT	SULT	.	Schistosoma mansoni	6183	.	Schistosoma	6181	Schistosomatidae	31245	Strigeidida	6180	Trematoda	6178	Platyhelminthes	6157	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02114	Protein	Solute carrier family 5 member 2 (SLC5A2)	Sodium/glucose cotransporter 2 (Na(+)/glucose cotransporter 2) (Low affinity sodium-glucose cotransporter) (Solute carrier family 5 member 2); SLC5A2; SGLT2	SLC5A2	6524	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000569576.5,SLC5A2-209,516; ENST00000568891.1,SLC5A2-208,660; ENST00000568188.1,SLC5A2-207,2467; ENST00000567051.1,SLC5A2-206,334; ENST00000565446.1,SLC5A2-205,449; ENST00000564197.1,SLC5A2-204,498; ENST00000562006.1,SLC5A2-203,995; ENST00000419665.6,SLC5A2-202,1852; ENST00000330498.4,SLC5A2-201,2267"	MEEHTEAGSAPEMGAQKALIDNPADILVIAAYFLLVIGVGLWSMCRTNRGTVGGYFLAGRSMVWWPVGASLFASNIGSGHFVGLAGTGAASGLAVAGFEWNALFVVLLLGWLFAPVYLTAGVITMPQYLRKRFGGRRIRLYLSVLSLFLYIFTKISVDMFSGAVFIQQALGWNIYASVIALLGITMIYTVTGGLAALMYTDTVQTFVILGGACILMGYAFHEVGGYSGLFDKYLGAATSLTVSEDPAVGNISSFCYRPRPDSYHLLRHPVTGDLPWPALLLGLTIVSGWYWCSDQVIVQRCLAGKSLTHIKAGCILCGYLKLTPMFLMVMPGMISRILYPDEVACVVPEVCRRVCGTEVGCSNIAYPRLVVKLMPNGLRGLMLAVMLAALMSSLASIFNSSSTLFTMDIYTRLRPRAGDRELLLVGRLWVVFIVVVSVAWLPVVQAAQGGQLFDYIQAVSSYLAPPVSAVFVLALFVPRVNEQGAFWGLIGGLLMGLARLIPEFSFGSGSCVQPSACPAFLCGVHYLYFAIVLFFCSGLLTLTVSLCTAPIPRKHLHRLVFSLRHSKEEREDLDADEQQGSSLPVQNGCPESAMEMNEPQAPAPSLFRQCLLWFCGMSRGGVGSPPPLTQEEAAAAARRLEDISEDPSWARVVNLNALLMMAVAVFLWGFYA	"Chromosome 16: 31,483,002-31,490,860 forward strand"	"Electrogenic Na(+)-coupled sugar simporter that actively transports D-glucose at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump. Has a primary role in D-glucose reabsorption from glomerular filtrate across the brush border of the early proximal tubules of the kidney."	PDB: 7VSI	HGNC:11037	SC5A2_HUMAN	reviewed	ENSG00000140675	.	.	.	.	.
Mol02115	Protein	Mitogen-activated protein kinase 8 (MAPK8)	Mitogen-activated protein kinase 8 (MAP kinase 8) (MAPK 8) (EC 2.7.11.24) (JNK-46) (Stress-activated protein kinase 1c) (SAPK1c) (Stress-activated protein kinase JNK1) (c-Jun N-terminal kinase 1); MAPK8; JNK1; PRKM8; SAPK1; SAPK1C	MAPK8	5599	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000482840.1,MAPK8-216,450; ENST00000476134.1,MAPK8-215,732; ENST00000471272.1,MAPK8-214,656; ENST00000469879.6,MAPK8-213,537; ENST00000469110.1,MAPK8-212,3595; ENST00000459755.1,MAPK8-211,2372; ENST00000432379.5,MAPK8-210,907; ENST00000429041.6,MAPK8-209,603; ENST00000426557.5,MAPK8-208,860; ENST00000395611.7,MAPK8-207,5844; ENST00000374189.6,MAPK8-206,5809; ENST00000374182.7,MAPK8-205,5638; ENST00000374179.8,MAPK8-204,6046; ENST00000374176.8,MAPK8-203,5628; ENST00000374174.1,MAPK8-202,739; ENST00000360332.7,MAPK8-201,5438"	MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMVCHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLEERTKNGVIRGQPSPLGAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR	"Chromosome 10: 48,306,639-48,439,360 forward strand"	"Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH. Phosphorylates the CLOCK-ARNTL/BMAL1 heterodimer and plays a role in the regulation of the circadian clock. Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity. Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteosomal degradation. Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1. In neurons, phosphorylates SYT4 which captures neuronal dense core vesicles at synapses. Phosphorylates EIF4ENIF1/4-ET in response to oxidative stress, promoting P-body assembly. Phosphorylates SIRT6 in response to oxidative stress, stimulating its mono-ADP-ribosyltransferase activity."	PDB: 1UKH; PDB: 1UKI; PDB: 2G01; PDB: 2GMX; PDB: 2H96; PDB: 2NO3; PDB: 2XRW; PDB: 2XS0; PDB: 3ELJ; PDB: 3O17; PDB: 3O2M; PDB: 3PZE; PDB: 3V3V; PDB: 3VUD; PDB: 3VUG; PDB: 3VUH; PDB: 3VUI; PDB: 3VUK; PDB: 3VUL; PDB: 3VUM; PDB: 4AWI; PDB: 4E73; PDB: 4G1W; PDB: 4HYS; PDB: 4HYU; PDB: 4IZY; PDB: 4L7F; PDB: 4QTD; PDB: 4UX9; PDB: 4YR8; PDB: 5LW1; PDB: 6F5E; PDB: 6ZR5	HGNC:6881	MK08_HUMAN	reviewed	ENSG00000107643	.	.	.	.	.
Mol02116	Protein	Thymidine kinase (TK)	Thymidine kinase (EC 2.7.1.21); TK; UL23	TK	.	Human alphaherpesvirus 1	10298	Human alphaherpesvirus 1	Simplexvirus	10294	Herpesviridae	10292	Herpesvirales	548681	Herviviricetes	2731363	Peploviricota	2731361	Heunggongvirae	2731360	.	MASYPCHQHASAFDQAARSRGHSNRRTALRPRRQQEATEVRLEQKMPTLLRVYIDGPHGMGKTTTTQLLVALGSRDDIVYVPEPMTYWQVLGASETIANIYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQGGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLAKRLRPMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLARTFAREMGEAN	.	Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors.	.	.	KITH_HHV1	reviewed	.	.	.	.	.	.
Mol02117	Protein	Amyloid-beta precursor protein (APP)	Amyloid-beta precursor protein (APP) (ABPP) (APPI) (Alzheimer disease amyloid A4 protein homolog) (Alzheimer disease amyloid protein) (Amyloid precursor protein) (Amyloid-beta (A4) precursor protein) (Amyloid-beta A4 protein) (Cerebral vascular amyloid peptide) (CVAP) (PreA4) (Protease nexin-II) (PN-II) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Amyloid intracellular domain 59) (AICD-59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Amyloid intracellular domain 57) (AICD-57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AICD-50) (AID(50)) (Gamma-CTF(50)); C31]; APP; A4; AD1	APP	351	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000346798.8,APP-201,3583; ENST00000348990.9,APP-202,3355; ENST00000354192.7,APP-203,3167; ENST00000357903.7,APP-204,3543; ENST00000358918.7,APP-205,2366; ENST00000359726.7,APP-206,3294; ENST00000415997.1,APP-207,541; ENST00000439274.6,APP-208,2517; ENST00000440126.7,APP-209,2846; ENST00000448850.5,APP-210,1846; ENST00000462267.1,APP-211,667; ENST00000463070.1,APP-212,582; ENST00000464867.1,APP-213,816; ENST00000466453.1,APP-214,374; ENST00000474136.5,APP-215,1309 ENST00000491395.5,APP-216,619; ENST00000548570.1,APP-217,361;"	MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN	"Chromosome 21: 25,880,550-26,171,128 reverse strand"	"Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1."	PDB: 1AAP; PDB: 1AMB; PDB: 1AMC; PDB: 1AML; PDB: 1BA4; PDB: 1BA6; PDB: 1BJB; PDB: 1BJC; PDB: 1BRC; PDB: 1CA0; PDB: 1HZ3; PDB: 1IYT; PDB: 1MWP; PDB: 1OWT; PDB: 1QCM; PDB: 1QWP; PDB: 1QXC; PDB: 1QYT; PDB: 1TAW; PDB: 1TKN; PDB: 1X11; PDB: 1Z0Q; PDB: 1ZE7; PDB: 1ZE9; PDB: 1ZJD; PDB: 2BEG; PDB: 2BP4; PDB: 2FJZ; PDB: 2FK1; PDB: 2FK2; PDB: 2FK3; PDB: 2FKL; PDB: 2FMA; PDB: 2G47; PDB: 2IPU; PDB: 2LFM; PDB: 2LLM; PDB: 2LMN; PDB: 2LMO; PDB: 2LMP; PDB: 2LMQ; PDB: 2LNQ; PDB: 2LOH; PDB: 2LP1; PDB: 2LZ3; PDB: 2LZ4; PDB: 2M4J; PDB: 2M9R; PDB: 2M9S; PDB: 2MGT; PDB: 2MJ1; PDB: 2MPZ; PDB: 2MVX; PDB: 2MXU; PDB: 2NAO; PDB: 2OTK; PDB: 2R0W; PDB: 2WK3; PDB: 2Y29; PDB: 2Y2A; PDB: 2Y3J; PDB: 2Y3K; PDB: 2Y3L; PDB: 3AYU; PDB: 3BAE; PDB: 3BKJ; PDB: 3DXC; PDB: 3DXD; PDB: 3DXE; PDB: 3GCI; PDB: 3IFL; PDB: 3IFN; PDB: 3IFO; PDB: 3IFP; PDB: 3JQ5; PDB: 3JQL; PDB: 3JTI; PDB: 3KTM; PDB: 3L33; PDB: 3L81; PDB: 3MOQ; PDB: 3MXC; PDB: 3MXY; PDB: 3NYJ; PDB: 3NYL; PDB: 3OVJ; PDB: 3OW9; PDB: 3PZZ; PDB: 3Q2X; PDB: 3SV1; PDB: 3U0T; PDB: 3UMH; PDB: 3UMI; PDB: 3UMK; PDB: 4HIX; PDB: 4JFN; PDB: 4M1C; PDB: 4MDR; PDB: 4MVI; PDB: 4MVK; PDB: 4MVL; PDB: 4NGE; PDB: 4OJF; PDB: 4ONF; PDB: 4ONG; PDB: 4PQD; PDB: 4PWQ; PDB: 4XXD; PDB: 5AEF; PDB: 5AM8; PDB: 5AMB; PDB: 5BUO; PDB: 5C67; PDB: 5CSZ; PDB: 5HOW; PDB: 5HOX; PDB: 5HOY; PDB: 5KK3; PDB: 5LFY; PDB: 5LV0; PDB: 5MY4; PDB: 5MYO; PDB: 5MYX; PDB: 5ONP; PDB: 5ONQ; PDB: 5OQV; PDB: 5TXD; PDB: 5VOS; PDB: 5VZY; PDB: 5W3P; PDB: 6CO3; PDB: 6GFI; PDB: 6ITU; PDB: 6IYC; PDB: 6NB9; PDB: 6O4J; PDB: 6OC9; PDB: 6OIZ; PDB: 6RHY; PDB: 6SHS; PDB: 6SZF; PDB: 6TI5; PDB: 6TI6; PDB: 6TI7; PDB: 6W0O; PDB: 6WXM; PDB: 6XOV; PDB: 6YHF; PDB: 6YHI; PDB: 6YHO; PDB: 6YHP; PDB: 6YHX; PDB: 7B3J; PDB: 7B3K; PDB: 7JXN; PDB: 7JXO; PDB: 7O1Q; PDB: 7Q4B; PDB: 7Q4M	HGNC:620	A4_HUMAN	reviewed	ENSG00000142192	.	.	.	.	.
Mol02118	LncRNA	Long non-protein coding RNA (lnc886)	nc886	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02120	Protein	Autolysins enzymes (ALTE)	altE	altE	.	Staphylococcus aureus	1280	Staphylococcus aureus	Staphylococcus	.	Staphylococcaceae	Bacillales	1385	1385	Bacilli	91061	Firmicutes	1239	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02121	Protein	Plasma membrane calcium-transporting ATPase 1 (ATP2B1)	Plasma membrane calcium-transporting ATPase 1 (EC 7.2.2.10) (Plasma membrane calcium ATPase isoform 1) (PMCA1) (Plasma membrane calcium pump isoform 1); ATP2B1	ATP2B1	397636	Guinea-pig	10141	.	Cavia	10140	Caviidae	10139	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSSSCT00000048359.3,6042; ENSSSCT00000069086.2,5293; ENSSSCT00000001005.5,5185; ENSSSCT00000001006.4,5174; ENSSSCT00000059392.3,5159; ENSSSCT00000046212.3,5132"	MGDMANNSVAYGGVKNSLKEANHDGDFGITLADVRALMELRSTDALRKIQESYGDVYGICTRLKTSPVEGLSGNPADIERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIVSLGLSFYQPPEGDNALCGEVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGINSQTGIIFTLLGAGGEEEEKKDEKKKEKKNKKQDGAIENRNKAKAQDGAAMEMQPLKSEEGGDGDEKDKKKANLPKKEKSVLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTFWVQKRPWLAECTPIYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYINEKHYKKIPEPEAIPPNILSYLVTGISVNCAYTSKILPPEKEGGLPRHVGNKTECALLGLLLDLKRDYQDVRNEIPEEALYKVYTFNSVRKSMSTVLKNSDGSYRIFSKGASEIILKKCFKILSANGEAKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEPEPEWDNENDIVTGLTCIAVVGIEDPVRPEVPDAIKKCQRAGITVRMVTGDNINTARAIATKCGILHPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTVSDQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASLALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKFFDIDSGRNAPLHAPPSEHYTIVFNTFVLMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQIIIVQFGGKPFSCSELSIEQWLWSIFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEEIPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQIRVVNAFRSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLIDDTDAEDDAPTKRNCSPPPSPNKNNNAVDSGIYLTIEMNKSATSSSPGSPLHSLETSL	"Primary_assembly 5: 92,935,694-93,061,405 forward strand."	Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis. Plays a role in blood pressure regulation through regulation of intracellular calcium concentration and nitric oxide production leading to regulation of vascular smooth muscle cells vasoconstriction. Positively regulates bone mineralization through absorption of calcium from the intestine. Plays dual roles in osteoclast differentiation and survival by regulating RANKL-induced calcium oscillations in preosteoclasts and mediating calcium extrusion in mature osteoclasts (By similarity). Regulates insulin sensitivity through calcium/calmodulin signaling pathway by regulating AKT1 activation and NOS3 activation in endothelial cells (By similarity). May play a role in synaptic transmission by modulating calcium and proton dynamics at the synaptic vesicles.	.	.	AT2B1_PIG	reviewed	ENSSSCG00000027898	.	.	.	.	.
Mol02123	Protein	Epithelial sodium channel (ENAC)	ENaC	ENaC	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02124	Protein	Siderophore export accessory protein MmpS5 (mmpS5)	Siderophore export accessory protein MmpS5; mmpS5; Rv0677c; MTV040.05c	mmpS5	888233	Mycobacteroides abscessus	36809	Mycobacteroides abscessus	Mycobacteroides	670516	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MIGTLKRAWIPLLILVVVAIAGFTVQRIRTFFGSEGILVTPKVFADDPEPFDPKVVEYEVSGSGSYVNINYLDLDAKPQRIDGAALPWSLTLKTTAPSAAPNILAQGDGTSITCRITVDGEVKDERTATGVDALTYCFVKSA	.	"Part of an export system, which is required for biosynthesis and secretion of siderophores. Essential for virulence."	.	.	MMPS5_MYCTU	reviewed	.	.	.	.	.	.
Mol02125	Protein	Oxygen-insensitive NAD(P)H nitroreductase (NFSB)	Oxygen-insensitive NAD(P)H nitroreductase (EC 1.-.-.-) (Dihydropteridine reductase) (EC 1.5.1.34) (FMN-dependent nitroreductase); nfsB; dprA; nfnB; nfsI; ntr; b0578; JW0567	nfsB	945778	Escherichia coli	562	Escherichia coli	Escherichia	.	Enterobacteriaceae	Enterobacterales	91347	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV	.	"Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species."	PDB: 1DS7; PDB: 1ICR; PDB: 1ICU; PDB: 1ICV; PDB: 1IDT; PDB: 1OO5; PDB: 1OO6; PDB: 1OON; PDB: 1OOQ; PDB: 1YKI; PDB: 1YLR; PDB: 1YLU; PDB: 3X21; PDB: 3X22	.	NFSB_ECOLI	reviewed	.	.	.	.	.	.
Mol02126	Protein	Nitrofurazone-reductase IIa (NFR2A)	Nitrofurazone-reductase Iia gene	Nitrofurazone-reductase Iia gene	.	Escherichia coli	562	Escherichia coli	Escherichia	.	Enterobacteriaceae	Enterobacterales	91347	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02127	Protein	Nitrofurazone-reductase IIb (NFR2B)	Nitrofurazone-reductase Iib gene	Nitrofurazone-reductase Iib gene	.	Escherichia coli	562	Escherichia coli	Escherichia	.	Enterobacteriaceae	Enterobacterales	91347	91347	Gammaproteobacteria	1236	Proteobacteria	1224	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02128	Protein	PAAQR7 (PAAQR7)	PAAQR7	PAAQR7	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02129	Protein	Pro-angiogenic factors	Pro-angiogenic factors gene	Pro-angiogenic factors gene	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02130	Protein	Cannabinoid receptor 1 (CB-R) (CB1) (CANN6)	Cannabinoid receptor 1 (CB-R) (CB1) (CANN6); CNR1; CNR	CNR1	1268	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000362094.6,CNR1-201,5244; ENST00000369499.3,CNR1-202,5561; ENST00000369501.3,CNR1-203,6019; ENST00000428600.3,CNR1-204,5542; ENST00000468898.2,CNR1-205,5312; ENST00000549890.2,CNR1-206,5502; ENST00000551417.2,CNR1-207,6200"	MKSILDGLADTTFRTITTDLLYVGSNDIQYEDIKGDMASKLGYFPQKFPLTSFRGSPFQEKMTAGDNPQLVPADQVNITEFYNKSLSSFKENEENIQCGENFMDIECFMVLNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFIDFHVFHRKDSRNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCEKLQSVCSDIFPHIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNAASVHRAAESCIKSTVKIAKVTMSVSTDTSAEAL	"Chromosome 6: 88,139,864-88,166,347 reverse strand"	"G-protein coupled receptor for endogenous cannabinoids (eCBs), including N-arachidonoylethanolamide (also called anandamide or AEA) and 2-arachidonoylglycerol (2-AG), as well as phytocannabinoids, such as delta(9)-tetrahydrocannabinol (THC). Mediates many cannabinoid-induced effects, acting, among others, on food intake, memory loss, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, chronic pain. Signaling typically involves reduction in cyclic AMP. In the hypothalamus, may have a dual effect on mitochondrial respiration depending upon the agonist dose and possibly upon the cell type. Increases respiration at low doses, while decreases respiration at high doses. At high doses, CNR1 signal transduction involves G-protein alpha-i protein activation and subsequent inhibition of mitochondrial soluble adenylate cyclase, decrease in cyclic AMP concentration, inhibition of protein kinase A (PKA)-dependent phosphorylation of specific subunits of the mitochondrial electron transport system, including NDUFS2. In the hypothalamus, inhibits leptin-induced reactive oxygen species (ROS) formation and mediates cannabinoid-induced increase in SREBF1 and FASN gene expression. In response to cannabinoids, drives the release of orexigenic beta-endorphin, but not that of melanocyte-stimulating hormone alpha/alpha-MSH, from hypothalamic POMC neurons, hence promoting food intake. In the hippocampus, regulates cellular respiration and energy production in response to cannabinoids. Involved in cannabinoid-dependent depolarization-induced suppression of inhibition (DSI), a process in which depolarization of CA1 postsynaptic pyramidal neurons mobilizes eCBs, which retrogradely activate presynaptic CB1 receptors, transiently decreasing GABAergic inhibitory neurotransmission. Also reduces excitatory synaptic transmission. In superior cervical ganglions and cerebral vascular smooth muscle cells, inhibits voltage-gated Ca(2+) channels in a constitutive, as well as agonist-dependent manner. In cerebral vascular smooth muscle cells, cannabinoid-induced inhibition of voltage-gated Ca(2+) channels leads to vasodilation and decreased vascular tone. Induces leptin production in adipocytes and reduces LRP2-mediated leptin clearance in the kidney, hence participating in hyperleptinemia. In adipose tissue, CNR1 signaling leads to increased expression of SREBF1, ACACA and FASN genes. In the liver, activation by endocannabinoids leads to increased de novo lipogenesis and reduced fatty acid catabolism, associated with increased expression of SREBF1/SREBP-1, GCK, ACACA, ACACB and FASN genes. May also affect de novo cholesterol synthesis and HDL-cholesteryl ether uptake. Peripherally modulates energy metabolism. In high carbohydrate diet-induced obesity, may decrease the expression of mitochondrial dihydrolipoyl dehydrogenase/DLD in striated muscles, as well as that of selected glucose/ pyruvate metabolic enzymes, hence affecting energy expenditure through mitochondrial metabolism. In response to cannabinoid anandamide, elicits a pro-inflammatory response in macrophages, which involves NLRP3 inflammasome activation and IL1B and IL18 secretion. In macrophages infiltrating pancreatic islets, this process may participate in the progression of type-2 diabetes and associated loss of pancreatic beta-cells."	PDB: 1LVQ; PDB: 1LVR; PDB: 2B0Y; PDB: 2KOE; PDB: 2MZ2; PDB: 2MZ3; PDB: 2MZA; PDB: 5TGZ; PDB: 5U09; PDB: 5XR8; PDB: 5XRA; PDB: 6KPG; PDB: 6KQI; PDB: 6N4B; PDB: 7V3Z	HGNC:2159	CNR1_HUMAN	reviewed	ENSG00000118432	.	.	.	.	.
Mol02131	Protein	WT1 associated protein (WTAP)	KIAA0105; MGC3925; Mum29589	WTAP	9589	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000650096.1,WTAP-208,3280; ENST00000631126.2,WTAP-207,1430; ENST00000621533.5,WTAP-206,2105; ENST00000614346.4,WTAP-205,1623; ENST00000494513.1,WTAP-204,635; ENST00000462110.1,WTAP-203,584; ENST00000358372.8,WTAP-202,3656; ENST00000337387.4,WTAP-201,1622"	MTNEEPLPKKVRLSETDFKVMARDELILRWKQYEAYVQALEGKYTDLNSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTTQIQYLKQVQQPSVAQLRSTMVDPAINLFFLKMKGELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKETRQQLAQYQQQQSQASAPSTSRTTASEPVEQSEATSKDCSRLTNGPSNGSSSRQRTSGSGFHREGNTTEDDFPSSPGNGNKSSNSSEERTGRGGSGYVNQLSAGYESVDSPTGSENSLTHQSNDTDSSHDPQEEKAVSGKGNRTVGSRHVQNGLDSSVNVQGSVL	"chr6:159,725,585-159,756,319 forward strand."	"Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing"	.	HGNC:16846	FL2D_HUMAN	Reviewed	ENSG00000146457	.	.	.	.	.
Mol02132	Protein	HSA17B7 (HSA17B7)	HSA17B7	HSA17B7	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02133	Protein	NSDH1 (NSDH1)	NSDH1	NSDH1	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02134	Protein	Protocadherin beta-9 (PCDHB9)	Protocadherin beta-9 (PCDH-beta-9) (Protocadherin-3H); PCDHB9; PCDH3H	PCDHB9	56127	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000624909.1,PCDHB9-203,616; ENST00000623266.1,PCDHB9-202,498; ENST00000316105.7,PCDHB9-201,4381"	MKTRGFSFPRQRQVLFLFLFWGVSLAGSGFGRYSVTEETEKGSFVVNLAKDLGLAEGELAARGTRVVSDDNKQYLLLDSHTGNLLTNEKLDREKLCGPKEPCMLYFQILMDDPFQIYRAELRVRDINDHSPVFRHKEMVLKISENTAEGTAFRLERAQDPDEGHNSIQNYTISSNSFFHIKISGSDEGMIYPELVLDKALDREEQEELSLTLTALDGGSPSRSGTSTIRIVVLDVNDNVPQFAQALYETQAPENSPVGSLIVKVSAGDADSGVNAEVSYSFFDASEDILTTFQINPFSGEIFLRELLDYELVNSYKINIQAMDGGGLSARCTVLIKVLDSNDNPPELIISSLSNSVAENSPGIVLAVFKIKDRDSGENGKTICYVQDNLPFFLKPSVDNFYILMTEGALDRESKAEYNITITVTDLGTPRLKTEHSITLQVSDVNDNAPAFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINADNGHLFALRSLDYEALQAFDFRVGASDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADLLTVYLVVALASVSSLFLLSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGHLVDVSGTGTLFQSYQYEVCLTGGSETGEFKFLKPITPHLPPHRGGKEIEENSTLPNSFGFNY	"Chromosome 5: 141,187,127-141,191,541 forward strand"	Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.	.	HGNC:8694	PCDB9_HUMAN	reviewed	ENSG00000177839	.	.	.	.	.
Mol02136	Protein	Leishmania miltefosine transporter (LMT)	LMT	LMT	.	Mycobacteroides abscessus	38568	Mycobacteroides abscessus	Mycobacteroides	670516	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02137	Protein	Miltefosine transporter beta subunit (ROS3)	Miltefosine transporter beta subunit; Ros3	Ros3	.	Mycobacteroides abscessus	38568	Mycobacteroides abscessus	Mycobacteroides	670516	Mycobacteriaceae	1762	Corynebacteriales	85007	Actinomycetia	1760	Actinobacteria	201174	.	.	.	MAPLPPKPHSKNRIEQQQLPHIYARHSPLSVSVVFFILAVAAIPIGVLVIVSGDLTTRLDFRYDHINSYKFAMGAAGEFAVNFPFNGTMYSSGVKTRLMFSLHQSLTAPVYMQYRLSPFFQNYRYFTASVDYSQLSGRASAISKLCAPFRFPGEATGDSVSGYYNPCGAYPWAMFNDSISLYRTDGTLICDGSAFTANGTSLAANNKCVKSGIARPSDVKERYNPPREIPGNGPMWSAGGNKSATDPYLREGYYYKEPGHKIPLSIDEDLIVWLDPAFTSDVTKNYRILNVDLPAGDYYFEITEQYPTAPYASHKFVQLATRSWIGGRSHVLGSLLIIMGGTAFIMAVTLLSVKYLIMPVYTEDI	.	.	.	.	Q0P0L8_LEIDO	unreviewed	.	.	.	.	.	.
Mol02138	Protein	DNA-directed RNA polymerase subunit beta (RPOB)	DNA-directed RNA polymerase subunit beta (RPOB)	.	.	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02143	LncRNA	Long non-protein coding RNA (RNAMVIH)	lncRNAMVIH	lncRNAMVIH	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02145	LncRNA	Long non-protein coding RNA (LINC00461)	LINC00461	LINC00461	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02146	Protein	DNA gyrase subunit A (GYRA)	gyrA CD630_00060	gyrA	66352444	Clostridioides difficile	272563	Clostridioides difficile	Clostridioides	1870884	Peptostreptococcaceae	186804	Eubacteriales	186802	Clostridia	186801	Firmicutes	1239	.	.	.	MEENNKILPIEIAEEMKKSYIDYSMSVIAGRALPDVRDGLKPVHRRILYSMSELNLTPDKPYRKSARIVGDVLGKYHPHGDTAVYYAMVRMAQDFSTRALLVDGHGNFGSVDGDSPAAMRYTEAKMSKLSLELLRDIEKETVDFKPNFDESLKEPSVLPARYPNLLVNGSNGIAVGMATSIPPHNLAEVIDATVYLIDNPECSVDDLIKFVQGPDFPTAAIIMGKESIAEAYRTGRGKVKVRSRAFIEELPKGKQQIIVTEIPYQVNKAKLVERIAELVKEKRIEGISDLRDESNRNGMRIVIELKRDANANIVLNNLYKHSQMEDTFSIIMLALVDGQPRVLNLKQILYHYIKHQEDVVTRRTKFELNKAEARAHILEGLKIALDNIDAVISLIRASKTGQEAKLGLIEKFKLTEIQAQAILDMRLQRLTGLERDKIEAEYEDLIKKINRLKEILADERLLLNVIKDEITIIKENYSDERRTEIRHAEGEIDMRDLISDEEIAITLTHFGYIKRLPSDTYKSQKRGGRGISALTTREEDFVRHLVTTTTHSRLLFFTNKGRVFKLNAYEIPEGKRQAKGTAIVNLLQLSADEKIATLIPIDGNDENEYLLLATKKGIVKKTKREEFKNINKSGLIAIGLRDDDELIGVELTDGKQEVLLVTKEGMSIRFDENDIRYMGRTAMGVKGITLSKEDFVVSMNLCSKGTDVLVVSKNGFGKRTNIEEYRSQIRAGKGIKTYNISEKTGTIVGADMVNEDDEIMIINSDGVLIRIRVNEISLFGRVTSGVKLMKTNDEVNVVSIAKINIEEE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	Q18C90_CLOD6	unreviewed	.	.	.	.	.	.
Mol02147	Protein	DNA gyrase subunit A (GYRA)	gyrA GBAA_0006	gyrA	45020040	Bacillus cereus	1392	Bacillus cereus	Bacillus 	1386	Bacillaceae 	186817	Bacillales	1385	Bacilli 	91061	Firmicutes  	1239	.	.	.	MSDNQQQARIREINISHEMRTSFLDYAMSVIVSRALPDVRDGLKPVHRRVLYAMNDLGITADKAYKKSARIVGEVIGKYHPHGDSAVYETMVRMAQDFSQRYMLVDGHGNFGSVDGDSAAAMRYTEARMSKISMELIRDISKNTIDYQDNYDGSEREPIVLPARFPNLLVNGTTGIAVGMATNIPPHQLGEVIDGVLALSHNPDITIAELMECIPGPDFPTAGLILGRSGIRRAYETGRGSIILRAKVEIEEKSNGKQSIIVTELPYQVNKARLIEKIAELVRDKKIEGITDLRDESDRNGMRIVMEVRRDANANVLLNNLYKHTALQTSFGINMLSLVNGEPQVLNLKQNLYHYLEHQKVVIRRRTAYELEKAEARAHILEGLRIALDHLDEVITLIRSSKTAEIAKQGLMERFGLSEKQAQAILDMRLQRLTGLEREKIEQEYQDLMKLIAELKAILADEEKVLEIIREELTEVKERFNDKRRTEITIGGMESIEDEDLIPEQNIAITLTHNGYIKRLPASTYKTQNRGGRGVQGMGTNDDDFVEHLLTTSTHDHILFFTNKGKVYRTKGYEIPEYSRTAKGIPIINLLGVDKGEWINAIIPIREFGDDEFLFFTTKQGISKRTPLSSFANIRTNGLIAISLREEDEVISVRLTSGDKDIIVGTSNGMLIRFNEQDVRSMGRNAAGVKAITLGEEDQVVGMEIVEEDVNVLIVTKNGYGKRTPIDEYRLQSRGGKGLKTCNITDKNGKLVAVKSVTGEEDIMLITAAGVIIRMPVDQISQMGRNTQGVRLIRLEDEQEVATVAKAQKDDEEETSEEVSSEE	.	"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner."	.	.	A0A6H3A7B1_BACAN	unreviewed	.	.	.	.	.	.
Mol02148	Protein	GTPase HRas (HRAS)	Hras Hras1	Hras	15461	Mus musculus	10090	Mus musculus	Mus	.	Muridae	Rodentia	9989	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000026572.11,Hras-201,2828; ENSMUST00000097957.11,Hras-202,1199; ENSMUST00000124314.3,Hras-203,1073; ENSMUST00000124971.2,Hras-204,1122; ENSMUST00000128993.2,Hras-205,1704; ENSMUST00000134008.2,Hras-206,447; ENSMUST00000168550.8,Hras-207,2272; "	MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS	"chr7:140,769,018-140,773,918[-]"	Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.	PDB: 6KYH	.	RASH_MOUSE	reviewed	ENSMUSG00000025499	.	.	.	.	.
Mol02149	Protein	Heat shock protein HSP 90 (HSP90 )	HSP90 CAALFM_C702030WA CaJ7.0234 CaO19.13868 CaO19.6515	HSP90	3636951	Candida albicans	237561	Candida albicans	Candida	5475	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	MADAKVETHEFTAEISQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPSQLESEPELFIRIIPQKDQKVLEIRDSGIGMTKADLVNNLGTIAKSGTKSFMEALSAGADVSMIGQFGVGFYSLFLVADHVQVISKHNDDEQYVWESNAGGKFTVTLDETNERLGRGTMLRLFLKEDQLEYLEEKRIKEVVKKHSEFVAYPIQLVVTKEVEKEVPETEEEDKAAEEDDKKPKLEEVKDEEDEKKEKKTKTVKEEVTETEELNKTKPLWTRNPSDITQDEYNAFYKSISNDWEDPLAVKHFSVEGQLEFRAILFVPKRAPFDAFESKKKKNNIKLYVRRVFITDDAEELIPEWLSFIKGVVDSEDLPLNLSREMLQQNKILKVIRKNIVKKMIETFNEISEDQEQFNQFYTAFSKNIKLGIHEDAQNRQSLAKLLRFYSTKSSEEMTSLSDYVTRMPEHQKNIYYITGESIKAVEKSPFLDALKAKNFEVLFMVDPIDEYAMTQLKEFEDKKLVDITKDFELEESDEEKAAREKEIKEYEPLTKALKDILGDQVEKVVVSYKLVDAPAAIRTGQFGWSANMERIMKAQALRDTTMSSYMSSKKTFEISPSSPIIKELKKKVETDGAEDKTVKDLTTLLFDTALLTSGFTLDEPSNFAHRINRLIALGLNIDDDSEETAVEPEATTTASTDEPAGESAMEEVD	.	"Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity)."	PDB: 6CJI; PDB: 6CJJ; PDB: 6CJL; PDB: 6CJP; PDB: 6CJR; PDB: 6CJS	.	HSP90_CANAL	reviewed	.	.	.	.	.	.
Mol02150	Protein	Major facilitator superfamily (MFS)	.	.	.	Candida albicans	237561	Candida albicans	Candida	5475	Debaryomycetaceae	766764	Saccharomycetales	4892	Saccharomycetes	4891	Ascomycota	4890	Fungi	4751	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02151	LncRNA	hsa-mir-92a 	hsa-mir-92a 	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02152	Circular RNA	hsa_circRNA_0000309	hsa_circRNA_0000309	hsa_circRNA_0000309	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02153	LncRNA	Mitochondrially encoded cytochrome c oxidase II (MT-CO2)	MT-CO2	MT-CO2	4513	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:7421	.	.	.	.	.	.	.	.
Mol02154	LncRNA	MX dynamin like GTPase 1 (MX1)	MX1	MX1	4599	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000288383.11,MX1-201,2777; ENST00000398598.8,MX1-202,2776; ENST00000398600.6,MX1-203,3470; ENST00000413778.6,MX1-204,2672; ENST00000417963.6,MX1-205,2303; ENST00000419044.6,MX1-206,3516; ENST00000424365.6,MX1-207,2701; ENST00000441677.6,MX1-208,1211; ENST00000455164.6,MX1-209,2810; ENST00000467510.2,MX1-210,4559; ENST00000468506.5,MX1-211,752; ENST00000478268.1,MX1-212,3202; ENST00000484465.1,MX1-213,388; ENST00000486275.2,MX1-214,3644; ENST00000491110.1,MX1-215,516; ENST00000619682.1,MX1-216,1980; ENST00000679386.1,MX1-217,3964; ENST00000679408.1,MX1-218,2687; ENST00000679445.1,MX1-219,3576; ENST00000679464.1,MX1-220,3653; ENST00000679528.1,MX1-221,1402; ENST00000679543.1,MX1-222,3309; ENST00000679626.1,MX1-223,3699; ENST00000679705.1,MX1-224,3256; ENST00000679911.1,MX1-225,3690; ENST00000680176.1,MX1-226,3302; ENST00000680182.1,MX1-227,3649; ENST00000680347.1,MX1-228,3553; ENST00000680364.1,MX1-229,3310; ENST00000680536.1,MX1-230,3205; ENST00000680629.1,MX1-231,3144; ENST00000680637.1,MX1-232,5778; ENST00000680760.1,MX1-233,3203; ENST00000680776.1,MX1-234,3325; ENST00000680942.1,MX1-235,2732; ENST00000680980.1,MX1-236,1637; ENST00000681039.1,MX1-237,3428; ENST00000681191.1,MX1-238,3640; ENST00000681266.1,MX1-239,3288; ENST00000681382.1,MX1-240,4675; ENST00000681415.1,MX1-241,3752; ENST00000681607.1,MX1-242,3289; ENST00000681671.1,MX1-243,3298; ENST00000681849.1,MX1-244,3251; ENST00000681857.1,MX1-245,3488; ENST00000681867.1,MX1-246,3527; ENST00000681896.1,MX1-247,3125; ENST00000681944.1,MX1-248,2724"	.	"chr21:41,420,020-41,470,071[+]"	.	.	HGNC:7532	.	.	ENSG00000157601	.	.	.	.	.
Mol02155	LncRNA	Deleted in lymphocytic leukemia 1 (DLEU1)	DLEU1	DLEU1	10301	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000413510.4,DLEU1-201,1807; ENST00000460525.6,DLEU1-202,1031; ENST00000461527.7,DLEU1-203,918; ENST00000462427.2,DLEU1-204,1120; ENST00000463357.5,DLEU1-205,274; ENST00000463474.7,DLEU1-206,1047; ENST00000467721.5,DLEU1-207,1455; ENST00000468168.5,DLEU1-208,982; ENST00000468522.5,DLEU1-209,1158; ENST00000469095.6,DLEU1-210,1596; ENST00000469127.5,DLEU1-211,320; ENST00000469754.3,DLEU1-212,2957; ENST00000470593.5,DLEU1-213,668; ENST00000470726.7,DLEU1-214,1051; ENST00000472136.5,DLEU1-215,720; ENST00000473075.3,DLEU1-216,583; ENST00000474630.6,DLEU1-217,1187; ENST00000475913.5,DLEU1-218,534; ENST00000476738.5,DLEU1-219,838; ENST00000478860.5,DLEU1-220,602; ENST00000479420.5,DLEU1-221,612; ENST00000483169.6,DLEU1-222,1304; ENST00000483444.5,DLEU1-223,332; ENST00000484529.5,DLEU1-224,400; ENST00000484606.1,DLEU1-225,400; ENST00000484869.6,DLEU1-226,1652; ENST00000485007.5,DLEU1-227,736; ENST00000486895.5,DLEU1-228,481; ENST00000489542.6,DLEU1-229,780; ENST00000490577.5,DLEU1-230,2440; ENST00000491341.5,DLEU1-231,1141; ENST00000491482.5,DLEU1-232,431; ENST00000491615.5,DLEU1-233,1451; ENST00000498557.5,DLEU1-234,639; ENST00000647700.1,DLEU1-235,1302; ENST00000650910.1,DLEU1-236,5265; ENST00000650996.1,DLEU1-237,871; ENST00000652753.1,DLEU1-238,754; ENST00000655550.1,DLEU1-239,2888; ENST00000658634.1,DLEU1-240,3789; ENST00000659280.2,DLEU1-241,1487; ENST00000668174.1,DLEU1-242,1926; ENST00000671384.1,DLEU1-243,3216"	.	"chr13:50,082,169-50,906,856[+]"	.	.	HGNC:13747	.	.	ENSG00000176124	.	.	.	.	.
Mol02156	LncRNA	HLA complex P5 (HCP5)	HCP5	HCP5	10866	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000414046.3,HCP5-201,9148; ENST00000460889.5,HCP5-202,465; ENST00000467369.2,HCP5-203,1024; ENST00000541196.3,HCP5-204,1689; ENST00000666495.2,HCP5-205,2005; ENST00000670109.1,HCP5-206,2591; ENST00000674016.1,HCP5-207,303"	.	"chr6:31,463,170-31,478,936[+]"	.	.	HGNC:21659	.	.	ENSG00000206337	.	.	.	.	.
Mol02157	LncRNA	Growth arrest specific 5 (GAS5)	Gas5	Gas5	14455	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000065709.13,Gas5-201,1316; ENSMUST00000159037.3,Gas5-202,3190; ENSMUST00000159119.9,Gas5-203,669; ENSMUST00000159153.9,Gas5-204,953; ENSMUST00000159157.9,Gas5-205,1202; ENSMUST00000159399.9,Gas5-206,2551; ENSMUST00000159404.9,Gas5-207,655; ENSMUST00000159438.8,Gas5-208,779; ENSMUST00000159663.9,Gas5-209,356; ENSMUST00000159706.9,Gas5-210,566; ENSMUST00000159890.9,Gas5-211,1090; ENSMUST00000160152.8,Gas5-212,712; ENSMUST00000160429.9,Gas5-213,768; ENSMUST00000160497.3,Gas5-214,1395; ENSMUST00000160516.3,Gas5-215,2947; ENSMUST00000160551.3,Gas5-216,2005; ENSMUST00000161005.9,Gas5-217,452; ENSMUST00000161229.8,Gas5-218,2556; ENSMUST00000161380.9,Gas5-219,783; ENSMUST00000161461.9,Gas5-220,808; ENSMUST00000161623.9,Gas5-221,1199; ENSMUST00000162163.9,Gas5-222,1634; ENSMUST00000162289.9,Gas5-223,910; ENSMUST00000162558.9,Gas5-224,505; ENSMUST00000163081.3,Gas5-225,2930; ENSMUST00000240769.1,Gas5-226,311; ENSMUST00000240786.1,Gas5-227,470; ENSMUST00000240868.1,Gas5-228,425; ENSMUST00000241068.1,Gas5-229,285; ENSMUST00000241235.1,Gas5-230,391; ENSMUST00000241381.1,Gas5-231,960; ENSMUST00000241982.1,Gas5-232,1275; ENSMUST00000242104.1,Gas5-233,428; ENSMUST00000242266.1,Gas5-234,607; ENSMUST00000242309.1,Gas5-235,898; ENSMUST00000242491.1,Gas5-236,394; ENSMUST00000242726.1,Gas5-237,298; ENSMUST00000242794.1,Gas5-238,409; ENSMUST00000243013.1,Gas5-239,469; ENSMUST00000243220.1,Gas5-240,431; ENSMUST00000243489.1,Gas5-241,1078; ENSMUST00000243677.1,Gas5-242,358; ENSMUST00000243966.1,Gas5-243,433; ENSMUST00000244019.1,Gas5-244,466; ENSMUST00000244153.1,Gas5-245,314; ENSMUST00000244324.1,Gas5-246,448; ENSMUST00000244371.1,Gas5-247,247; ENSMUST00000244436.1,Gas5-248,1390; ENSMUST00000244699.1,Gas5-249,569; ENSMUST00000245083.1,Gas5-250,372; ENSMUST00000245163.1,Gas5-251,315; ENSMUST00000245204.1,Gas5-252,1271; ENSMUST00000246027.1,Gas5-253,694; ENSMUST00000246077.1,Gas5-254,1086; ENSMUST00000246359.1,Gas5-255,368; ENSMUST00000246481.1,Gas5-256,1213; ENSMUST00000246488.1,Gas5-257,278; ENSMUST00000246582.1,Gas5-258,862; ENSMUST00000246652.1,Gas5-259,470; ENSMUST00000246916.1,Gas5-260,1000; ENSMUST00000247022.1,Gas5-261,690; ENSMUST00000247032.1,Gas5-262,466; ENSMUST00000247046.1,Gas5-263,1816; ENSMUST00000247065.1,Gas5-264,415; ENSMUST00000247178.1,Gas5-265,412; ENSMUST00000247189.1,Gas5-266,293; ENSMUST00000247213.1,Gas5-267,624; ENSMUST00000247271.1,Gas5-268,1144; ENSMUST00000247311.1,Gas5-269,1441; ENSMUST00000247325.1,Gas5-270,2742; ENSMUST00000247331.1,Gas5-271,313; ENSMUST00000247341.1,Gas5-272,1045; ENSMUST00000247356.1,Gas5-273,1576; ENSMUST00000247369.1,Gas5-274,2185; ENSMUST00000247375.1,Gas5-275,2303; ENSMUST00000247377.1,Gas5-276,948; ENSMUST00000247402.1,Gas5-277,649; ENSMUST00000247411.1,Gas5-278,1761; ENSMUST00000247420.1,Gas5-279,1135; ENSMUST00000247435.1,Gas5-280,2126; ENSMUST00000247450.1,Gas5-281,951; ENSMUST00000247473.1,Gas5-282,2195; ENSMUST00000247477.1,Gas5-283,1377; ENSMUST00000247479.1,Gas5-284,678; ENSMUST00000247489.1,Gas5-285,510; ENSMUST00000247494.1,Gas5-286,1581; ENSMUST00000247508.1,Gas5-287,904; ENSMUST00000247512.1,Gas5-288,391; ENSMUST00000247514.1,Gas5-289,573; ENSMUST00000247518.1,Gas5-290,1238; ENSMUST00000247527.1,Gas5-291,1768; ENSMUST00000247532.1,Gas5-292,2817; ENSMUST00000247543.1,Gas5-293,3376; ENSMUST00000247549.1,Gas5-294,1819; ENSMUST00000247560.1,Gas5-295,1006; ENSMUST00000247570.1,Gas5-296,395; ENSMUST00000247573.1,Gas5-297,1563; ENSMUST00000247583.1,Gas5-298,1457; ENSMUST00000247586.1,Gas5-299,614; ENSMUST00000247597.1,Gas5-300,2730; ENSMUST00000247610.1,Gas5-301,1994; ENSMUST00000247611.1,Gas5-302,1572; ENSMUST00000247613.1,Gas5-303,2740; ENSMUST00000247615.1,Gas5-304,1767; ENSMUST00000247626.1,Gas5-305,491; ENSMUST00000247632.1,Gas5-306,1823; ENSMUST00000247635.1,Gas5-307,583; ENSMUST00000247638.1,Gas5-308,916; ENSMUST00000247640.1,Gas5-309,542; ENSMUST00000247644.1,Gas5-310,307; ENSMUST00000247650.1,Gas5-311,1934; ENSMUST00000247651.1,Gas5-312,339; ENSMUST00000247653.1,Gas5-313,965; ENSMUST00000247662.1,Gas5-314,2370; ENSMUST00000247667.1,Gas5-315,1141; ENSMUST00000247668.1,Gas5-316,1519; ENSMUST00000247670.1,Gas5-317,1581; ENSMUST00000247671.1,Gas5-318,1630; ENSMUST00000247674.1,Gas5-319,1576; ENSMUST00000247676.1,Gas5-320,374; ENSMUST00000247679.1,Gas5-321,1047; ENSMUST00000247681.1,Gas5-322,1007; ENSMUST00000247683.1,Gas5-323,655; ENSMUST00000247688.1,Gas5-324,1999; ENSMUST00000247691.1,Gas5-325,692; ENSMUST00000247693.1,Gas5-326,1812; ENSMUST00000247694.1,Gas5-327,1943; ENSMUST00000247697.1,Gas5-328,696; ENSMUST00000247698.1,Gas5-329,2633; ENSMUST00000247703.1,Gas5-330,1623; ENSMUST00000247704.1,Gas5-331,2369; ENSMUST00000247705.1,Gas5-332,1273; ENSMUST00000247709.1,Gas5-333,702; ENSMUST00000247710.1,Gas5-334,1954; ENSMUST00000247713.1,Gas5-335,372; ENSMUST00000247714.1,Gas5-336,451; ENSMUST00000247715.1,Gas5-337,1688; ENSMUST00000247716.1,Gas5-338,437; ENSMUST00000247717.1,Gas5-339,858; ENSMUST00000247719.1,Gas5-340,1266; ENSMUST00000247722.1,Gas5-341,583; ENSMUST00000247723.1,Gas5-342,2641; ENSMUST00000247724.1,Gas5-343,638; ENSMUST00000247725.1,Gas5-344,1082; ENSMUST00000247729.1,Gas5-345,1951; ENSMUST00000247731.1,Gas5-346,398; ENSMUST00000247732.1,Gas5-347,407; ENSMUST00000247734.1,Gas5-348,1377; ENSMUST00000247735.1,Gas5-349,2005"	.	"chr1:160,861,992-160,866,116[+]"	.	.	.	.	.	.	.	.	.	.	.
Mol02158	LncRNA	Gonadotropin releasing hormone 1 (Gnrh1)	Gnrh1	Gnrh1	14714	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000111095.4,Gnrh1-201,486; ENSMUST00000223929.2,Gnrh1-202,428; ENSMUST00000223951.2,Gnrh1-203,411"	.	"chr14:67,982,630-67,986,888[+]"	.	.	.	.	.	.	.	.	.	.	.
Mol02159	LncRNA	"H19, imprinted maternally expressed transcript (H19)"	H19	H19	14955	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000132294.9,H19-201,1217; ENSMUST00000136359.9,H19-202,2296; ENSMUST00000140716.3,H19-203,2508; ENSMUST00000149974.2,H19-204,935; ENSMUST00000152754.10,H19-205,2285; ENSMUST00000228259.2,H19-206,761; ENSMUST00000228514.2,H19-207,1178; ENSMUST00000246404.1,H19-208,752; ENSMUST00000246665.1,H19-209,2354; ENSMUST00000247116.1,H19-210,1958; ENSMUST00000247195.1,H19-211,2620; ENSMUST00000247478.1,H19-212,770; ENSMUST00000247519.1,H19-213,1939"	.	"chr7:142,129,262-142,131,886[-]"	.	.	.	.	.	ENSMUSG00000000031	.	.	.	.	.
Mol02160	LncRNA	"Matrin 3, pseudogene 2 (Matr3-ps2)"	Matr3-ps2	Matr3-ps2	17186	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	ENSMUSG00000089748	.	.	.	.	.
Mol02161	LncRNA	Maternally expressed 3 (MEG3)	Meg3	Meg3	17263	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000124106.9,Meg3-201,3341; ENSMUST00000126289.9,Meg3-202,1818; ENSMUST00000128178.2,Meg3-203,457; ENSMUST00000128458.3,Meg3-204,695; ENSMUST00000129245.9,Meg3-205,1531; ENSMUST00000143272.8,Meg3-206,5971; ENSMUST00000143836.9,Meg3-207,1908; ENSMUST00000143847.9,Meg3-208,1651; ENSMUST00000146701.8,Meg3-209,14548; ENSMUST00000150851.2,Meg3-210,421; ENSMUST00000166636.10,Meg3-211,1378; ENSMUST00000243087.1,Meg3-212,1694; ENSMUST00000243937.1,Meg3-213,1737; ENSMUST00000245180.1,Meg3-214,1786; ENSMUST00000245678.1,Meg3-215,3254; ENSMUST00000245731.1,Meg3-216,2850; ENSMUST00000245868.1,Meg3-217,2072; ENSMUST00000245940.1,Meg3-218,2582; ENSMUST00000245972.1,Meg3-219,2029; ENSMUST00000245980.1,Meg3-220,2009; ENSMUST00000245986.1,Meg3-221,1564; ENSMUST00000246047.1,Meg3-222,1575; ENSMUST00000246056.1,Meg3-223,2121; ENSMUST00000246081.1,Meg3-224,1702; ENSMUST00000246084.1,Meg3-225,1577; ENSMUST00000246113.1,Meg3-226,2129; ENSMUST00000246141.1,Meg3-227,1732; ENSMUST00000246154.1,Meg3-228,1774; ENSMUST00000246204.1,Meg3-229,1968; ENSMUST00000246209.1,Meg3-230,1689; ENSMUST00000246289.1,Meg3-231,1609; ENSMUST00000246369.1,Meg3-232,1660; ENSMUST00000246414.1,Meg3-233,2087; ENSMUST00000246427.1,Meg3-234,1829; ENSMUST00000246444.1,Meg3-235,2886; ENSMUST00000246462.1,Meg3-236,1657; ENSMUST00000246499.1,Meg3-237,1867; ENSMUST00000246513.1,Meg3-238,1653; ENSMUST00000246523.1,Meg3-239,1924; ENSMUST00000246553.1,Meg3-240,1794; ENSMUST00000246567.1,Meg3-241,2085; ENSMUST00000246647.1,Meg3-242,2044; ENSMUST00000246700.1,Meg3-243,1711; ENSMUST00000246776.1,Meg3-244,1575; ENSMUST00000246826.1,Meg3-245,1736; ENSMUST00000246852.1,Meg3-246,1742; ENSMUST00000246856.1,Meg3-247,1701; ENSMUST00000246883.1,Meg3-248,1615; ENSMUST00000246906.1,Meg3-249,1889; ENSMUST00000246940.1,Meg3-250,1934; ENSMUST00000246963.1,Meg3-251,1877; ENSMUST00000246994.1,Meg3-252,2657; ENSMUST00000247058.1,Meg3-253,1533; ENSMUST00000247082.1,Meg3-254,1692; ENSMUST00000247084.1,Meg3-255,2624; ENSMUST00000247113.1,Meg3-256,1908; ENSMUST00000247179.1,Meg3-257,2220; ENSMUST00000247194.1,Meg3-258,1752; ENSMUST00000247243.1,Meg3-259,1819; ENSMUST00000247257.1,Meg3-260,2616; ENSMUST00000247320.1,Meg3-261,1718; ENSMUST00000247335.1,Meg3-262,1617; ENSMUST00000247357.1,Meg3-263,703; ENSMUST00000247387.1,Meg3-264,1750"	.	"chr12:109,506,879-109,538,165[+]"	.	.	.	.	.	ENSMUSG00000021268	.	.	.	.	.
Mol02162	LncRNA	Small nucleolar RNA host gene 14 (SNHG14)	Snhg14	Snhg14	52480	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02163	LncRNA	Nucleic acid binding protein 1 (NABP1)	NABP1	NABP1	64859	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000307834.9,NABP1-201,1914; ENST00000307849.7,NABP1-202,3002; ENST00000409510.5,NABP1-203,843; ENST00000410026.7,NABP1-204,11524; ENST00000425611.9,NABP1-205,2269; ENST00000435931.1,NABP1-206,915; ENST00000451500.5,NABP1-207,2015; ENST00000462712.5,NABP1-208,961; ENST00000462824.1,NABP1-209,567; ENST00000491331.5,NABP1-210,855; ENST00000674172.1,NABP1-211,9440; ENST00000674187.1,NABP1-212,8976; ENST00000674262.1,NABP1-213,12359; ENST00000674360.1,NABP1-214,11728; ENST00000674406.1,NABP1-215,11895; ENST00000674414.1,NABP1-216,12192"	.	"chr2:191,678,068-191,741,097[+]"	.	.	HGNC:26232	.	.	ENSG00000173559	.	.	.	.	.
Mol02164	LncRNA	Nuclear paraspeckle assembly transcript 1 (NEAT1)	Neat1	Neat1	66961	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000173672.3,Neat1-201,21163; ENSMUST00000174287.2,Neat1-202,3004; ENSMUST00000174829.2,Neat1-203,1030; ENSMUST00000232969.2,Neat1-204,711"	.	"chr19:5,874,736-5,895,898[-]"	.	.	.	.	.	ENSMUSG00000092274	.	.	.	.	.
Mol02165	LncRNA	"Family with sequence similarity 120A, opposite strand (Fam120aos)"	Fam120aos	Fam120aos	68128	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02166	LncRNA	Metastasis associated lung adenocarcinoma transcript 1 (non-coding RNA) (Malat1)	Malat1	Malat1	72289	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000172812.4,Malat1-201,6988; ENSMUST00000173314.2,Malat1-202,556; ENSMUST00000173499.2,Malat1-203,485; ENSMUST00000174808.2,Malat1-204,656; ENSMUST00000245150.1,Malat1-205,887; ENSMUST00000245771.1,Malat1-206,1690"	.	"chr19:5,845,717-5,852,704[-]"	.	.	.	.	.	ENSMUSG00000092341	.	.	.	.	.
Mol02167	LncRNA	Growth arrest specific 5 (GAS5)	Gas5	Gas5	81714	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02168	LncRNA	AFAP1 antisense RNA 1 (AFAP1-AS1)	AFAP1-AS1	AFAP1-AS1	84740	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000608442.2,AFAP1-AS1-201,6808; ENST00000674004.1,AFAP1-AS1-202,5444"	.	"chr4:7,754,077-7,778,928[+]"	.	.	HGNC:28141	.	.	ENSG00000272620	.	.	.	.	.
Mol02169	LncRNA	Functional intergenic repeating RNA element (Firre)	Firre	Firre	103012	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000124842.8,Firre-201,1145; ENSMUST00000136518.8,Firre-202,715; ENSMUST00000143999.9,Firre-203,2139; ENSMUST00000148530.3,Firre-204,716; ENSMUST00000203672.2,Firre-205,490; ENSMUST00000203933.3,Firre-206,5555; ENSMUST00000204729.2,Firre-207,525; ENSMUST00000204974.4,Firre-208,5819; ENSMUST00000204991.3,Firre-209,1754; ENSMUST00000205059.3,Firre-210,884; ENSMUST00000243106.1,Firre-211,988; ENSMUST00000243634.1,Firre-212,1758"	.	"chrX:49,644,621-49,724,198[-]"	.	.	.	.	.	ENSMUSG00000085396	.	.	.	.	.
Mol02170	LncRNA	Peptidylprolyl isomerase F (cyclophilin F) (Ppif)	Ppif	Ppif	105675	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000022419.7,Ppif-201,1549; ENSMUST00000125881.2,Ppif-202,3637; ENSMUST00000223872.2,Ppif-203,1664"	.	"chr14:25,694,578-25,700,892[+]"	.	.	.	.	.	ENSMUSG00000021868	.	.	.	.	.
Mol02171	LncRNA	Long non-protein coding RNA 52 (LINC00052)	LINC00052	LINC00052	145978	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000560153.2,LINC00052-201,1966"	.	"chr15:87,576,929-87,579,866[+]"	.	.	HGNC:26455	.	.	ENSG00000259527	.	.	.	.	.
Mol02172	LncRNA	HNF1A antisense RNA 1 (HNF1A-AS1)	HNF1A-AS1	HNF1A-AS1	283460	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000433033.3,HNF1A-AS1-201,718; ENST00000535301.2,HNF1A-AS1-202,546; ENST00000537361.1,HNF1A-AS1-203,659; ENST00000539163.1,HNF1A-AS1-204,2455; ENST00000619441.1,HNF1A-AS1-205,343; ENST00000646404.1,HNF1A-AS1-206,557; ENST00000647473.1,HNF1A-AS1-207,1144; ENST00000701238.1,HNF1A-AS1-208,582; ENST00000701967.1,HNF1A-AS1-209,357"	.	"chr12:120,941,728-120,980,968[-]"	.	.	HGNC:26785	.	.	ENSG00000241388	.	.	.	.	.
Mol02173	LncRNA	Predicted gene 14461 (Gm14461)	Gm14461	Gm14461	329436	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000067618.6,Gm14461-201,1781; ENSMUST00000144728.3,Gm14461-202,1054; ENSMUST00000145972.9,Gm14461-203,784; ENSMUST00000240576.1,Gm14461-204,473; ENSMUST00000240577.1,Gm14461-205,919; ENSMUST00000240578.1,Gm14461-206,1077; ENSMUST00000240579.1,Gm14461-207,498; ENSMUST00000240580.1,Gm14461-208,1003; ENSMUST00000240581.1,Gm14461-209,1261; ENSMUST00000240582.1,Gm14461-210,1151; ENSMUST00000240583.1,Gm14461-211,1346; ENSMUST00000240584.1,Gm14461-212,1185; ENSMUST00000240585.1,Gm14461-213,1534; ENSMUST00000240586.1,Gm14461-214,1181; ENSMUST00000240587.1,Gm14461-215,1348; ENSMUST00000240588.1,Gm14461-216,1212; ENSMUST00000240590.1,Gm14461-217,1610; ENSMUST00000240591.1,Gm14461-218,1449; ENSMUST00000240592.1,Gm14461-219,1444; ENSMUST00000240593.1,Gm14461-220,1053; ENSMUST00000240594.1,Gm14461-221,1183; ENSMUST00000240595.1,Gm14461-222,889; ENSMUST00000240596.1,Gm14461-223,967; ENSMUST00000240597.1,Gm14461-224,1156; ENSMUST00000240598.1,Gm14461-225,818; ENSMUST00000240599.1,Gm14461-226,1629; ENSMUST00000240600.1,Gm14461-227,966; ENSMUST00000240601.1,Gm14461-228,1313; ENSMUST00000240602.1,Gm14461-229,830; ENSMUST00000240603.1,Gm14461-230,1758; ENSMUST00000240604.1,Gm14461-231,1544; ENSMUST00000240605.1,Gm14461-232,703; ENSMUST00000240606.1,Gm14461-233,1145; ENSMUST00000240607.1,Gm14461-234,604; ENSMUST00000240608.1,Gm14461-235,882; ENSMUST00000240609.1,Gm14461-236,1153; ENSMUST00000240610.1,Gm14461-237,950; ENSMUST00000240611.1,Gm14461-238,1706; ENSMUST00000240612.1,Gm14461-239,1194; ENSMUST00000240613.1,Gm14461-240,1850; ENSMUST00000240614.1,Gm14461-241,1124; ENSMUST00000240615.1,Gm14461-242,1047; ENSMUST00000240616.1,Gm14461-243,1273; ENSMUST00000240617.1,Gm14461-244,507; ENSMUST00000240618.1,Gm14461-245,1048; ENSMUST00000240619.1,Gm14461-246,1556; ENSMUST00000240620.1,Gm14461-247,1467; ENSMUST00000240621.1,Gm14461-248,491; ENSMUST00000240622.1,Gm14461-249,846; ENSMUST00000240623.1,Gm14461-250,724; ENSMUST00000240624.1,Gm14461-251,717; ENSMUST00000240625.1,Gm14461-252,996; ENSMUST00000240626.1,Gm14461-253,897; ENSMUST00000240627.1,Gm14461-254,1362; ENSMUST00000240628.1,Gm14461-255,1163; ENSMUST00000240629.1,Gm14461-256,1254; ENSMUST00000240630.1,Gm14461-257,1347; ENSMUST00000240631.1,Gm14461-258,1371; ENSMUST00000240632.1,Gm14461-259,657; ENSMUST00000240633.1,Gm14461-260,1444; ENSMUST00000240634.1,Gm14461-261,1050; ENSMUST00000240635.1,Gm14461-262,1329; ENSMUST00000240636.1,Gm14461-263,1324; ENSMUST00000240637.1,Gm14461-264,1001; ENSMUST00000240638.1,Gm14461-265,1053; ENSMUST00000240639.1,Gm14461-266,1464; ENSMUST00000240640.1,Gm14461-267,1508; ENSMUST00000240641.1,Gm14461-268,1411; ENSMUST00000240642.1,Gm14461-269,1169; ENSMUST00000240643.1,Gm14461-270,861; ENSMUST00000240644.1,Gm14461-271,894; ENSMUST00000240645.1,Gm14461-272,1529; ENSMUST00000240646.1,Gm14461-273,1478; ENSMUST00000240647.1,Gm14461-274,1243; ENSMUST00000240648.1,Gm14461-275,1176; ENSMUST00000240649.1,Gm14461-276,1467; ENSMUST00000240650.1,Gm14461-277,1451; ENSMUST00000240651.1,Gm14461-278,1010; ENSMUST00000240652.1,Gm14461-279,1163; ENSMUST00000240653.1,Gm14461-280,1005; ENSMUST00000240654.1,Gm14461-281,1463; ENSMUST00000240655.1,Gm14461-282,1610; ENSMUST00000240656.1,Gm14461-283,1123; ENSMUST00000240657.1,Gm14461-284,1232; ENSMUST00000240658.1,Gm14461-285,1189; ENSMUST00000240659.1,Gm14461-286,763; ENSMUST00000240660.1,Gm14461-287,1535; ENSMUST00000240661.1,Gm14461-288,584; ENSMUST00000240662.1,Gm14461-289,2342; ENSMUST00000240663.1,Gm14461-290,1634; ENSMUST00000240664.1,Gm14461-291,1144; ENSMUST00000240665.1,Gm14461-292,1169; ENSMUST00000240666.1,Gm14461-293,1480; ENSMUST00000240667.1,Gm14461-294,920; ENSMUST00000240668.1,Gm14461-295,1420; ENSMUST00000240669.1,Gm14461-296,1190"	.	"chr2:77,878,840-78,132,796[+]"	.	.	.	.	.	ENSMUSG00000054510	.	.	.	.	.
Mol02174	LncRNA	Long non-protein coding RNA 221 (LINC00221)	LINC00221	LINC00221	338005	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000603633.3,LINC00221-201,1829; ENST00000619530.1,LINC00221-202,1499; ENST00000620337.5,LINC00221-203,1586; ENST00000659544.1,LINC00221-204,1235"	.	"chr14:106,482,435-106,521,073[+]"	.	.	HGNC:20169	.	.	ENSG00000270816	.	.	.	.	.
Mol02175	LncRNA	Growth arrest associated LncRNA 1 (GASAL1)	GASAL1	GASAL1	401472	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:53461	.	.	.	.	.	.	.	.
Mol02176	LncRNA	Taurine up-regulated 1 (TUG1)	Tug1	Tug1	544752	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000132077.4,Tug1-201,6719; ENSMUST00000144852.2,Tug1-202,4720; ENSMUST00000153313.9,Tug1-203,5112; ENSMUST00000182330.2,Tug1-204,382; ENSMUST00000193809.2,Tug1-205,1612; ENSMUST00000226545.2,Tug1-206,1246; ENSMUST00000226724.2,Tug1-207,3853; ENSMUST00000227137.2,Tug1-208,935"	.	"chr11:3,589,785-3,599,673[-]"	.	.	.	.	.	ENSMUSG00000056579	.	.	.	.	.
Mol02177	LncRNA	Non-coding RNA activated by DNA damage (NORAD)	NORAD	NORAD	647979	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000565493.2,NORAD-201,5401"	.	"chr20:36,045,618-36,051,018[-]"	.	.	HGNC:44311	.	.	ENSG00000260032	.	.	.	.	.
Mol02178	miscRNA	Sme2 (sme2)	sme2	sme2	5802740	Schizosaccharomyces pombe	4896	Schizosaccharomyces pombe	Schizosaccharomyces	4895	Schizosaccharomycetaceae	4894	Schizosaccharomycetales	34346	Schizosaccharomycetes	147554	Ascomycota	4890	Fungi	4751	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02179	miscRNA	Omt3 (omt3)	omt3	omt3	5802960	Schizosaccharomyces pombe	4896	Schizosaccharomyces pombe	Schizosaccharomyces	4895	Schizosaccharomycetaceae	4894	Schizosaccharomycetales	34346	Schizosaccharomycetes	147554	Ascomycota	4890	Fungi	4751	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02180	LncRNA	COX2 (COX2)	COX2	COX2	5912281	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	ENSMUSG00000032487	.	.	.	.	.
Mol02181	LncRNA	Taurine up-regulated 1 (TUG1)	Tug1	Tug1	100125371	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02182	LncRNA	GABPB1 antisense RNA 1 (GABPB1-AS1)	GABPB1-AS1	GABPB1-AS1	100129387	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:44157	.	.	ENSG00000244879	.	.	.	.	.
Mol02183	LncRNA	psoriasis susceptibility 1 candidate 3 (PSORS1C3)	PSORS1C3	PSORS1C3	100130889	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:17203	.	.	.	.	.	.	.	.
Mol02184	LncRNA	LMCD1 antisense RNA 1 (LMCD1-AS1)	LMCD1-AS1	LMCD1-AS1	100288428	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000420095.2,LMCD1-AS1-201,2621; ENST00000439407.1,LMCD1-AS1-202,576; ENST00000441861.5,LMCD1-AS1-203,2683; ENST00000446281.5,LMCD1-AS1-204,932; ENST00000452802.6,LMCD1-AS1-205,2519; ENST00000455811.2,LMCD1-AS1-206,524; ENST00000458666.1,LMCD1-AS1-207,581; ENST00000654635.1,LMCD1-AS1-208,4540; ENST00000656911.1,LMCD1-AS1-209,2207; ENST00000659617.1,LMCD1-AS1-210,1968"	.	"chr3:7,951,263-8,611,924[-]"	.	.	HGNC:44477	.	.	ENSG00000227110	.	.	.	.	.
Mol02185	LncRNA	FAS antisense RNA 1 (FAS-AS1)	FAS-AS1	FAS-AS1	100302740	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:37128	.	.	.	.	.	.	.	.
Mol02186	LncRNA	Long non-protein coding RNA 673 (LINC00673)	LINC00673	LINC00673	100499467	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000453722.6,LINC00511-201,1716; ENST00000457958.7,LINC00511-202,1626; ENST00000577773.3,LINC00511-203,880; ENST00000577828.6,LINC00511-204,656; ENST00000578206.2,LINC00511-205,1732; ENST00000579631.2,LINC00511-206,448; ENST00000580175.2,LINC00511-207,208; ENST00000580199.7,LINC00511-208,678; ENST00000580500.5,LINC00511-209,561; ENST00000580861.2,LINC00511-210,701; ENST00000580948.1,LINC00511-211,475; ENST00000581183.3,LINC00511-212,860; ENST00000581549.2,LINC00511-213,2266; ENST00000581801.7,LINC00511-214,855; ENST00000582712.2,LINC00511-215,2586; ENST00000583460.2,LINC00511-216,1778; ENST00000584749.2,LINC00511-217,173; ENST00000647593.1,LINC00511-218,1690; ENST00000647611.1,LINC00511-219,762; ENST00000647652.1,LINC00511-220,3700; ENST00000647706.2,LINC00511-221,2532; ENST00000647735.1,LINC00511-222,496; ENST00000647850.1,LINC00511-223,111; ENST00000647871.2,LINC00511-224,1958; ENST00000647953.1,LINC00511-225,2292; ENST00000648054.1,LINC00511-226,1027; ENST00000648069.1,LINC00511-227,1713; ENST00000648088.1,LINC00511-228,669; ENST00000648104.2,LINC00511-229,1264; ENST00000648176.2,LINC00511-230,1647; ENST00000648203.1,LINC00511-231,746; ENST00000648220.1,LINC00511-232,668; ENST00000648248.1,LINC00511-233,1468; ENST00000648297.1,LINC00511-234,1823; ENST00000648401.1,LINC00511-235,2214; ENST00000648403.1,LINC00511-236,1556; ENST00000648411.1,LINC00511-237,1843; ENST00000648428.1,LINC00511-238,780; ENST00000648500.1,LINC00511-239,219; ENST00000648520.1,LINC00511-240,1888; ENST00000648522.1,LINC00511-241,1351; ENST00000648559.1,LINC00511-242,261; ENST00000648623.2,LINC00511-243,2522; ENST00000648631.1,LINC00511-244,2929; ENST00000648667.1,LINC00511-245,1751; ENST00000648672.2,LINC00511-246,841; ENST00000648840.1,LINC00511-247,502; ENST00000648907.1,LINC00511-248,736; ENST00000648952.1,LINC00511-249,1893; ENST00000648954.1,LINC00511-250,689; ENST00000649013.1,LINC00511-251,266; ENST00000649074.1,LINC00511-252,1905; ENST00000649172.1,LINC00511-253,1788; ENST00000649197.1,LINC00511-254,937; ENST00000649250.1,LINC00511-255,1978; ENST00000649269.1,LINC00511-256,789; ENST00000649311.1,LINC00511-257,1815; ENST00000649330.1,LINC00511-258,230; ENST00000649332.1,LINC00511-259,509; ENST00000649343.1,LINC00511-260,1552; ENST00000649350.1,LINC00511-261,2527; ENST00000649366.1,LINC00511-262,2028; ENST00000649407.1,LINC00511-263,1045; ENST00000649433.1,LINC00511-264,1836; ENST00000649440.2,LINC00511-265,1159; ENST00000649489.1,LINC00511-266,1682; ENST00000649532.1,LINC00511-267,1045; ENST00000649553.1,LINC00511-268,819; ENST00000649595.2,LINC00511-269,471; ENST00000649597.1,LINC00511-270,1206; ENST00000649614.1,LINC00511-271,1098; ENST00000649647.1,LINC00511-272,2060; ENST00000649733.1,LINC00511-273,1742; ENST00000649793.2,LINC00511-274,2208; ENST00000649833.1,LINC00511-275,1772; ENST00000649881.1,LINC00511-276,2078; ENST00000649936.1,LINC00511-277,796; ENST00000650016.1,LINC00511-278,508; ENST00000650033.1,LINC00511-279,3766; ENST00000650051.1,LINC00511-280,2207; ENST00000650083.1,LINC00511-281,1329; ENST00000650121.1,LINC00511-282,108; ENST00000650131.3,LINC00511-283,2292; ENST00000650161.1,LINC00511-284,791; ENST00000650180.1,LINC00511-285,691; ENST00000650191.1,LINC00511-286,951; ENST00000650194.2,LINC00511-287,762; ENST00000650211.1,LINC00511-288,977; ENST00000650212.1,LINC00511-289,2174; ENST00000650227.1,LINC00511-290,1126; ENST00000650289.2,LINC00511-291,862; ENST00000650313.1,LINC00511-292,1995; ENST00000650357.1,LINC00511-293,325; ENST00000650371.1,LINC00511-294,2061; ENST00000650419.2,LINC00511-295,952; ENST00000650423.1,LINC00511-296,1455; ENST00000650476.1,LINC00511-297,826; ENST00000650482.1,LINC00511-298,1202; ENST00000650483.1,LINC00511-299,1888; ENST00000650499.1,LINC00511-300,231; ENST00000650510.1,LINC00511-301,692; ENST00000650550.2,LINC00511-302,2041; ENST00000650554.1,LINC00511-303,514; ENST00000650570.1,LINC00511-304,617; ENST00000650600.1,LINC00511-305,117; ENST00000650602.2,LINC00511-306,1510; ENST00000701652.1,LINC00511-307,1773"	.	"chr17:72,290,091-72,640,472[-]"	.	.	HGNC:44354	.	.	ENSG00000227036	.	.	.	.	.
Mol02187	LncRNA	HOX transcript antisense RNA (HOTAIR)	Hotair	Hotair	100503872	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000151949.6,Hotair-201,2009"	.	"chr15:102,852,494-102,856,165[-]"	.	.	.	.	.	ENSMUSG00000086903	.	.	.	.	.
Mol02188	LncRNA	MELTF antisense RNA 1 (MELTF-AS1)	MELTF-AS1	MELTF-AS1	100507057	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000414354.3,MELTF-AS1-201,679; ENST00000415244.1,MELTF-AS1-202,951; ENST00000424769.1,MELTF-AS1-203,356; ENST00000437064.1,MELTF-AS1-204,306; ENST00000446695.1,MELTF-AS1-205,204"	.	"chr3:196,999,460-197,004,744[+]"	.	.	HGNC:40373	.	.	ENSG00000228109	.	.	.	.	.
Mol02189	LncRNA	Long non-protein coding RNA 707 (LINC00707)	LINC00707	LINC00707	100507127	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000436383.2,LINC00707-201,3098; ENST00000648093.1,LINC00707-202,1296; ENST00000648398.1,LINC00707-203,1639; ENST00000648637.1,LINC00707-204,1699; ENST00000649029.1,LINC00707-205,1647; ENST00000649110.1,LINC00707-206,1377; ENST00000649625.1,LINC00707-207,810; ENST00000650314.1,LINC00707-208,3105; ENST00000650412.1,LINC00707-209,1351"	.	"chr10:6,779,549-6,879,450[+]"	.	.	HGNC:44691	.	.	ENSG00000238266	.	.	.	.	.
Mol02190	LncRNA	HIF1A antisense RNA 1 (HIF1A-AS1)	HIF1A-AS1	HIF1A-AS1	100750246	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:43014	.	.	.	.	.	.	.	.
Mol02191	LncRNA	BLACAT1 overlapping LEMD1 locus (BLACAT1)	BLACAT1	BLACAT1	101669762	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000625854.1,BLACAT1-201,516; ENST00000626538.2,BLACAT1-202,6454; ENST00000629113.2,BLACAT1-203,2204; ENST00000629624.3,BLACAT1-204,6306"	.	"chr1:205,434,885-205,457,091[-]"	.	.	HGNC:48597	.	.	ENSG00000281406 	.	.	.	.	.
Mol02192	LncRNA	LncRNA neighboring enhancer of FOXA2 (LNCNEF)	LNCNEF	LNCNEF	101929685	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000422494.1,LNCNEF-201,659"	.	"chr20:22,587,522-22,607,517[-]"	.	.	HGNC:50656	.	.	ENSG00000237396	.	.	.	.	.
Mol02193	LncRNA	LOC102551356 uncharacterized LOC102551356 (LOC102551356)	LOC102551356	LOC102551356	102551356	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02194	LncRNA	"prostaglandin-endoperoxide synthase 2, opposite strand 2 (Ptgs2os2)"	Ptgs2os2	Ptgs2os2	102639566	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENSMUST00000181308.2,Ptgs2os2-201,1745; ENSMUST00000241512.1,Ptgs2os2-202,973; ENSMUST00000241778.1,Ptgs2os2-203,767; ENSMUST00000241946.1,Ptgs2os2-204,1007; ENSMUST00000243329.1,Ptgs2os2-205,593; ENSMUST00000244201.1,Ptgs2os2-206,935; ENSMUST00000245671.1,Ptgs2os2-207,948; ENSMUST00000245797.1,Ptgs2os2-208,955; ENSMUST00000245901.1,Ptgs2os2-209,905"	.	"chr1:150,034,794-150,040,836[-]"	.	.	.	.	.	ENSMUSG00000097754	.	.	.	.	.
Mol02195	LncRNA	tumor protein p53 pathway corepressor 1 (TP53COR1)	TP53COR1	TP53COR1	102800311	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:43652	.	.	.	.	.	.	.	.
Mol02196	LncRNA	Long non-protein coding RNA 1391 (LINC01391)	LINC01391	LINC01391	103344930	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000477059.1,LINC01391-201,483; ENST00000483650.1,LINC01391-202,865; ENST00000495287.1,LINC01391-203,3538"	.	"chr3:138,935,189-138,944,020[-]"	.	.	HGNC:50666	.	.	ENSG00000244578	.	.	.	.	.
Mol02197	LncRNA	myosin heavy chain associated RNA transcript (MHRT)	MHRT	MHRT	104564225	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:51291	.	.	.	.	.	.	.	.
Mol02198	LncRNA	SIRT1 antisense RNA (SIRT1-AS)	SIRT1-AS	SIRT1-AS	106633813	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	HGNC:51912	.	.	.	.	.	.	.	.
Mol02199	LncRNA	LOC107053293 uncharacterized LOC107053293 (LOC107053293)	LOC107053293	LOC107053293	107053293	Gallus gallus	9031	Gallus gallus	Gallus	9030	Phasianidae	9005	Galliformes	8976	Aves	8782	Chordata	7711	Metazoa	33208	"ENSGALT00010028583.1,N/A,13688; ENSGALT00010028585.1,,N/A,14415; ENSGALT00010028587.1,N/A,14295; ENSGALT00010028589.1,N/A,1974"	.	"Primary_assembly 4:76,412,160-76,438,386[+]"	.	.	.	.	.	ENSGALG00010011944	.	.	.	.	.
Mol02200	LncRNA	Ewing sarcoma associated transcript 1 (EWSAT1)	EWSAT1	EWSAT1	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02201	LncRNA	Urothelial cancer associated 1 (UCA1)	UCA1	UCA1	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02202	LncRNA	HOX transcript antisense RNA (HOTAIR)	HOTAIR	HOTAIR	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02203	LncRNA	Nuclear paraspeckle assembly transcript 1 (NEAT1)	NEAT1	NEAT1	.	Danio rerio	7955	Danio rerio	Danio	7954	Danionidae	2743709	Cypriniformes	7952	Actinopteri	186623	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02204	LncRNA	Metastasis associated lung adenocarcinoma transcript 1 (MALAT1)	MALAT1	MALAT1	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02205	LncRNA	Hepatocellular carcinoma up-regulated long non-coding RNA (HULC)	HULC	HULC	.	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02206	LncRNA	Long non-protein coding RNA (N336694)	N336694	N336694	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02207	LncRNA	Long non-protein coding RNA (LNC010561)	LNC010561	LNC010561	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02208	LncRNA	Long non-protein coding RNA (RP11-138 J23.1)	RP11-138 J23.1	RP11-138 J23.1	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02209	LncRNA	Long non-protein coding RNA (RAMS11)	RAMS11	RAMS11	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02210	LncRNA	Long non-protein coding RNA (CRCAL-3)	CRCAL-3	CRCAL-3	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02211	LncRNA	Long non-protein coding RNA (LNC-CETP-3)	LNC-CETP-3	LNC-CETP-3	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02212	LncRNA	Long non-protein coding RNA (HNF4A-AS1)	HNF4A-AS1	HNF4A-AS1	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02213	LncRNA	Long non-protein coding RNA (RP11-166P13.3)	RP11-166P13.3	RP11-166P13.3	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02214	LncRNA	Long non-protein coding RNA (MIRT2)	MIRT2	MIRT2	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02215	LncRNA	Long non-protein coding RNA (UC.333)	UC.333	UC.333	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02216	LncRNA	Long non-protein coding RNA (RISA)	RISA	RISA	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02217	LncRNA	Long non-protein coding RNA (GPX3-AS)	GPX3-AS	GPX3-AS	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02218	LncRNA	Long non-protein coding RNA (AK003290)	AK003290	AK003290	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02219	LncRNA	Long non-protein coding RNA (CHRF)	CHRF	CHRF	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02220	LncRNA	Long non-protein coding RNA (LncRNA-241)	LNCRNA-241	LNCRNA-241	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02221	LncRNA	Long non-protein coding RNA (MIAT2)	MIAT2	MIAT2	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02222	LncRNA	Long non-protein coding RNA (UC.457)	UC.457	UC.457	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02223	LncRNA	Long non-protein coding RNA (A_30_P01029806)	A_30_P01029806	A_30_P01029806	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02224	LncRNA	Long non-protein coding RNA (LOC284930)	LOC284930	LOC284930	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02225	LncRNA	Long non-protein coding RNA (LncRNA584)	LNCRNA584	LNCRNA584	.	Schizosaccharomyces pombe	4896	Schizosaccharomyces pombe	Schizosaccharomyces	4895	Schizosaccharomycetaceae	4894	Schizosaccharomycetales	34346	Schizosaccharomycetes	147554	Ascomycota	4890	Fungi	4751	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02226	LncRNA	Long non-protein coding RNA (UC.333)	UC.333	UC.333	.	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02227	LncRNA	Long non-protein coding RNA (PU.1 AS)	PU.1 AS	PU.1 AS	.	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02228	LncRNA	Long non-protein coding RNA (SRA)	SRA	SRA	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02229	LncRNA	Long non-protein coding RNA (LncRNA3037)	LNCRNA3037	LNCRNA3037	.	Gallus gallus	9031	Gallus gallus	Gallus	9030	Phasianidae	9005	Galliformes	8976	Aves	8782	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02230	LncRNA	Long non-protein coding RNA (NONRATT007560.2)	NONRATT007560.2	NONRATT007560.2	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02231	LncRNA	Long non-protein coding RNA (SNHG7)	SNHG7	SNHG7	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02232	LncRNA	Long non-protein coding RNA (ACART)	ACART	ACART	.	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02233	LncRNA	Long non-protein coding RNA (B3GALT5-AS1)	B3GALT5-AS1	B3GALT5-AS1	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02234	LncRNA	Long non-protein coding RNA (GM26669)	GM26669	GM26669	.	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02235	LncRNA	Long non-protein coding RNA (GM16076)	GM16076	GM16076	.	Mus musculus	10090	Mus musculus	Mus	10088	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol02236	LncRNA	Long non-protein coding RNA (JHDM1D-AS1)	JHDM1D-AS1	JHDM1D-AS1	.	Rattus norvegicus	10116	Rattus norvegicus	Rattus	10114	Muridae	10066	Rodentia	9989	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol03000	Piwi-interacting RNA	Long non-protein coding RNA (AC023115.3)	.	.	.	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	.	.	.	.	.	.	.	.	.	.	.	.	.	.
Mol03001	Protein	Acetyl-CoA acetyltransferase 2 (ACAT2)	ACAT2; ACTL	ACAT2	39	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000367048.5,ACAT2-201,1520; ENST00000467951.1,ACAT2-202,856; ENST00000472052.1,ACAT2-203,1641"	MNAGSDPVVIVSAARTIIGSFNGALAAVPVQDLGSTVIKEVLKRATVAPEDVSEVIFGHVLAAGCGQNPVRQASVGAGIPYSVPAWSCQMICGSGLKAVCLAVQSIGIGDSSIVVAGGMENMSKAPHLAYLRTGVKIGEMPLTDSILCDGLTDAFHNCHMGITAENVAKKWQVSREDQDKVAVLSQNRTENAQKAGHFDKEIVPVLVSTRKGLIEVKTDEFPRHGSNIEAMSKLKPYFLTDGTGTVTPANASGINDGAAAVVLMKKSEADKRGLTPLARIVSWSQVGVEPSIMGIGPIPAIKQAVTKAGWSLEDVDIFEINEAFAAVSAAIVKELGLNPEKVNIEGGAIALGHPLGASGCRILVTLLHTLERMGRSRGVAALCIGGGMGIAMCVQRE	"chr6:159,762,045-159,779,112[+]"	Involved in the biosynthetic pathway of cholesterol.	PDB: 1WL4; PDB: 1WL5	HGNC:94	THIC_HUMAN	reviewed	ENSG00000120437	.	.	.	.	.
Mol03002	Protein	Adrenoceptor beta 3 (ADRB3)	ADRB3; ADRB3R; B3AR	ADRB3	155	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000345060.5,ADRB3-201,2585; ENST00000520341.2,ADRB3-202,1624"	MAPWPHENSSLAPWPDLPTLAPNTANTSGLPGVPWEAALAGALLALAVLATVGGNLLVIVAIAWTPRLQTMTNVFVTSLAAADLVMGLLVVPPAATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGALVTKRCARTAVVLVWVVSAAVSFAPIMSQWWRVGADAEAQRCHSNPRCCAFASNMPYVLLSSSVSFYLPLLVMLFVYARVFVVATRQLRLLRGELGRFPPEESPPAPSRSLAPAPVGTCAPPEGVPACGRRPARLLPLREHRALCTLGLIMGTFTLCWLPFFLANVLRALGGPSLVPGPAFLALNWLGYANSAFNPLIYCRSPDFRSAFRRLLCRCGRRLPPEPCAAARPALFPSGVPAARSSPAQPRLCQRLDGASWGVS	"chr8:37,962,990-37,966,599[-]"	Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.	.	HGNC:288	ADRB3_HUMAN	reviewed	ENSG00000188778	.	.	.	.	.
Mol03003	Protein	Aldehyde dehydrogenase 1 family member A1 (ALDH1A1)	ALDH1A1; ALDC; ALDH1; PUMB1	ALDH1A1	216	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000297785.8,ALDH1A1-201,2096; ENST00000376939.5,ALDH1A1-202,822; ENST00000419959.5,ALDH1A1-203,806; ENST00000446946.1,ALDH1A1-204,805; ENST00000482210.5,ALDH1A1-205,879; ENST00000493113.1,ALDH1A1-206,604; ENST00000493311.1,ALDH1A1-207,209"	MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS	"chr9:72,900,671-73,080,442[-]"	"Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid. Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic. Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins. Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission."	PDB: 4WB9; PDB: 4WJ9; PDB: 4WP7; PDB: 4WPN; PDB: 4X4L; PDB: 5AC2; PDB: 5L2M; PDB: 5L2N; PDB: 5L2O; PDB: 5TEI; PDB: 6DUM; PDB: 7JWS; PDB: 7JWT; PDB: 7JWU; PDB: 7JWV; PDB: 7JWW	HGNC:402	AL1A1_HUMAN	reviewed	ENSG00000165092	.	.	.	.	.
Mol03004	Protein	Aldo-keto reductase family 1 member B (AKR1B1)	AKR1B1; ALDR1; ALR2	AKR1B1	231	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000285930.9,AKR1B1-201,1361; ENST00000426422.1,AKR1B1-202,521; ENST00000434222.5,AKR1B1-203,1852; ENST00000462784.1,AKR1B1-204,598; ENST00000465351.5,AKR1B1-205,1930; ENST00000467251.1,AKR1B1-206,723; ENST00000467829.1,AKR1B1-207,561; ENST00000484592.5,AKR1B1-208,639; ENST00000487438.5,AKR1B1-209,557; ENST00000489022.5,AKR1B1-210,577; ENST00000491741.5,AKR1B1-211,1188; ENST00000497983.5,AKR1B1-212,534; ENST00000498373.1,AKR1B1-213,549; ENST00000498771.5,AKR1B1-214,858"	MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF	"chr7:134,442,356-134,459,284[-]"	"Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosacharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Displays low enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal. Catalyzes the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related phospholipid aldehydes that are generated from the oxydation of phosphotidylcholine and phosphatdyleethanolamides. Plays a role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls)."	PDB: 1ABN; PDB: 1ADS; PDB: 1AZ1; PDB: 1AZ2; PDB: 1EF3; PDB: 1EL3; PDB: 1IEI; PDB: 1MAR; PDB: 1PWL; PDB: 1PWM; PDB: 1T40; PDB: 1T41; PDB: 1US0; PDB: 1X96; PDB: 1X97; PDB: 1X98; PDB: 1XGD; PDB: 1Z3N; PDB: 1Z89; PDB: 1Z8A; PDB: 2ACQ; PDB: 2ACR; PDB: 2ACS; PDB: 2ACU; PDB: 2AGT; PDB: 2DUX; PDB: 2DUZ; PDB: 2DV0; PDB: 2F2K; PDB: 2FZ8; PDB: 2FZ9; PDB: 2FZB; PDB: 2FZD; PDB: 2HV5; PDB: 2HVN; PDB: 2HVO; PDB: 2I16; PDB: 2I17; PDB: 2IKG; PDB: 2IKH; PDB: 2IKI; PDB: 2IKJ; PDB: 2INE; PDB: 2INZ; PDB: 2IPW; PDB: 2IQ0; PDB: 2IQD; PDB: 2IS7; PDB: 2ISF; PDB: 2J8T; PDB: 2NVC; PDB: 2NVD; PDB: 2PD5; PDB: 2PD9; PDB: 2PDB; PDB: 2PDC; PDB: 2PDF; PDB: 2PDG; PDB: 2PDH; PDB: 2PDI; PDB: 2PDJ; PDB: 2PDK; PDB: 2PDL; PDB: 2PDM; PDB: 2PDN; PDB: 2PDP; PDB: 2PDQ; PDB: 2PDU; PDB: 2PDW; PDB: 2PDX; PDB: 2PDY; PDB: 2PEV; PDB: 2PF8; PDB: 2PFH; PDB: 2PZN; PDB: 2QXW; PDB: 2R24; PDB: 3BCJ; PDB: 3DN5; PDB: 3G5E; PDB: 3GHR; PDB: 3GHS; PDB: 3GHT; PDB: 3GHU; PDB: 3LBO; PDB: 3LD5; PDB: 3LEN; PDB: 3LEP; PDB: 3LQG; PDB: 3LQL; PDB: 3LZ3; PDB: 3LZ5; PDB: 3M0I; PDB: 3M4H; PDB: 3M64; PDB: 3MB9; PDB: 3MC5; PDB: 3ONB; PDB: 3ONC; PDB: 3P2V; PDB: 3Q65; PDB: 3Q67; PDB: 3RX2; PDB: 3RX3; PDB: 3RX4; PDB: 3S3G; PDB: 3T42; PDB: 3U2C; PDB: 3V35; PDB: 3V36; PDB: 4GCA; PDB: 4GQ0; PDB: 4IGS; PDB: 4JIR; PDB: 4LAU; PDB: 4LAZ; PDB: 4LB3; PDB: 4LB4; PDB: 4LBR; PDB: 4LBS; PDB: 4NKC; PDB: 4PR4; PDB: 4PRR; PDB: 4PRT; PDB: 4PUU; PDB: 4PUW; PDB: 4Q7B; PDB: 4QBX; PDB: 4QR6; PDB: 4QX4; PDB: 4QXI; PDB: 4RPQ; PDB: 4XZH; PDB: 4XZI; PDB: 4YS1; PDB: 4YU1; PDB: 5HA7; PDB: 5OU0; PDB: 5OUJ; PDB: 5OUK; PDB: 6F7R; PDB: 6F81; PDB: 6F82; PDB: 6F84; PDB: 6F8O; PDB: 6SYW; PDB: 6T27; PDB: 6T3P; PDB: 6T5G; PDB: 6T7Q; PDB: 6TD8; PDB: 6TUC; PDB: 6TUF; PDB: 6TXP; PDB: 6XUM; PDB: 6Y03; PDB: 6Y1P	HGNC:381	ALDR_HUMAN	reviewed	ENSG00000085662	.	.	.	.	.
Mol03005	Protein	Baculoviral IAP repeat containing 2 (BIRC2)	BIRC2; API1; MIHB; RNF48	BIRC2	329	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000227758.7,BIRC2-201,3764; ENST00000527465.1,BIRC2-202,595; ENST00000527808.1,BIRC2-203,709; ENST00000527910.5,BIRC2-204,4073; ENST00000528344.1,BIRC2-205,866; ENST00000530675.5,BIRC2-206,1927; ENST00000531259.5,BIRC2-207,572; ENST00000532672.5,BIRC2-208,2617; ENST00000532832.5,BIRC2-209,505; ENST00000533742.5,BIRC2-210,720; ENST00000534130.1,BIRC2-211,627; ENST00000534646.5,BIRC2-212,562; ENST00000613397.4,BIRC2-213,4066"	MHKTASQRLFPGPSYQNIKSIMEDSTILSDWTNSNKQKMKYDFSCELYRMSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKLGDSPIQKHKQLYPSCSFIQNLVSASLGSTSKNTSPMRNSFAHSLSPTLEHSSLFSGSYSSLSPNPLNSRAVEDISSSRTNPYSYAMSTEEARFLTYHMWPLTFLSPSELARAGFYYIGPGDRVACFACGGKLSNWEPKDDAMSEHRRHFPNCPFLENSLETLRFSISNLSMQTHAARMRTFMYWPSSVPVQPEQLASAGFYYVGRNDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEFLIRMKGQEFVDEIQGRYPHLLEQLLSTSDTTGEENADPPIIHFGPGESSSEDAVMMNTPVVKSALEMGFNRDLVKQTVQSKILTTGENYKTVNDIVSALLNAEDEKREEEKEKQAEEMASDDLSLIRKNRMALFQQLTCVLPILDNLLKANVINKQEHDIIKQKTQIPLQARELIDTILVKGNAAANIFKNCLKEIDSTLYKNLFVDKNMKYIPTEDVSGLSLEEQLRRLQEERTCKVCMDKEVSVVFIPCGHLVVCQECAPSLRKCPICRGIIKGTVRTFLS	"chr11:102,347,211-102,378,670[+]"	"Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle."	PDB: 1QBH; PDB: 2L9M; PDB: 3D9T; PDB: 3D9U; PDB: 3M1D; PDB: 3MUP; PDB: 3OZ1; PDB: 3T6P; PDB: 3UW4; PDB: 4EB9; PDB: 4HY4; PDB: 4HY5; PDB: 4KMN; PDB: 4LGE; PDB: 4LGU; PDB: 4MTI; PDB: 4MU7; PDB: 5M6N; PDB: 6EXW; PDB: 6HPR; PDB: 6W74; PDB: 6W7O; PDB: 6W8I	HGNC:590	BIRC2_HUMAN	reviewed	ENSG00000110330	.	.	.	.	.
Mol03006	Protein	Calcitonin gene-related peptide 1 (CALCA)	CALCA; CALC1	CALCA	796	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000331587.9,CALCA-201,840; ENST00000361010.7,CALCA-202,916; ENST00000396372.2,CALCA-203,581; ENST00000469608.5,CALCA-204,679; ENST00000486207.5,CALCA-205,851; ENST00000494746.1,CALCA-206,1837"	MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSRIIAQKRACDTATCVTHRLAGLLSRSGGVVKNNFVPTNVGSKAFGRRRRDLQA	"chr11:14,966,668-14,972,351[-]"	"CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. It also elevates platelet cAMP."	PDB: 6E3Y; PDB: 7KNU	.	CALCA_HUMAN	reviewed	ENSG00000110680	.	.	.	.	.
Mol03007	Protein	B-lymphocyte antigen CD20 (CD20)	MS4A1; CD20	CD20	931	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000345732.9,MS4A1-201,3556; ENST00000389939.2,MS4A1-202,3372; ENST00000527101.5,MS4A1-203,582; ENST00000528313.1,MS4A1-204,928; ENST00000530482.1,MS4A1-205,484; ENST00000532073.5,MS4A1-206,2560; ENST00000532418.1,MS4A1-207,582; ENST00000532491.5,MS4A1-208,558; ENST00000533306.6,MS4A1-209,607; ENST00000534503.5,MS4A1-210,933; ENST00000534668.6,MS4A1-211,3467; ENST00000674194.1,MS4A1-212,2499"	MTTPRNSVNGTFPAEPMKGPIAMQSGPKPLFRRMSSLVGPTQSFFMRESKTLGAVQIMNGLFHIALGGLLMIPAGIYAPICVTVWYPLWGGIMYIISGSLLAATEKNSRKCLVKGKMIMNSLSLFAAISGMILSIMDILNIKISHFLKMESLNFIRAHTPYINIYNCEPANPSEKNSPSTQYCYSIQSLFLGILSVMLIFAFFQELVIAGIVENEWKRTCSRPKSNIVLLSAEEKKEQTIEIKEEVVGLTETSSQPKNEEDIEIIPIQEEEEEETETNFPEPPQDQESSPIENDSSP	"chr11:60,455,846-60,470,752[+]"	"B-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes. Functions as a store-operated calcium (SOC) channel component promoting calcium influx after activation by the B-cell receptor/BCR."	PDB: 2OSL; PDB: 3BKY; PDB: 3PP4; PDB: 6VJA; PDB: 6Y90; PDB: 6Y92; PDB: 6Y97; PDB: 6Y9A	.	CD20_HUMAN	reviewed	ENSG00000156738	.	.	.	.	.
Mol03008	Protein	CD36 molecule (CD36)	CD36; GP3B; GP4	CD36	948	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000309881.11,CD36-201,2094; ENST00000394788.7,CD36-202,1942; ENST00000413265.5,CD36-203,855; ENST00000419819.2,CD36-204,1686; ENST00000426978.5,CD36-205,565; ENST00000428497.5,CD36-206,541; ENST00000432207.5,CD36-207,1808; ENST00000433696.6,CD36-208,1985; ENST00000435819.5,CD36-209,2365; ENST00000436384.5,CD36-210,536; ENST00000438020.5,CD36-211,720; ENST00000441034.2,CD36-212,545; ENST00000441109.6,CD36-213,499; ENST00000447544.7,CD36-214,4598; ENST00000464213.1,CD36-215,6179; ENST00000478292.2,CD36-216,462; ENST00000480599.6,CD36-217,888; ENST00000482059.6,CD36-218,569; ENST00000488048.1,CD36-219,496; ENST00000526804.5,CD36-220,496; ENST00000534394.5,CD36-221,1741; ENST00000538969.5,CD36-222,1922; ENST00000544133.5,CD36-223,1914; ENST00000648416.1,CD36-224,842"	MGCDRNCGLIAGAVIGAVLAVFGGILMPVGDLLIQKTIKKQVVLEEGTIAFKNWVKTGTEVYRQFWIFDVQNPQEVMMNSSNIQVKQRGPYTYRVRFLAKENVTQDAEDNTVSFLQPNGAIFEPSLSVGTEADNFTVLNLAVAAASHIYQNQFVQMILNSLINKSKSSMFQVRTLRELLWGYRDPFLSLVPYPVTTTVGLFYPYNNTADGVYKVFNGKDNISKVAIIDTYKGKRNLSYWESHCDMINGTDAASFPPFVEKSQVLQFFSSDICRSIYAVFESDVNLKGIPVYRFVLPSKAFASPVENPDNYCFCTEKIISKNCTSYGVLDISKCKEGRPVYISLPHFLYASPDVSEPIDGLNPNEEEHRTYLDIEPITGFTLQFAKRLQVNLLVKPSEKIQVLKNLKRNYIVPILWLNETGTIGDEKANMFRSQVTGKINLLGLIEMILLSVGVVMFVAFMISYCACRSKTIK	"chr7:80,369,575-80,679,277[+]"	"Multifunctional glycoprotein that acts as receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (Probable). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption. Mechanistically, binding of fatty acids activates downstream kinase LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and inactivates it resulting in the subsequent depalmitoylation of CD36 and caveolar endocytosis. In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway. Involved in oral fat perception and preferences. Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions. In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract. Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis. Receptor for thrombospondins, THBS1 and THBS2, mediating their antiangiogenic effects. As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome. Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway."	PDB: 5LGD	HGNC:1663	CD36_HUMAN	reviewed	ENSG00000135218	.	.	.	.	.
Mol03009	Protein	Ectonucleoside triphosphate diphosphohydrolase 5 (ENTPD5)	ENTPD5; CD39L4; PCPH	ENTPD5	957	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000334696.11,ENTPD5-201,5261; ENST00000553284.5,ENTPD5-202,904; ENST00000554664.5,ENTPD5-203,1119; ENST00000555829.5,ENTPD5-204,691; ENST00000556108.5,ENTPD5-205,451; ENST00000556242.5,ENTPD5-206,1437; ENST00000557325.5,ENTPD5-207,3096; ENST00000557681.1,ENTPD5-208,452"	MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLLQSLGISH	"chr14:73,958,010-74,019,399[-]"	"Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP. In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER."	.	HGNC:3367	ENTP5_HUMAN	reviewed	ENSG00000187097	.	.	.	.	.
Mol03010	Protein	Cyclin dependent kinase 7 (CDK7)	CDK7; CAK; CAK1; CDKN7; MO15; STK1	CDK7	1022	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000256443.8,CDK7-201,1426; ENST00000502604.5,CDK7-202,1455; ENST00000504147.5,CDK7-203,722; ENST00000506563.5,CDK7-204,728; ENST00000506789.5,CDK7-205,477; ENST00000508726.5,CDK7-206,531; ENST00000510106.5,CDK7-207,818; ENST00000512687.5,CDK7-208,905; ENST00000512985.1,CDK7-209,261; ENST00000513629.1,CDK7-210,885; ENST00000514676.5,CDK7-211,1164; ENST00000515180.5,CDK7-212,486; ENST00000515391.5,CDK7-213,809; ENST00000626796.2,CDK7-214,358; ENST00000629350.2,CDK7-215,1149"	MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF	"chr5:69,234,795-69,277,430[+]"	"Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition."	PDB: 1UA2; PDB: 6O9L; PDB: 6XBZ; PDB: 6XD3; PDB: 7B5O; PDB: 7B5Q; PDB: 7EGB; PDB: 7EGC; PDB: 7ENA; PDB: 7ENC; PDB: 7LBM; PDB: 7NVR	HGNC:1778	CDK7_HUMAN	reviewed	ENSG00000134058	.	.	.	.	.
Mol03011	Protein	DNA topoisomerase 2-alpha (TOP2A)	TOP2; TP2A; TOPIIA; TOP2alpha	TOP2A	7153	Homo sapiens	9606	Homo sapiens	Homo	9605	Hominidae	9604	Primates	9443	Mammalia	40674	Chordata	7711	Metazoa	33208	"ENST00000581055.1,TOP2A-205,579; ENST00000578412.1,TOP2A-204,882; ENST00000577706.1,TOP2A-203,554; ENST00000577541.1,TOP2A-202,420; ENST00000423485.6,TOP2A-201,5695"	MEVSPLQPVNENMQVNKIKKNEDAKKRLSVERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNLISIWNNGKGIPVVEHKVEKMYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGEMELKPFNGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNKLPVKGFRSYVDMYLKDKLDETGNSLKVIHEQVNHRWEVCLTMSEKGFQQISFVNSIATSKGGRHVDYVADQIVTKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQPKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQVQLNKKCSAVKHNRIKGIPKLDDANDAGGRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEMAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQIDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQTTTYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSSLARLLFPPKDDHTLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREIVNNIRRLMDGEEPLPMLPSYKNFKGTIEELAPNQYVISGEVAILNSTTIEISELPVRTWTQTYKEQVLEPMLNGTEKTPPLITDYREYHTDTTVKFVVKMTEEKLAEAERVGLHKVFKLQTSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESAKLNNQARFILEKIDGKIIIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDNEKETEKSDSVTDSGPTFNYLLDMPLWYLTKEKKDELCRLRNEKEQELDTLKRKSPSDLWKEDLATFIEELEAVEAKEKQDEQVGLPGKGGKAKGKKTQMAEVLPSPRGQRVIPRITIEMKAEAEKKNKKKIKNENTEGSPQEDGVELEGLKQRLEKKQKREPGTKTKKQTTLAFKPIKKGKKRNPWSDSESDRSSDESNFDVPPRETEPRRAATKTKFTMDLDSDEDFSDFDEKTDDEDFVPSDASPPKTKTSPKLSNKELKPQKSVVSDLEADDVKGSVPLSSSPPATHFPDETEITNPVPKKNVTVKKTAAKSQSSTSTTGAKKRAAPKGTKRDPALNSGVSQKPDPAKTKNRRKRKPSTSDDSDSNFEKIVSKAVTSKKSKGESDDFHMDFDSAVAPRAKSVRAKKPIKYLEESDEDDLF	"chr17: 40,388,525-40,417,896[+]"	"Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand."	.	HGNC:11989	TOP2A_HUMAN	reviewed	ENSG00000131747	.	.	.	.	.