GT2D1_HUMAN
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 03-AUG-2022, entry version 196.
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; 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; 119.
DR IntAct; Q9UHL9; 68.
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; Q9UHL9; -.
DR PeptideAtlas; Q9UHL9; -.
DR PRIDE; Q9UHL9; -.
DR ProteomicsDB; 84377; -. [Q9UHL9-1]
DR ProteomicsDB; 84378; -. [Q9UHL9-2]
DR ProteomicsDB; 84379; -. [Q9UHL9-3]
DR Antibodypedia; 14624; 394 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 CTD; 9569; -.
DR DisGeNET; 9569; -.
DR GeneCards; 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; SNQIPVM; -.
DR OrthoDB; 115381at2759; -.
DR PhylomeDB; Q9UHL9; -.
DR TreeFam; TF352524; -.
DR PathwayCommons; Q9UHL9; -.
DR SignaLink; Q9UHL9; -.
DR SIGNOR; Q9UHL9; -.
DR BioGRID-ORCS; 9569; 17 hits in 1080 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 191 other tissues.
DR ExpressionAtlas; Q9UHL9; baseline and differential.
DR Genevisible; Q9UHL9; HS.
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 transcription, DNA-templated; 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; -; 5.
DR InterPro; IPR004212; GTF2I.
DR InterPro; IPR036647; GTF2I-like_rpt_sf.
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; 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
