WBP11_HUMAN
ID WBP11_HUMAN Reviewed; 641 AA.
AC Q9Y2W2; Q96AY8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=WW domain-binding protein 11 {ECO:0000305};
DE Short=WBP-11;
DE AltName: Full=Npw38-binding protein;
DE Short=NpwBP;
DE AltName: Full=SH3 domain-binding protein SNP70;
DE AltName: Full=Splicing factor that interacts with PQBP-1 and PP1;
GN Name=WBP11 {ECO:0000312|HGNC:HGNC:16461}; Synonyms=NPWBP, SIPP1, SNP70;
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], PROTEIN SEQUENCE OF 2-25, FUNCTION, INTERACTION
RP WITH PQBP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-192; ARG-197 AND
RP LYS-198.
RX PubMed=10593949; DOI=10.1074/jbc.274.51.36513;
RA Komuro A., Saeki M., Kato S.;
RT "Association of two nuclear proteins, Npw38 and NpwBP, via the interaction
RT between the WW domain and a novel proline-rich motif containing glycine and
RT arginine.";
RL J. Biol. Chem. 274:36513-36519(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11375989; DOI=10.1074/jbc.m103142200;
RA Craggs G., Finan P.M., Lawson D., Wingfield J., Perera T., Gadher S.,
RA Totty N.F., Kellie S.;
RT "A nuclear SH3 domain-binding protein that colocalizes with mRNA splicing
RT factors and intermediate filament-containing perinuclear networks.";
RL J. Biol. Chem. 276:30552-30560(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Muscle, and Placenta;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14640981; DOI=10.1042/bj20030950;
RA Llorian M., Beullens M., Andres I., Ortiz J.M., Bollen M.;
RT "SIPP1, a novel pre-mRNA splicing factor and interactor of protein
RT phosphatase-1.";
RL Biochem. J. 378:229-238(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-283, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP 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 INTERACTION WITH WBP4.
RX PubMed=19592703; DOI=10.1074/jbc.m109.024828;
RA Huang X., Beullens M., Zhang J., Zhou Y., Nicolaescu E., Lesage B., Hu Q.,
RA Wu J., Bollen M., Shi Y.;
RT "Structure and function of the two tandem WW domains of the pre-mRNA
RT splicing factor FBP21 (formin-binding protein 21).";
RL J. Biol. Chem. 284:25375-25387(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-353; SER-361 AND
RP SER-364, AND 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13, 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 [10]
RP INTERACTION WITH PQBP1.
RX PubMed=20410308; DOI=10.1074/jbc.m109.084525;
RA Tapia V.E., Nicolaescu E., McDonald C.B., Musi V., Oka T., Inayoshi Y.,
RA Satteson A.C., Mazack V., Humbert J., Gaffney C.J., Beullens M.,
RA Schwartz C.E., Landgraf C., Volkmer R., Pastore A., Farooq A., Bollen M.,
RA Sudol M.;
RT "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome
RT protein PQBP1 affects its binding activity and deregulates pre-mRNA
RT splicing.";
RL J. Biol. Chem. 285:19391-19401(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP 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 [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-237; SER-279; SER-283;
RP SER-353; SER-361 AND SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-237 AND SER-600, AND
RP 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-361 AND SER-364, 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-557 AND LYS-572, 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).
RN [18]
RP VARIANTS VCTRL VAL-57; 94-ARG--LEU-641 DEL; 162-GLN--LEU-641 DEL AND
RP 230-ARG--LEU-641 DEL.
RX PubMed=33276377; DOI=10.1093/hmg/ddaa258;
RA Martin E.M.M.A., Enriquez A., Sparrow D.B., Humphreys D.T.,
RA McInerney-Leo A.M., Leo P.J., Duncan E.L., Iyer K.R., Greasby J.A., Ip E.,
RA Giannoulatou E., Sheng D., Wohler E., Dimartino C., Amiel J., Capri Y.,
RA Lehalle D., Mory A., Wilnai Y., Lebenthal Y., Gharavi A.G., Krzemien G.G.,
RA Miklaszewska M., Steiner R.D., Raggio C., Blank R., Baris Feldman H.,
RA Milo Rasouly H., Sobreira N.L.M., Jobling R., Gordon C.T., Giampietro P.F.,
RA Dunwoodie S.L., Chapman G.;
RT "Heterozygous loss of WBP11 function causes multiple congenital defects in
RT humans and mice.";
RL Hum. Mol. Genet. 29:3662-3678(2020).
CC -!- FUNCTION: Activates pre-mRNA splicing. May inhibit PP1 phosphatase
CC activity. {ECO:0000269|PubMed:10593949, ECO:0000269|PubMed:11375989,
CC ECO:0000269|PubMed:14640981}.
CC -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC (By similarity).
CC Interacts via the PGR motif with PQBP1 in the nucleus. Interacts with
CC the WW domains of WBP4. {ECO:0000250, ECO:0000269|PubMed:10593949,
CC ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:20410308}.
CC -!- INTERACTION:
CC Q9Y2W2; Q49AR2: C5orf22; NbExp=5; IntAct=EBI-714455, EBI-746224;
CC Q9Y2W2; O95400: CD2BP2; NbExp=2; IntAct=EBI-714455, EBI-768015;
CC Q9Y2W2; P06241: FYN; NbExp=3; IntAct=EBI-714455, EBI-515315;
CC Q9Y2W2; P62993: GRB2; NbExp=4; IntAct=EBI-714455, EBI-401755;
CC Q9Y2W2; Q96EZ8: MCRS1; NbExp=5; IntAct=EBI-714455, EBI-348259;
CC Q9Y2W2; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-714455, EBI-10288852;
CC Q9Y2W2; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-714455, EBI-10269566;
CC Q9Y2W2; Q15365: PCBP1; NbExp=2; IntAct=EBI-714455, EBI-946095;
CC Q9Y2W2; P62136: PPP1CA; NbExp=4; IntAct=EBI-714455, EBI-357253;
CC Q9Y2W2; O60828: PQBP1; NbExp=11; IntAct=EBI-714455, EBI-713867;
CC Q9Y2W2; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-714455, EBI-11984663;
CC Q9Y2W2; Q15436: SEC23A; NbExp=3; IntAct=EBI-714455, EBI-81088;
CC Q9Y2W2; Q96BS2: TESC; NbExp=3; IntAct=EBI-714455, EBI-740653;
CC Q9Y2W2; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-714455, EBI-3650647;
CC Q9Y2W2; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-714455, EBI-7353612;
CC Q9Y2W2; PRO_0000045603 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-714455, EBI-6927928;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly located in
CC the nucleus with granular heterogeneous distribution. Excluded from
CC nucleoli in interphase cells, distributed throughout cytoplasm in
CC dividing cells. Colocalized with SC35 and U2B in the nucleus. In the
CC cytoplasm, associates with the intermediate filament protein vimentin.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the heart,
CC pancreas, kidney skeletal muscle, placenta and brain (at protein
CC level). Weakly expressed in liver and lung.
CC {ECO:0000269|PubMed:11375989}.
CC -!- DISEASE: Vertebral, cardiac, tracheoesophageal, renal, and limb defects
CC (VCTRL) [MIM:619227]: An autosomal dominant disorder with incomplete
CC penetrance and variable expressivity, characterized by cardiac,
CC vertebral, tracheo-esophageal, renal and limb defects. Some patients
CC also exhibit craniofacial abnormalities. {ECO:0000269|PubMed:33276377}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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DR EMBL; AB029309; BAA88410.1; -; mRNA.
DR EMBL; AF118023; AAD30425.1; -; mRNA.
DR EMBL; BC001621; AAH01621.1; -; mRNA.
DR EMBL; BC016441; AAH16441.2; -; mRNA.
DR EMBL; BC023532; AAH23532.1; -; mRNA.
DR CCDS; CCDS8666.1; -.
DR RefSeq; NP_057396.1; NM_016312.2.
DR PDB; 7ABF; EM; 3.90 A; X=1-641.
DR PDB; 7ABG; EM; 7.80 A; X=1-641.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; Q9Y2W2; -.
DR SMR; Q9Y2W2; -.
DR BioGRID; 119702; 143.
DR CORUM; Q9Y2W2; -.
DR ELM; Q9Y2W2; -.
DR IntAct; Q9Y2W2; 50.
DR MINT; Q9Y2W2; -.
DR STRING; 9606.ENSP00000261167; -.
DR GlyGen; Q9Y2W2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2W2; -.
DR MetOSite; Q9Y2W2; -.
DR PhosphoSitePlus; Q9Y2W2; -.
DR BioMuta; WBP11; -.
DR DMDM; 74735242; -.
DR EPD; Q9Y2W2; -.
DR jPOST; Q9Y2W2; -.
DR MassIVE; Q9Y2W2; -.
DR MaxQB; Q9Y2W2; -.
DR PaxDb; Q9Y2W2; -.
DR PeptideAtlas; Q9Y2W2; -.
DR PRIDE; Q9Y2W2; -.
DR ProteomicsDB; 85915; -.
DR Antibodypedia; 23669; 124 antibodies from 22 providers.
DR DNASU; 51729; -.
DR Ensembl; ENST00000261167.7; ENSP00000261167.2; ENSG00000084463.8.
DR GeneID; 51729; -.
DR KEGG; hsa:51729; -.
DR MANE-Select; ENST00000261167.7; ENSP00000261167.2; NM_016312.3; NP_057396.1.
DR UCSC; uc001rci.4; human.
DR CTD; 51729; -.
DR DisGeNET; 51729; -.
DR GeneCards; WBP11; -.
DR HGNC; HGNC:16461; WBP11.
DR HPA; ENSG00000084463; Low tissue specificity.
DR MalaCards; WBP11; -.
DR MIM; 618083; gene.
DR MIM; 619227; phenotype.
DR neXtProt; NX_Q9Y2W2; -.
DR OpenTargets; ENSG00000084463; -.
DR PharmGKB; PA38144; -.
DR VEuPathDB; HostDB:ENSG00000084463; -.
DR eggNOG; KOG4672; Eukaryota.
DR GeneTree; ENSGT01040000240567; -.
DR HOGENOM; CLU_028337_1_0_1; -.
DR InParanoid; Q9Y2W2; -.
DR OMA; NKEPPGV; -.
DR OrthoDB; 1304995at2759; -.
DR PhylomeDB; Q9Y2W2; -.
DR TreeFam; TF323226; -.
DR PathwayCommons; Q9Y2W2; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9Y2W2; -.
DR BioGRID-ORCS; 51729; 619 hits in 1079 CRISPR screens.
DR ChiTaRS; WBP11; human.
DR GeneWiki; WBP11; -.
DR GenomeRNAi; 51729; -.
DR Pharos; Q9Y2W2; Tbio.
DR PRO; PR:Q9Y2W2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y2W2; protein.
DR Bgee; ENSG00000084463; Expressed in sural nerve and 204 other tissues.
DR ExpressionAtlas; Q9Y2W2; baseline and differential.
DR Genevisible; Q9Y2W2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR019007; WW_dom-bd_prot_11.
DR PANTHER; PTHR13361; PTHR13361; 1.
DR Pfam; PF09429; Wbp11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Disease variant; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; rRNA processing; Ubl conjugation.
FT CHAIN 1..641
FT /note="WW domain-binding protein 11"
FT /id="PRO_0000065945"
FT REGION 1..45
FT /note="Required for nuclear import"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..221
FT /note="Interaction with PP1"
FT /evidence="ECO:0000250"
FT REGION 236..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..310
FT /note="Interaction with PP1"
FT /evidence="ECO:0000250"
FT REGION 587..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..133
FT /evidence="ECO:0000255"
FT MOTIF 455..466
FT /note="PGR"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..364
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 192
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 236
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q923D5"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 565
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q923D5"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 557
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 57
FT /note="M -> V (in VCTRL; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33276377"
FT /id="VAR_085325"
FT VARIANT 94..641
FT /note="Missing (in VCTRL)"
FT /evidence="ECO:0000269|PubMed:33276377"
FT /id="VAR_085326"
FT VARIANT 162..641
FT /note="Missing (in VCTRL)"
FT /evidence="ECO:0000269|PubMed:33276377"
FT /id="VAR_085327"
FT VARIANT 230..641
FT /note="Missing (in VCTRL)"
FT /evidence="ECO:0000269|PubMed:33276377"
FT /id="VAR_085328"
FT MUTAGEN 192
FT /note="R->A: Loss of PQBP1-binding; when associated with A-
FT 197 and A-198."
FT /evidence="ECO:0000269|PubMed:10593949"
FT MUTAGEN 197
FT /note="R->A: Loss of PQBP1-binding; when associated with A-
FT 192 and A-198."
FT /evidence="ECO:0000269|PubMed:10593949"
FT MUTAGEN 198
FT /note="K->A: Loss of PQBP1-binding; when associated with A-
FT 192 and A-197."
FT /evidence="ECO:0000269|PubMed:10593949"
SQ SEQUENCE 641 AA; 69998 MW; C94F9687D132CE77 CRC64;
MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP KQIIRDMEKL
DEMEFNPVQQ PQLNEKVLKD KRKKLRETFE RILRLYEKEN PDIYKELRKL EVEYEQKRAQ
LSQYFDAVKN AQHVEVESIP LPDMPHAPSN ILIQDIPLPG AQPPSILKKT SAYGPPTRAV
SILPLLGHGV PRLPPGRKPP GPPPGPPPPQ VVQMYGRKVG FALDLPPRRR DEDMLYSPEL
AQRGHDDDVS STSEDDGYPE DMDQDKHDDS TDDSDTDKSD GESDGDEFVH RDNGERDNNE
EKKSGLSVRF ADMPGKSRKK KKNMKELTPL QAMMLRMAGQ EIPEEGREVE EFSEDDDEDD
SDDSEAEKQS QKQHKEESHS DGTSTASSQQ QAPPQSVPPS QIQAPPMPGP PPLGPPPAPP
LRPPGPPTGL PPGPPPGAPP FLRPPGMPGL RGPLPRLLPP GPPPGRPPGP PPGPPPGLPP
GPPPRGPPPR LPPPAPPGIP PPRPGMMRPP LVPPLGPAPP GLFPPAPLPN PGVLSAPPNL
IQRPKADDTS AATIEKKATA TISAKPQITN PKAEITRFVP TALRVRRENK GATAAPQRKS
EDDSAVPLAK AAPKSGPSVP VSVQTKDDVY EAFMKEMEGL L
