GTF2I_HUMAN
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 03-AUG-2022, entry version 217.
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}.
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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; 256.
DR CORUM; P78347; -.
DR DIP; DIP-24252N; -.
DR IntAct; P78347; 82.
DR MINT; P78347; -.
DR STRING; 9606.ENSP00000460070; -.
DR GlyGen; P78347; 1 site, 1 O-linked glycan (1 site).
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 PRIDE; 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; 445 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 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 PhylomeDB; P78347; -.
DR TreeFam; TF352524; -.
DR PathwayCommons; P78347; -.
DR SignaLink; P78347; -.
DR SIGNOR; P78347; -.
DR BioGRID-ORCS; 2969; 70 hits in 1076 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:0100026; P:positive regulation of DNA repair by transcription from RNA polymerase II promoter; IDA:ARUK-UCL.
DR Gene3D; 3.90.1460.10; -; 6.
DR InterPro; IPR004212; GTF2I.
DR InterPro; IPR036647; GTF2I-like_rpt_sf.
DR InterPro; IPR016659; TF_II-I.
DR Pfam; PF02946; GTF2I; 6.
DR PIRSF; PIRSF016441; TF_II-I; 1.
DR SUPFAM; SSF117773; SSF117773; 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
