SRRM2

Protein-coding gene in the species Homo sapiens
SRRM2
Identifiers
AliasesSRRM2, 300-KD, CWF21, Cwc21, SRL300, SRm300, HSPC075, serine/arginine repetitive matrix 2
External IDsOMIM: 606032; MGI: 1923206; HomoloGene: 130678; GeneCards: SRRM2; OMA:SRRM2 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for SRRM2
Genomic location for SRRM2
Band16p13.3Start2,752,626 bp[1]
End2,772,538 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for SRRM2
Genomic location for SRRM2
Band17|17 A3.3Start24,009,506 bp[2]
End24,043,715 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right uterine tube

  • right hemisphere of cerebellum

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • body of uterus

  • canal of the cervix

  • tibial nerve

  • epithelium of colon

  • fundus

  • body of stomach
Top expressed in
  • Rostral migratory stream

  • otolith organ

  • utricle

  • genital tubercle

  • tail of embryo

  • ventromedial nucleus

  • neural layer of retina

  • mammillary body

  • cerebellar cortex

  • inferior colliculus
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • C2H2 zinc finger domain binding
  • protein N-terminus binding
  • RNA binding
Cellular component
  • Cajal body
  • nuclear speck
  • catalytic step 2 spliceosome
  • spliceosomal complex
  • nucleus
  • nucleoplasm
  • U2-type catalytic step 2 spliceosome
  • U2-type precatalytic spliceosome
Biological process
  • mRNA processing
  • RNA splicing
  • mRNA splicing, via spliceosome
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23524

75956

Ensembl

ENSG00000167978

ENSMUSG00000039218

UniProt

Q9UQ35

Q8BTI8

RefSeq (mRNA)

NM_016333

NM_175229
NM_001368687

RefSeq (protein)

NP_057417

NP_780438
NP_001355616

Location (UCSC)Chr 16: 2.75 – 2.77 MbChr 17: 24.01 – 24.04 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/arginine repetitive matrix protein 2 is a protein that in humans is encoded by the SRRM2 gene.[5][6][7]

Interactions

SRRM2 has been shown to interact with Pinin.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167978 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039218 – 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. ^ 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.
  6. ^ 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.
  7. ^ "Entrez Gene: SRRM2 serine/arginine repetitive matrix 2".
  8. ^ 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. Bibcode:2004PNAS..10112130B. 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. S2CID 2371325.
  • 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. Bibcode:2006PNAS..103.5391N. 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. S2CID 14294292.
  • 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. S2CID 7827573.
  • 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.


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