ID   SR140_HUMAN             Reviewed;        1029 AA.
AC   O15042; A0PJ60; Q0D2M1; Q2NKQ7; Q9BR70;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=U2 snRNP-associated SURP motif-containing protein;
DE   AltName: Full=140 kDa Ser/Arg-rich domain protein;
DE   AltName: Full=U2-associated protein SR140;
GN   Name=U2SURP; Synonyms=KIAA0332, SR140;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 2-1029 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 1-189 (ISOFORMS 1/2).
RC   TISSUE=Lung, and Urinary bladder;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1029 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [4]
RP   IDENTIFICATION (ISOFORM 1), AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12234937; DOI=10.1093/emboj/cdf480;
RA   Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.;
RT   "Characterization of novel SF3b and 17S U2 snRNP proteins, including a
RT   human Prp5p homologue and an SF3b DEAD-box protein.";
RL   EMBO J. 21:4978-4988(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-811, 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND SER-800, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND SER-800, 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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-760, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20858735; DOI=10.1158/1541-7786.mcr-10-0042;
RA   Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
RT   "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage
RT   response pathways.";
RL   Mol. Cancer Res. 8:1388-1398(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; SER-811; THR-931;
RP   SER-946 AND SER-948, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-485; SER-788 AND
RP   SER-811, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-202; SER-236 AND
RP   SER-485, AND 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND THR-719, 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   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-760, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-208, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80; LYS-145; LYS-168; LYS-208;
RP   LYS-748; LYS-749; LYS-760; LYS-822; LYS-829 AND LYS-832, AND IDENTIFICATION
RP   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   -!- SUBUNIT: Interacts with ERBB4. {ECO:0000269|PubMed:20858735}.
CC   -!- INTERACTION:
CC       O15042; P98175: RBM10; NbExp=2; IntAct=EBI-310697, EBI-721525;
CC       O15042; P52756: RBM5; NbExp=2; IntAct=EBI-310697, EBI-714003;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O15042-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O15042-2; Sequence=VSP_023523;
CC       Name=3;
CC         IsoId=O15042-3; Sequence=VSP_023522, VSP_023524;
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16323.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAI05605.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AC018450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC026304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006474; AAH06474.1; -; mRNA.
DR   EMBL; BC016323; AAH16323.1; ALT_SEQ; mRNA.
DR   EMBL; BC105604; AAI05605.1; ALT_SEQ; mRNA.
DR   EMBL; BC111692; AAI11693.1; -; mRNA.
DR   EMBL; AB002330; BAA20790.1; -; mRNA.
DR   EMBL; BK000564; DAA00075.1; -; mRNA.
DR   CCDS; CCDS46928.1; -. [O15042-1]
DR   RefSeq; NP_001073884.1; NM_001080415.1. [O15042-1]
DR   RefSeq; NP_001307148.1; NM_001320219.1. [O15042-2]
DR   RefSeq; NP_001307149.1; NM_001320220.1. [O15042-3]
DR   RefSeq; NP_001307151.1; NM_001320222.1.
DR   RefSeq; XP_016861527.1; XM_017006038.1.
DR   RefSeq; XP_016861528.1; XM_017006039.1.
DR   AlphaFoldDB; O15042; -.
DR   SMR; O15042; -.
DR   BioGRID; 116932; 343.
DR   CORUM; O15042; -.
DR   IntAct; O15042; 60.
DR   MINT; O15042; -.
DR   STRING; 9606.ENSP00000418563; -.
DR   GlyGen; O15042; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O15042; -.
DR   MetOSite; O15042; -.
DR   PhosphoSitePlus; O15042; -.
DR   SwissPalm; O15042; -.
DR   BioMuta; U2SURP; -.
DR   EPD; O15042; -.
DR   jPOST; O15042; -.
DR   MassIVE; O15042; -.
DR   MaxQB; O15042; -.
DR   PaxDb; 9606-ENSP00000418563; -.
DR   PeptideAtlas; O15042; -.
DR   ProteomicsDB; 48397; -. [O15042-1]
DR   ProteomicsDB; 48398; -. [O15042-2]
DR   ProteomicsDB; 48399; -. [O15042-3]
DR   Pumba; O15042; -.
DR   Antibodypedia; 48172; 155 antibodies from 23 providers.
DR   DNASU; 23350; -.
DR   Ensembl; ENST00000473835.7; ENSP00000418563.1; ENSG00000163714.18. [O15042-1]
DR   GeneID; 23350; -.
DR   KEGG; hsa:23350; -.
DR   MANE-Select; ENST00000473835.7; ENSP00000418563.1; NM_001080415.2; NP_001073884.1.
DR   UCSC; uc003evh.2; human. [O15042-1]
DR   AGR; HGNC:30855; -.
DR   CTD; 23350; -.
DR   DisGeNET; 23350; -.
DR   GeneCards; U2SURP; -.
DR   HGNC; HGNC:30855; U2SURP.
DR   HPA; ENSG00000163714; Low tissue specificity.
DR   MIM; 617849; gene.
DR   neXtProt; NX_O15042; -.
DR   OpenTargets; ENSG00000163714; -.
DR   VEuPathDB; HostDB:ENSG00000163714; -.
DR   eggNOG; KOG0151; Eukaryota.
DR   GeneTree; ENSGT00390000010687; -.
DR   HOGENOM; CLU_010743_1_0_1; -.
DR   InParanoid; O15042; -.
DR   OMA; FKSRVCN; -.
DR   OrthoDB; 9814at2759; -.
DR   PhylomeDB; O15042; -.
DR   TreeFam; TF318729; -.
DR   PathwayCommons; O15042; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; O15042; -.
DR   BioGRID-ORCS; 23350; 767 hits in 1157 CRISPR screens.
DR   ChiTaRS; U2SURP; human.
DR   GenomeRNAi; 23350; -.
DR   Pharos; O15042; Tbio.
DR   PRO; PR:O15042; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O15042; Protein.
DR   Bgee; ENSG00000163714; Expressed in calcaneal tendon and 210 other cell types or tissues.
DR   ExpressionAtlas; O15042; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd21370; cwf21_SR140; 1.
DR   CDD; cd12223; RRM_SR140; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 6.10.140.420; -; 1.
DR   Gene3D; 1.10.10.790; Surp module; 1.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR047488; SR140_cwf21.
DR   InterPro; IPR035009; SR140_RRM.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR035967; SWAP/Surp_sf.
DR   PANTHER; PTHR23140; RNA PROCESSING PROTEIN LD23810P; 1.
DR   PANTHER; PTHR23140:SF0; U2 SNRNP-ASSOCIATED SURP MOTIF-CONTAINING PROTEIN; 1.
DR   Pfam; PF04818; CID; 1.
DR   Pfam; PF08312; cwf21; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF01805; Surp; 1.
DR   SMART; SM01115; cwf21; 1.
DR   SMART; SM00582; RPR; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00648; SWAP; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF109905; Surp module (SWAP domain); 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50128; SURP; 1.
DR   Genevisible; O15042; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..1029
FT                   /note="U2 snRNP-associated SURP motif-containing protein"
FT                   /id="PRO_0000280070"
FT   DOMAIN          274..355
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REPEAT          430..473
FT                   /note="SURP motif"
FT   DOMAIN          534..679
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          92..121
FT                   /evidence="ECO:0000255"
FT   COILED          192..232
FT                   /evidence="ECO:0000255"
FT   COILED          837..915
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        7..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..806
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..924
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..984
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1029
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         719
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         760
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         788
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT   MOD_RES         800
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         811
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         931
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         946
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         948
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CROSSLNK        80
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        145
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        168
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        208
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        748
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        749
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        760
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        822
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        829
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        832
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..409
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023522"
FT   VAR_SEQ         256
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023523"
FT   VAR_SEQ         410..424
FT                   /note="KTLSQAIVKVVIPTE -> MLLCYRHLKTKRILR (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023524"
SQ   SEQUENCE   1029 AA;  118292 MW;  7AB9235C63299714 CRC64;
     MADKTPGGSQ KASSKTRSSD VHSSGSSDAH MDASGPSDSD MPSRTRPKSP RKHNYRNESA
     RESLCDSPHQ NLSRPLLENK LKAFSIGKMS TAKRTLSKKE QEELKKKEDE KAAAEIYEEF
     LAAFEGSDGN KVKTFVRGGV VNAAKEEHET DEKRGKIYKP SSRFADQKNP PNQSSNERPP
     SLLVIETKKP PLKKGEKEKK KSNLELFKEE LKQIQEERDE RHKTKGRLSR FEPPQSDSDG
     QRRSMDAPSR RNRSSGVLDD YAPGSHDVGD PSTTNLYLGN INPQMNEEML CQEFGRFGPL
     ASVKIMWPRT DEERARERNC GFVAFMNRRD AERALKNLNG KMIMSFEMKL GWGKAVPIPP
     HPIYIPPSMM EHTLPPPPSG LPFNAQPRER LKNPNAPMLP PPKNKEDFEK TLSQAIVKVV
     IPTERNLLAL IHRMIEFVVR EGPMFEAMIM NREINNPMFR FLFENQTPAH VYYRWKLYSI
     LQGDSPTKWR TEDFRMFKNG SFWRPPPLNP YLHGMSEEQE TEAFVEEPSK KGALKEEQRD
     KLEEILRGLT PRKNDIGDAM VFCLNNAEAA EEIVDCITES LSILKTPLPK KIARLYLVSD
     VLYNSSAKVA NASYYRKFFE TKLCQIFSDL NATYRTIQGH LQSENFKQRV MTCFRAWEDW
     AIYPEPFLIK LQNIFLGLVN IIEEKETEDV PDDLDGAPIE EELDGAPLED VDGIPIDATP
     IDDLDGVPIK SLDDDLDGVP LDATEDSKKN EPIFKVAPSK WEAVDESELE AQAVTTSKWE
     LFDQHEESEE EENQNQEEES EDEEDTQSSK SEEHHLYSNP IKEEMTESKF SKYSEMSEEK
     RAKLREIELK VMKFQDELES GKRPKKPGQS FQEQVEHYRD KLLQREKEKE LERERERDKK
     DKEKLESRSK DKKEKDECTP TRKERKRRHS TSPSPSRSSS GRRVKSPSPK SERSERSERS
     HKESSRSRSS HKDSPRDVSK KAKRSPSGSR TPKRSRRSRS RSPKKSGKKS RSQSRSPHRS
     HKKSKKNKH
//