ID   E9PFE2_HUMAN            Unreviewed;       960 AA.
AC   E9PFE2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=General transcription factor II-I repeat domain-containing protein 1 {ECO:0000256|ARBA:ARBA00072433};
GN   Name=GTF2IRD1 {ECO:0000313|Ensembl:ENSP00000418383.1};
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 {ECO:0000313|Ensembl:ENSP00000418383.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000418383.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11237011; DOI=10.1038/35057062;
RG   International Human Genome Sequencing Consortium;
RA   Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA   Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA   Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA   McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA   Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA   Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA   Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA   Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA   Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA   Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA   Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA   Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA   Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA   Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA   Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA   Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA   Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA   Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA   Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA   Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA   Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA   Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA   Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA   Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA   Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA   Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA   Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA   Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA   Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA   Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA   Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA   Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA   Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA   Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA   Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA   Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA   Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA   Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA   McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA   Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA   Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA   Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA   Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA   Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA   Shizuya H., Choi S., Chen Y.J.;
RT   "Initial sequencing and analysis of the human genome.";
RL   Nature 409:860-921(2001).
RN   [2] {ECO:0000313|Ensembl:ENSP00000418383.1, ECO:0000313|Proteomes:UP000005640}
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., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W.,
RA   Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R.,
RA   Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R.,
RA   Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E.,
RA   Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D.,
RA   Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3] {ECO:0000313|Ensembl:ENSP00000418383.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496913; DOI=10.1038/nature03001;
RG   International Human Genome Sequencing Consortium;
RT   "Finishing the euchromatic sequence of the human genome.";
RL   Nature 431:931-945(2004).
RN   [4] {ECO:0007829|PubMed:17081983}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [5] {ECO:0007829|PubMed:17525332}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R., 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   [6] {ECO:0007829|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [7] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [8] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
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   [9] {ECO:0007829|PubMed:25218447}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447;
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   [10] {ECO:0007829|PubMed:25114211}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211;
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   [11] {ECO:0007829|PubMed:25772364}
RP   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   [12] {ECO:0007829|PubMed:25755297}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.O114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson 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   [13] {ECO:0007829|PubMed:28112733}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733;
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   [14] {ECO:0000313|Ensembl:ENSP00000418383.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00058906}.
CC   -!- SUBUNIT: Interacts with the retinoblastoma protein (RB1) via its C-
CC       terminus. {ECO:0000256|ARBA:ARBA00063804}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00484}.
CC   -!- SIMILARITY: Belongs to the TFII-I family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00484}.
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DR   EMBL; AC004851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC005015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC211433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF495976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001397817.1; NM_001410888.1.
DR   RefSeq; XP_006716245.1; XM_006716182.4.
DR   RefSeq; XP_054215361.1; XM_054359386.1.
DR   AlphaFoldDB; E9PFE2; -.
DR   SMR; E9PFE2; -.
DR   MassIVE; E9PFE2; -.
DR   ProteomicsDB; 20082; -.
DR   Antibodypedia; 14624; 389 antibodies from 34 providers.
DR   DNASU; 9569; -.
DR   Ensembl; ENST00000476977.5; ENSP00000418383.1; ENSG00000006704.12.
DR   GeneID; 9569; -.
DR   UCSC; uc003uar.1; human.
DR   CTD; 9569; -.
DR   DisGeNET; 9569; -.
DR   HGNC; HGNC:4661; GTF2IRD1.
DR   VEuPathDB; HostDB:ENSG00000006704; -.
DR   GeneTree; ENSGT00940000159414; -.
DR   OrthoDB; 9876044at2759; -.
DR   BioGRID-ORCS; 9569; 17 hits in 1158 CRISPR screens.
DR   ChiTaRS; GTF2IRD1; human.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000006704; Expressed in lower esophagus mucosa and 193 other cell types or tissues.
DR   ExpressionAtlas; E9PFE2; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR   FunFam; 3.90.1460.10:FF:000002; General transcription factor II-I isoform 1; 1.
DR   FunFam; 3.90.1460.10:FF:000005; general transcription factor II-I repeat domain-containing protein 1; 1.
DR   FunFam; 3.90.1460.10:FF:000006; General transcription factor II-I repeat domain-containing protein 1; 1.
DR   FunFam; 3.90.1460.10:FF:000007; General transcription factor II-I repeat domain-containing protein 1; 1.
DR   FunFam; 3.90.1460.10:FF:000008; General transcription factor II-I repeat domain-containing protein 1; 1.
DR   Gene3D; 3.90.1460.10; GTF2I-like; 5.
DR   InterPro; IPR004212; GTF2I.
DR   InterPro; IPR036647; GTF2I-like_rpt_sf.
DR   InterPro; IPR016659; TF_II-I.
DR   PANTHER; PTHR46304; GENERAL TRANSCRIPTION FACTOR II-I REPEAT DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46304:SF1; GENERAL TRANSCRIPTION FACTOR II-I REPEAT DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF02946; GTF2I; 5.
DR   PIRSF; PIRSF016441; TF_II-I; 1.
DR   SUPFAM; SSF117773; GTF2I-like repeat; 5.
DR   PROSITE; PS51139; GTF2I; 5.
PE   1: Evidence at protein level;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00484}; Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00484}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:E9PFE2,
KW   ECO:0007829|ProteomicsDB:E9PFE2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE-
KW   ProRule:PRU00484};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PROSITE-ProRule:PRU00484};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   REPEAT          119..213
FT                   /note="GTF2I-like"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00484"
FT   REPEAT          342..436
FT                   /note="GTF2I-like"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00484"
FT   REPEAT          556..650
FT                   /note="GTF2I-like"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00484"
FT   REPEAT          681..775
FT                   /note="GTF2I-like"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00484"
FT   REPEAT          778..872
FT                   /note="GTF2I-like"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00484"
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          877..913
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..908
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  106049 MW;  E08A2EF95D7859D2 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 IMDSQERDSG
     DPLVDESLKR QGFQENYDAR LSRIDIANTL REQVQDLFNK KYGEALGIKY PVQVPYKRIK
     SNPGSVIIEG LPPGIPFRKP CTFGSQNLER ILAVADKIKF TVTRPFQGLI PKPDEDDANR
     LGEKVILREQ VKELFNEKYG EALGLNRPVL VPYKLIRDSP DAVEVTGLPD DIPFRNPNTY
     DIHRLEKILK AREHVRMVII NQLQPFAEIC NDAKVPAKDS SIPKRKRKRV SEGNSVSSSS
     SSSSSSSSNP DSVASANQIS LVVKLHRFGL RHSSLWPSPL CLAGPSTLGC GPRGRGGTGL
//