ID GT2D1_HUMAN Reviewed; 959 AA. AC Q9UHL9; O95444; Q6DSU6; Q75MX7; Q86UM3; Q8WVC4; Q9UHK8; Q9UI91; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 30-NOV-2016, entry version 159. DE RecName: Full=General transcription factor II-I repeat domain-containing protein 1; DE Short=GTF2I repeat domain-containing protein 1; DE AltName: Full=General transcription factor III; DE AltName: Full=MusTRD1/BEN; DE AltName: Full=Muscle TFII-I repeat domain-containing protein 1; DE AltName: Full=Slow-muscle-fiber enhancer-binding protein; DE AltName: Full=USE B1-binding protein; DE AltName: Full=Williams-Beuren syndrome chromosomal region 11 protein; DE AltName: Full=Williams-Beuren syndrome chromosomal region 12 protein; GN Name=GTF2IRD1; GN Synonyms=CREAM1, GTF3, MUSTRD1, RBAP2, WBSCR11, WBSCR12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Muscle; RX PubMed=9774679; DOI=10.1128/MCB.18.11.6641; RA O'Mahoney J.V., Guven K.L., Lin J., Joya J.E., Robinson C.S., RA Wade R.P., Hardeman E.C.; RT "Identification of a novel slow-muscle-fiber enhancer binding protein, RT MUSTRD1."; RL Mol. Cell. Biol. 18:6641-6652(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Colon carcinoma; RX PubMed=10198167; DOI=10.1006/geno.1999.5784; RA Osborne L.R., Campbell T., Daradich A., Scherer S.W., Tsui L.-C.; RT "Identification of a putative transcription factor gene (WBSCR11) that RT is commonly deleted in Williams-Beuren syndrome."; RL Genomics 57:279-284(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=10573005; DOI=10.1038/sj.ejhg.5200396; RA Tassabehji M., Carette M., Wilmot C., Donnai D., Read A.P., RA Metcalfe K.; RT "A transcription factor involved in skeletal muscle gene expression is RT deleted in patients with Williams syndrome."; RL Eur. J. Hum. Genet. 7:737-747(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-652. RX PubMed=10575229; RA Franke Y., Peoples R.J., Francke U.; RT "Identification of GTF2IRD1, a putative transcription factor within RT the Williams-Beuren syndrome deletion at 7q11.23."; RL Cytogenet. Cell Genet. 86:296-304(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1, RP MUTAGENESIS, AND VARIANT VAL-652. RC TISSUE=Cervix carcinoma, Fetal spleen, and Placenta; RX PubMed=10642537; DOI=10.1042/bj3450749; RA Yan X., Zhao X., Qian M., Guo N., Gong X., Zhu X.; RT "Characterization and gene structure of a novel retinoblastoma- RT protein-associated protein similar to the transcription regulator RT TFII-I."; RL Biochem. J. 345:749-757(2000). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Cunliffe P., Hart-Holden N., Hinsley T., Sharrocks A.D., RA Tassabehji M.; RT "GTF2IRD1 represses transcription from a conserved DNA element RT upstream of three separate promoters."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP VAL-652. 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION. RX PubMed=11438732; DOI=10.1073/pnas.141222298; RA Tussie-Luna M.I., Bayarsaihan D., Ruddle F.H., Roy A.L.; RT "Repression of TFII-I-dependent transcription by nuclear exclusion."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7789-7794(2001). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION RP 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 (ISOFORM 3), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION RP BY 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION RP 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-212; LYS-225; LYS-271; RP LYS-337; LYS-436; LYS-443; LYS-579; LYS-638; LYS-684 AND LYS-787, AND RP IDENTIFICATION BY MASS 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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-443, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-212; LYS-225; LYS-271; RP LYS-308; LYS-337; LYS-436; LYS-443; LYS-638; LYS-724; LYS-787; LYS-829 RP AND LYS-889, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-271; LYS-436; LYS-443; RP LYS-638 AND LYS-724, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 RT replication stress reveals novel small ubiquitin-like modified target RT proteins and acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [19] RP STRUCTURE BY NMR OF 128-203 AND 565-877. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RSGI RUH-048 and RUH-057, a GTF2I domain in RT human."; RL Submitted (MAR-2007) to the PDB data bank. CC -!- FUNCTION: May be a transcription regulator involved in cell-cycle CC progression and skeletal muscle differentiation. May repress GTF2I CC transcriptional functions, by preventing its nuclear residency, or CC by inhibiting its transcriptional activation. May contribute to CC slow-twitch fiber type specificity during myogenesis and in CC regenerating muscles. Binds troponin I slow-muscle fiber enhancer CC (USE B1). Binds specifically and with high affinity to the EFG CC sequences derived from the early enhancer of HOXC8 (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:11438732}. CC -!- SUBUNIT: Interacts with the retinoblastoma protein (RB1) via its CC C-terminus. {ECO:0000269|PubMed:10642537}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UHL9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UHL9-2; Sequence=VSP_003873; CC Note=Contains a phosphoserine at position 654. CC {ECO:0000244|PubMed:17525332}; CC Name=3; CC IsoId=Q9UHL9-3; Sequence=VSP_043425, VSP_003873; CC Note=Contains a phosphoserine at position 686. CC {ECO:0000244|PubMed:17525332}; CC -!- TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle, CC heart, fibroblast, bone and fetal tissues. Expressed at lower CC levels in all other tissues tested. CC -!- DEVELOPMENTAL STAGE: Highly expressed in developing and CC regenerating muscles, at the time of myofiber diversification. CC -!- DOMAIN: The N-terminal half may have an activating activity. CC -!- DISEASE: Note=GTF2IRD1 is located in the Williams-Beuren syndrome CC (WBS) critical region. WBS results from a hemizygous deletion of CC several genes on chromosome 7q11.23, thought to arise as a CC consequence of unequal crossing over between highly homologous CC low-copy repeat sequences flanking the deleted region. CC Haploinsufficiency of GTF2IRD1 may be the cause of certain CC cardiovascular and musculo-skeletal abnormalities observed in the CC disease. CC -!- SIMILARITY: Belongs to the TFII-I family. {ECO:0000255|PROSITE- CC ProRule:PRU00484}. CC -!- SIMILARITY: Contains 5 GTF2I-like repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00484}. 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; AF118270; AAD14687.2; -; mRNA. DR EMBL; AF104923; AAD27668.1; -; mRNA. DR EMBL; AF151354; AAF19786.1; -; mRNA. DR EMBL; AF156489; AAF17358.1; -; mRNA. DR EMBL; AF089107; AAF21796.1; -; mRNA. DR EMBL; AY648295; AAT68469.1; -; mRNA. DR EMBL; AC004851; AAS00362.1; -; Genomic_DNA. DR EMBL; AC005015; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005231; AAP21877.1; -; Genomic_DNA. DR EMBL; BC018136; AAH18136.1; -; mRNA. DR CCDS; CCDS47613.1; -. [Q9UHL9-2] DR CCDS; CCDS5571.1; -. [Q9UHL9-1] DR CCDS; CCDS56492.1; -. [Q9UHL9-3] DR RefSeq; NP_001186136.1; NM_001199207.1. [Q9UHL9-3] DR RefSeq; NP_005676.3; NM_005685.3. [Q9UHL9-2] DR RefSeq; NP_057412.1; NM_016328.2. [Q9UHL9-1] DR RefSeq; XP_016868293.1; XM_017012804.1. [Q9UHL9-2] DR UniGene; Hs.647056; -. DR PDB; 2D99; NMR; -; A=128-203. DR PDB; 2DN5; NMR; -; A=802-877. DR PDB; 2DZQ; NMR; -; A=565-650. DR PDB; 2DZR; NMR; -; A=705-790. DR PDBsum; 2D99; -. DR PDBsum; 2DN5; -. DR PDBsum; 2DZQ; -. DR PDBsum; 2DZR; -. DR ProteinModelPortal; Q9UHL9; -. DR SMR; Q9UHL9; -. DR BioGrid; 114939; 27. DR IntAct; Q9UHL9; 12. DR MINT; MINT-1209004; -. DR STRING; 9606.ENSP00000397566; -. DR iPTMnet; Q9UHL9; -. DR PhosphoSitePlus; Q9UHL9; -. DR BioMuta; GTF2IRD1; -. DR DMDM; 21263630; -. DR PaxDb; Q9UHL9; -. DR PeptideAtlas; Q9UHL9; -. DR PRIDE; Q9UHL9; -. DR DNASU; 9569; -. DR Ensembl; ENST00000265755; ENSP00000265755; ENSG00000006704. [Q9UHL9-1] DR Ensembl; ENST00000424337; ENSP00000408477; ENSG00000006704. [Q9UHL9-2] DR Ensembl; ENST00000455841; ENSP00000397566; ENSG00000006704. [Q9UHL9-3] DR GeneID; 9569; -. DR KEGG; hsa:9569; -. DR UCSC; uc032zrv.2; human. [Q9UHL9-1] DR CTD; 9569; -. DR DisGeNET; 9569; -. DR GeneCards; GTF2IRD1; -. DR HGNC; HGNC:4661; GTF2IRD1. DR HPA; HPA044254; -. DR MalaCards; GTF2IRD1; -. DR MIM; 604318; gene. DR neXtProt; NX_Q9UHL9; -. DR OpenTargets; ENSG00000006704; -. DR Orphanet; 904; Williams syndrome. DR PharmGKB; PA29047; -. DR eggNOG; ENOG410IEPZ; Eukaryota. DR eggNOG; ENOG41100H8; LUCA. DR GeneTree; ENSGT00530000063863; -. DR HOGENOM; HOG000112829; -. DR HOVERGEN; HBG051855; -. DR InParanoid; Q9UHL9; -. DR KO; K03121; -. DR OMA; HFVIKRM; -. DR OrthoDB; EOG091G019P; -. DR PhylomeDB; Q9UHL9; -. DR TreeFam; TF352524; -. DR BioCyc; ZFISH:ENSG00000006704-MONOMER; -. DR EvolutionaryTrace; Q9UHL9; -. DR GeneWiki; GTF2IRD1; -. DR GenomeRNAi; 9569; -. DR PRO; PR:Q9UHL9; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000006704; -. DR CleanEx; HS_GTF2IRD1; -. DR ExpressionAtlas; Q9UHL9; baseline and differential. DR Genevisible; Q9UHL9; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; NAS:UniProtKB. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:UniProtKB. DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0014886; P:transition between slow and fast fiber; IEA:Ensembl. DR Gene3D; 3.90.1460.10; -; 5. DR InterPro; IPR004212; GTF2I. DR InterPro; IPR016659; TF_II-I. DR Pfam; PF02946; GTF2I; 5. DR PIRSF; PIRSF016441; TF_II-I; 1. DR SUPFAM; SSF117773; SSF117773; 5. DR PROSITE; PS51139; GTF2I; 5. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Developmental protein; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Transcription; Transcription regulation; Ubl conjugation; KW Williams-Beuren syndrome. FT CHAIN 1 959 General transcription factor II-I repeat FT domain-containing protein 1. FT /FTId=PRO_0000083870. FT REPEAT 119 213 GTF2I-like 1. FT REPEAT 342 436 GTF2I-like 2. FT REPEAT 556 650 GTF2I-like 3. FT REPEAT 696 790 GTF2I-like 4. FT REPEAT 793 887 GTF2I-like 5. FT MOTIF 898 905 Nuclear localization signal. FT {ECO:0000255}. FT COMPBIAS 906 930 Ser-rich. FT MOD_RES 448 448 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 271 271 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 308 308 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25772364}. FT CROSSLNK 337 337 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 436 436 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 443 443 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25114211, FT ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 579 579 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 638 638 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 684 684 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25755297, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 787 787 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25772364}. FT CROSSLNK 829 829 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25772364}. FT CROSSLNK 889 889 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25772364}. FT VAR_SEQ 89 89 R -> LSAAQHRAATSQLEGRVVRRVLTVASRALCPTG FT (in isoform 3). {ECO:0000303|Ref.6}. FT /FTId=VSP_043425. FT VAR_SEQ 656 670 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:10198167, FT ECO:0000303|PubMed:10575229, FT ECO:0000303|PubMed:9774679, FT ECO:0000303|Ref.6}. FT /FTId=VSP_003873. FT VARIANT 652 652 M -> V (in dbSNP:rs2301895). FT {ECO:0000269|PubMed:10575229, FT ECO:0000269|PubMed:10642537, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_013446. FT MUTAGEN 898 959 Missing: Cytoplasmic localization. FT {ECO:0000269|PubMed:10642537}. FT CONFLICT 111 111 G -> S (in Ref. 1; AAD14687 and 2; FT AAD27668). {ECO:0000305}. FT CONFLICT 378 378 R -> Q (in Ref. 5; AAF21796). FT {ECO:0000305}. FT HELIX 128 144 {ECO:0000244|PDB:2D99}. FT HELIX 154 159 {ECO:0000244|PDB:2D99}. FT TURN 161 163 {ECO:0000244|PDB:2D99}. FT STRAND 164 168 {ECO:0000244|PDB:2D99}. FT TURN 178 180 {ECO:0000244|PDB:2D99}. FT HELIX 183 192 {ECO:0000244|PDB:2D99}. FT TURN 193 195 {ECO:0000244|PDB:2D99}. FT STRAND 197 203 {ECO:0000244|PDB:2D99}. FT HELIX 565 580 {ECO:0000244|PDB:2DZQ}. FT HELIX 591 596 {ECO:0000244|PDB:2DZQ}. FT TURN 598 600 {ECO:0000244|PDB:2DZQ}. FT STRAND 601 605 {ECO:0000244|PDB:2DZQ}. FT TURN 615 617 {ECO:0000244|PDB:2DZQ}. FT HELIX 620 628 {ECO:0000244|PDB:2DZQ}. FT TURN 629 632 {ECO:0000244|PDB:2DZQ}. FT STRAND 634 638 {ECO:0000244|PDB:2DZQ}. FT HELIX 640 642 {ECO:0000244|PDB:2DZQ}. FT HELIX 705 721 {ECO:0000244|PDB:2DZR}. FT HELIX 731 736 {ECO:0000244|PDB:2DZR}. FT STRAND 738 745 {ECO:0000244|PDB:2DZR}. FT HELIX 755 757 {ECO:0000244|PDB:2DZR}. FT HELIX 760 769 {ECO:0000244|PDB:2DZR}. FT TURN 770 772 {ECO:0000244|PDB:2DZR}. FT STRAND 774 777 {ECO:0000244|PDB:2DZR}. FT HELIX 802 817 {ECO:0000244|PDB:2DN5}. FT HELIX 828 833 {ECO:0000244|PDB:2DN5}. FT STRAND 837 842 {ECO:0000244|PDB:2DN5}. FT STRAND 852 854 {ECO:0000244|PDB:2DN5}. FT HELIX 857 864 {ECO:0000244|PDB:2DN5}. FT TURN 865 869 {ECO:0000244|PDB:2DN5}. FT STRAND 871 876 {ECO:0000244|PDB:2DN5}. SQ SEQUENCE 959 AA; 106057 MW; 7DA3097879701540 CRC64; MALLGKRCDV PTNGCGPDRW NSAFTRKDEI ITSLVSALDS MCSALSKLNA EVACVAVHDE SAFVVGTEKG RMFLNARKEL QSDFLRFCRG PPWKDPEAEH PKKVQRGEGG GRSLPRSSLE HGSDVYLLRK MVEEVFDVLY SEALGRASVV PLPYERLLRE PGLLAVQGLP EGLAFRRPAE YDPKALMAIL EHSHRIRFKL KRPLEDGGRD SKALVELNGV SLIPKGSRDC GLHGQAPKVP PQDLPPTATS SSMASFLYST ALPNHAIREL KQEAPSCPLA PSDLGLSRPM PEPKATGAQD FSDCCGQKPT GPGGPLIQNV HASKRILFSI VHDKSEKWDA FIKETEDINT LRECVQILFN SRYAEALGLD HMVPVPYRKI ACDPEAVEIV GIPDKIPFKR PCTYGVPKLK RILEERHSIH FIIKRMFDER IFTGNKFTKD TTKLEPASPP EDTSAEVSRA TVLDLAGNAR SDKGSMSEDC GPGTSGELGG LRPIKIEPED LDIIQVTVPD PSPTSEEMTD SMPGHLPSED SGYGMEMLTD KGLSEDARPE ERPVEDSHGD VIRPLRKQVE LLFNTRYAKA IGISEPVKVP YSKFLMHPEE LFVVGLPEGI SLRRPNCFGI AKLRKILEAS NSIQFVIKRP ELLTEGVKEP IMDSQGTASS LGFSPPALPP ERDSGDPLVD ESLKRQGFQE NYDARLSRID IANTLREQVQ DLFNKKYGEA LGIKYPVQVP YKRIKSNPGS VIIEGLPPGI PFRKPCTFGS QNLERILAVA DKIKFTVTRP FQGLIPKPDE DDANRLGEKV ILREQVKELF NEKYGEALGL NRPVLVPYKL IRDSPDAVEV TGLPDDIPFR NPNTYDIHRL EKILKAREHV RMVIINQLQP FAEICNDAKV PAKDSSIPKR KRKRVSEGNS VSSSSSSSSS SSSNPDSVAS ANQISLVQWP MYMVDYAGLN VQLPGPLNY //