SRSF9_HUMAN
ID SRSF9_HUMAN Reviewed; 221 AA.
AC Q13242; Q52LD1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Serine/arginine-rich splicing factor 9;
DE AltName: Full=Pre-mRNA-splicing factor SRp30C;
DE AltName: Full=Splicing factor, arginine/serine-rich 9;
GN Name=SRSF9; Synonyms=SFRS9, SRP30C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Colon;
RX PubMed=7556075; DOI=10.1002/j.1460-2075.1995.tb00108.x;
RA Screaton G.R., Caceres J.F., Mayeda A., Bell M.V., Plebanski M.,
RA Jackson D.G., Bell J.I., Krainer A.R.;
RT "Identification and characterization of three members of the human SR
RT family of pre-mRNA splicing factors.";
RL EMBO J. 14:4336-4349(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
RA Lathrop M., Cox R.D., Bell G.I.;
RT "Transcription map of the 5cM region surrounding the hepatocyte nuclear
RT factor-1a/MODY3 gene on chromosome 12.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH DUSP11.
RX PubMed=9685386; DOI=10.1074/jbc.273.32.20347;
RA Yuan Y., Li D.-M., Sun H.;
RT "PIR1, a novel phosphatase that exhibits high affinity to RNA
RT ribonucleoprotein complexes.";
RL J. Biol. Chem. 273:20347-20353(1998).
RN [6]
RP INTERACTION WITH SAFB/SAFB1.
RX PubMed=9671816; DOI=10.1093/nar/26.15.3542;
RA Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L.,
RA Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.;
RT "SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements.";
RL Nucleic Acids Res. 26:3542-3549(1998).
RN [7]
RP INTERACTION WITH C1QBP.
RX PubMed=10022843; DOI=10.1093/emboj/18.4.1014;
RA Petersen-Mahrt S.K., Estmer C., Ohrmalm C., Matthews D.A., Russell W.C.,
RA Akusjarvi G.;
RT "The splicing factor-associated protein, p32, regulates RNA splicing by
RT inhibiting ASF/SF2 RNA binding and phosphorylation.";
RL EMBO J. 18:1014-1024(1999).
RN [8]
RP FUNCTION, INTERACTION WITH NOL3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10196175; DOI=10.1074/jbc.274.16.10951;
RA Stoss O., Schwaiger F.-W., Cooper T.A., Stamm S.;
RT "Alternative splicing determines the intracellular localization of the
RT novel nuclear protein Nop30 and its interaction with the splicing factor
RT SRp30c.";
RL J. Biol. Chem. 274:10951-10962(1999).
RN [9]
RP INTERACTION WITH SAFB/SAFB1, AND SUBCELLULAR LOCATION.
RX PubMed=11694584; DOI=10.1091/mbc.12.11.3502;
RA Denegri M., Chiodi I., Corioni M., Cobianchi F., Riva S., Biamonti G.;
RT "Stress-induced nuclear bodies are sites of accumulation of pre-mRNA
RT processing factors.";
RL Mol. Biol. Cell 12:3502-3514(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH TRA2B.
RX PubMed=11875052; DOI=10.1093/hmg/11.5.577;
RA Young P.J., DiDonato C.J., Hu D., Kothary R., Androphy E.J., Lorson C.L.;
RT "SRp30c-dependent stimulation of survival motor neuron (SMN) exon 7
RT inclusion is facilitated by a direct interaction with hTra2 beta 1.";
RL Hum. Mol. Genet. 11:577-587(2002).
RN [11]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12024014; DOI=10.1128/mcb.22.12.4001-4010.2002;
RA Simard M.J., Chabot B.;
RT "SRp30c is a repressor of 3' splice site utilization.";
RL Mol. Cell. Biol. 22:4001-4010(2002).
RN [12]
RP FUNCTION, INTERACTION WITH NSEP1, AND SUBCELLULAR LOCATION.
RX PubMed=12604611; DOI=10.1074/jbc.m212518200;
RA Raffetseder U., Frye B., Rauen T., Juerchott K., Royer H.-D., Jansen P.L.,
RA Mertens P.R.;
RT "Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear
RT YB-1 shuttling and alternative splice site selection.";
RL J. Biol. Chem. 278:18241-18248(2003).
RN [13]
RP FUNCTION.
RX PubMed=15009090; DOI=10.1111/j.1356-9597.2004.00709.x;
RA Kondo S., Yamamoto N., Murakami T., Okumura M., Mayeda A., Imaizumi K.;
RT "Tra2 beta, SF2/ASF and SRp30c modulate the function of an exonic splicing
RT enhancer in exon 10 of tau pre-mRNA.";
RL Genes Cells 9:121-130(2004).
RN [14]
RP FUNCTION.
RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x;
RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is
RT regulated by an intricate interplay of cis elements and trans factors.";
RL J. Neurochem. 88:1078-1090(2004).
RN [15]
RP FUNCTION, AND INTERACTION WITH SRSF6 AND TRA2B.
RX PubMed=15695522; DOI=10.1074/jbc.m413846200;
RA Wang Y., Wang J., Gao L., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exons 2 and 10, which are misregulated in neurodegenerative diseases,
RT are partly regulated by silencers which bind a SRp30c SRp55 complex that
RT either recruits or antagonizes htra2beta1.";
RL J. Biol. Chem. 280:14230-14239(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; TYR-192; SER-195;
RP SER-211 AND SER-216, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP INTERACTION WITH HABP4.
RX PubMed=19523114; DOI=10.1111/j.1742-4658.2009.07092.x;
RA Bressan G.C., Quaresma A.J., Moraes E.C., Manfiolli A.O., Passos D.O.,
RA Gomes M.D., Kobarg J.;
RT "Functional association of human Ki-1/57 with pre-mRNA splicing events.";
RL FEBS J. 276:3770-3783(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-211 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-193; SER-204;
RP SER-208; SER-211 AND SER-216, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND TYR-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Plays a role in constitutive splicing and can modulate the
CC selection of alternative splice sites. Represses the splicing of
CC MAPT/Tau exon 10. {ECO:0000269|PubMed:10196175,
CC ECO:0000269|PubMed:11875052, ECO:0000269|PubMed:12024014,
CC ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:15009090,
CC ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:15695522,
CC ECO:0000269|PubMed:7556075}.
CC -!- SUBUNIT: Interacts with KHDRBS3 (By similarity). Interacts with HABP4
CC (PubMed:19523114). Interacts with NOL3/ARC/NOP30 (PubMed:10196175).
CC Interacts with NSEP1/YB-1/YB1 (PubMed:12604611). Interacts with
CC SAFB/SAFB1 (PubMed:9671816, PubMed:11694584). Interacts with
CC SRSF6/SFRS6 (PubMed:15695522). Interacts with TRA2B/SFRS10
CC (PubMed:11875052, PubMed:15695522). Interacts with C1QBP
CC (PubMed:10022843). May also interact with DUSP11/PIR1(PubMed:11694584).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9D0B0,
CC ECO:0000269|PubMed:10022843, ECO:0000269|PubMed:10196175,
CC ECO:0000269|PubMed:11694584, ECO:0000269|PubMed:11875052,
CC ECO:0000269|PubMed:12604611, ECO:0000269|PubMed:15695522,
CC ECO:0000269|PubMed:19523114, ECO:0000269|PubMed:9671816,
CC ECO:0000269|PubMed:9685386}.
CC -!- INTERACTION:
CC Q13242; Q5JVS0: HABP4; NbExp=2; IntAct=EBI-2949710, EBI-523625;
CC Q13242; P38159: RBMX; NbExp=3; IntAct=EBI-2949710, EBI-743526;
CC Q13242; Q15287: RNPS1; NbExp=3; IntAct=EBI-2949710, EBI-395959;
CC Q13242; P62995: TRA2B; NbExp=3; IntAct=EBI-2949710, EBI-725485;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10196175,
CC ECO:0000269|PubMed:11694584, ECO:0000269|PubMed:12024014,
CC ECO:0000269|PubMed:12604611}. Note=Cellular stresses such as heat shock
CC may induce localization to discrete nuclear bodies termed SAM68 nuclear
CC bodies (SNBs), HAP bodies, or stress bodies. Numerous splicing factors
CC including SRSF1/SFRS1/SF2, SRSF7/SFRS7, SAFB and KHDRBS1/SAM68
CC accumulate at these structures, which may participate in the post-
CC transcriptional regulation of mRNAs in stressed cells.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the heart, kidney,
CC pancreas and placenta, and at lower levels in the brain, liver, lung
CC and skeletal muscle. {ECO:0000269|PubMed:10196175}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; U30825; AAA93069.1; -; mRNA.
DR EMBL; U87279; AAD00626.1; -; Genomic_DNA.
DR EMBL; U87277; AAD00626.1; JOINED; Genomic_DNA.
DR EMBL; U87278; AAD00626.1; JOINED; Genomic_DNA.
DR EMBL; AL021546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093971; AAH93971.1; -; mRNA.
DR EMBL; BC093973; AAH93973.1; -; mRNA.
DR CCDS; CCDS9199.1; -.
DR PIR; S59075; S59075.
DR RefSeq; NP_003760.1; NM_003769.2.
DR AlphaFoldDB; Q13242; -.
DR SMR; Q13242; -.
DR BioGRID; 114231; 170.
DR CORUM; Q13242; -.
DR DIP; DIP-40741N; -.
DR IntAct; Q13242; 45.
DR MINT; Q13242; -.
DR STRING; 9606.ENSP00000229390; -.
DR ChEMBL; CHEMBL4295813; -.
DR GlyGen; Q13242; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13242; -.
DR PhosphoSitePlus; Q13242; -.
DR SwissPalm; Q13242; -.
DR BioMuta; SRSF9; -.
DR DMDM; 3929377; -.
DR CPTAC; CPTAC-441; -.
DR CPTAC; CPTAC-442; -.
DR EPD; Q13242; -.
DR jPOST; Q13242; -.
DR MassIVE; Q13242; -.
DR MaxQB; Q13242; -.
DR PaxDb; Q13242; -.
DR PeptideAtlas; Q13242; -.
DR PRIDE; Q13242; -.
DR ProteomicsDB; 59246; -.
DR TopDownProteomics; Q13242; -.
DR Antibodypedia; 31480; 268 antibodies from 28 providers.
DR DNASU; 8683; -.
DR Ensembl; ENST00000229390.8; ENSP00000229390.3; ENSG00000111786.9.
DR GeneID; 8683; -.
DR KEGG; hsa:8683; -.
DR MANE-Select; ENST00000229390.8; ENSP00000229390.3; NM_003769.3; NP_003760.1.
DR UCSC; uc001tyi.4; human.
DR CTD; 8683; -.
DR DisGeNET; 8683; -.
DR GeneCards; SRSF9; -.
DR HGNC; HGNC:10791; SRSF9.
DR HPA; ENSG00000111786; Low tissue specificity.
DR MIM; 601943; gene.
DR neXtProt; NX_Q13242; -.
DR OpenTargets; ENSG00000111786; -.
DR PharmGKB; PA35707; -.
DR VEuPathDB; HostDB:ENSG00000111786; -.
DR eggNOG; KOG0105; Eukaryota.
DR GeneTree; ENSGT00940000156839; -.
DR HOGENOM; CLU_012062_34_0_1; -.
DR InParanoid; Q13242; -.
DR OMA; SYIRVCP; -.
DR OrthoDB; 1315388at2759; -.
DR PhylomeDB; Q13242; -.
DR TreeFam; TF106261; -.
DR PathwayCommons; Q13242; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q13242; -.
DR BioGRID-ORCS; 8683; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; SRSF9; human.
DR GeneWiki; SFRS9; -.
DR GenomeRNAi; 8683; -.
DR Pharos; Q13242; Tbio.
DR PRO; PR:Q13242; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q13242; protein.
DR Bgee; ENSG00000111786; Expressed in endometrium epithelium and 211 other tissues.
DR ExpressionAtlas; Q13242; baseline and differential.
DR Genevisible; Q13242; HS.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0006376; P:mRNA splice site selection; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR CDD; cd12768; RRM2_SRSF9; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034995; SRSF9_RRM2.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Ubl conjugation.
FT CHAIN 1..221
FT /note="Serine/arginine-rich splicing factor 9"
FT /id="PRO_0000081935"
FT DOMAIN 14..89
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 111..187
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 188..200
FT /note="Interaction with SAFB1"
FT REGION 189..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 192
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 214
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 221 AA; 25542 MW; 1EE7BD8601CD80C0 CRC64;
MSGWADERGG EGDGRIYVGN LPTDVREKDL EDLFYKYGRI REIELKNRHG LVPFAFVRFE
DPRDAEDAIY GRNGYDYGQC RLRVEFPRTY GGRGGWPRGG RNGPPTRRSD FRVLVSGLPP
SGSWQDLKDH MREAGDVCYA DVQKDGVGMV EYLRKEDMEY ALRKLDDTKF RSHEGETSYI
RVYPERSTSY GYSRSRSGSR GRDSPYQSRG SPHYFSPFRP Y
