SRRM2

Serine/arginine repetitive matrix 2
Identifiers
Symbols	SRRM2 ; 300-KD; CWF21; Cwc21; HSPC075; SRL300; SRm300
External IDs	OMIM: 606032 MGI: 1923206 HomoloGene: 130678 GeneCards: SRRM2 Gene
Gene ontology Molecular function • poly(A) RNA binding • protein N-terminus binding • C2H2 zinc finger domain binding Cellular component • nucleoplasm • Cajal body • nuclear speck • catalytic step 2 spliceosome Biological process • mRNA splicing, via spliceosome Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23524	75956
Ensembl	ENSG00000167978	ENSMUSG00000039218
UniProt	Q9UQ35	Q8BTI8
RefSeq (mRNA)	NM_016333	NM_175229
RefSeq (protein)	NP_057417	NP_780438
Location (UCSC)	Chr 16: 2.75 – 2.77 Mb	Chr 17: 23.8 – 23.82 Mb
PubMed search

Serine/arginine repetitive matrix protein 2 is a protein that in humans is encoded by the SRRM2 gene.^[1][2][3]

Interactions

SRRM2 has been shown to interact with Pinin.^[4]

References

1. Blencowe BJ, Baurén G, Eldridge AG, Issner R, Nickerson JA, Rosonina E, Sharp PA (Feb 2000). "The SRm160/300 splicing coactivator subunits". RNA 6 (1): 111–20. doi:10.1017/S1355838200991982. PMC 1369899. PMID 10668804.
2. Sawada Y, Miura Y, Umeki K, Tamaoki T, Fujinaga K, Ohtaki S (Sep 2000). "Cloning and characterization of a novel RNA-binding protein SRL300 with RS domains". Biochim. Biophys. Acta 1492 (1): 191–5. doi:10.1016/s0167-4781(00)00065-8. PMID 11004489.
3. "Entrez Gene: SRRM2 serine/arginine repetitive matrix 2".
4. Zimowska G, Shi J, Munguba G, Jackson MR, Alpatov R, Simmons MN, Shi Y, Sugrue SP (Nov 2003). "Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal epithelial cells". Invest. Ophthalmol. Vis. Sci. 44 (11): 4715–23. doi:10.1167/iovs.03-0240. PMID 14578391.

Further reading

• Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841.
• Blencowe BJ, Issner R, Nickerson JA, Sharp PA (1998). "A coactivator of pre-mRNA splicing". Genes Dev. 12 (7): 996–1009. doi:10.1101/gad.12.7.996. PMC 316672. PMID 9531537.
• McGarvey T, Rosonina E, McCracken S, Li Q, Arnaout R, Mientjes E, Nickerson JA, Awrey D, Greenblatt J, Grosveld G, Blencowe BJ (2000). "The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes". J. Cell Biol. 150 (2): 309–20. doi:10.1083/jcb.150.2.309. PMC 2180225. PMID 10908574.
• Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
• Zimowska G, Shi J, Munguba G, Jackson MR, Alpatov R, Simmons MN, Shi Y, Sugrue SP (2003). "Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal epithelial cells". Invest. Ophthalmol. Vis. Sci. 44 (11): 4715–23. doi:10.1167/iovs.03-0240. PMID 14578391.
• Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (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.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (2004). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell Proteomics 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
• Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell Proteomics 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
• Kim JE, Tannenbaum SR, White FM (2005). "Global phosphoproteome of HT-29 human colon adenocarcinoma cells". J. Proteome Res. 4 (4): 1339–46. doi:10.1021/pr050048h. PMID 16083285.
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (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.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.