ID GTF2I_HUMAN Reviewed; 998 AA. AC P78347; O14743; O15359; O43546; O43588; O43589; Q75M85; Q75M86; Q75M87; AC Q75M88; Q86U51; Q9BSZ4; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2001, sequence version 2. DT 28-JUN-2023, entry version 222. DE RecName: Full=General transcription factor II-I; DE Short=GTFII-I; DE Short=TFII-I; DE AltName: Full=Bruton tyrosine kinase-associated protein 135; DE Short=BAP-135; DE Short=BTK-associated protein 135; DE AltName: Full=SRF-Phox1-interacting protein; DE Short=SPIN; DE AltName: Full=Williams-Beuren syndrome chromosomal region 6 protein; GN Name=GTF2I; Synonyms=BAP135, WBSCR6; 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), AND PROTEIN SEQUENCE OF 162-171; RP 366-372; 646-658 AND 940-956. RX PubMed=9384587; DOI=10.1093/emboj/16.23.7091; RA Roy A.L., Du H., Gregor P.D., Novina C.D., Martinez E., Roeder R.G.; RT "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts RT physically and functionally with USF1."; RL EMBO J. 16:7091-7104(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF 291-294 AND RP 316-333. RC TISSUE=Cervix carcinoma; RX PubMed=9334314; DOI=10.1101/gad.11.19.2482; RA Grueneberg D.A., Henry R.W., Brauer A., Novina C.D., Cheriyath V., RA Roy A.L., Gilman M.; RT "A multifunctional DNA-binding protein that promotes the formation of serum RT response factor/homeodomain complexes: identity to TFII-I."; RL Genes Dev. 11:2482-2493(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF 144-154; RP 495-514 AND 681-702. RX PubMed=9012831; DOI=10.1073/pnas.94.2.604; RA Yang W., Desiderio S.; RT "BAP-135, a target for Bruton's tyrosine kinase in response to B cell RT receptor engagement."; RL Proc. Natl. Acad. Sci. U.S.A. 94:604-609(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). RX PubMed=9466987; DOI=10.1093/hmg/7.3.325; RA Perez Jurado L.A., Wang Y.-K., Peoples R., Coloma A., Cruces J., RA Francke U.; RT "A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren RT syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, RT a phosphorylation target of BTK."; RL Hum. Mol. Genet. 7:325-334(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Lymph, and Ovary; 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 PROTEIN SEQUENCE OF 2-20; 131-140; 178-185; 364-371; 444-456; 495-514; RP 540-555; 574-594; 620-628; 870-878; 917-927 AND 929-937, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Colon adenocarcinoma; RA Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.; RL Submitted (JUL-2007) to UniProtKB. RN [10] RP INTERACTION WITH BTK, FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=10373551; DOI=10.1128/mcb.19.7.5014; RA Novina C.D., Kumar S., Bajpai U., Cheriyath V., Zhang K., Pillai S., RA Wortis H.H., Roy A.L.; RT "Regulation of nuclear localization and transcriptional activity of TFII-I RT by Bruton's tyrosine kinase."; RL Mol. Cell. Biol. 19:5014-5024(1999). RN [11] RP PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, RP FUNCTION, AND MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503. RX PubMed=11373296; DOI=10.1074/jbc.m103692200; RA Egloff A.M., Desiderio S.; RT "Identification of phosphorylation sites for Bruton's tyrosine kinase RT within the transcriptional regulator BAP/TFII-I."; RL J. Biol. Chem. 276:27806-27815(2001). RN [12] RP PHOSPHORYLATION AT SER-412 AND SER-784 BY PRKG1, AND INTERACTION WITH RP PRKG1. RX PubMed=12082086; DOI=10.1074/jbc.m112332200; RA Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S., RA Pilz R.B.; RT "cGMP-dependent protein kinase I beta physically and functionally interacts RT with the transcriptional regulator TFII-I."; RL J. Biol. Chem. 277:32003-32014(2002). RN [13] RP SUMOYLATION. RX PubMed=15561718; DOI=10.1074/jbc.m411718200; RA Gocke C.B., Yu H., Kang J.; RT "Systematic identification and analysis of mammalian small ubiquitin-like RT modifier substrates."; RL J. Biol. Chem. 280:5004-5012(2005). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [15] RP INTERACTION WITH ARID3A AND BTK, PHOSPHORYLATION AT TYR-248, AND FUNCTION. RX PubMed=16738337; DOI=10.1128/mcb.02009-05; RA Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F.; RT "Induction of immunoglobulin heavy-chain transcription through the RT transcription factor Bright requires TFII-I."; RL Mol. Cell. Biol. 26:4758-4768(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-207; SER-210 AND RP THR-558, AND IDENTIFICATION 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND THR-558, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; THR-558 AND SER-823, AND RP IDENTIFICATION 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-103; SER-210; RP SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-823, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 (ISOFORM 2), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 (ISOFORM 4), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-221; LYS-343; LYS-353; RP LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, AND IDENTIFICATION BY MASS RP 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 [30] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-221 AND LYS-991, AND RP IDENTIFICATION BY 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 [31] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-130; LYS-221; LYS-326; RP LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND RP LYS-991, 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 [32] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-221; LYS-456; LYS-488; RP LYS-561; LYS-664; LYS-816 AND LYS-991, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE 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 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 [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [34] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35; LYS-86; LYS-92; LYS-94; RP LYS-130; LYS-140; LYS-185; LYS-219; LYS-221; LYS-326; LYS-343; LYS-353; RP LYS-380; LYS-435; LYS-450; LYS-456; LYS-488; LYS-494; LYS-526; LYS-561; RP LYS-660; LYS-664; LYS-670; LYS-680; LYS-715; LYS-816; LYS-827; LYS-861; RP LYS-864; LYS-879; LYS-891 AND LYS-991, AND IDENTIFICATION BY MASS RP 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 [35] RP STRUCTURE BY NMR OF 102-197 AND 361-554. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RSGI RUH-052, a GTF2I domain in human."; RL Submitted (AUG-2007) to the PDB data bank. CC -!- FUNCTION: Interacts with the basal transcription machinery by CC coordinating the formation of a multiprotein complex at the C-FOS CC promoter, and linking specific signal responsive activator complexes. CC Promotes the formation of stable high-order complexes of SRF and PHOX1 CC and interacts cooperatively with PHOX1 to promote serum-inducible CC transcription of a reporter gene deriven by the C-FOS serum response CC element (SRE). Acts as a coregulator for USF1 by binding independently CC two promoter elements, a pyrimidine-rich initiator (Inr) and an CC upstream E-box. Required for the formation of functional ARID3A DNA- CC binding complexes and for activation of immunoglobulin heavy-chain CC transcription upon B-lymphocyte activation. CC {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, CC ECO:0000269|PubMed:16738337}. CC -!- SUBUNIT: Homodimer (Potential). Interacts with SRF and PHOX1. Binds a CC pyrimidine-rich initiator (Inr) and a recognition site (E-box) for CC upstream stimulatory factor 1 (USF1). Associates with the PH domain of CC Bruton's tyrosine kinase (BTK). May be a component of a BHC histone CC deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, CC RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. CC Interacts with BTK and ARID3A. Interacts with isoform beta of PRKG1. CC {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, CC ECO:0000269|PubMed:12082086, ECO:0000269|PubMed:16738337, ECO:0000305}. CC -!- INTERACTION: CC P78347; P38398: BRCA1; NbExp=5; IntAct=EBI-359622, EBI-349905; CC P78347; Q06187: BTK; NbExp=6; IntAct=EBI-359622, EBI-624835; CC P78347-2; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-12033200, EBI-11978055; CC P78347-2; P63010-2: AP2B1; NbExp=4; IntAct=EBI-12033200, EBI-11529439; CC P78347-2; P78358: CTAG1B; NbExp=5; IntAct=EBI-12033200, EBI-1188472; CC P78347-2; Q9C005: DPY30; NbExp=7; IntAct=EBI-12033200, EBI-744973; CC P78347-2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-12033200, EBI-2130429; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10373551}. Nucleus CC {ECO:0000255|PROSITE-ProRule:PRU00484, ECO:0000269|PubMed:10373551}. CC Note=Colocalizes with BTK in the cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P78347-1; Sequence=Displayed; CC Name=2; CC IsoId=P78347-2; Sequence=VSP_003867, VSP_003868; CC Name=3; CC IsoId=P78347-3; Sequence=VSP_003867; CC Name=4; CC IsoId=P78347-4; Sequence=VSP_003868; CC Name=5; CC IsoId=P78347-5; Sequence=VSP_003867, VSP_055195, VSP_055196; CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 1 is strongly expressed in CC fetal brain, weakly in adult brain, muscle, and lymphoblasts and is CC almost undetectable in other adult tissues, while the other isoforms CC are equally expressed in all adult tissues. CC -!- PTM: Transiently phosphorylated on tyrosine residues by BTK in response CC to B-cell receptor stimulation. Phosphorylation on Tyr-248 and Tyr-398, CC and perhaps, on Tyr-503 contributes to BTK-mediated transcriptional CC activation. {ECO:0000269|PubMed:10373551, ECO:0000269|PubMed:11373296, CC ECO:0000269|PubMed:12082086, ECO:0000269|PubMed:16738337}. CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:15561718}. CC -!- DISEASE: Note=GTF2I 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 GTF2I may CC 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; AF015553; AAB70791.1; -; mRNA. DR EMBL; Y14946; CAA75163.1; -; mRNA. DR EMBL; U77948; AAB48826.1; -; mRNA. DR EMBL; AF035737; AAC08312.1; -; mRNA. DR EMBL; AF038967; AAC08313.1; -; mRNA. DR EMBL; AF038968; AAC08314.1; -; mRNA. DR EMBL; AF038969; AAC08315.1; -; mRNA. DR EMBL; BT007450; AAP36118.1; -; mRNA. DR EMBL; AC005231; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC083884; AAS07460.1; -; Genomic_DNA. DR EMBL; AC083884; AAS07461.1; -; Genomic_DNA. DR EMBL; AC083884; AAS07462.1; -; Genomic_DNA. DR EMBL; AC083884; AAS07463.1; -; Genomic_DNA. DR EMBL; AC083884; AAS07464.1; -; Genomic_DNA. DR EMBL; AC004883; AAL93085.1; -; Genomic_DNA. DR EMBL; CH471200; EAW69598.1; -; Genomic_DNA. DR EMBL; BC004472; AAH04472.1; -; mRNA. DR EMBL; BC070484; AAH70484.1; -; mRNA. DR CCDS; CCDS47614.1; -. [P78347-2] DR CCDS; CCDS5573.1; -. [P78347-1] DR CCDS; CCDS5574.1; -. [P78347-3] DR CCDS; CCDS5575.1; -. [P78347-4] DR CCDS; CCDS64680.1; -. [P78347-5] DR PIR; T03829; T03829. DR PIR; T09492; T09492. DR RefSeq; NP_001157108.1; NM_001163636.2. DR RefSeq; NP_001267729.1; NM_001280800.1. [P78347-5] DR RefSeq; NP_001509.3; NM_001518.4. [P78347-2] DR RefSeq; NP_127492.1; NM_032999.3. [P78347-1] DR RefSeq; NP_127493.1; NM_033000.3. [P78347-3] DR RefSeq; NP_127494.1; NM_033001.3. [P78347-4] DR PDB; 2D9B; NMR; -; A=102-197. DR PDB; 2DN4; NMR; -; A=361-446. DR PDB; 2ED2; NMR; -; A=466-551. DR PDB; 2EJE; NMR; -; A=854-954. DR PDBsum; 2D9B; -. DR PDBsum; 2DN4; -. DR PDBsum; 2ED2; -. DR PDBsum; 2EJE; -. DR AlphaFoldDB; P78347; -. DR SMR; P78347; -. DR BioGRID; 109224; 353. DR CORUM; P78347; -. DR DIP; DIP-24252N; -. DR IntAct; P78347; 82. DR MINT; P78347; -. DR STRING; 9606.ENSP00000460070; -. DR GlyCosmos; P78347; 1 site, 1 glycan. DR GlyGen; P78347; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P78347; -. DR MetOSite; P78347; -. DR PhosphoSitePlus; P78347; -. DR SwissPalm; P78347; -. DR BioMuta; GTF2I; -. DR DMDM; 17865459; -. DR CPTAC; CPTAC-1349; -. DR EPD; P78347; -. DR jPOST; P78347; -. DR MassIVE; P78347; -. DR PaxDb; P78347; -. DR PeptideAtlas; P78347; -. DR ProteomicsDB; 57578; -. [P78347-1] DR ProteomicsDB; 57579; -. [P78347-2] DR ProteomicsDB; 57580; -. [P78347-3] DR ProteomicsDB; 57581; -. [P78347-4] DR ProteomicsDB; 69770; -. DR Antibodypedia; 73029; 468 antibodies from 34 providers. DR DNASU; 2969; -. DR Ensembl; ENST00000443166.5; ENSP00000404240.1; ENSG00000263001.8. [P78347-5] DR Ensembl; ENST00000573035.6; ENSP00000460070.1; ENSG00000263001.8. [P78347-1] DR Ensembl; ENST00000614986.4; ENSP00000484526.1; ENSG00000263001.8. [P78347-3] DR Ensembl; ENST00000620879.4; ENSP00000477837.1; ENSG00000263001.8. [P78347-2] DR Ensembl; ENST00000621734.4; ENSP00000482476.1; ENSG00000263001.8. [P78347-4] DR GeneID; 2969; -. DR KEGG; hsa:2969; -. DR MANE-Select; ENST00000573035.6; ENSP00000460070.1; NM_032999.4; NP_127492.1. DR UCSC; uc003uat.5; human. [P78347-1] DR AGR; HGNC:4659; -. DR CTD; 2969; -. DR DisGeNET; 2969; -. DR GeneCards; GTF2I; -. DR HGNC; HGNC:4659; GTF2I. DR HPA; ENSG00000263001; Low tissue specificity. DR MalaCards; GTF2I; -. DR MIM; 601679; gene. DR neXtProt; NX_P78347; -. DR OpenTargets; ENSG00000263001; -. DR Orphanet; 904; Williams syndrome. DR PharmGKB; PA29045; -. DR VEuPathDB; HostDB:ENSG00000263001; -. DR eggNOG; ENOG502QWD0; Eukaryota. DR GeneTree; ENSGT00940000160349; -. DR HOGENOM; CLU_011773_0_0_1; -. DR InParanoid; P78347; -. DR OrthoDB; 5308582at2759; -. DR PhylomeDB; P78347; -. DR TreeFam; TF352524; -. DR PathwayCommons; P78347; -. DR SignaLink; P78347; -. DR SIGNOR; P78347; -. DR BioGRID-ORCS; 2969; 74 hits in 1155 CRISPR screens. DR ChiTaRS; GTF2I; human. DR EvolutionaryTrace; P78347; -. DR GeneWiki; GTF2I; -. DR GenomeRNAi; 2969; -. DR Pharos; P78347; Tbio. DR PRO; PR:P78347; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P78347; protein. DR Bgee; ENSG00000263001; Expressed in ganglionic eminence and 154 other tissues. DR ExpressionAtlas; P78347; baseline and differential. DR Genevisible; P78347; HS. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL. 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:ARUK-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ARUK-UCL. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro. DR Gene3D; 3.90.1460.10; GTF2I-like; 6. DR InterPro; IPR004212; GTF2I. DR InterPro; IPR036647; GTF2I-like_rpt_sf. DR InterPro; IPR016659; TF_II-I. DR PANTHER; PTHR46304:SF2; GENERAL TRANSCRIPTION FACTOR II-I; 1. DR PANTHER; PTHR46304; GENERAL TRANSCRIPTION FACTOR II-I REPEAT DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF02946; GTF2I; 6. DR PIRSF; PIRSF016441; TF_II-I; 1. DR SUPFAM; SSF117773; GTF2I-like repeat; 6. DR PROSITE; PS51139; GTF2I; 6. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation; Williams-Beuren syndrome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..998 FT /note="General transcription factor II-I" FT /id="PRO_0000083872" FT REPEAT 103..197 FT /note="GTF2I-like 1" FT REPEAT 352..446 FT /note="GTF2I-like 2" FT REPEAT 457..551 FT /note="GTF2I-like 3" FT REPEAT 562..656 FT /note="GTF2I-like 4" FT REPEAT 724..818 FT /note="GTF2I-like 5" FT REPEAT 859..953 FT /note="GTF2I-like 6" FT REGION 241..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 662..681 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 687..714 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 816..836 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 958..998 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 320..327 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 688..713 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 130 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 248 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000269|PubMed:11373296, FT ECO:0000269|PubMed:16738337" FT MOD_RES 353 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8" FT MOD_RES 398 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000269|PubMed:11373296" FT MOD_RES 412 FT /note="Phosphoserine; by PKG/PRKG1" FT /evidence="ECO:0000269|PubMed:12082086, FT ECO:0007744|PubMed:23186163" FT MOD_RES 450 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8" FT MOD_RES 503 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000269|PubMed:11373296" FT MOD_RES 517 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 556 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8" FT MOD_RES 558 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 668 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 674 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 715 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9ESZ8" FT MOD_RES 722 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 784 FT /note="Phosphoserine; by PKG/PRKG1" FT /evidence="ECO:0000269|PubMed:12082086, FT ECO:0007744|PubMed:23186163" FT MOD_RES 823 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT CROSSLNK 35 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 86 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 92 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:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 130 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 140 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 185 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 219 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 221 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 221 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" 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 326 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 343 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 353 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 380 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 435 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 450 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 456 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 488 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 494 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 526 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 561 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 660 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 664 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 670 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 680 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 715 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 816 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 827 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 861 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 864 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 879 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 891 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 991 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 991 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" 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 VAR_SEQ 255..274 FT /note="Missing (in isoform 2, isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9012831, ECO:0000303|PubMed:9334314, FT ECO:0000303|PubMed:9384587, ECO:0000303|PubMed:9466987, FT ECO:0000303|Ref.5" FT /id="VSP_003867" FT VAR_SEQ 294..314 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9012831, ECO:0000303|PubMed:9334314, FT ECO:0000303|PubMed:9384587, ECO:0000303|PubMed:9466987" FT /id="VSP_003868" FT VAR_SEQ 294 FT /note="D -> G (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5" FT /id="VSP_055195" FT VAR_SEQ 295..998 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5" FT /id="VSP_055196" FT VARIANT 174 FT /note="L -> V (in dbSNP:rs1057896)" FT /id="VAR_051026" FT MUTAGEN 248 FT /note="Y->F: Abolishes BTK-mediated transcriptional FT activation. Abolishes BTK-mediated phosphorylation and FT impairs BTK-mediated transcriptional activation; when FT associated with F-398 and F-503." FT /evidence="ECO:0000269|PubMed:11373296" FT MUTAGEN 398 FT /note="Y->F: Abolishes BTK-mediated transcriptional FT activation. Abolishes BTK-mediated phosphorylation and FT impairs BTK-mediated transcriptional activation; when FT associated with F-248 and F-503." FT /evidence="ECO:0000269|PubMed:11373296" FT MUTAGEN 460 FT /note="Y->F: No change on BTK-mediated transcriptional FT activation." FT /evidence="ECO:0000269|PubMed:11373296" FT MUTAGEN 503 FT /note="Y->F: Impairs BTK-mediated transcriptional FT activation. Abolishes BTK-mediated phosphorylation and FT impairs BTK-mediated transcriptional activation; when FT associated with F-248 and F-398." FT /evidence="ECO:0000269|PubMed:11373296" FT CONFLICT 174 FT /note="L -> G (in Ref. 3; AAB48826)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="A -> G (in Ref. 3; AAB48826)" FT /evidence="ECO:0000305" FT CONFLICT 481 FT /note="A -> R (in Ref. 1; AAB70791)" FT /evidence="ECO:0000305" FT CONFLICT 634 FT /note="R -> H (in Ref. 3; AAB48826)" FT /evidence="ECO:0000305" FT CONFLICT 960 FT /note="E -> K (in Ref. 3; AAB48826)" FT /evidence="ECO:0000305" FT HELIX 106..128 FT /evidence="ECO:0007829|PDB:2D9B" FT HELIX 138..143 FT /evidence="ECO:0007829|PDB:2D9B" FT STRAND 146..152 FT /evidence="ECO:0007829|PDB:2D9B" FT HELIX 167..175 FT /evidence="ECO:0007829|PDB:2D9B" FT TURN 176..179 FT /evidence="ECO:0007829|PDB:2D9B" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:2D9B" FT HELIX 361..376 FT /evidence="ECO:0007829|PDB:2DN4" FT HELIX 387..392 FT /evidence="ECO:0007829|PDB:2DN4" FT TURN 393..396 FT /evidence="ECO:0007829|PDB:2DN4" FT STRAND 397..401 FT /evidence="ECO:0007829|PDB:2DN4" FT TURN 411..413 FT /evidence="ECO:0007829|PDB:2DN4" FT HELIX 416..424 FT /evidence="ECO:0007829|PDB:2DN4" FT TURN 426..428 FT /evidence="ECO:0007829|PDB:2DN4" FT STRAND 430..434 FT /evidence="ECO:0007829|PDB:2DN4" FT TURN 437..439 FT /evidence="ECO:0007829|PDB:2DN4" FT HELIX 466..482 FT /evidence="ECO:0007829|PDB:2ED2" FT HELIX 492..497 FT /evidence="ECO:0007829|PDB:2ED2" FT TURN 499..501 FT /evidence="ECO:0007829|PDB:2ED2" FT STRAND 502..506 FT /evidence="ECO:0007829|PDB:2ED2" FT TURN 516..518 FT /evidence="ECO:0007829|PDB:2ED2" FT HELIX 521..529 FT /evidence="ECO:0007829|PDB:2ED2" FT TURN 530..533 FT /evidence="ECO:0007829|PDB:2ED2" FT STRAND 535..539 FT /evidence="ECO:0007829|PDB:2ED2" FT HELIX 541..544 FT /evidence="ECO:0007829|PDB:2ED2" FT TURN 856..858 FT /evidence="ECO:0007829|PDB:2EJE" FT HELIX 861..883 FT /evidence="ECO:0007829|PDB:2EJE" FT HELIX 894..899 FT /evidence="ECO:0007829|PDB:2EJE" FT STRAND 901..907 FT /evidence="ECO:0007829|PDB:2EJE" FT TURN 918..920 FT /evidence="ECO:0007829|PDB:2EJE" FT HELIX 923..931 FT /evidence="ECO:0007829|PDB:2EJE" FT TURN 932..935 FT /evidence="ECO:0007829|PDB:2EJE" FT STRAND 937..942 FT /evidence="ECO:0007829|PDB:2EJE" FT MOD_RES P78347-2:278 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES P78347-4:298 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" SQ SEQUENCE 998 AA; 112416 MW; 4CFA2C19002869B9 CRC64; MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDSTQHVP SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQSESE GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW //