SRS11_HUMAN
ID SRS11_HUMAN Reviewed; 484 AA.
AC Q05519; Q5T758; Q8IWE6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Serine/arginine-rich splicing factor 11;
DE AltName: Full=Arginine-rich 54 kDa nuclear protein;
DE Short=p54;
DE AltName: Full=Splicing factor, arginine/serine-rich 11;
GN Name=SRSF11; Synonyms=SFRS11;
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 1).
RC TISSUE=Hepatoma;
RX PubMed=1896467; DOI=10.1073/pnas.88.18.8189;
RA Chaudhary N., McMahon C., Blobel G.;
RT "Primary structure of a human arginine-rich nuclear protein that
RT colocalizes with spliceosome components.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8189-8193(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [5]
RP INTERACTION WITH PUF60.
RX PubMed=10606266; DOI=10.1017/s1355838299991938;
RA Page-McCaw P.S., Amonlirdviman K., Sharp P.A.;
RT "PUF60: a novel U2AF65-related splicing activity.";
RL RNA 5:1548-1560(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-434, 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-483, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-414; SER-434;
RP THR-447; SER-449; SER-464 AND SER-483, AND IDENTIFICATION BY MASS
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-434; THR-447;
RP SER-449 AND SER-483, 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-212; SER-323;
RP THR-325; SER-434; SER-456 AND SER-483, AND IDENTIFICATION BY MASS
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-434 AND SER-449, 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197 AND LYS-211, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: May function in pre-mRNA splicing.
CC -!- SUBUNIT: Interacts with PUF60. {ECO:0000269|PubMed:10606266}.
CC -!- INTERACTION:
CC Q05519; Q66PJ3-3: ARL6IP4; NbExp=3; IntAct=EBI-1051785, EBI-10248982;
CC Q05519; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-1051785, EBI-5280499;
CC Q05519; P14921: ETS1; NbExp=2; IntAct=EBI-1051785, EBI-913209;
CC Q05519; O43716: GATC; NbExp=3; IntAct=EBI-1051785, EBI-6929453;
CC Q05519; Q5T013: HYI; NbExp=3; IntAct=EBI-1051785, EBI-749235;
CC Q05519; Q9UHX1: PUF60; NbExp=6; IntAct=EBI-1051785, EBI-1053259;
CC Q05519; Q14498: RBM39; NbExp=3; IntAct=EBI-1051785, EBI-395290;
CC Q05519; Q14498-3: RBM39; NbExp=3; IntAct=EBI-1051785, EBI-6654703;
CC Q05519; O00560: SDCBP; NbExp=3; IntAct=EBI-1051785, EBI-727004;
CC Q05519; Q8WXA9: SREK1; NbExp=3; IntAct=EBI-1051785, EBI-1044237;
CC Q05519; Q92844: TANK; NbExp=3; IntAct=EBI-1051785, EBI-356349;
CC Q05519; G4XUV3; NbExp=3; IntAct=EBI-1051785, EBI-10177989;
CC Q05519-2; P30049: ATP5F1D; NbExp=3; IntAct=EBI-11975029, EBI-1049505;
CC Q05519-2; Q9UI36-2: DACH1; NbExp=3; IntAct=EBI-11975029, EBI-10186082;
CC Q05519-2; Q68J44: DUSP29; NbExp=3; IntAct=EBI-11975029, EBI-1054321;
CC Q05519-2; O43716: GATC; NbExp=6; IntAct=EBI-11975029, EBI-6929453;
CC Q05519-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11975029, EBI-16439278;
CC Q05519-2; P26367: PAX6; NbExp=3; IntAct=EBI-11975029, EBI-747278;
CC Q05519-2; Q9UHX1-2: PUF60; NbExp=6; IntAct=EBI-11975029, EBI-11529177;
CC Q05519-2; Q14498: RBM39; NbExp=5; IntAct=EBI-11975029, EBI-395290;
CC Q05519-2; O00560: SDCBP; NbExp=3; IntAct=EBI-11975029, EBI-727004;
CC Q05519-2; Q8WXA9: SREK1; NbExp=6; IntAct=EBI-11975029, EBI-1044237;
CC Q05519-2; P78362: SRPK2; NbExp=3; IntAct=EBI-11975029, EBI-593303;
CC Q05519-2; A7MD48: SRRM4; NbExp=3; IntAct=EBI-11975029, EBI-3867173;
CC Q05519-2; Q05519-2: SRSF11; NbExp=3; IntAct=EBI-11975029, EBI-11975029;
CC Q05519-2; Q66K41-2: ZNF385C; NbExp=3; IntAct=EBI-11975029, EBI-12055653;
CC Q05519-2; G4XUV3; NbExp=8; IntAct=EBI-11975029, EBI-10177989;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with spliceosome
CC components.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q05519-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05519-2; Sequence=VSP_043376;
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; M74002; AAA35554.1; -; mRNA.
DR EMBL; AL353771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06459.1; -; Genomic_DNA.
DR EMBL; BC040436; AAH40436.1; -; mRNA.
DR CCDS; CCDS53332.1; -. [Q05519-2]
DR CCDS; CCDS647.1; -. [Q05519-1]
DR PIR; A40988; A40988.
DR RefSeq; NP_001177916.1; NM_001190987.1. [Q05519-2]
DR RefSeq; NP_004759.1; NM_004768.3. [Q05519-1]
DR RefSeq; XP_011540729.1; XM_011542427.2.
DR RefSeq; XP_016858301.1; XM_017002812.1.
DR RefSeq; XP_016858302.1; XM_017002813.1.
DR AlphaFoldDB; Q05519; -.
DR SMR; Q05519; -.
DR BioGRID; 114709; 187.
DR CORUM; Q05519; -.
DR IntAct; Q05519; 43.
DR MINT; Q05519; -.
DR STRING; 9606.ENSP00000359988; -.
DR GlyGen; Q05519; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q05519; -.
DR PhosphoSitePlus; Q05519; -.
DR SwissPalm; Q05519; -.
DR BioMuta; SRSF11; -.
DR DMDM; 8134672; -.
DR EPD; Q05519; -.
DR jPOST; Q05519; -.
DR MassIVE; Q05519; -.
DR MaxQB; Q05519; -.
DR PaxDb; Q05519; -.
DR PeptideAtlas; Q05519; -.
DR PRIDE; Q05519; -.
DR ProteomicsDB; 58334; -. [Q05519-1]
DR ProteomicsDB; 58335; -. [Q05519-2]
DR Antibodypedia; 1615; 145 antibodies from 23 providers.
DR DNASU; 9295; -.
DR Ensembl; ENST00000370949.2; ENSP00000359987.2; ENSG00000116754.14. [Q05519-1]
DR Ensembl; ENST00000370950.7; ENSP00000359988.3; ENSG00000116754.14. [Q05519-1]
DR Ensembl; ENST00000370951.5; ENSP00000359989.1; ENSG00000116754.14. [Q05519-2]
DR GeneID; 9295; -.
DR KEGG; hsa:9295; -.
DR MANE-Select; ENST00000370949.2; ENSP00000359987.2; NM_001350605.2; NP_001337534.1.
DR UCSC; uc001des.4; human. [Q05519-1]
DR CTD; 9295; -.
DR DisGeNET; 9295; -.
DR GeneCards; SRSF11; -.
DR HGNC; HGNC:10782; SRSF11.
DR HPA; ENSG00000116754; Low tissue specificity.
DR MIM; 602010; gene.
DR neXtProt; NX_Q05519; -.
DR OpenTargets; ENSG00000116754; -.
DR PharmGKB; PA35698; -.
DR VEuPathDB; HostDB:ENSG00000116754; -.
DR eggNOG; KOG4676; Eukaryota.
DR GeneTree; ENSGT00730000110872; -.
DR InParanoid; Q05519; -.
DR OrthoDB; 1460556at2759; -.
DR PhylomeDB; Q05519; -.
DR TreeFam; TF106266; -.
DR PathwayCommons; Q05519; -.
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-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q05519; -.
DR BioGRID-ORCS; 9295; 684 hits in 1090 CRISPR screens.
DR ChiTaRS; SRSF11; human.
DR GeneWiki; SFRS11; -.
DR GenomeRNAi; 9295; -.
DR Pharos; Q05519; Tbio.
DR PRO; PR:Q05519; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q05519; protein.
DR Bgee; ENSG00000116754; Expressed in visceral pleura and 204 other tissues.
DR ExpressionAtlas; Q05519; baseline and differential.
DR Genevisible; Q05519; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
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; IPR034447; SRSF11.
DR PANTHER; PTHR32343:SF6; PTHR32343:SF6; 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 Acetylation; Alternative splicing; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..484
FT /note="Serine/arginine-rich splicing factor 11"
FT /id="PRO_0000081939"
FT DOMAIN 33..113
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 247..255
FT /note="1"
FT REPEAT 258..265
FT /note="2"
FT REPEAT 267..274
FT /note="3"
FT REPEAT 275..282
FT /note="4"
FT REPEAT 285..292
FT /note="5"
FT REPEAT 293..300
FT /note="6"
FT REPEAT 302..309
FT /note="7"
FT REPEAT 321..328
FT /note="8"
FT REPEAT 334..341
FT /note="9"
FT REPEAT 346..353
FT /note="10"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..353
FT /note="10 X 8 AA approximate repeats of R-R-S-R-S-R-S-R"
FT COMPBIAS 247..309
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..381
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 434
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 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 420
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043376"
SQ SEQUENCE 484 AA; 53542 MW; 1211E96DDC0A3182 CRC64;
MSNTTVVPST AGPGPSGGPG GGGGGGGGGG GTEVIQVTNV SPSASSEQMR TLFGFLGKID
ELRLFPPDDS PLPVSSRVCF VKFHDPDSAV VAQHLTNTVF VDRALIVVPY AEGVIPDEAK
ALSLLAPANA VAGLLPGGGL LPTPNPLTQI GAVPLAALGA PTLDPALAAL GLPGANLNSQ
SLAADQLLKL MSTVDPKLNH VAAGLVSPSL KSDTSSKEIE EAMKRVREAQ SLISAAIEPD
KKEEKRRHSR SRSRSRRRRT PSSSRHRRSR SRSRRRSHSK SRSRRRSKSP RRRRSHSRER
GRRSRSTSKT RDKKKEDKEK KRSKTPPKSY STARRSRSAS RERRRRRSRS GTRSPKKPRS
PKRKLSRSPS PRRHKKEKKK DKDKERSRDE RERSTSKKKK SKDKEKDRER KSESDKDVKQ
VTRDYDEEEQ GYDSEKEKKE EKKPIETGSP KTKECSVEKG TGDSLRESKV NGDDHHEEDM
DMSD
