SRSF6_HUMAN
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 03-AUG-2022, entry version 220.
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 -!- 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}.
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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; 455.
DR CORUM; Q13247; -.
DR IntAct; Q13247; 54.
DR MINT; Q13247; -.
DR STRING; 9606.ENSP00000244020; -.
DR GlyGen; Q13247; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13247; -.
DR PhosphoSitePlus; Q13247; -.
DR SwissPalm; Q13247; -.
DR BioMuta; SRSF6; -.
DR DMDM; 20981728; -.
DR EPD; Q13247; -.
DR jPOST; Q13247; -.
DR MassIVE; Q13247; -.
DR MaxQB; Q13247; -.
DR PaxDb; Q13247; -.
DR PeptideAtlas; Q13247; -.
DR PRIDE; Q13247; -.
DR ProteomicsDB; 59250; -. [Q13247-1]
DR ProteomicsDB; 59251; -. [Q13247-2]
DR ProteomicsDB; 59252; -. [Q13247-3]
DR TopDownProteomics; Q13247-1; -. [Q13247-1]
DR Antibodypedia; 27122; 117 antibodies from 29 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 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; DRVSHSH; -.
DR OrthoDB; 1315388at2759; -.
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-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q13247; -.
DR BioGRID-ORCS; 6431; 435 hits in 1093 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 202 other tissues.
DR ExpressionAtlas; Q13247; baseline and differential.
DR Genevisible; Q13247; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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 selection; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:MGI.
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 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; IPR029541; SRSF6.
DR InterPro; IPR034511; SRSF6_RRM1.
DR PANTHER; PTHR23147:SF82; PTHR23147:SF82; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 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 Reference proteome; Repeat; Repressor; 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)"
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
