SRS10_HUMAN
ID SRS10_HUMAN Reviewed; 262 AA.
AC O75494; A6NFM6; A6NI42; A6NIU7; B4DJP9; O60572; Q5JRH9; Q5JRI0; Q5JRI2;
AC Q5JRI3; Q5JRI4; Q96G09; Q96P17;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Serine/arginine-rich splicing factor 10;
DE AltName: Full=40 kDa SR-repressor protein;
DE Short=SRrp40;
DE AltName: Full=FUS-interacting serine-arginine-rich protein 1;
DE AltName: Full=Splicing factor SRp38;
DE AltName: Full=Splicing factor, arginine/serine-rich 13A;
DE AltName: Full=TLS-associated protein with Ser-Arg repeats;
DE Short=TASR;
DE Short=TLS-associated protein with SR repeats;
DE AltName: Full=TLS-associated serine-arginine protein;
DE Short=TLS-associated SR protein;
GN Name=SRSF10; Synonyms=FUSIP1, FUSIP2, SFRS13A, TASR;
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] (ISOFORM 3), AND INTERACTION WITH FUS.
RC TISSUE=Leukemia;
RX PubMed=9774382; DOI=10.1074/jbc.273.43.27761;
RA Yang L., Embree L.J., Tsai S., Hickstein D.D.;
RT "Oncoprotein TLS interacts with serine-arginine proteins involved in RNA
RT splicing.";
RL J. Biol. Chem. 273:27761-27764(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10779324; DOI=10.1128/mcb.20.10.3345-3354.2000;
RA Yang L., Embree L.J., Hickstein D.D.;
RT "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by serine-
RT arginine proteins.";
RL Mol. Cell. Biol. 20:3345-3354(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11684676; DOI=10.1074/jbc.m103967200;
RA Cowper A.E., Caceres J.F., Mayeda A., Screaton G.R.;
RT "Serine-arginine (SR) protein-like factors that antagonize authentic SR
RT proteins and regulate alternative splicing.";
RL J. Biol. Chem. 276:48908-48914(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, AND
RP PHOSPHORYLATION.
RX PubMed=12419250; DOI=10.1016/s0092-8674(02)01038-3;
RA Shin C., Manley J.L.;
RT "The SR protein SRp38 represses splicing in M Phase cells.";
RL Cell 111:407-417(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING (ISOFORMS 2
RP AND 3), AND TISSUE SPECIFICITY.
RX PubMed=11891055; DOI=10.1016/s0378-1119(02)00382-7;
RA Clinton J.M., Chansky H.A., Odell D.D., Zielinska-Kwiatkowska A.,
RA Hickstein D.D., Yang L.;
RT "Characterization and expression of the human gene encoding two
RT translocation liposarcoma protein-associated serine-arginine (TASR)
RT proteins.";
RL Gene 284:141-147(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
RC TISSUE=Thalamus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Muscle, Placenta, and Uterus;
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 [9]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH SNRNP70 AND TRA2B.
RX PubMed=14765198; DOI=10.1038/nature02288;
RA Shin C., Feng Y., Manley J.L.;
RT "Dephosphorylated SRp38 acts as a splicing repressor in response to heat
RT shock.";
RL Nature 427:553-558(2004).
RN [10]
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-129; SER-131 AND SER-133, 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-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-133; SER-158 AND
RP SER-160, AND 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-106; SER-108; SER-131 AND
RP SER-133, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 AND SER-160
RP (ISOFORM 4), 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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-106; SER-108;
RP SER-129; SER-131 AND SER-133, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-133, 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 [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH YTHDC1.
RX PubMed=26876937; DOI=10.1016/j.molcel.2016.01.012;
RA Xiao W., Adhikari S., Dahal U., Chen Y.S., Hao Y.J., Sun B.F., Sun H.Y.,
RA Li A., Ping X.L., Lai W.Y., Wang X., Ma H.L., Huang C.M., Yang Y.,
RA Huang N., Jiang G.B., Wang H.L., Zhou Q., Wang X.J., Zhao Y.L., Yang Y.G.;
RT "Nuclear m(6)A reader YTHDC1 regulates mRNA splicing.";
RL Mol. Cell 61:507-519(2016).
CC -!- FUNCTION: Splicing factor that in its dephosphorylated form acts as a
CC general repressor of pre-mRNA splicing (PubMed:11684676,
CC PubMed:12419250, PubMed:14765198). Seems to interfere with the U1 snRNP
CC 5'-splice recognition of SNRNP70 (PubMed:14765198). Required for
CC splicing repression in M-phase cells and after heat shock
CC (PubMed:14765198). Also acts as a splicing factor that specifically
CC promotes exon skipping during alternative splicing (PubMed:26876937).
CC Interaction with YTHDC1, a RNA-binding protein that recognizes and
CC binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from
CC binding to its mRNA-binding sites close to m6A-containing regions,
CC leading to inhibit exon skipping during alternative splicing
CC (PubMed:26876937). May be involved in regulation of alternative
CC splicing in neurons, with isoform 1 acting as a positive and isoform 3
CC as a negative regulator (PubMed:12419250).
CC {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:12419250,
CC ECO:0000269|PubMed:14765198, ECO:0000269|PubMed:26876937}.
CC -!- SUBUNIT: The phosphorylated but not the dephosphorylated form interacts
CC with TRA2B/SFRS10 (PubMed:14765198). The dephosphorylated form
CC interacts with SNRNP70 (PubMed:14765198). Isoform 1 interacts with FUS
CC C-terminus (PubMed:9774382). Isoform 3 interacts with FUS C-terminus
CC (PubMed:9774382). Interacts with YTHDC1, leading to inhibit RNA-binding
CC activity of SRSF10 (PubMed:26876937). {ECO:0000269|PubMed:14765198,
CC ECO:0000269|PubMed:26876937, ECO:0000269|PubMed:9774382}.
CC -!- INTERACTION:
CC O75494; P49759-3: CLK1; NbExp=3; IntAct=EBI-353655, EBI-11981867;
CC O75494; P49761: CLK3; NbExp=3; IntAct=EBI-353655, EBI-745579;
CC O75494; Q15287: RNPS1; NbExp=3; IntAct=EBI-353655, EBI-395959;
CC O75494; P78362: SRPK2; NbExp=2; IntAct=EBI-353655, EBI-593303;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11684676,
CC ECO:0000269|PubMed:26876937}. Cytoplasm {ECO:0000269|PubMed:11684676}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=TASR-1;
CC IsoId=O75494-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75494-2; Sequence=VSP_010421;
CC Name=3; Synonyms=TASR-2, SRp38-2;
CC IsoId=O75494-3; Sequence=VSP_010424, VSP_010425;
CC Name=4;
CC IsoId=O75494-4; Sequence=VSP_010422, VSP_010423, VSP_010425;
CC Name=5;
CC IsoId=O75494-5; Sequence=VSP_043697, VSP_043698, VSP_010423,
CC VSP_010425;
CC Name=6;
CC IsoId=O75494-6; Sequence=VSP_010421, VSP_010424, VSP_010425;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11684676,
CC ECO:0000269|PubMed:11891055}.
CC -!- PTM: Phosphorylated. Fully dephosphorylated in mitosis and partially
CC dephosphorylated on heat shock. {ECO:0000269|PubMed:12419250,
CC ECO:0000269|PubMed:14765198}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AF047448; AAC70918.1; -; mRNA.
DR EMBL; AF067730; AAC26727.1; -; mRNA.
DR EMBL; AF449427; AAL57514.1; -; mRNA.
DR EMBL; AY150180; AAN65380.1; -; mRNA.
DR EMBL; AY150181; AAN65381.1; -; mRNA.
DR EMBL; AF419331; AAL16665.1; -; mRNA.
DR EMBL; AF419332; AAL16666.1; -; Genomic_DNA.
DR EMBL; AY048592; AAL06098.1; -; Genomic_DNA.
DR EMBL; AY048592; AAL06099.1; -; Genomic_DNA.
DR EMBL; AK001286; BAA91601.1; -; mRNA.
DR EMBL; AK001656; BAG50956.1; -; mRNA.
DR EMBL; AK296175; BAG58911.1; -; mRNA.
DR EMBL; AL590609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001107; AAH01107.1; -; mRNA.
DR EMBL; BC005039; AAH05039.1; -; mRNA.
DR EMBL; BC010074; AAH10074.1; -; mRNA.
DR CCDS; CCDS30629.1; -. [O75494-3]
DR CCDS; CCDS30630.1; -. [O75494-1]
DR CCDS; CCDS53280.1; -. [O75494-5]
DR CCDS; CCDS53281.1; -. [O75494-6]
DR CCDS; CCDS53282.1; -. [O75494-2]
DR CCDS; CCDS53283.1; -. [O75494-4]
DR RefSeq; NP_001177934.1; NM_001191005.2. [O75494-2]
DR RefSeq; NP_001177935.1; NM_001191006.2. [O75494-4]
DR RefSeq; NP_001177936.1; NM_001191007.2. [O75494-6]
DR RefSeq; NP_001177938.1; NM_001191009.2. [O75494-5]
DR RefSeq; NP_006616.1; NM_006625.5. [O75494-3]
DR RefSeq; NP_473357.1; NM_054016.3. [O75494-1]
DR AlphaFoldDB; O75494; -.
DR SMR; O75494; -.
DR BioGRID; 115990; 209.
DR IntAct; O75494; 70.
DR MINT; O75494; -.
DR STRING; 9606.ENSP00000420195; -.
DR GlyGen; O75494; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75494; -.
DR PhosphoSitePlus; O75494; -.
DR SwissPalm; O75494; -.
DR BioMuta; SRSF10; -.
DR EPD; O75494; -.
DR jPOST; O75494; -.
DR MassIVE; O75494; -.
DR MaxQB; O75494; -.
DR PaxDb; O75494; -.
DR PeptideAtlas; O75494; -.
DR PRIDE; O75494; -.
DR ProteomicsDB; 50048; -. [O75494-1]
DR ProteomicsDB; 50049; -. [O75494-2]
DR ProteomicsDB; 50050; -. [O75494-3]
DR ProteomicsDB; 50051; -. [O75494-4]
DR ProteomicsDB; 50052; -. [O75494-5]
DR ProteomicsDB; 63091; -.
DR TopDownProteomics; O75494-1; -. [O75494-1]
DR TopDownProteomics; O75494-2; -. [O75494-2]
DR TopDownProteomics; O75494-3; -. [O75494-3]
DR TopDownProteomics; O75494-4; -. [O75494-4]
DR TopDownProteomics; O75494-5; -. [O75494-5]
DR Antibodypedia; 60384; 278 antibodies from 25 providers.
DR DNASU; 10772; -.
DR Ensembl; ENST00000343255.9; ENSP00000344149.4; ENSG00000188529.15. [O75494-2]
DR Ensembl; ENST00000344989.10; ENSP00000342913.5; ENSG00000188529.15. [O75494-3]
DR Ensembl; ENST00000374452.9; ENSP00000363576.5; ENSG00000188529.15. [O75494-4]
DR Ensembl; ENST00000453840.7; ENSP00000388991.3; ENSG00000188529.15. [O75494-6]
DR Ensembl; ENST00000484146.6; ENSP00000419813.2; ENSG00000188529.15. [O75494-5]
DR Ensembl; ENST00000492112.3; ENSP00000420195.1; ENSG00000188529.15. [O75494-1]
DR GeneID; 10772; -.
DR KEGG; hsa:10772; -.
DR MANE-Select; ENST00000492112.3; ENSP00000420195.1; NM_054016.4; NP_473357.1.
DR UCSC; uc057dhz.1; human. [O75494-1]
DR CTD; 10772; -.
DR DisGeNET; 10772; -.
DR GeneCards; SRSF10; -.
DR HGNC; HGNC:16713; SRSF10.
DR HPA; ENSG00000188529; Low tissue specificity.
DR MIM; 605221; gene.
DR neXtProt; NX_O75494; -.
DR OpenTargets; ENSG00000188529; -.
DR PharmGKB; PA28427; -.
DR VEuPathDB; HostDB:ENSG00000188529; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154450; -.
DR HOGENOM; CLU_012062_10_2_1; -.
DR InParanoid; O75494; -.
DR OMA; MVREKFK; -.
DR PhylomeDB; O75494; -.
DR TreeFam; TF351864; -.
DR PathwayCommons; O75494; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; O75494; -.
DR BioGRID-ORCS; 10772; 589 hits in 1062 CRISPR screens.
DR ChiTaRS; SRSF10; human.
DR GeneWiki; FUSIP1; -.
DR GenomeRNAi; 10772; -.
DR Pharos; O75494; Tbio.
DR PRO; PR:O75494; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75494; protein.
DR Bgee; ENSG00000188529; Expressed in ventricular zone and 202 other tissues.
DR ExpressionAtlas; O75494; baseline and differential.
DR Genevisible; O75494; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0050733; F:RS domain binding; NAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0016482; P:cytosolic transport; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; IDA:UniProtKB.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; NAS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034476; SRSF10.
DR PANTHER; PTHR23147:SF87; PTHR23147:SF87; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..262
FT /note="Serine/arginine-rich splicing factor 10"
FT /id="PRO_0000081593"
FT DOMAIN 10..88
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 116..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 146..165
FT /note="NSRPTGRPRRSRSHSDNDRF -> KPNCSWNTQYSSAYYTSRKI (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043697"
FT VAR_SEQ 147
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010421"
FT VAR_SEQ 164..173
FT /note="RFKHRNRSFS -> SQVSKKKNER (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_010422"
FT VAR_SEQ 165..183
FT /note="FKHRNRSFSRSKSNSRSRS -> PNCSWNTQYSSAYYTSRKI (in
FT isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12419250,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9774382"
FT /id="VSP_010424"
FT VAR_SEQ 166..173
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043698"
FT VAR_SEQ 174..183
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010423"
FT VAR_SEQ 184..262
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12419250,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9774382"
FT /id="VSP_010425"
FT MOD_RES O75494-3:168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES O75494-4:158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES O75494-4:160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
SQ SEQUENCE 262 AA; 31301 MW; 205F95D36CBBFAB4 CRC64;
MSRYLRPPNT SLFVRNVADD TRSEDLRREF GRYGPIVDVY VPLDFYTRRP RGFAYVQFED
VRDAEDALHN LDRKWICGRQ IEIQFAQGDR KTPNQMKAKE GRNVYSSSRY DDYDRYRRSR
SRSYERRRSR SRSFDYNYRR SYSPRNSRPT GRPRRSRSHS DNDRFKHRNR SFSRSKSNSR
SRSKSQPKKE MKAKSRSRSA SHTKTRGTSK TDSKTHYKSG SRYEKESRKK EPPRSKSQSR
SQSRSRSKSR SRSWTSPKSS GH
