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 27-MAR-2024, entry version 205. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., Wade R.P., RA 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 is RT 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., 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; DOI=10.1159/000015322; RA Franke Y., Peoples R.J., Francke U.; RT "Identification of GTF2IRD1, a putative transcription factor within the RT 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, MUTAGENESIS, RP 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-protein- RT associated protein similar to the transcription regulator 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., Tassabehji M.; RT "GTF2IRD1 represses transcription from a conserved DNA element upstream of RT 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., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., 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., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA 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 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 project: RT 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 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 [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, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA 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 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY RP 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; LYS-337; RP LYS-436; LYS-443; LYS-579; LYS-638; LYS-684 AND LYS-787, AND IDENTIFICATION RP 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 MASS RP 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; LYS-308; RP LYS-337; LYS-436; LYS-443; LYS-638; LYS-724; LYS-787; LYS-829 AND LYS-889, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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; LYS-638 RP AND LYS-724, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-94; LYS-184; LYS-212; RP LYS-225; LYS-238; LYS-271; LYS-294; LYS-308; LYS-337; LYS-436; LYS-439; RP LYS-443; LYS-567; LYS-579; LYS-588; LYS-622; LYS-638; LYS-684; LYS-724; RP LYS-732; LYS-772; LYS-774; LYS-787; LYS-829; LYS-889 AND LYS-893, RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-638; LYS-648 AND LYS-669 (ISOFORM RP 2), SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-670; LYS-680 AND LYS-701 RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [20] 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 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 by CC inhibiting its transcriptional activation. May contribute to slow- CC twitch fiber type specificity during myogenesis and in regenerating CC muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds CC specifically and with high affinity to the EFG sequences derived from CC the early enhancer of HOXC8 (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:11438732}. CC -!- SUBUNIT: Interacts with the retinoblastoma protein (RB1) via its C- CC terminus. {ECO:0000269|PubMed:10642537}. CC -!- INTERACTION: CC Q9UHL9; Q6VMQ6: ATF7IP; NbExp=3; IntAct=EBI-372530, EBI-928732; CC Q9UHL9; Q58WW2: DCAF6; NbExp=2; IntAct=EBI-372530, EBI-2559044; CC Q9UHL9; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-372530, EBI-739467; CC Q9UHL9; Q96CB8: INTS12; NbExp=3; IntAct=EBI-372530, EBI-1049156; CC Q9UHL9; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-372530, EBI-12516603; CC Q9UHL9; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-372530, EBI-748896; CC Q9UHL9; Q13835: PKP1; NbExp=2; IntAct=EBI-372530, EBI-2513407; CC Q9UHL9; Q9UBW7: ZMYM2; NbExp=5; IntAct=EBI-372530, EBI-2797576; CC Q9UHL9; Q80W88: Homez; Xeno; NbExp=2; IntAct=EBI-372530, EBI-12516872; CC Q9UHL9; P51860: Nap1l2; Xeno; NbExp=3; IntAct=EBI-372530, EBI-12516895; CC Q9UHL9; Q9CWY3: Setd6; Xeno; NbExp=3; IntAct=EBI-372530, EBI-10768425; CC Q9UHL9; Q9JLM4: Zmym3; Xeno; NbExp=3; IntAct=EBI-372530, EBI-12517169; 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 Name=3; CC IsoId=Q9UHL9-3; Sequence=VSP_043425, VSP_003873; CC -!- TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle, heart, CC fibroblast, bone and fetal tissues. Expressed at lower levels in all CC other tissues tested. CC -!- DEVELOPMENTAL STAGE: Highly expressed in developing and regenerating CC 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 (WBS) CC critical region. WBS results from a hemizygous deletion of several CC genes on chromosome 7q11.23, thought to arise as a consequence of CC unequal crossing over between highly homologous low-copy repeat CC sequences flanking the deleted region. Haploinsufficiency of GTF2IRD1 CC may be the cause of certain cardiovascular and musculo-skeletal CC abnormalities observed in the disease. CC -!- SIMILARITY: Belongs to the TFII-I family. {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 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 AlphaFoldDB; Q9UHL9; -. DR SMR; Q9UHL9; -. DR BioGRID; 114939; 123. DR IntAct; Q9UHL9; 70. DR MINT; Q9UHL9; -. DR STRING; 9606.ENSP00000397566; -. DR CarbonylDB; Q9UHL9; -. DR iPTMnet; Q9UHL9; -. DR PhosphoSitePlus; Q9UHL9; -. DR BioMuta; GTF2IRD1; -. DR DMDM; 21263630; -. DR EPD; Q9UHL9; -. DR jPOST; Q9UHL9; -. DR MassIVE; Q9UHL9; -. DR MaxQB; Q9UHL9; -. DR PaxDb; 9606-ENSP00000397566; -. DR PeptideAtlas; Q9UHL9; -. DR ProteomicsDB; 84377; -. [Q9UHL9-1] DR ProteomicsDB; 84378; -. [Q9UHL9-2] DR ProteomicsDB; 84379; -. [Q9UHL9-3] DR Antibodypedia; 14624; 435 antibodies from 32 providers. DR DNASU; 9569; -. DR Ensembl; ENST00000265755.7; ENSP00000265755.3; ENSG00000006704.11. [Q9UHL9-1] DR Ensembl; ENST00000424337.7; ENSP00000408477.2; ENSG00000006704.11. [Q9UHL9-2] DR Ensembl; ENST00000455841.6; ENSP00000397566.2; ENSG00000006704.11. [Q9UHL9-3] DR GeneID; 9569; -. DR KEGG; hsa:9569; -. DR MANE-Select; ENST00000424337.7; ENSP00000408477.2; NM_005685.4; NP_005676.3. [Q9UHL9-2] DR UCSC; uc032zrv.2; human. [Q9UHL9-1] DR AGR; HGNC:4661; -. DR CTD; 9569; -. DR DisGeNET; 9569; -. DR GeneCards; GTF2IRD1; -. DR GeneReviews; GTF2IRD1; -. DR HGNC; HGNC:4661; GTF2IRD1. DR HPA; ENSG00000006704; Tissue enhanced (skeletal). DR MalaCards; GTF2IRD1; -. DR MIM; 604318; gene. DR neXtProt; NX_Q9UHL9; -. DR OpenTargets; ENSG00000006704; -. DR Orphanet; 904; Williams syndrome. DR PharmGKB; PA29047; -. DR VEuPathDB; HostDB:ENSG00000006704; -. DR eggNOG; ENOG502QPVX; Eukaryota. DR GeneTree; ENSGT00940000159414; -. DR HOGENOM; CLU_014412_0_0_1; -. DR InParanoid; Q9UHL9; -. DR OMA; VFDVLYX; -. DR OrthoDB; 5308582at2759; -. DR PhylomeDB; Q9UHL9; -. DR TreeFam; TF352524; -. DR PathwayCommons; Q9UHL9; -. DR SignaLink; Q9UHL9; -. DR SIGNOR; Q9UHL9; -. DR BioGRID-ORCS; 9569; 17 hits in 1158 CRISPR screens. DR ChiTaRS; GTF2IRD1; human. DR EvolutionaryTrace; Q9UHL9; -. DR GeneWiki; GTF2IRD1; -. DR GenomeRNAi; 9569; -. DR Pharos; Q9UHL9; Tbio. DR PRO; PR:Q9UHL9; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9UHL9; Protein. DR Bgee; ENSG00000006704; Expressed in lower esophagus mucosa and 193 other cell types or tissues. DR ExpressionAtlas; Q9UHL9; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; NAS:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro. DR GO; GO:0014886; P:transition between slow and fast fiber; IEA:Ensembl. DR Gene3D; 3.90.1460.10; GTF2I-like; 5. DR InterPro; IPR004212; GTF2I. DR InterPro; IPR036647; GTF2I-like_rpt_sf. DR InterPro; IPR016659; TF_II-I. DR PANTHER; PTHR46304; GENERAL TRANSCRIPTION FACTOR II-I REPEAT DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR46304:SF1; GENERAL TRANSCRIPTION FACTOR II-I REPEAT DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF02946; GTF2I; 5. DR PIRSF; PIRSF016441; TF_II-I; 1. DR SUPFAM; SSF117773; GTF2I-like repeat; 5. DR PROSITE; PS51139; GTF2I; 5. DR Genevisible; Q9UHL9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Developmental protein; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Transcription; Transcription regulation; Ubl conjugation; KW Williams-Beuren syndrome. FT CHAIN 1..959 FT /note="General transcription factor II-I repeat domain- FT containing protein 1" FT /id="PRO_0000083870" FT REPEAT 119..213 FT /note="GTF2I-like 1" FT REPEAT 342..436 FT /note="GTF2I-like 2" FT REPEAT 556..650 FT /note="GTF2I-like 3" FT REPEAT 696..790 FT /note="GTF2I-like 4" FT REPEAT 793..887 FT /note="GTF2I-like 5" FT REGION 96..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 230..250 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 468..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 654..679 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 892..927 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 898..905 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 908..927 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 448 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 27 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 94 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 184 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 212 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 225 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 238 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 271 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 294 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 308 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 337 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 436 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 439 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 443 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 567 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 579 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 588 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 622 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 638 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 684 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 724 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 732 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 772 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 774 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 787 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, 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:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 889 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 893 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 89 FT /note="R -> LSAAQHRAATSQLEGRVVRRVLTVASRALCPTG (in isoform FT 3)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_043425" FT VAR_SEQ 656..670 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10198167, FT ECO:0000303|PubMed:10575229, ECO:0000303|PubMed:9774679, FT ECO:0000303|Ref.6" FT /id="VSP_003873" FT VARIANT 652 FT /note="M -> V (in dbSNP:rs2301895)" FT /evidence="ECO:0000269|PubMed:10575229, FT ECO:0000269|PubMed:10642537, ECO:0000269|PubMed:15489334" FT /id="VAR_013446" FT MUTAGEN 898..959 FT /note="Missing: Cytoplasmic localization." FT /evidence="ECO:0000269|PubMed:10642537" FT CONFLICT 111 FT /note="G -> S (in Ref. 1; AAD14687 and 2; AAD27668)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="R -> Q (in Ref. 5; AAF21796)" FT /evidence="ECO:0000305" FT HELIX 128..144 FT /evidence="ECO:0007829|PDB:2D99" FT HELIX 154..159 FT /evidence="ECO:0007829|PDB:2D99" FT TURN 161..163 FT /evidence="ECO:0007829|PDB:2D99" FT STRAND 164..168 FT /evidence="ECO:0007829|PDB:2D99" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:2D99" FT HELIX 183..192 FT /evidence="ECO:0007829|PDB:2D99" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:2D99" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:2D99" FT HELIX 565..580 FT /evidence="ECO:0007829|PDB:2DZQ" FT HELIX 591..596 FT /evidence="ECO:0007829|PDB:2DZQ" FT TURN 598..600 FT /evidence="ECO:0007829|PDB:2DZQ" FT STRAND 601..605 FT /evidence="ECO:0007829|PDB:2DZQ" FT TURN 615..617 FT /evidence="ECO:0007829|PDB:2DZQ" FT HELIX 620..628 FT /evidence="ECO:0007829|PDB:2DZQ" FT TURN 629..632 FT /evidence="ECO:0007829|PDB:2DZQ" FT STRAND 634..638 FT /evidence="ECO:0007829|PDB:2DZQ" FT HELIX 640..642 FT /evidence="ECO:0007829|PDB:2DZQ" FT HELIX 705..721 FT /evidence="ECO:0007829|PDB:2DZR" FT HELIX 731..736 FT /evidence="ECO:0007829|PDB:2DZR" FT STRAND 738..745 FT /evidence="ECO:0007829|PDB:2DZR" FT HELIX 755..757 FT /evidence="ECO:0007829|PDB:2DZR" FT HELIX 760..769 FT /evidence="ECO:0007829|PDB:2DZR" FT TURN 770..772 FT /evidence="ECO:0007829|PDB:2DZR" FT STRAND 774..777 FT /evidence="ECO:0007829|PDB:2DZR" FT HELIX 802..817 FT /evidence="ECO:0007829|PDB:2DN5" FT HELIX 828..833 FT /evidence="ECO:0007829|PDB:2DN5" FT STRAND 837..842 FT /evidence="ECO:0007829|PDB:2DN5" FT STRAND 852..854 FT /evidence="ECO:0007829|PDB:2DN5" FT HELIX 857..864 FT /evidence="ECO:0007829|PDB:2DN5" FT TURN 865..869 FT /evidence="ECO:0007829|PDB:2DN5" FT STRAND 871..876 FT /evidence="ECO:0007829|PDB:2DN5" FT MOD_RES Q9UHL9-2:654 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT CROSSLNK Q9UHL9-2:638 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK Q9UHL9-2:648 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK Q9UHL9-2:669 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT MOD_RES Q9UHL9-3:686 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT CROSSLNK Q9UHL9-3:670 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK Q9UHL9-3:680 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK Q9UHL9-3:701 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" 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 //