ID SRSF6_HUMAN Reviewed; 344 AA. AC Q13247; B7Z6J3; E1P5W6; Q13244; Q13245; Q96J06; Q9UJB8; Q9Y3N7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2002, sequence version 2. DT 27-NOV-2024, entry version 233. DE RecName: Full=Serine/arginine-rich splicing factor 6; DE AltName: Full=Pre-mRNA-splicing factor SRP55; DE AltName: Full=Splicing factor, arginine/serine-rich 6; GN Name=SRSF6; Synonyms=SFRS6, SRP55; 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] (ISOFORMS SRP55-1; SRP55-2 AND SRP55-3). 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 [LARGE SCALE MRNA] (ISOFORM SRP55-2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP55-1). RC TISSUE=Placenta; 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 [6] RP PROTEIN SEQUENCE OF 21-27 AND 47-55. RX PubMed=1577277; DOI=10.1101/gad.6.5.837; RA Zahler A.M., Lane W.S., Stolk J.A., Roth M.B.; RT "SR proteins: a conserved family of pre-mRNA splicing factors."; RL Genes Dev. 6:837-847(1992). RN [7] RP INTERACTION WITH SREK1. RX PubMed=10757789; DOI=10.1128/mcb.20.9.3049-3057.2000; RA Barnard D.C., Patton J.G.; RT "Identification and characterization of a novel serine-arginine-rich RT splicing regulatory protein."; RL Mol. Cell. Biol. 20:3049-3057(2000). RN [8] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=12549914; DOI=10.1021/bi026753a; RA Tran Q., Roesser J.R.; RT "SRp55 is a regulator of calcitonin/CGRP alternative RNA splicing."; RL Biochemistry 42:951-957(2003). RN [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-314 AND SER-316, AND RP IDENTIFICATION BY 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299 AND SER-303, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-314 AND SER-316, 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 [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-84; SER-303; SER-314 RP AND SER-316, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [16] {ECO:0000305} RP SUBCELLULAR LOCATION, INTERACTION WITH DYRK1A, FUNCTION, PHOSPHORYLATION AT RP SER-303, AND MUTAGENESIS OF SER-280; SER-303 AND SER-316. RX PubMed=22767602; DOI=10.1074/jbc.m112.355412; RA Yin X., Jin N., Gu J., Shi J., Zhou J., Gong C.X., Iqbal K., RA Grundke-Iqbal I., Liu F.; RT "Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A) RT modulates serine/arginine-rich protein 55 (SRp55)-promoted Tau exon 10 RT inclusion."; RL J. Biol. Chem. 287:30497-30506(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-299 AND SER-303, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY RP 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 [19] RP FUNCTION, AND RNA-BINDING. RX PubMed=24440982; DOI=10.1038/nsmb.2756; RA Jensen M.A., Wilkinson J.E., Krainer A.R.; RT "Splicing factor SRSF6 promotes hyperplasia of sensitized skin."; RL Nat. Struct. Mol. Biol. 21:189-197(2014). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, 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). RN [21] RP VARIANT [LARGE SCALE ANALYSIS] GLN-145. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role in constitutive splicing and modulates the CC selection of alternative splice sites. Plays a role in the alternative CC splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre- CC mRNA and promotes the expression of alternatively spliced TNC. Plays a CC role in wound healing and in the regulation of keratinocyte CC differentiation and proliferation via its role in alternative splicing. CC {ECO:0000269|PubMed:12549914, ECO:0000269|PubMed:15009664, CC ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:24440982}. CC -!- SUBUNIT: Binds SREK1/SFRS12. Interacts with DYRK1A. CC {ECO:0000269|PubMed:10757789, ECO:0000269|PubMed:22767602}. CC -!- INTERACTION: CC Q13247; Q9NQ29-3: LUC7L; NbExp=3; IntAct=EBI-745230, EBI-6654742; CC Q13247; Q9Y383: LUC7L2; NbExp=7; IntAct=EBI-745230, EBI-352851; CC Q13247; Q15287: RNPS1; NbExp=3; IntAct=EBI-745230, EBI-395959; CC Q13247; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-745230, EBI-539478; CC Q13247; Q08170: SRSF4; NbExp=4; IntAct=EBI-745230, EBI-722621; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12549914, CC ECO:0000269|PubMed:22767602}. Nucleus speckle CC {ECO:0000269|PubMed:22767602}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=SRP55-1; CC IsoId=Q13247-1; Sequence=Displayed; CC Name=SRP55-2; CC IsoId=Q13247-2; Sequence=VSP_005869, VSP_005870; CC Name=SRP55-3; CC IsoId=Q13247-3; Sequence=VSP_005871; CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain. CC Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by CC DYRK1A modulates alternative splice site selection and inhibits the CC expression of MAPT/Tau exon 10. {ECO:0000269|PubMed:22767602}. CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U30883; AAA93073.1; -; mRNA. DR EMBL; U30828; AAA93071.1; -; mRNA. DR EMBL; U30829; AAA93072.1; -; mRNA. DR EMBL; AK300411; BAH13279.1; -; mRNA. DR EMBL; AL031681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75964.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75967.1; -; Genomic_DNA. DR EMBL; BC006832; AAH06832.1; -; mRNA. DR CCDS; CCDS13318.1; -. [Q13247-1] DR PIR; S59043; S59043. DR RefSeq; NP_006266.2; NM_006275.5. [Q13247-1] DR AlphaFoldDB; Q13247; -. DR SMR; Q13247; -. DR BioGRID; 112329; 520. DR CORUM; Q13247; -. DR IntAct; Q13247; 385. DR MINT; Q13247; -. DR STRING; 9606.ENSP00000244020; -. DR BindingDB; Q13247; -. DR ChEMBL; CHEMBL5169149; -. DR GlyGen; Q13247; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q13247; -. DR PhosphoSitePlus; Q13247; -. DR SwissPalm; Q13247; -. DR BioMuta; SRSF6; -. DR DMDM; 20981728; -. DR jPOST; Q13247; -. DR MassIVE; Q13247; -. DR PaxDb; 9606-ENSP00000244020; -. DR PeptideAtlas; Q13247; -. DR ProteomicsDB; 59250; -. [Q13247-1] DR ProteomicsDB; 59251; -. [Q13247-2] DR ProteomicsDB; 59252; -. [Q13247-3] DR Pumba; Q13247; -. DR TopDownProteomics; Q13247-1; -. [Q13247-1] DR Antibodypedia; 27122; 118 antibodies from 28 providers. DR DNASU; 6431; -. DR Ensembl; ENST00000244020.5; ENSP00000244020.3; ENSG00000124193.16. [Q13247-1] DR Ensembl; ENST00000483871.6; ENSP00000433544.1; ENSG00000124193.16. [Q13247-2] DR GeneID; 6431; -. DR KEGG; hsa:6431; -. DR MANE-Select; ENST00000244020.5; ENSP00000244020.3; NM_006275.6; NP_006266.2. DR UCSC; uc010zwg.3; human. [Q13247-1] DR AGR; HGNC:10788; -. DR CTD; 6431; -. DR DisGeNET; 6431; -. DR GeneCards; SRSF6; -. DR HGNC; HGNC:10788; SRSF6. DR HPA; ENSG00000124193; Low tissue specificity. DR MIM; 601944; gene. DR neXtProt; NX_Q13247; -. DR OpenTargets; ENSG00000124193; -. DR PharmGKB; PA35704; -. DR VEuPathDB; HostDB:ENSG00000124193; -. DR eggNOG; KOG0106; Eukaryota. DR GeneTree; ENSGT00940000155448; -. DR HOGENOM; CLU_1916372_0_0_1; -. DR InParanoid; Q13247; -. DR OMA; RSKETGC; -. DR OrthoDB; 132255at2759; -. DR PhylomeDB; Q13247; -. DR TreeFam; TF351335; -. DR PathwayCommons; Q13247; -. 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-72165; mRNA Splicing - Minor Pathway. DR Reactome; R-HSA-72187; mRNA 3'-end processing. DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination. DR SignaLink; Q13247; -. DR BioGRID-ORCS; 6431; 450 hits in 1169 CRISPR screens. DR ChiTaRS; SRSF6; human. DR GeneWiki; SFRS6; -. DR GenomeRNAi; 6431; -. DR Pharos; Q13247; Tbio. DR PRO; PR:Q13247; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q13247; protein. DR Bgee; ENSG00000124193; Expressed in right uterine tube and 204 other cell types or tissues. DR ExpressionAtlas; Q13247; baseline and differential. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0006376; P:mRNA splice site recognition; IMP:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; IMP:UniProtKB. DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; IEA:Ensembl. DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IDA:MGI. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:MGI. DR GO; GO:0010837; P:regulation of keratinocyte proliferation; IMP:UniProtKB. DR GO; GO:0061041; P:regulation of wound healing; IMP:UniProtKB. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR CDD; cd12596; RRM1_SRSF6; 1. DR CDD; cd12766; RRM2_SRSF6; 1. DR FunFam; 3.30.70.330:FF:000028; Putative serine/arginine-rich splicing factor 4; 1. DR FunFam; 3.30.70.330:FF:000190; serine/arginine-rich splicing factor 4 isoform X1; 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; IPR034511; SRSF6_RRM1. DR PANTHER; PTHR48038; RIBONUCLEOPROTEIN RB97D; 1. DR PANTHER; PTHR48038:SF1; RIBONUCLEOPROTEIN RB97D; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Direct protein sequencing; KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repeat; Repressor; KW RNA-binding; Ubl conjugation. FT CHAIN 1..344 FT /note="Serine/arginine-rich splicing factor 6" FT /id="PRO_0000081930" FT DOMAIN 1..72 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 110..183 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 75..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 176..344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 189..249 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 250..295 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 84 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 165 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q3TWW8" FT MOD_RES 297 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 303 FT /note="Phosphoserine; by DYRK1A" FT /evidence="ECO:0000269|PubMed:22767602, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CROSSLNK 182 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 86..135 FT /note="SGGGGYSSRRTSGRDKYGPPVRTEYRLIVENLSSRCSWQDLKDFMRQAGE FT -> MTNGAEAVSTEAKMTAFPDWPWLFHTLCDPCPMTLWLTLPEAMTTAAFCH (in FT isoform SRP55-2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:7556075" FT /id="VSP_005869" FT VAR_SEQ 136..344 FT /note="Missing (in isoform SRP55-2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:7556075" FT /id="VSP_005870" FT VAR_SEQ 313..344 FT /note="RSVSPPPKRATSRSRSRSRSKSRSRSRSSSRD -> LKLGARFMSQQGTESL FT YSLASSC (in isoform SRP55-3)" FT /evidence="ECO:0000303|PubMed:7556075" FT /id="VSP_005871" FT VARIANT 145 FT /note="R -> Q (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs2017559129)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035489" FT MUTAGEN 280 FT /note="S->A: No effect on regulation of alternative FT splicing of MAPT/Tau exon 10 by DYRK1A." FT /evidence="ECO:0000269|PubMed:22767602" FT MUTAGEN 303 FT /note="S->A: Abolishes regulatory effect of DYRK1A on FT alternative splicing of MAPT/Tau exon 10." FT /evidence="ECO:0000269|PubMed:22767602" FT MUTAGEN 316 FT /note="S->A: No effect on regulation of alternative FT splicing of MAPT/Tau exon 10 by DYRK1A." FT /evidence="ECO:0000269|PubMed:22767602" FT CONFLICT 64 FT /note="R -> H (in Ref. 1; AAA93073/AAA93071/AAA93072)" FT /evidence="ECO:0000305" SQ SEQUENCE 344 AA; 39587 MW; 72305506CE948B94 CRC64; MPRVYIGRLS YNVREKDIQR FFSGYGRLLE VDLKNGYGFV EFEDSRDADD AVYELNGKEL CGERVIVEHA RGPRRDRDGY SYGSRSGGGG YSSRRTSGRD KYGPPVRTEY RLIVENLSSR CSWQDLKDFM RQAGEVTYAD AHKERTNEGV IEFRSYSDMK RALDKLDGTE INGRNIRLIE DKPRTSHRRS YSGSRSRSRS RRRSRSRSRR SSRSRSRSIS KSRSRSRSRS KGRSRSRSKG RKSRSKSKSK PKSDRGSHSH SRSRSKDEYE KSRSRSRSRS PKENGKGDIK SKSRSRSQSR SNSPLPVPPS KARSVSPPPK RATSRSRSRS RSKSRSRSRS SSRD //