ID PCGF2_HUMAN Reviewed; 344 AA. AC P35227; A6NGD8; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 211. DE RecName: Full=Polycomb group RING finger protein 2; DE AltName: Full=DNA-binding protein Mel-18; DE AltName: Full=RING finger protein 110; DE AltName: Full=Zinc finger protein 144; GN Name=PCGF2; Synonyms=MEL18, RNF110, ZNF144; 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]. RX PubMed=8325509; DOI=10.1016/0378-1119(93)90275-8; RA Ishida A., Asano H., Hasegawa M., Koseki H., Ono T., Yoshida M.C., RA Taniguchi M., Kanno M.; RT "Cloning and chromosome mapping of the human Mel-18 gene which encodes a RT DNA-binding protein with a new 'RING-finger' motif."; RL Gene 129:249-255(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, and 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-344, 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 IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND INTERACTION WITH CBX8; RING1 AND RP RNF2. RX PubMed=19636380; DOI=10.1371/journal.pone.0006380; RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., RA Rodriguez-Niedenfuhr M., Gil J., Peters G.; RT "Several distinct polycomb complexes regulate and co-localize on the INK4a RT tumor suppressor locus."; RL PLoS ONE 4:E6380-E6380(2009). RN [8] RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=21282530; DOI=10.1074/mcp.m110.002642; RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.; RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1 RT Complexes in mammalian cells."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [9] RP FUNCTION, AND SUBUNIT. RX PubMed=26151332; DOI=10.1038/ncomms8621; RA Taherbhoy A.M., Huang O.W., Cochran A.G.; RT "BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase."; RL Nat. Commun. 6:7621-7621(2015). RN [10] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-88, 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). RN [11] RP INVOLVEMENT IN TPFS, AND VARIANTS TPFS LEU-65 AND SER-65. RX PubMed=30343942; DOI=10.1016/j.ajhg.2018.09.012; RA Turnpenny P.D., Wright M.J., Sloman M., Caswell R., van Essen A.J., RA Gerkes E., Pfundt R., White S.M., Shaul-Lotan N., Carpenter L., RA Schaefer G.B., Fryer A., Innes A.M., Forbes K.P., Chung W.K., RA McLaughlin H., Henderson L.B., Roberts A.E., Heath K.E., RA Paumard-Hernandez B., Gener B., Fawcett K.A., Gjergja-Juraski R., RA Pilz D.T., Fry A.E.; RT "Missense mutations of the Pro65 residue of PCGF2 cause a recognizable RT syndrome associated with craniofacial, neurological, cardiovascular, and RT skeletal features."; RL Am. J. Hum. Genet. 103:786-793(2018). CC -!- FUNCTION: Transcriptional repressor. Binds specifically to the DNA CC sequence 5'-GACTNGACT-3'. Has tumor suppressor activity. May play a CC role in control of cell proliferation and/or neural cell development. CC Regulates proliferation of early T progenitor cells by maintaining CC expression of HES1. Also plays a role in antero-posterior specification CC of the axial skeleton and negative regulation of the self-renewal CC activity of hematopoietic stem cells (By similarity). Component of a CC Polycomb group (PcG) multiprotein PRC1-like complex, a complex class CC required to maintain the transcriptionally repressive state of many CC genes, including Hox genes, throughout development. PcG PRC1 complex CC acts via chromatin remodeling and modification of histones; it mediates CC monoubiquitination of histone H2A 'Lys-119', rendering chromatin CC heritably changed in its expressibility (PubMed:26151332). Within the CC PRC1-like complex, regulates RNF2 ubiquitin ligase activity CC (PubMed:26151332). {ECO:0000250|UniProtKB:P23798, CC ECO:0000269|PubMed:26151332}. CC -!- SUBUNIT: Exists as both a monomer and homodimer (By similarity). CC Component of a PRC1-like complex (PubMed:19636380, PubMed:21282530, CC PubMed:26151332). Interacts with CBX8, RING1 and RNF2 CC (PubMed:19636380). Interacts with CBX7 (By similarity). Interacts with CC PHC2 (By similarity). {ECO:0000250|UniProtKB:P23798, CC ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530}. CC -!- INTERACTION: CC P35227; O95503: CBX6; NbExp=3; IntAct=EBI-2129767, EBI-3951758; CC P35227; O95931: CBX7; NbExp=6; IntAct=EBI-2129767, EBI-3923843; CC P35227; Q9HC52: CBX8; NbExp=11; IntAct=EBI-2129767, EBI-712912; CC P35227; Q9HCE1: MOV10; NbExp=2; IntAct=EBI-2129767, EBI-1055820; CC P35227; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-2129767, EBI-448407; CC P35227; P78364: PHC1; NbExp=11; IntAct=EBI-2129767, EBI-725403; CC P35227; Q8IXK0: PHC2; NbExp=8; IntAct=EBI-2129767, EBI-713786; CC P35227; Q06587: RING1; NbExp=13; IntAct=EBI-2129767, EBI-752313; CC P35227; Q99496: RNF2; NbExp=16; IntAct=EBI-2129767, EBI-722416; CC P35227; P32856-2: STX2; NbExp=3; IntAct=EBI-2129767, EBI-11956649; CC P35227; Q12933: TRAF2; NbExp=3; IntAct=EBI-2129767, EBI-355744; CC P35227; P0CG48: UBC; NbExp=2; IntAct=EBI-2129767, EBI-3390054; CC P35227; P51784: USP11; NbExp=5; IntAct=EBI-2129767, EBI-306876; CC P35227; Q93009: USP7; NbExp=5; IntAct=EBI-2129767, EBI-302474; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}. CC -!- TISSUE SPECIFICITY: Detected in all tissues examined with high CC expression found in placenta lung and kidney and low expression, in CC liver, pancreas and skeletal muscle. CC -!- PTM: Phosphorylated. Homodimer formation is regulated by CC phosphorylation with only unphosphorylated proteins forming homodimers. CC {ECO:0000250|UniProtKB:P23798}. CC -!- DISEASE: Turnpenny-Fry syndrome (TPFS) [MIM:618371]: A syndrome CC characterized by facial dysmorphism, intellectual disability, feeding CC problems, impaired growth, and a range of brain, cardiovascular, and CC skeletal abnormalities. Craniofacial features include frontal bossing, CC sparse hair, malar hypoplasia, small palpebral fissures and oral stoma, CC and dysplastic ears. {ECO:0000269|PubMed:30343942}. Note=The disease is CC caused by variants affecting the gene represented 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; D13969; BAA03074.1; -; mRNA. DR EMBL; BX647429; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC006449; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471152; EAW60528.1; -; Genomic_DNA. DR EMBL; BC004858; AAH04858.1; -; mRNA. DR EMBL; BC024255; AAH24255.1; -; mRNA. DR CCDS; CCDS32638.1; -. DR PIR; JN0717; JN0717. DR RefSeq; NP_009075.1; NM_007144.2. DR RefSeq; XP_005257697.1; XM_005257640.2. DR RefSeq; XP_005257698.1; XM_005257641.4. DR RefSeq; XP_005257699.1; XM_005257642.3. DR RefSeq; XP_016880505.1; XM_017025016.1. DR AlphaFoldDB; P35227; -. DR SMR; P35227; -. DR BioGRID; 113497; 90. DR ComplexPortal; CPX-2260; Non-canonical polycomb repressive complex 1.2, RING1-YAF2 variant. DR ComplexPortal; CPX-2276; Non-canonical polycomb repressive complex 1.2, RNF2-RYBP variant. DR ComplexPortal; CPX-2280; Non-canonical polycomb repressive complex 1.2, RNF2-YAF2 variant. DR ComplexPortal; CPX-2480; Polycomb repressive complex 1, RING1-PCGF2-CBX2-PHC3 variant. DR ComplexPortal; CPX-2594; Polycomb repressive complex 1, RING1-PCGF2-CBX4-PHC1 variant. DR ComplexPortal; CPX-2598; Polycomb repressive complex 1, RING1-PCGF2-CBX6-PHC3 variant. DR ComplexPortal; CPX-2600; Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC1 variant. DR ComplexPortal; CPX-2601; Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC2 variant. DR ComplexPortal; CPX-2605; Polycomb repressive complex 1, RING1-PCGF2-CBX2-PHC1 variant. DR ComplexPortal; CPX-2609; Polycomb repressive complex 1, RING1-PCGF2-CBX2-PHC2 variant. DR ComplexPortal; CPX-2613; Polycomb repressive complex 1, RING1-PCGF2-CBX4-PHC2 variant. DR ComplexPortal; CPX-2615; Polycomb repressive complex 1, RING1-PCGF2-CBX4-PHC3 variant. DR ComplexPortal; CPX-2616; Polycomb repressive complex 1, RING1-PCGF2-CBX6-PHC1 variant. DR ComplexPortal; CPX-2617; Polycomb repressive complex 1, RING1-PCGF2-CBX6-PHC2 variant. DR ComplexPortal; CPX-2619; Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC3 variant. DR ComplexPortal; CPX-2621; Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC1 variant. DR ComplexPortal; CPX-2622; Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC2 variant. DR ComplexPortal; CPX-2623; Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC3 variant. DR ComplexPortal; CPX-2630; Non-canonical polycomb repressive complex 1.2, RING1-RYBP variant. DR ComplexPortal; CPX-7519; Polycomb repressive complex 1, RING2-PCGF2-CBX2-PHC1 variant. DR ComplexPortal; CPX-7522; Polycomb repressive complex 1, RING2-PCGF2-CBX2-PHC2 variant. DR ComplexPortal; CPX-7523; Polycomb repressive complex 1, RING2-PCGF2-CBX2-PHC3 variant. DR ComplexPortal; CPX-7524; Polycomb repressive complex 1, RING2-PCGF2-CBX4-PHC1 variant. DR ComplexPortal; CPX-7525; Polycomb repressive complex 1, RING2-PCGF2-CBX4-PHC3 variant. DR ComplexPortal; CPX-7526; Polycomb repressive complex 1, RING2-PCGF2-CBX4-PHC2 variant. DR ComplexPortal; CPX-7527; Polycomb repressive complex 1, RING2-PCGF2-CBX6-PHC1 variant. DR ComplexPortal; CPX-7528; Polycomb repressive complex 1, RING2-PCGF2-CBX6-PHC2 variant. DR ComplexPortal; CPX-7529; Polycomb repressive complex 1, RING2-PCGF2-CBX6-PHC3 variant. DR ComplexPortal; CPX-7530; Polycomb repressive complex 1, RING2-PCGF2-CBX7-PHC1 variant. DR ComplexPortal; CPX-7531; Polycomb repressive complex 1, RING2-PCGF2-CBX7-PHC2 variant. DR ComplexPortal; CPX-7532; Polycomb repressive complex 1, RING2-PCGF2-CBX7-PHC3 variant. DR ComplexPortal; CPX-7533; Polycomb repressive complex 1, RING2-PCGF2-CBX8-PHC1 variant. DR ComplexPortal; CPX-7534; Polycomb repressive complex 1, RING2-PCGF2-CBX8-PHC2 variant. DR ComplexPortal; CPX-7535; Polycomb repressive complex 1, RING2-PCGF2-CBX8-PHC3 variant. DR DIP; DIP-41880N; -. DR IntAct; P35227; 49. DR MINT; P35227; -. DR STRING; 9606.ENSP00000482063; -. DR GlyGen; P35227; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P35227; -. DR PhosphoSitePlus; P35227; -. DR BioMuta; PCGF2; -. DR DMDM; 462585; -. DR EPD; P35227; -. DR jPOST; P35227; -. DR MassIVE; P35227; -. DR MaxQB; P35227; -. DR PaxDb; 9606-ENSP00000482063; -. DR PeptideAtlas; P35227; -. DR ProteomicsDB; 54992; -. DR Pumba; P35227; -. DR Antibodypedia; 72907; 294 antibodies from 35 providers. DR DNASU; 7703; -. DR Ensembl; ENST00000610440.1; ENSP00000478517.1; ENSG00000278644.2. DR Ensembl; ENST00000611883.4; ENSP00000478970.1; ENSG00000277258.5. DR Ensembl; ENST00000616199.4; ENSP00000482063.1; ENSG00000277258.5. DR Ensembl; ENST00000620225.5; ENSP00000482815.1; ENSG00000277258.5. DR Ensembl; ENST00000631566.1; ENSP00000488872.1; ENSG00000278644.2. DR Ensembl; ENST00000631610.1; ENSP00000488868.1; ENSG00000278644.2. DR GeneID; 7703; -. DR KEGG; hsa:7703; -. DR MANE-Select; ENST00000620225.5; ENSP00000482815.1; NM_007144.3; NP_009075.1. DR UCSC; uc002hqp.2; human. DR AGR; HGNC:12929; -. DR CTD; 7703; -. DR DisGeNET; 7703; -. DR GeneCards; PCGF2; -. DR HGNC; HGNC:12929; PCGF2. DR HPA; ENSG00000277258; Low tissue specificity. DR MalaCards; PCGF2; -. DR MIM; 600346; gene. DR MIM; 618371; phenotype. DR neXtProt; NX_P35227; -. DR OpenTargets; ENSG00000277258; -. DR PharmGKB; PA37516; -. DR VEuPathDB; HostDB:ENSG00000277258; -. DR eggNOG; KOG2660; Eukaryota. DR GeneTree; ENSGT00940000159730; -. DR HOGENOM; CLU_046427_0_0_1; -. DR InParanoid; P35227; -. DR OMA; NCHQMQP; -. DR OrthoDB; 460116at2759; -. DR PhylomeDB; P35227; -. DR TreeFam; TF324206; -. DR PathwayCommons; P35227; -. DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins. DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis. DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6. DR SignaLink; P35227; -. DR SIGNOR; P35227; -. DR BioGRID-ORCS; 7703; 20 hits in 1204 CRISPR screens. DR ChiTaRS; PCGF2; human. DR GeneWiki; PCGF2; -. DR GenomeRNAi; 7703; -. DR Pharos; P35227; Tbio. DR PRO; PR:P35227; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P35227; Protein. DR Bgee; ENSG00000277258; Expressed in cortical plate and 96 other cell types or tissues. DR ExpressionAtlas; P35227; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB. DR GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB. DR GO; GO:0001739; C:sex chromatin; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central. DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl. DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB. DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR CDD; cd17164; RAWUL_PCGF2; 1. DR CDD; cd16736; RING-HC_PCGF4; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR032443; RAWUL. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR10825:SF31; POLYCOMB GROUP RING FINGER PROTEIN 2; 1. DR PANTHER; PTHR10825; RING FINGER DOMAIN-CONTAINING, POLYCOMB GROUP COMPONENT; 1. DR Pfam; PF16207; RAWUL; 1. DR Pfam; PF13923; zf-C3HC4_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; P35227; HS. PE 1: Evidence at protein level; KW Disease variant; DNA-binding; Intellectual disability; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..344 FT /note="Polycomb group RING finger protein 2" FT /id="PRO_0000055984" FT ZN_FING 18..57 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 240..344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 81..95 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 241..258 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 265..292 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 301..333 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 344 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT CROSSLNK 51 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 88 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 65 FT /note="P -> L (in TPFS)" FT /evidence="ECO:0000269|PubMed:30343942" FT /id="VAR_082085" FT VARIANT 65 FT /note="P -> S (in TPFS)" FT /evidence="ECO:0000269|PubMed:30343942" FT /id="VAR_082086" SQ SEQUENCE 344 AA; 37788 MW; A910BCD4C0CE9927 CRC64; MHRTTRIKIT ELNPHLMCAL CGGYFIDATT IVECLHSFCK TCIVRYLETN KYCPMCDVQV HKTRPLLSIR SDKTLQDIVY KLVPGLFKDE MKRRRDFYAA YPLTEVPNGS NEDRGEVLEQ EKGALSDDEI VSLSIEFYEG ARDRDEKKGP LENGDGDKEK TGVRFLRCPA AMTVMHLAKF LRNKMDVPSK YKVEVLYEDE PLKEYYTLMD IAYIYPWRRN GPLPLKYRVQ PACKRLTLAT VPTPSEGTNT SGASECESVS DKAPSPATLP ATSSSLPSPA TPSHGSPSSH GPPATHPTSP TPPSTASGAT TAANGGSLNC LQTPSSTSRG RKMTVNGAPV PPLT //