General Information of the Molecule (ID: Mol00391)
Name
Gem-associated protein 2 (SIP1) ,Homo sapiens
Synonyms
Gemin-2; Component of gems 2; Survival of motor neuron protein-interacting protein 1; SMN-interacting protein 1; SIP1
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Molecule Type
Protein
Gene Name
GEMIN2
Gene ID
8487
Location
chr14:39114285-39136973[+]
Sequence
MRRAELAGLKTMAWVPAESAVEELMPRLLPVEPCDLTEGFDPSVPPRTPQEYLRRVQIEA
AQCPDVVVAQIDPKKLKRKQSVNISLSGCQPAPEGYSPTLQWQQQQVAQFSTVRQNVNKH
RSHWKSQQLDSNVTMPKSEDEEGWKKFCLGEKLCADGAVGPATNESPGIDYVQIGFPPLL
SIVSRMNQATVTSVLEYLSNWFGERDFTPELGRWLYALLACLEKPLLPEAHSLIRQLARR
CSEVRLLVDSKDDERVPALNLLICLVSRYFDQRDLADEPS
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Function
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.
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Uniprot ID
GEMI2_HUMAN
Ensembl ID
ENSG00000092208
HGNC ID
HGNC:10884
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Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Primates
Family: Hominidae
Genus: Homo
Species: Homo sapiens
Type(s) of Resistant Mechanism of This Molecule
  RTDM: Regulation by the Disease Microenvironment
Drug Resistance Data Categorized by Drug
Approved Drug(s)
1 drug(s) in total
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Gefitinib
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Drug Resistance Data Categorized by Their Corresponding Mechanisms
       Regulation by the Disease Microenvironment (RTDM) Click to Show/Hide
Disease Class: Lung cancer [1]
Resistant Disease Lung cancer [ICD-11: 2C25.5]
Resistant Drug Gefitinib
Molecule Alteration Expression
Up-regulation
Experimental Note Revealed Based on the Cell Line Data
Cell Pathway Regulation Beta-catenin signaling pathway Activation hsa04520
Cell invasion Activation hsa05200
Cell proliferation Activation hsa05200
In Vitro Model 95D cells Lung Homo sapiens (Human) CVCL_7110
95C cells Lung Homo sapiens (Human) CVCL_7109
YTMLC-90 cells Lung Homo sapiens (Human) CVCL_6959
In Vivo Model BALB/c nude mouse xenograft model Mus musculus
Experiment for
Molecule Alteration
Western blot analysis
Experiment for
Drug Resistance
EdU assay
Mechanism Description HOTAIR also regulates non-small-cell lung cancer proliferation, migration and invasion through epithelial-mesenchymal transition and the beta-catenin pathway.
Disease- and Tissue-specific Abundances of This Molecule
ICD Disease Classification 02
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Lung cancer [ICD-11: 2C25]
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Differential expression of molecule in resistant diseases
The Studied Tissue Lung
The Specified Disease Lung cancer
The Expression Level of Disease Section Compare with the Healthy Individual Tissue p-value: 1.13E-19; Fold-change: 3.91E-01; Z-score: 9.22E-01
The Expression Level of Disease Section Compare with the Adjacent Tissue p-value: 2.62E-23; Fold-change: 7.14E-01; Z-score: 1.34E+00
Molecule expression in the normal tissue adjacent to the diseased tissue of patients
Molecule expression in the diseased tissue of patients
Molecule expression in the normal tissue of healthy individuals
Disease-specific Molecule Abundances Click to View the Clearer Original Diagram
Tissue-specific Molecule Abundances in Healthy Individuals
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References
Ref 1 HOTAIR, a long noncoding RNA, is a marker of abnormal cell cycle regulation in lung cancer. Cancer Sci. 2018 Sep;109(9):2717-2733. doi: 10.1111/cas.13745.

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