Serrate RNA effector molecule homolog

Serrate, RNA effector molecule
Identifiers
Symbols	SRRT ; ARS2; ASR2; serrate
External IDs	OMIM: 614469 MGI: 1933527 HomoloGene: 9298 GeneCards: SRRT Gene
Gene ontology Molecular function • DNA binding • protein binding • poly(A) RNA binding Cellular component • nucleus • nucleoplasm • cytoplasm Biological process • transcription, DNA-templated • regulation of transcription, DNA-templated • cell proliferation • primary miRNA processing • response to arsenic-containing substance • positive regulation of neurogenesis • neuronal stem cell maintenance Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	51593	83701
Ensembl	ENSG00000087087	ENSMUSG00000037364
UniProt	Q9BXP5	Q99MR6
RefSeq (mRNA)	NM_001128852	NM_001109909
RefSeq (protein)	NP_001122324	NP_001103379
Location (UCSC)	Chr 7: 100.88 – 100.89 Mb	Chr 5: 137.3 – 137.31 Mb
PubMed search

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.^[1]

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 the SOX2 promoter and positively regulating its transcription.

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

References

1. "Entrez Gene: ARS2 ARS2 protein".

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. 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.
• 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. 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.
• 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.