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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //