SRS10_MOUSE
ID SRS10_MOUSE Reviewed; 262 AA.
AC Q9R0U0; B1AV44; B1AV45; O70307; O88468; Q3TGW7; Q8CFZ1; Q9R0T9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/arginine-rich splicing factor 10;
DE AltName: Full=FUS-interacting serine-arginine-rich protein 1;
DE AltName: Full=Neural-salient serine/arginine-rich protein;
DE AltName: Full=Neural-specific SR protein;
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, Nssr, Sfrs13a, Srsf13a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
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] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10583508; DOI=10.1046/j.1365-2443.1999.00286.x;
RA Komatsu M., Kominami E., Arahata K., Tsukahara T.;
RT "Cloning and characterization of two neural-salient serine/arginine-rich
RT (NSSR) proteins involved in the regulation of alternative splicing in
RT neurones.";
RL Genes Cells 4:593-606(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Limb;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-158 AND SER-160 (ISOFORM 3), AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Splicing factor that in its dephosphorylated form acts as a
CC general repressor of pre-mRNA splicing. Seems to interfere with the U1
CC snRNP 5'-splice recognition of SNRNP70. Required for splicing
CC repression in M-phase cells and after heat shock. Also acts as a
CC splicing factor that specifically promotes exon skipping during
CC alternative splicing. Interaction with YTHDC1, a RNA-binding protein
CC that recognizes and binds N6-methyladenosine (m6A)-containing RNAs,
CC prevents SRSF10 from binding to its mRNA-binding sites close to m6A-
CC containing regions, leading to inhibit exon skipping during alternative
CC splicing (By similarity). May be involved in regulation of alternative
CC splicing in neurons (PubMed:10583508). {ECO:0000250|UniProtKB:O75494,
CC ECO:0000269|PubMed:10583508}.
CC -!- SUBUNIT: The phosphorylated but not the dephosphorylated form interacts
CC with TRA2B/SFRS10. The dephosphorylated form interacts with SNRNP70.
CC Interacts with FUS C-terminus. Interacts with YTHDC1, leading to
CC inhibit RNA-binding activity of SRSF10. {ECO:0000250|UniProtKB:O75494}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:10583508}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TASR-1, NSSR1;
CC IsoId=Q9R0U0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R0U0-2; Sequence=VSP_010426;
CC Name=3; Synonyms=TASR-2, NSSR2;
CC IsoId=Q9R0U0-3; Sequence=VSP_010427, VSP_010428;
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in brain and
CC testis. {ECO:0000269|PubMed:10583508}.
CC -!- PTM: Phosphorylated. Fully dephosphorylated in mitosis and partially
CC dephosphorylated on heat shock. {ECO:0000250|UniProtKB:O75494}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AF042383; AAC70916.1; -; mRNA.
DR EMBL; AB015894; BAA35092.1; -; mRNA.
DR EMBL; AB015895; BAA35093.1; -; mRNA.
DR EMBL; AF060490; AAC26715.1; -; mRNA.
DR EMBL; AK014345; BAB29286.1; -; mRNA.
DR EMBL; AK168524; BAE40403.1; -; mRNA.
DR EMBL; AK168558; BAE40431.1; -; mRNA.
DR EMBL; AL672076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037591; AAH37591.1; -; mRNA.
DR EMBL; BC043060; AAH43060.1; -; mRNA.
DR EMBL; BC083082; AAH83082.1; -; mRNA.
DR CCDS; CCDS18791.1; -. [Q9R0U0-3]
DR CCDS; CCDS38922.1; -. [Q9R0U0-1]
DR CCDS; CCDS71493.1; -. [Q9R0U0-2]
DR RefSeq; NP_001073856.1; NM_001080387.2. [Q9R0U0-1]
DR RefSeq; NP_001271124.1; NM_001284195.1. [Q9R0U0-2]
DR RefSeq; NP_001271125.1; NM_001284196.1.
DR RefSeq; NP_034308.1; NM_010178.3. [Q9R0U0-3]
DR AlphaFoldDB; Q9R0U0; -.
DR SMR; Q9R0U0; -.
DR BioGRID; 199597; 7.
DR IntAct; Q9R0U0; 2.
DR STRING; 10090.ENSMUSP00000101479; -.
DR iPTMnet; Q9R0U0; -.
DR PhosphoSitePlus; Q9R0U0; -.
DR EPD; Q9R0U0; -.
DR jPOST; Q9R0U0; -.
DR MaxQB; Q9R0U0; -.
DR PaxDb; Q9R0U0; -.
DR PRIDE; Q9R0U0; -.
DR ProteomicsDB; 258612; -. [Q9R0U0-1]
DR ProteomicsDB; 258613; -. [Q9R0U0-2]
DR ProteomicsDB; 258614; -. [Q9R0U0-3]
DR Antibodypedia; 60384; 278 antibodies from 25 providers.
DR DNASU; 14105; -.
DR Ensembl; ENSMUST00000097844; ENSMUSP00000095455; ENSMUSG00000028676. [Q9R0U0-2]
DR Ensembl; ENSMUST00000105853; ENSMUSP00000101479; ENSMUSG00000028676. [Q9R0U0-1]
DR Ensembl; ENSMUST00000126641; ENSMUSP00000114564; ENSMUSG00000028676. [Q9R0U0-3]
DR GeneID; 14105; -.
DR KEGG; mmu:14105; -.
DR UCSC; uc008vhd.2; mouse. [Q9R0U0-2]
DR UCSC; uc033ifn.1; mouse. [Q9R0U0-1]
DR CTD; 10772; -.
DR MGI; MGI:1333805; Srsf10.
DR VEuPathDB; HostDB:ENSMUSG00000028676; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154450; -.
DR HOGENOM; CLU_012062_10_2_1; -.
DR InParanoid; Q9R0U0; -.
DR OMA; MVREKFK; -.
DR OrthoDB; 1533297at2759; -.
DR PhylomeDB; Q9R0U0; -.
DR TreeFam; TF351864; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 14105; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Srsf10; mouse.
DR PRO; PR:Q9R0U0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9R0U0; protein.
DR Bgee; ENSMUSG00000028676; Expressed in embryonic post-anal tail and 268 other tissues.
DR ExpressionAtlas; Q9R0U0; baseline and differential.
DR Genevisible; Q9R0U0; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR GO; GO:0016482; P:cytosolic transport; IDA:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
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; ISO:MGI.
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 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; 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_0000081594"
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:0000250|UniProtKB:O75494"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75494"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75494"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75494"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75494"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75494"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75494"
FT VAR_SEQ 147
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010426"
FT VAR_SEQ 165..183
FT /note="FKHRNRSFSRSKSNSRSRS -> PNCSWNTQYSSAYYTSRKI (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10583508,
FT ECO:0000303|PubMed:9774382"
FT /id="VSP_010427"
FT VAR_SEQ 184..262
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10583508,
FT ECO:0000303|PubMed:9774382"
FT /id="VSP_010428"
FT CONFLICT 22
FT /note="R -> Q (in Ref. 6; AAH37591)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="R -> T (in Ref. 2; BAA35092/BAA35093)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9R0U0-3:158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q9R0U0-3:160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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
