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UniProtKB/Swiss-Prot entry Q9UQ35


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SRRM2_HUMAN
Primary accession number Q9UQ35
Secondary accession numbers A6NKB9 O15038 O94803 Q6NSL3 Q6PIM3 Q6PK40 Q8IW17 Q96GY7 Q9P0G1 Q9UHA8 Q9UQ36 Q9UQ37 Q9UQ38 Q9UQ40
Integrated into Swiss-Prot on September 5, 2006
Sequence was last modified on March 6, 2007 (Sequence version 2)
Annotations were last modified on    July 1, 2008 (Entry version 50)
Name and origin of the protein
Protein name Serine/arginine repetitive matrix protein 2
Synonyms Serine/arginine-rich splicing factor-related nuclear matrix protein of 300 kDa
Ser/Arg-related nuclear matrix protein
SR-related nuclear matrix protein of 300 kDa
Splicing coactivator subunit SRm300
300 kDa nuclear matrix antigen
Gene name
Name: SRRM2
Synonyms: KIAA0324, SRL300, SRM300
ORFNames: HSPC075
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
TISSUE=Cervix carcinoma;
DOI=10.1016/S0167-4781(00)00065-8; PubMed=11004489 [NCBI, ExPASy, EBI, Israel, Japan]
Sawada Y., Miura Y., Umeki K., Tamaoki T., Fujinaga K., Ohtaki S.;
"Cloning and characterization of a novel RNA-binding protein SRL300 with RS domains.";
Biochim. Biophys. Acta 1492:191-195(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 1223-1226 AND 2587-2597, AND FUNCTION.
DOI=10.1017/S1355838200991982; PubMed=10668804 [NCBI, ExPASy, EBI, Israel, Japan]
Blencowe B.J., Bauren G., Eldridge A.G., Issner R., Nickerson J.A., Rosonina E., Sharp P.A.;
"The SRm160/300 splicing coactivator subunits.";
RNA 6:111-120(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-804.
TISSUE=Brain;
DOI=10.1093/dnares/4.2.141; PubMed=9205841 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"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. 4:141-150(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03187; PubMed=15616553 [NCBI, ExPASy, EBI, Israel, Japan]
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1018 AND 2555-2752.
TISSUE=Blood, Embryonic testis carcinoma, Placenta, Retinoblastoma, and Rhabdomyosarcoma;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 1-11; 44-51; 116-130; 137-155; 357-401; 1001-1013; 1041-1058; 1101-1111; 1119-1128; 1138-1158; 1224-1277; 1316-1352; 1394-1412; 1539-1556; 2104-2113; 2120-2129; 2132-2163; 2181-2221; 2232-2392; 2431-2460 AND 2690-2698, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
Submitted (JUL-2007) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-185.
TISSUE=Umbilical cord blood;
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
"Human partial CDS from cd34+ stem cells.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[9]
IDENTIFICATION IN A PRE-MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRP70; SNRPA1 AND SRRM1.
PubMed=9531537 [NCBI, ExPASy, EBI, Israel, Japan]
Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.;
"A coactivator of pre-mRNA splicing.";
Genes Dev. 12:996-1009(1998).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
DOI=10.1017/S1355838202021088; PubMed=11991638 [NCBI, ExPASy, EBI, Israel, Japan]
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.";
RNA 8:426-439(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-250; THR-252; THR-274; SER-297; SER-351; SER-353; THR-367; SER-424; SER-820; SER-857; THR-866; SER-901; THR-903; SER-908; SER-914; SER-988; SER-994; THR-1003; THR-1043; SER-1069; SER-1073; SER-1079; SER-1083; SER-1103; SER-1124; SER-1132; SER-1179; SER-1214; SER-1219; SER-1320; SER-1326; SER-1397; SER-1404; SER-1421; SER-1423; SER-1441; SER-1443; SER-1444; THR-1453; SER-1483; SER-1499; SER-1501; SER-1502; THR-1511; SER-1517; SER-1519; SER-1522; SER-1559; SER-1579; SER-1581; SER-1582; SER-1600; SER-1601; SER-1618; SER-1621; THR-1880; THR-1962; SER-2044; SER-2046; SER-2071; THR-2092; THR-2104; SER-2272; SER-2335; SER-2382; SER-2398; SER-2407; THR-2409; SER-2426; SER-2449; SER-2581; SER-2692; SER-2694 AND SER-2714, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-924; SER-1382; SER-1387; SER-1497; SER-1501; SER-1502; SER-1600; SER-1601; SER-1616; SER-1620; SER-1621 AND SER-2100, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2675; SER-2677; SER-2684; SER-2688; SER-2702; SER-2706; THR-2738 AND SER-2740, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-367; SER-778; SER-780; SER-783; SER-871; SER-876; SER-952; SER-954; SER-1072; SER-1073; SER-1878; THR-1880; SER-2032; THR-2034; SER-2044; SER-2046; SER-2272; THR-2289; THR-2291; THR-2316; SER-2382; SER-2449; SER-2692 AND SER-2694, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1124; SER-1188; SER-1329; SER-2032; SER-2044; SER-2067; SER-2272; SER-2692 AND SER-2694, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1531 AND SER-1975, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-323; SER-377; THR-383; THR-384; SER-387; SER-395; SER-398; THR-400; SER-415; SER-418; THR-428; SER-435; SER-440; SER-755; SER-759; SER-761; SER-763; SER-764; SER-774; SER-778; SER-780; SER-783; SER-883; THR-885; SER-890; SER-894; SER-895; SER-950; SER-952; SER-954; THR-983; SER-988; SER-994; TYR-996; THR-1063; SER-1069; THR-1071; SER-1072; SER-1073; SER-1099; SER-1101; SER-1103; THR-1106; SER-1110; SER-1112; SER-1124; SER-1129; THR-1205; THR-1208; SER-1218; SER-1219; SER-1320; SER-1329; SER-1397; SER-1398; SER-1403; SER-1404; THR-1413; SER-1415; THR-1492; SER-1497; SER-1499; SER-1501; SER-1502; THR-1571; SER-1579; SER-1581; SER-1582; SER-1592; SER-1596; SER-1598; SER-1600; SER-1601; SER-1616; SER-1618; SER-1620; SER-1621; SER-1636; SER-1638; SER-1640; SER-1641; SER-1657; SER-1658; SER-1682; THR-1684; SER-1690; SER-1691; SER-1693; SER-1694; SER-1876; SER-1878; THR-1880; SER-1958; SER-1960; THR-1962; SER-2018; SER-2020; THR-2022; SER-2030; SER-2032; THR-2034; SER-2042; SER-2044; SER-2046; SER-2067; THR-2069; SER-2071; SER-2272; SER-2407 AND THR-2409, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-387; SER-398; SER-2436 AND SER-2453, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-875; SER-954; THR-983; SER-988; THR-1003; SER-1014; THR-1043; THR-1106; SER-1112; SER-1320; SER-1419; SER-1878; THR-1880; SER-2046; SER-2100; SER-2132; THR-2397; SER-2398; SER-2581 AND SER-2694, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-297; SER-322; SER-323; SER-1404; THR-1413; SER-2272; SER-2398; SER-2407; THR-2409; SER-2688 AND SER-2694, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
Comments
  • FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes. May be involved in pre-mRNA processing events. Binds to RNA.
  • SUBUNIT: Component of the active spliceosome. Found in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
  • INTERACTION:
    Q16611:BAK1; NbExp=1; IntAct=EBI-1050142, EBI-519866;
    Q15287:RNPS1; NbExp=1; IntAct=EBI-1050142, EBI-395959;
    P31946:YWHAB; NbExp=1; IntAct=EBI-1050142, EBI-359815;
    P61981:YWHAG; NbExp=1; IntAct=EBI-1050142, EBI-359832;
  • SUBCELLULAR LOCATION: Nucleus speckle.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9UQ35-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9UQ35-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_020187.
    Name3
    Isoform IDQ9UQ35-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_020184, VSP_020185, VSP_020186.
  • TISSUE SPECIFICITY: Expressed in liver, placenta, and white blood cells.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
  • SIMILARITY: Belongs to the CWC21 family.
  • SEQUENCE CAUTION:
    • Sequence=AAF21439.1; Type=Frameshift; Positions=Several;
    • Sequence=AAF28898.1; Type=Frameshift; Positions=167, 175, 179;
    • Sequence=AAH70050.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB015644; BAA34957.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB016087; BAA83713.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB016089; BAA83715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB016090; BAA83716.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB016091; BAA83717.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB016092; BAA83718.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF201422; AAF21439.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB002322; BAA20782.3; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC092117; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CH471112; EAW85478.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007752; AAH07752.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009062; AAH09062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032416; AAH32416.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC041155; AAH41155.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070050; AAH70050.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF161338; AAF28898.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057417.3; -.
UniGene Hs.433343
3D structure databases
ModBase Q9UQ35.
Protein-protein interaction databases
IntAct Q9UQ35; -.
PTM databases
PhosphoSite Q9UQ35; -.
Organism-specific databases
HGNC HGNC:16639; SRRM2.
GeneLynx SRRM2; Homo sapiens.
GenAtlas SRRM2.
MIM 606032; gene. [NCBI / EBI]
PharmGKB PA38178; -.
GeneCards Q9UQ35.
HUGE KIAA0324.
Gene expression databases
ArrayExpress Q9UQ35; -.
GermOnline ENSG00000167978; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR013170; mRNA_splic_Cwf21.
Graphical view of domain structure.
Pfam PF08312; cwf21; 1.
Pfam graphical view of domain structure.
BLOCKS Q9UQ35.
Genome annotation databases
Ensembl ENSG00000167978; Homo sapiens. [Contig view]
GeneID 23524; -.
KEGG hsa:23524; -.
NMPDR fig|9606.3.peg.11582; -.
Phylogenomic databases
HOVERGEN Q9UQ35; -.
Other
SOURCE SRRM2; Homo sapiens.
ProtoNet Q9UQ35.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; RNA-binding; Spliceosome.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2752  2752     Serine/arginine repetitive matrix protein 2. PRO_0000248154
REGION   197    259  63     Sufficient for RNA-binding. 
COILED   60     92  33     Potential. 
COMPBIAS   177   2731  2555     Ser-rich. 
COMPBIAS   186    246  61     Lys-rich. 
COMPBIAS   350    447  98     Pro-rich. 
COMPBIAS   462    816  355     Arg-rich. 
COMPBIAS   1666   2089  424     Arg-rich. 
COMPBIAS   2182   2378  197     Ala-rich. 
COMPBIAS   2673   2750  78     Arg-rich. 
MOD_RES   1      1        N-acetylmethionine. 
MOD_RES   142    142        Phosphoserine. 
MOD_RES   250    250        Phosphoserine. 
MOD_RES   252    252        Phosphothreonine. 
MOD_RES   274    274        Phosphothreonine. 
MOD_RES   295    295        Phosphoserine. 
MOD_RES   297    297        Phosphoserine. 
MOD_RES   322    322        Phosphoserine. 
MOD_RES   323    323        Phosphoserine. 
MOD_RES   351    351        Phosphoserine. 
MOD_RES   353    353        Phosphoserine. 
MOD_RES   367    367        Phosphothreonine. 
MOD_RES   377    377        Phosphoserine. 
MOD_RES   383    383        Phosphothreonine. 
MOD_RES   384    384        Phosphothreonine. 
MOD_RES   387    387        Phosphoserine. 
MOD_RES   395    395        Phosphoserine. 
MOD_RES   398    398        Phosphoserine. 
MOD_RES   400    400        Phosphothreonine. 
MOD_RES   404    404        Phosphoserine (By similarity). 
MOD_RES   408    408        Phosphoserine (By similarity). 
MOD_RES   415    415        Phosphoserine. 
MOD_RES   418    418        Phosphoserine. 
MOD_RES   424    424        Phosphoserine. 
MOD_RES   428    428        Phosphothreonine. 
MOD_RES   435    435        Phosphoserine. 
MOD_RES   436    436        Phosphoserine (By similarity). 
MOD_RES   437    437        Phosphoserine (By similarity). 
MOD_RES   440    440        Phosphoserine. 
MOD_RES   755    755        Phosphoserine. 
MOD_RES   759    759        Phosphoserine. 
MOD_RES   761    761        Phosphoserine. 
MOD_RES   763    763        Phosphoserine. 
MOD_RES   764    764        Phosphoserine. 
MOD_RES   774    774        Phosphoserine. 
MOD_RES   778    778        Phosphoserine. 
MOD_RES   780    780        Phosphoserine. 
MOD_RES   783    783        Phosphoserine. 
MOD_RES   820    820        Phosphoserine. 
MOD_RES   846    846        Phosphoserine (By similarity). 
MOD_RES   848    848        Phosphothreonine (By similarity). 
MOD_RES   857    857        Phosphoserine. 
MOD_RES   866    866        Phosphothreonine. 
MOD_RES   871    871        Phosphoserine. 
MOD_RES   875    875        Phosphoserine. 
MOD_RES   876    876        Phosphoserine. 
MOD_RES   883    883        Phosphoserine. 
MOD_RES   885    885        Phosphothreonine. 
MOD_RES   890    890        Phosphoserine. 
MOD_RES   894    894        Phosphoserine. 
MOD_RES   895    895        Phosphoserine. 
MOD_RES   901    901        Phosphoserine. 
MOD_RES   903    903        Phosphothreonine. 
MOD_RES   908    908        Phosphoserine. 
MOD_RES   914    914        Phosphoserine. 
MOD_RES   924    924        Phosphoserine.