SRSF1_MOUSE
ID SRSF1_MOUSE Reviewed; 248 AA.
AC Q6PDM2; B2KGJ5; Q3UCH2; Q5SXC5; Q8BJV3; Q8C1H9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Serine/arginine-rich splicing factor 1 {ECO:0000305};
DE AltName: Full=ASF/SF2;
DE AltName: Full=Pre-mRNA-splicing factor SRp30a;
DE AltName: Full=Splicing factor, arginine/serine-rich 1;
GN Name=Srsf1 {ECO:0000312|MGI:MGI:98283}; Synonyms=Sfrs1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, Eye, and Medulla oblongata;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic 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 [4]
RP PROTEIN SEQUENCE OF 18-28.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION BY CLK1; CLK2; CLK3 AND CLK4.
RX PubMed=9307018; DOI=10.1042/bj3260693;
RA Nayler O., Stamm S., Ullrich A.;
RT "Characterization and comparison of four serine- and arginine-rich (SR)
RT protein kinases.";
RL Biochem. J. 326:693-700(1997).
RN [6]
RP FUNCTION.
RX PubMed=15652482; DOI=10.1016/j.cell.2004.11.036;
RA Xu X., Yang D., Ding J.-H., Wang W., Chu P.-H., Dalton N.D., Wang H.-Y.,
RA Bermingham J.R. Jr., Ye Z., Liu F., Rosenfeld M.G., Manley J.L.,
RA Ross J. Jr., Chen J., Xiao R.-P., Cheng H., Fu X.-D.;
RT "ASF/SF2-regulated CaMKIIdelta alternative splicing temporally reprograms
RT excitation-contraction coupling in cardiac muscle.";
RL Cell 120:59-72(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
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).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-93; ARG-97 AND ARG-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [10]
RP FUNCTION, INTERACTION WITH ILDR1 AND ILDR2, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=28785060; DOI=10.1038/s41598-017-07530-z;
RA Liu Y., Nie H., Liu C., Zhai X., Sang Q., Wang Y., Shi D., Wang L., Xu Z.;
RT "Angulin proteins ILDR1 and ILDR2 regulate alternative pre-mRNA splicing
RT through binding to splicing factors TRA2A, TRA2B, or SRSF1.";
RL Sci. Rep. 7:7466-7466(2017).
RN [11]
RP STRUCTURE BY NMR OF 113-207.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in splicing factor 2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in preventing exon skipping, ensuring the
CC accuracy of splicing and regulating alternative splicing
CC (PubMed:28785060). Interacts with other spliceosomal components, via
CC the RS domains, to form a bridge between the 5'- and 3'-splice site
CC binding components, U1 snRNP and U2AF. Can stimulate binding of U1
CC snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA
CC sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the
CC decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-
CC CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a
CC powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer
CC (ASE) which can specifically activate ASE-dependent splicing (By
CC similarity). Specifically regulates alternative splicing of cardiac
CC isoforms of CAMK2D, LDB3/CYPHER and TNNT2/CTNT during heart remodeling
CC at the juvenile to adult transition. The inappropriate accumulation of
CC a neonatal and neuronal isoform of CAMKD2 in the adult heart results in
CC aberrant calcium handling and defective excitation-contraction coupling
CC in cardiomyocytes. May function as export adapter involved in mRNA
CC nuclear export through the TAP/NXF1 pathway (PubMed:15652482).
CC {ECO:0000250|UniProtKB:Q07955, ECO:0000269|PubMed:15652482,
CC ECO:0000269|PubMed:28785060}.
CC -!- SUBUNIT: Consists of two polypeptides of p32 and p33. Identified in the
CC spliceosome C complex. Component of a ribonucleoprotein complex
CC containing mRNAs and RNA-binding proteins including DDX5, HNRNPH2 and
CC SRSF1 as well as splicing regulator ARVCF (By similarity). In vitro,
CC self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds
CC SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF.
CC Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with
CC ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus). Interacts with
CC SRPK1 and a sliding docking interaction is essential for its sequential
CC and processive phosphorylation by SRPK1. Interacts with NXF1. Interacts
CC with CCNL1, CCNL2 and CDK11B. Interacts with RRP1B. Interacts (when
CC phosphorylated in its RS domain) with TNPO3; promoting nuclear import.
CC Interacts with ILDR1 (via C-terminus) and ILDR2 (PubMed:28785060).
CC {ECO:0000250|UniProtKB:Q07955, ECO:0000269|PubMed:28785060}.
CC -!- INTERACTION:
CC Q6PDM2; Q8R409: Hexim1; NbExp=4; IntAct=EBI-2550360, EBI-6261031;
CC Q6PDM2; P08775: Polr2a; NbExp=2; IntAct=EBI-2550360, EBI-2549849;
CC Q6PDM2; P70318: Tial1; NbExp=3; IntAct=EBI-2550360, EBI-299820;
CC Q6PDM2; P70191: Traf5; NbExp=2; IntAct=EBI-2550360, EBI-523899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q07955}. Nucleus
CC speckle {ECO:0000269|PubMed:28785060}. Note=In nuclear speckles.
CC Shuttles between the nucleus and the cytoplasm. Nuclear import is
CC mediated via interaction with TNPO3. {ECO:0000250|UniProtKB:Q07955}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PDM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PDM2-2; Sequence=VSP_013770, VSP_013773;
CC Name=3;
CC IsoId=Q6PDM2-3; Sequence=VSP_013771, VSP_013772;
CC -!- TISSUE SPECIFICITY: Expressed in inner ear.
CC {ECO:0000269|PubMed:28785060}.
CC -!- DOMAIN: The RRM 2 domain plays an important role in governing both the
CC binding mode and the phosphorylation mechanism of the RS domain by
CC SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly
CC directional (C-terminus to N-terminus) phosphorylation reaction in
CC which the RS domain slides through an extended electronegative channel
CC separating the docking groove of SRPK1 and the active site. RRM 2 binds
CC toward the periphery of the active site and guides the directional
CC phosphorylation mechanism. Both the RS domain and an RRM domain are
CC required for nucleocytoplasmic shuttling (By similarity).
CC {ECO:0000250|UniProtKB:Q07955}.
CC -!- PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by
CC SRPK1 at multiple serines in its RS domain via a directional (C-
CC terminal to N-terminal) and a dual-track mechanism incorporating both
CC processive phosphorylation (in which the kinase stays attached to the
CC substrate after each round of phosphorylation) and distributive
CC phosphorylation steps (in which the kinase and substrate dissociate
CC after each phosphorylation event). The RS domain of SRSF1 binds to a
CC docking groove in the large lobe of the kinase domain of SRPK1 and this
CC induces certain structural changes in SRPK1 and/or RRM 2 domain of
CC SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation.
CC The cycles continue for several phosphorylation steps in a processive
CC manner (steps 1-8) until the last few phosphorylation steps
CC (approximately steps 9-12). During that time, a mechanical stress
CC induces the unfolding of the beta-4 motif in RRM 2, which then docks at
CC the docking groove of SRPK1. This also signals RRM 2 to begin to
CC dissociate, which facilitates SRSF1 dissociation after phosphorylation
CC is completed (By similarity). {ECO:0000250|UniProtKB:Q07955}.
CC -!- PTM: Asymmetrically dimethylated at arginines, probably by PRMT1,
CC methylation promotes localization to nuclear speckles.
CC {ECO:0000250|UniProtKB:Q07955}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AK018176; BAC25546.1; -; mRNA.
DR EMBL; AK078715; BAC37367.1; -; mRNA.
DR EMBL; AK150535; BAE29641.1; -; mRNA.
DR EMBL; AL593853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU406964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046773; AAH46773.1; -; mRNA.
DR EMBL; BC058627; AAH58627.1; -; mRNA.
DR CCDS; CCDS36273.1; -. [Q6PDM2-1]
DR CCDS; CCDS36274.1; -. [Q6PDM2-2]
DR PIR; S26404; S26404.
DR RefSeq; NP_001071635.1; NM_001078167.2. [Q6PDM2-2]
DR RefSeq; NP_775550.2; NM_173374.4. [Q6PDM2-1]
DR PDB; 1X4C; NMR; -; A=113-207.
DR PDBsum; 1X4C; -.
DR AlphaFoldDB; Q6PDM2; -.
DR SMR; Q6PDM2; -.
DR BioGRID; 225922; 104.
DR DIP; DIP-48723N; -.
DR IntAct; Q6PDM2; 81.
DR MINT; Q6PDM2; -.
DR STRING; 10090.ENSMUSP00000120595; -.
DR iPTMnet; Q6PDM2; -.
DR PhosphoSitePlus; Q6PDM2; -.
DR SwissPalm; Q6PDM2; -.
DR EPD; Q6PDM2; -.
DR jPOST; Q6PDM2; -.
DR MaxQB; Q6PDM2; -.
DR PaxDb; Q6PDM2; -.
DR PeptideAtlas; Q6PDM2; -.
DR PRIDE; Q6PDM2; -.
DR ProteomicsDB; 257410; -. [Q6PDM2-1]
DR ProteomicsDB; 257411; -. [Q6PDM2-2]
DR ProteomicsDB; 257412; -. [Q6PDM2-3]
DR TopDownProteomics; Q6PDM2-1; -. [Q6PDM2-1]
DR Antibodypedia; 4585; 315 antibodies from 35 providers.
DR DNASU; 110809; -.
DR Ensembl; ENSMUST00000079866; ENSMUSP00000133517; ENSMUSG00000018379. [Q6PDM2-2]
DR Ensembl; ENSMUST00000139129; ENSMUSP00000120595; ENSMUSG00000018379. [Q6PDM2-1]
DR GeneID; 110809; -.
DR KEGG; mmu:110809; -.
DR UCSC; uc007kvc.2; mouse. [Q6PDM2-1]
DR UCSC; uc007kvd.2; mouse. [Q6PDM2-2]
DR CTD; 6426; -.
DR MGI; MGI:98283; Srsf1.
DR VEuPathDB; HostDB:ENSMUSG00000018379; -.
DR eggNOG; KOG0105; Eukaryota.
DR GeneTree; ENSGT00940000155585; -.
DR HOGENOM; CLU_012062_34_0_1; -.
DR InParanoid; Q6PDM2; -.
DR OMA; HRMQISG; -.
DR OrthoDB; 1321443at2759; -.
DR PhylomeDB; Q6PDM2; -.
DR TreeFam; TF106261; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 110809; 28 hits in 73 CRISPR screens.
DR ChiTaRS; Srsf1; mouse.
DR EvolutionaryTrace; Q6PDM2; -.
DR PRO; PR:Q6PDM2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PDM2; protein.
DR Bgee; ENSMUSG00000018379; Expressed in retinal neural layer and 83 other tissues.
DR ExpressionAtlas; Q6PDM2; baseline and differential.
DR Genevisible; Q6PDM2; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0044547; F:DNA topoisomerase binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IMP:MGI.
DR GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0050733; F:RS domain binding; IPI:MGI.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IGI:MGI.
DR GO; GO:0097398; P:cellular response to interleukin-17; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IDA:MGI.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048255; P:mRNA stabilization; IDA:MGI.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISO:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR GO; GO:0110012; P:protein localization to P-body; IDA:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IDA:MGI.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR CDD; cd12597; RRM1_SRSF1; 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; IPR034520; SRSF1_RRM1.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Spliceosome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT CHAIN 2..248
FT /note="Serine/arginine-rich splicing factor 1"
FT /id="PRO_0000081912"
FT DOMAIN 16..91
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 121..195
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 88..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..247
FT /note="Interaction with SAFB1"
FT /evidence="ECO:0000250"
FT COMPBIAS 205..225
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955, ECO:0000255"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 38
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 93
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 93
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 97
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 97
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 109
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 109
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT CROSSLNK 38
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q07955"
FT VAR_SEQ 185..203
FT /note="GETAYIRVKVDGPRSPSYG -> VGYTLILFFGQNWIQFS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013770"
FT VAR_SEQ 185..199
FT /note="GETAYIRVKVDGPRS -> TYLKRWIKNALD (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_013771"
FT VAR_SEQ 200..248
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_013772"
FT VAR_SEQ 204..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013773"
FT CONFLICT 119
FT /note="S -> A (in Ref. 1; BAC25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..164
FT /note="FVR -> CVP (in Ref. 1; BAC25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="G -> W (in Ref. 1; BAC25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..196
FT /note="RVKVDG -> PRIVDR (in Ref. 1; BAC25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..210
FT /note="SR -> VC (in Ref. 1; BAC25546)"
FT /evidence="ECO:0000305"
FT CONFLICT 226..228
FT /note="YSP -> DSR (in Ref. 1; BAC25546)"
FT /evidence="ECO:0000305"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1X4C"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:1X4C"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1X4C"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1X4C"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:1X4C"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:1X4C"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:1X4C"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:1X4C"
SQ SEQUENCE 248 AA; 27745 MW; C28A0B2F112EA713 CRC64;
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE
FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE
NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF
RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR
HSRSRSRT
