Serrate RNA effector molecule homolog

SRRT
Identifiers
Aliases	SRRT , ARS2, ASR2, serrate, serrate, RNA effector molecule
External IDs	OMIM: 614469 MGI: 1933527 HomoloGene: 9298 GeneCards: SRRT
Gene location (Human) Chr. Chromosome 7 (human) [1] Band 7q22.1 Start 100,875,103 bp [1] End 100,888,664 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 G2 Start 137,293,966 bp [2] End 137,305,936 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sural nerve anterior pituitary right lobe of thyroid gland canal of the cervix left lobe of thyroid gland right uterine tube left uterine tube skin of abdomen spleen minor salivary gland Top expressed in bone marrow thymus islet of Langerhans ovary olfactory bulb spleen cerebellum cerebellar cortex hypothalamus mirror More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA binding protein binding nucleic acid binding RNA binding Cellular component cytoplasm nucleus nucleoplasm protein-containing complex Biological process positive regulation of neurogenesis gene silencing cell population proliferation regulation of transcription, DNA-templated response to arsenic-containing substance transcription, DNA-templated neuronal stem cell population maintenance primary miRNA processing mRNA splicing, via spliceosome snRNA transcription by RNA polymerase II mRNA processing Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51593 83701 Ensembl ENSG00000087087 ENSMUSG00000037364 UniProt Q9BXP5 Q99MR6 RefSeq (mRNA) NM_001128852 NM_001128853 NM_001128854 NM_015908 NM_182800 NM_001109909 NM_001109910 NM_031405 NM_001359602 RefSeq (protein) NP_001122324 NP_001122325 NP_001122326 NP_056992 NP_001103379 NP_001103380 NP_113582 NP_001346531 Location (UCSC) Chr 7: 100.88 – 100.89 Mb Chr 5: 137.29 – 137.31 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Serrate RNA effector molecule homolog (SRRT) also known as arsenite-resistance protein 2 (ARS2) is a protein that in humans is encoded by the SRRT gene. ^[5]

The SRRT gene product plays a role in RNA-mediated gene silencing (RNAi) by miRNAs. Independently of its activity on miRNAs, it is necessary and sufficient to promote neural stem cell self-renewal, by directly binding to the SOX2 promoter and positively regulating its transcription. It enables the binding activity of the mRNA cap binding complex and the adaptor activity of certain protein molecules. It can be found in the nucleoplasm and is part of the ribonucleoprotein complex. It is involved in cell cycle progression around the S phase. ^[6]

It does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Diseases associated with SRRT include spondylocostal dysostosis and cerebral arteriopathy.

References

1. GRCh38: Ensembl release 89: ENSG00000087087 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000037364 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: ARS2 ARS2 protein".
6. "SRRT Gene". GeneCards. Retrieved 31 January 2023.

Further reading

• Rossman TG, Wang Z (1999). "Expression cloning for arsenite-resistance resulted in isolation of tumor-suppressor fau cDNA: possible involvement of the ubiquitin system in arsenic carcinogenesis". Carcinogenesis. 20 (2): 311–6. doi: 10.1093/carcin/20.2.311 . PMID   10069470.
• Wilson MD, Riemer C, Martindale DW, et al. (2001). "Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5". Nucleic Acids Res. 29 (6): 1352–65. doi:10.1093/nar/29.6.1352. PMC   29746 . PMID   11239002.
• Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology". Science. 300 (5620): 767–72. Bibcode:2003Sci...300..767S. doi:10.1126/science.1083423. PMC   2882961 . PMID   12690205.
• Di Y, Li J, Zhang Y, et al. (2004). "HCC-associated protein HCAP1, a variant of GEMIN4, interacts with zinc-finger proteins". J. Biochem. 133 (6): 713–8. doi:10.1093/jb/mvg091. PMID   12869526.
• Obuse C, Yang H, Nozaki N, et al. (2004). "Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localized with the centromeric region in interphase". Genes Cells. 9 (2): 105–20. doi: 10.1111/j.1365-2443.2004.00705.x . PMID   15009096. S2CID   21813024.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi: 10.1073/pnas.0404720101 . PMC   514446 . PMID   15302935.
• Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi: 10.1074/mcp.M400085-MCP200 . PMID   15345747.
• Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID   16964243. S2CID   14294292.
• Szafranski K, Schindler S, Taudien S, et al. (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns". Genome Biology. 8 (8): R154. doi: 10.1186/gb-2007-8-8-r154 . PMC   2374985 . PMID   17672918.