ID TAF1_HUMAN Reviewed; 1893 AA.
AC P21675; A5CVC8; A5CVC9; A5CVD0; A5CVD1; B1Q2X3; Q59FZ3; Q6IUZ1; Q70Q86;
AC Q70Q87; Q70T00; Q70T01; Q70T02; Q70T03;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2023, sequence version 3.
DT 27-MAR-2024, entry version 241.
DE RecName: Full=Transcription initiation factor TFIID subunit 1 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000269|PubMed:15870300};
DE EC=2.7.11.1;
DE AltName: Full=Cell cycle gene 1 protein;
DE AltName: Full=TBP-associated factor 250 kDa;
DE Short=p250;
DE AltName: Full=Transcription initiation factor TFIID 250 kDa subunit;
DE Short=TAF(II)250;
DE Short=TAFII-250;
DE Short=TAFII250;
GN Name=TAF1 {ECO:0000312|HGNC:HGNC:11535}; Synonyms=BA2R, CCG1, CCGS, TAF2A;
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 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Laryngeal carcinoma;
RX PubMed=2038334; DOI=10.1128/mcb.11.6.3317-3325.1991;
RA Sekiguchi T., Nohiro Y., Nakamura Y., Hisamoto N., Nishimoto T.;
RT "The human CCG1 gene, essential for progression of the G1 phase, encodes a
RT 210-kilodalton nuclear DNA-binding protein.";
RL Mol. Cell. Biol. 11:3317-3325(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TBP AND TAFS.
RX PubMed=7680771; DOI=10.1038/362175a0;
RA Ruppert S., Wang E.H., Tjian R.;
RT "Cloning and expression of human TAFII250: a TBP-associated factor
RT implicated in cell-cycle regulation.";
RL Nature 362:175-179(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N-TAF1), AND INVOLVEMENT IN DYT3.
RC TISSUE=Brain;
RX PubMed=17273961; DOI=10.1086/512129;
RA Makino S., Kaji R., Ando S., Tomizawa M., Yasuno K., Goto S., Matsumoto S.,
RA Tabuena M.D., Maranon E., Dantes M., Lee L.V., Ogasawara K., Tooyama I.,
RA Akatsu H., Nishimura M., Tamiya G.;
RT "Reduced neuron-specific expression of the TAF1 gene is associated with X-
RT linked dystonia-parkinsonism.";
RL Am. J. Hum. Genet. 80:393-406(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT VAL-290.
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-1604 (ISOFORM 1).
RX PubMed=3169001; DOI=10.1002/j.1460-2075.1988.tb02996.x;
RA Sekiguchi T., Miyata T., Nishimoto T.;
RT "Molecular cloning of the cDNA of human X chromosomal gene (CCG1) which
RT complements the temperature-sensitive G1 mutants, tsBN462 and ts13, of the
RT BHK cell line.";
RL EMBO J. 7:1683-1687(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 858-1893 (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1368-1893 (ISOFORMS 2A; 2C; 2D AND 2E),
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1519-1893 (ISOFORM 16), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1749-1893 (ISOFORM 15), AND INVOLVEMENT IN DYT3.
RC TISSUE=Fetal brain;
RX PubMed=12928496; DOI=10.1073/pnas.1831949100;
RA Nolte D., Niemann S., Muller U.;
RT "Specific sequence changes in multiple transcript system DYT3 are
RT associated with X-linked dystonia parkinsonism.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10347-10352(2003).
RN [9]
RP SEQUENCE REVISION (ISOFORMS 2A; 2C; 2D AND 2E), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1368-1893 (ISOFORMS 2E; 2G; 2H AND 2I), AND ALTERNATIVE SPLICING.
RX PubMed=17952504; DOI=10.1007/s00335-007-9063-z;
RA Herzfeld T., Nolte D., Muller U.;
RT "Structural and functional analysis of the human TAF1/DYT3 multiple
RT transcript system.";
RL Mamm. Genome 18:787-795(2007).
RN [10]
RP FUNCTION.
RX PubMed=8450888; DOI=10.1038/362179a0;
RA Hisatake K., Hasegawa S., Takada R., Nakatani Y., Horikoshi M.,
RA Roeder R.G.;
RT "The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle
RT regulatory protein CCG1.";
RL Nature 362:179-181(1993).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-137 AND SER-328, AND
RP ATP-BINDING.
RX PubMed=8625415; DOI=10.1016/s0092-8674(00)81055-7;
RA Dikstein R., Ruppert S., Tjian R.;
RT "TAFII250 is a bipartite protein kinase that phosphorylates the base
RT transcription factor RAP74.";
RL Cell 84:781-790(1996).
RN [12]
RP INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION).
RX PubMed=8647434; DOI=10.1101/gad.10.11.1369;
RA Damania B., Alwine J.C.;
RT "TAF-like function of SV40 large T antigen.";
RL Genes Dev. 10:1369-1381(1996).
RN [13]
RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 ICP4 (MICROBIAL INFECTION).
RX PubMed=8649420; DOI=10.1128/mcb.16.6.3085;
RA Carrozza M.J., DeLuca N.A.;
RT "Interaction of the viral activator protein ICP4 with TFIID through
RT TAF250.";
RL Mol. Cell. Biol. 16:3085-3093(1996).
RN [14]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=9660973; DOI=10.1016/s1097-2765(00)80089-1;
RA O'Brien T., Tjian R.;
RT "Functional analysis of the human TAFII250 N-terminal kinase domain.";
RL Mol. Cell 1:905-911(1998).
RN [15]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH RB1, AND ATP-BINDING.
RX PubMed=9858607; DOI=10.1128/mcb.19.1.846;
RA Siegert J.L., Robbins P.D.;
RT "Rb inhibits the intrinsic kinase activity of TATA-binding protein-
RT associated factor TAFII250.";
RL Mol. Cell. Biol. 19:846-854(1999).
RN [16]
RP INTERACTION WITH ASF1A.
RX PubMed=10759893; DOI=10.1046/j.1365-2443.2000.00319.x;
RA Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.;
RT "A human homologue of yeast anti-silencing factor has histone chaperone
RT activity.";
RL Genes Cells 5:221-233(2000).
RN [17]
RP FUNCTION.
RX PubMed=11278496; DOI=10.1074/jbc.m009385200;
RA Solow S., Salunek M., Ryan R., Lieberman P.M.;
RT "Taf(II) 250 phosphorylates human transcription factor IIA on serine
RT residues important for TBP binding and transcription activity.";
RL J. Biol. Chem. 276:15886-15892(2001).
RN [18]
RP ACTIVITY REGULATION, AND INTERACTION WITH TAF7.
RX PubMed=11592977; DOI=10.1073/pnas.211444798;
RA Gegonne A., Weissman J.D., Singer D.S.;
RT "TAFII55 binding to TAFII250 inhibits its acetyltransferase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12432-12437(2001).
RN [19]
RP INTERACTION WITH ASF1A.
RX PubMed=12093919; DOI=10.1073/pnas.142627899;
RA Chimura T., Kuzuhara T., Horikoshi M.;
RT "Identification and characterization of CIA/ASF1 as an interactor of
RT bromodomains associated with TFIID.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002).
RN [20]
RP INTERACTION WITH ASF1A AND ASF1B.
RX PubMed=12842904; DOI=10.1074/jbc.m303549200;
RA Umehara T., Horikoshi M.;
RT "Transcription initiation factor IID-interactive histone chaperone CIA-II
RT implicated in mammalian spermatogenesis.";
RL J. Biol. Chem. 278:35660-35667(2003).
RN [21]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=15053879; DOI=10.1016/s1097-2765(04)00123-6;
RA Li H.-H., Li A.G., Sheppard H.M., Liu X.;
RT "Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role for
RT TAF1 in cell G1 progression.";
RL Mol. Cell 13:867-878(2004).
RN [22]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [23]
RP HISTONE ACETYLTRANSFERASE ACTIVITY, AND MUTAGENESIS OF GLU-742 AND
RP 848-MET--ASP-850.
RX PubMed=15870300; DOI=10.1128/mcb.25.10.4321-4332.2005;
RA Hilton T.L., Li Y., Dunphy E.L., Wang E.H.;
RT "TAF1 histone acetyltransferase activity in Sp1 activation of the cyclin D1
RT promoter.";
RL Mol. Cell. Biol. 25:4321-4332(2005).
RN [24]
RP 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1847, AND IDENTIFICATION BY
RP 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1721 (ISOFORMS 2A AND 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1723 (ISOFORM 2G),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1718 (ISOFORM 16), 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 [27]
RP ACTIVITY REGULATION.
RX PubMed=22711989; DOI=10.1128/mcb.00416-12;
RA Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.;
RT "Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene
RT transcription by TFIID subunits TAF1 and TAF7.";
RL Mol. Cell. Biol. 32:3358-3369(2012).
RN [28]
RP MISCELLANEOUS.
RX PubMed=23184149; DOI=10.1093/hmg/dds499;
RA Herzfeld T., Nolte D., Grznarova M., Hofmann A., Schultze J.L., Muller U.;
RT "X-linked dystonia parkinsonism syndrome (XDP, lubag): disease-specific
RT sequence change DSC3 in TAF1/DYT3 affects genes in vesicular transport and
RT dopamine metabolism.";
RL Hum. Mol. Genet. 22:941-951(2013).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP 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 [30]
RP SUBCELLULAR LOCATION.
RX PubMed=25593309; DOI=10.1101/gad.252189.114;
RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W.,
RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.;
RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of
RT transcription-associated DNA damage that promotes homologous
RT recombination.";
RL Genes Dev. 29:197-211(2015).
RN [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-570 AND LYS-583, AND
RP IDENTIFICATION BY MASS 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 [32]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1380-1659.
RX PubMed=10827952; DOI=10.1126/science.288.5470.1422;
RA Jacobson R.H., Ladurner A.G., King D.S., Tjian R.;
RT "Structure and function of a human TAFII250 double bromodomain module.";
RL Science 288:1422-1425(2000).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 1522-1656, AND SUBUNIT.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 600-1236 IN COMPLEX WITH TAF7,
RP FUNCTION, AND INTERACTION WITH TAF7.
RX PubMed=25412659; DOI=10.1038/cr.2014.148;
RA Wang H., Curran E.C., Hinds T.R., Wang E.H., Zheng N.;
RT "Crystal structure of a TAF1-TAF7 complex in human transcription factor IID
RT reveals a promoter binding module.";
RL Cell Res. 24:1433-1444(2014).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1518-1659 IN COMPLEX WITH
RP CROTONYLATED OR BUTYRYLATED HISTONE H4.
RX PubMed=26365797; DOI=10.1016/j.str.2015.08.004;
RA Flynn E.M., Huang O.W., Poy F., Oppikofer M., Bellon S.F., Tang Y.,
RA Cochran A.G.;
RT "A subset of human bromodomains recognizes butyryllysine and crotonyllysine
RT histone peptide modifications.";
RL Structure 23:1801-1814(2015).
RN [36]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.50 ANGSTROMS), AND SUBCELLULAR
RP LOCATION.
RX PubMed=27007846; DOI=10.1038/nature17394;
RA Louder R.K., He Y., Lopez-Blanco J.R., Fang J., Chacon P., Nogales E.;
RT "Structure of promoter-bound TFIID and model of human pre-initiation
RT complex assembly.";
RL Nature 531:604-609(2016).
RN [37] {ECO:0007744|PDB:6FIC}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1380-1659.
RA Mathea S., Suh J.L., Salah E., Tallant C., Siejka P., Pike A.C.W.,
RA von Delft F., Arrowsmith C.H., Edwards A.M., Bountra C., James L.I.,
RA Frye S.V., Knapp S.;
RT "Bivalent Inhibitor UNC4512 Bound to the TAF1 Bromodomain Tandem.";
RL Submitted (JAN-2018) to the PDB data bank.
RN [38] {ECO:0007744|PDB:6P39, ECO:0007744|PDB:6P3A}
RP X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) OF 1521-1656.
RA Seo H.-S., Dhe-Paganon S.;
RT "Crystal Structure Analysis of TAF1 Bromodomain.";
RL Submitted (MAY-2019) to the PDB data bank.
RN [39] {ECO:0007744|PDB:7JJG}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1522-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to
RT ATR kinase inhibitor AZ20.";
RL Submitted (JUL-2020) to the PDB data bank.
RN [40] {ECO:0007744|PDB:7JJH}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the unliganded tandem bromodomain (BD1, BD2) of human
RT TAF1.";
RL Submitted (JUL-2020) to the PDB data bank.
RN [41] {ECO:0007744|PDB:7JSP}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1522-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to
RT the ATR kinase inhibitor AZD6738.";
RL Submitted (AUG-2020) to the PDB data bank.
RN [42] {ECO:0007744|PDB:7JTC}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1522-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to
RT ZS1-322.";
RL Submitted (AUG-2020) to the PDB data bank.
RN [43] {ECO:0007744|PDB:7K03}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1 and BD2) of human TAF1
RT bound to ATR kinase inhibitor AZD6738.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [44] {ECO:0007744|PDB:7K0D}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound
RT to mTORC1/2 inhibitor AZD3147.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [45] {ECO:0007744|PDB:7K0U}
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 1522-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to
RT PLK1 kinase inhibitor BI2536.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [46] {ECO:0007744|PDB:7K1P}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1522-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to
RT bromosporine.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [47] {ECO:0007744|PDB:7K27}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound
RT to ATR inhibitor AZ20.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [48] {ECO:0007744|PDB:7K3O}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1522-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the unliganded second bromodomain (BD2) of human
RT TAF1.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [49] {ECO:0007744|PDB:7K42}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1522-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to
RT dioxane.";
RL Submitted (SEP-2020) to the PDB data bank.
RN [50] {ECO:0007744|PDB:7K6F}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Bikowitz M.J., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 in
RT complex with MES (2-(N-morpholino)ethanesulfonic acid).";
RL Submitted (SEP-2020) to the PDB data bank.
RN [51] {ECO:0007744|PDB:7L6X}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound
RT to GNE-371.";
RL Submitted (DEC-2020) to the PDB data bank.
RN [52] {ECO:0007744|PDB:7LB0}
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound
RT to ZS1-295.";
RL Submitted (JAN-2021) to the PDB data bank.
RN [53] {ECO:0007744|PDB:7LB1}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound
RT to ZS1-585.";
RL Submitted (JAN-2021) to the PDB data bank.
RN [54] {ECO:0007744|PDB:7LB2}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound
RT to ZS1-589.";
RL Submitted (JAN-2021) to the PDB data bank.
RN [55] {ECO:0007744|PDB:7N42}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1394-1656.
RA Karim M.R., Schonbrunn E.;
RT "Crystal structure of the tandem bromodomain of human TAF1 (TAF1-T) bound
RT to ZS1-681.";
RL Submitted (JUN-2021) to the PDB data bank.
RN [56] {ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.04 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE TFIID COMPLEX, AND SUBUNIT.
RX PubMed=33795473; DOI=10.1126/science.aba8490;
RA Chen X., Qi Y., Wu Z., Wang X., Li J., Zhao D., Hou H., Li Y., Yu Z.,
RA Liu W., Wang M., Ren Y., Li Z., Yang H., Xu Y.;
RT "Structural insights into preinitiation complex assembly on core
RT promoters.";
RL Science 372:0-0(2021).
RN [57]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-290; GLY-318; ASP-474; LYS-672 AND
RP ILE-712.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [58]
RP INVOLVEMENT IN MRXS33, AND VARIANTS MRXS33 SER-596; ARG-807; HIS-976;
RP TRP-1246; THR-1337; HIS-1452 AND HIS-1517.
RX PubMed=26637982; DOI=10.1016/j.ajhg.2015.11.005;
RA O'Rawe J.A., Wu Y., Doerfel M.J., Rope A.F., Au P.Y., Parboosingh J.S.,
RA Moon S., Kousi M., Kosma K., Smith C.S., Tzetis M., Schuette J.L.,
RA Hufnagel R.B., Prada C.E., Martinez F., Orellana C., Crain J.,
RA Caro-Llopis A., Oltra S., Monfort S., Jimenez-Barron L.T., Swensen J.,
RA Ellingwood S., Smith R., Fang H., Ospina S., Stegmann S., Den Hollander N.,
RA Mittelman D., Highnam G., Robison R., Yang E., Faivre L., Roubertie A.,
RA Riviere J.B., Monaghan K.G., Wang K., Davis E.E., Katsanis N.,
RA Kalscheuer V.M., Wang E.H., Metcalfe K., Kleefstra T., Innes A.M.,
RA Kitsiou-Tzeli S., Rosello M., Keegan C.E., Lyon G.J.;
RT "TAF1 Variants Are Associated with Dysmorphic Features, Intellectual
RT Disability, and Neurological Manifestations.";
RL Am. J. Hum. Genet. 97:922-932(2015).
RN [59]
RP VARIANTS ASP-493 AND CYS-1190.
RX PubMed=25644381; DOI=10.1038/mp.2014.193;
RA Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P.,
RA Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T., Love M.I.,
RA Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M., Fischer U.,
RA Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N., Castelnau L.,
RA Rucci J., Montjean R., Dorseuil O., Billuart P., Stuhlmann T., Shaw M.,
RA Corbett M.A., Gardner A., Willis-Owen S., Tan C., Friend K.L., Belet S.,
RA van Roozendaal K.E., Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R.,
RA O'Keeffe S., Chenna R., van Boemmel A., Goeke J., Hackett A., Field M.,
RA Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G.,
RA Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B.,
RA Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P.,
RA Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M.,
RA Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B.,
RA Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R.,
RA Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H.,
RA Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.;
RT "X-exome sequencing of 405 unresolved families identifies seven novel
RT intellectual disability genes.";
RL Mol. Psychiatry 21:133-148(2016).
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription (PubMed:33795473). TFIID recognizes and binds promoters
CC with or without a TATA box via its subunit TBP, a TATA-box-binding
CC protein, and promotes assembly of the pre-initiation complex (PIC)
CC (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated
CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7,
CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF1 is
CC the largest component and core scaffold of the TFIID complex, involved
CC in nucleating complex assembly (PubMed:25412659, PubMed:27007846,
CC PubMed:33795473). TAF1 forms a promoter DNA binding subcomplex of
CC TFIID, together with TAF7 and TAF2 (PubMed:33795473). Contains novel
CC N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or
CC transphosphorylate other transcription factors (PubMed:25412659,
CC PubMed:8625415). Phosphorylates TP53 on 'Thr-55' which leads to MDM2-
CC mediated degradation of TP53 (PubMed:25412659). Phosphorylates GTF2A1
CC and GTF2F1 on Ser residues (PubMed:25412659). Possesses DNA-binding
CC activity (PubMed:25412659). Essential for progression of the G1 phase
CC of the cell cycle (PubMed:11278496, PubMed:15053879, PubMed:2038334,
CC PubMed:8450888, PubMed:8625415, PubMed:9660973, PubMed:9858607).
CC Exhibits histone acetyltransferase activity towards histones H3 and H4
CC (PubMed:15870300). {ECO:0000269|PubMed:11278496,
CC ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15870300,
CC ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:25412659,
CC ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:33795473,
CC ECO:0000269|PubMed:8450888, ECO:0000269|PubMed:8625415,
CC ECO:0000269|PubMed:9660973, ECO:0000269|PubMed:9858607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:15870300};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Autophosphorylates on Ser residues
CC (PubMed:8625415). Inhibited by retinoblastoma tumor suppressor protein,
CC RB1 (PubMed:9858607). Binding to TAF7 or CIITA inhibits the histone
CC acetyltransferase activity (PubMed:11592977, PubMed:22711989).
CC {ECO:0000269|PubMed:11592977, ECO:0000269|PubMed:22711989,
CC ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9858607}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein TBP, and a number of TBP-
CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5,
CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:7680771,
CC PubMed:33795473). Interacts with TAF7; the interaction is direct
CC (PubMed:25412659, PubMed:11592977). TAF1, when part of the TFIID
CC complex, interacts with C-terminus of TP53 (PubMed:15053879). Part of a
CC TFIID-containing RNA polymerase II pre-initiation complex that is
CC composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1,
CC GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2,
CC TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13
CC (PubMed:27007846). Component of some MLL1/MLL complex, at least
CC composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and
CC RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70,
CC INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31,
CC RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
CC and TEX10 (PubMed:15960975). RB1 interacts with the N-terminal domain
CC of TAF1 (PubMed:9858607). Interacts with ASF1A and ASF1B
CC (PubMed:10759893, PubMed:12093919, PubMed:12842904). Interacts (via
CC bromo domains) with acetylated lysine residues on the N-terminus of
CC histone H1.4, H2A, H2B, H3 and H4 (in vitro) (PubMed:22464331).
CC {ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:11592977,
CC ECO:0000269|PubMed:12093919, ECO:0000269|PubMed:12842904,
CC ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:25412659,
CC ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:33795473,
CC ECO:0000269|PubMed:7680771, ECO:0000269|PubMed:9858607}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 Large T antigen.
CC {ECO:0000269|PubMed:8647434}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
CC ICP4. {ECO:0000269|PubMed:8649420}.
CC -!- INTERACTION:
CC P21675; P35269: GTF2F1; NbExp=3; IntAct=EBI-491289, EBI-457886;
CC P21675; P20226: TBP; NbExp=10; IntAct=EBI-491289, EBI-355371;
CC P21675; P03255; Xeno; NbExp=3; IntAct=EBI-491289, EBI-2603114;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2038334,
CC ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:27007846}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=15;
CC Comment=the TAF1/DYT3 multiple transcript system is composed of 38
CC evolutionary conserved exons plus 5 downstream exons referred to as
CC exons d1-d5 that are primate-specific. Multiple highly polymorphic
CC variants can be generated by splicing exons d3 and d4 to various
CC combinations of exons 1-37. {ECO:0000305|PubMed:17952504};
CC Name=2;
CC IsoId=P21675-2; Sequence=Displayed;
CC Name=1;
CC IsoId=P21675-1; Sequence=VSP_061988;
CC Name=13;
CC IsoId=P21675-13; Sequence=VSP_061987, VSP_061988;
CC Name=14;
CC IsoId=P21675-14; Sequence=VSP_061987;
CC Name=15;
CC IsoId=P21675-15; Sequence=VSP_061999, VSP_062000;
CC Name=16;
CC IsoId=P21675-16; Sequence=VSP_061996, VSP_061998;
CC Name=N-TAF1; Synonyms=TA14-391;
CC IsoId=P21675-17; Sequence=VSP_061995;
CC Name=2a;
CC IsoId=P21675-18; Sequence=VSP_061997, VSP_061998;
CC Name=2c;
CC IsoId=P21675-19; Sequence=VSP_061998;
CC Name=2d;
CC IsoId=P21675-20; Sequence=VSP_061995, VSP_061998;
CC Name=2e;
CC IsoId=P21675-21; Sequence=VSP_061993, VSP_061994;
CC Name=2g;
CC IsoId=P21675-22; Sequence=VSP_061995, VSP_061997, VSP_061998;
CC Name=2h;
CC IsoId=P21675-23; Sequence=VSP_061990, VSP_061991;
CC Name=2i;
CC IsoId=P21675-24; Sequence=VSP_061989, VSP_061992;
CC Name=4;
CC IsoId=P21675-25; Sequence=VSP_061997;
CC -!- DOMAIN: The Bromo domain mediates interaction with histones that have
CC acetylated lysine residues at specific positions (PubMed:22464331). The
CC second domain also recognizes and binds histones that are butyrylated
CC and crotonylated (PubMed:26365797). {ECO:0000269|PubMed:22464331,
CC ECO:0000269|PubMed:26365797}.
CC -!- PTM: Phosphorylated by casein kinase II in vitro.
CC {ECO:0000269|PubMed:8625415}.
CC -!- DISEASE: Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: An X-linked
CC dystonia-parkinsonism disorder. Dystonia is defined by the presence of
CC sustained involuntary muscle contractions, often leading to abnormal
CC postures. DYT3 is characterized by severe progressive torsion dystonia
CC followed by parkinsonism. It has a well-defined pathology of extensive
CC neuronal loss and mosaic gliosis in the striatum (caudate nucleus and
CC putamen) which appears to resemble that in Huntington disease.
CC {ECO:0000269|PubMed:12928496, ECO:0000269|PubMed:17273961}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 33
CC (MRXS33) [MIM:300966]: A syndrome characterized by intellectual
CC deficit, delayed psychomotor development, delayed speech and language,
CC and characteristic facial features. {ECO:0000269|PubMed:26637982}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform 16]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2a]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay (Probable). Includes a downstream (d) exon and is
CC preferentially expressed in brain (Probable). May play a role in the
CC regulation of genes involved in dopamine processing and transport
CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}.
CC -!- MISCELLANEOUS: [Isoform 2c]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay (Probable). Includes a downstream (d) exon and is
CC preferentially expressed in brain (Probable). May play a role in the
CC regulation of genes involved in dopamine processing and transport
CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}.
CC -!- MISCELLANEOUS: [Isoform 2d]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay (Probable). Includes a downstream (d) exon and is
CC preferentially expressed in brain (Probable). May play a role in the
CC regulation of genes involved in dopamine processing and transport
CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}.
CC -!- MISCELLANEOUS: [Isoform 2e]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay (Probable). Includes a downstream (d) exon and is
CC preferentially expressed in brain (Probable). May play a role in the
CC regulation of genes involved in dopamine processing and transport
CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}.
CC -!- MISCELLANEOUS: [Isoform 2h]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay (Probable). Includes a downstream (d) exon and is
CC preferentially expressed in brain (Probable). May play a role in the
CC regulation of genes involved in dopamine processing and transport
CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}.
CC -!- MISCELLANEOUS: [Isoform 2i]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay (Probable). Includes a downstream (d) exon and is
CC preferentially expressed in brain (Probable). May play a role in the
CC regulation of genes involved in dopamine processing and transport
CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}.
CC -!- MISCELLANEOUS: [Isoform 2g]: Includes a downstream (d) exon and is
CC preferentially expressed in brain (Probable). May play a role in the
CC regulation of genes involved in dopamine processing and transport
CC (Probable). {ECO:0000305|PubMed:17952504}.
CC -!- MISCELLANEOUS: [Isoform 15]: May be produced at very low levels due to
CC a premature stop CC codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform N-TAF1]: Only detected in brain, highest
CC expression in the caudate nucleus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30073.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal and C-terminal part.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf1/";
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; D90359; BAA14374.1; -; mRNA.
DR EMBL; AB300418; BAG15901.1; -; mRNA.
DR EMBL; AY623109; AAT38105.1; -; Genomic_DNA.
DR EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X07024; CAA30073.1; ALT_SEQ; mRNA.
DR EMBL; AB209316; BAD92553.1; -; mRNA.
DR EMBL; AJ549247; CAD70490.1; -; mRNA.
DR EMBL; AJ549248; CAD70491.3; -; mRNA.
DR EMBL; AJ549249; CAD70492.2; -; mRNA.
DR EMBL; AJ549250; CAD70493.3; -; mRNA.
DR EMBL; AJ555148; CAD87527.2; -; mRNA.
DR EMBL; AJ555149; CAD87528.2; -; mRNA.
DR EMBL; AM711892; CAM98555.1; -; mRNA.
DR EMBL; AM711893; CAM98556.1; -; mRNA.
DR EMBL; AM711894; CAM98557.1; -; mRNA.
DR EMBL; AM711895; CAM98558.1; -; mRNA.
DR CCDS; CCDS14412.2; -. [P21675-14]
DR CCDS; CCDS35325.2; -. [P21675-13]
DR PIR; A40262; A40262.
DR RefSeq; NP_001273003.1; NM_001286074.1.
DR RefSeq; NP_004597.2; NM_004606.4. [P21675-14]
DR RefSeq; NP_620278.1; NM_138923.3. [P21675-13]
DR RefSeq; XP_005262352.1; XM_005262295.1.
DR PDB; 1EQF; X-ray; 2.10 A; A=1380-1659.
DR PDB; 3AAD; X-ray; 3.30 A; A=1363-1650.
DR PDB; 3UV4; X-ray; 1.89 A; A/B=1522-1656.
DR PDB; 3UV5; X-ray; 2.03 A; A=1394-1656.
DR PDB; 4RGW; X-ray; 2.30 A; A=600-1236.
DR PDB; 4YYM; X-ray; 1.50 A; A/B=1518-1659.
DR PDB; 4YYN; X-ray; 1.85 A; A/B=1518-1659.
DR PDB; 5FUR; EM; 8.50 A; G=1-1893.
DR PDB; 5I1Q; X-ray; 1.50 A; A=1518-1659.
DR PDB; 5I29; X-ray; 1.21 A; A=1518-1659.
DR PDB; 5MG2; X-ray; 1.75 A; A=1522-1656.
DR PDB; 6BQD; X-ray; 2.14 A; A/B=1522-1651.
DR PDB; 6FIC; X-ray; 2.18 A; T=1380-1659.
DR PDB; 6MZD; EM; 9.80 A; A=21-1893.
DR PDB; 6MZL; EM; 23.00 A; A=1-1893.
DR PDB; 6MZM; EM; 7.50 A; A=609-1104.
DR PDB; 6P38; X-ray; 2.80 A; A=1522-1656.
DR PDB; 6P39; X-ray; 2.94 A; A=1521-1656.
DR PDB; 6P3A; X-ray; 2.99 A; A/B=1522-1656.
DR PDB; 7EDX; EM; 4.50 A; A=1-1893.
DR PDB; 7EG7; EM; 6.20 A; A=1-1893.
DR PDB; 7EG8; EM; 7.40 A; A=1-1893.
DR PDB; 7EG9; EM; 3.70 A; A=1-1893.
DR PDB; 7EGA; EM; 4.10 A; A=1-1893.
DR PDB; 7EGB; EM; 3.30 A; A=1-1893.
DR PDB; 7EGC; EM; 3.90 A; A=1-1893.
DR PDB; 7EGD; EM; 6.75 A; A=1-1893.
DR PDB; 7EGE; EM; 9.00 A; A=1-1893.
DR PDB; 7EGH; EM; 3.04 A; A=1-1893.
DR PDB; 7EGI; EM; 9.82 A; A=1-1893.
DR PDB; 7EGJ; EM; 8.64 A; A=1-1893.
DR PDB; 7ENA; EM; 4.07 A; DA=1-1893.
DR PDB; 7ENC; EM; 4.13 A; DA=1-1893.
DR PDB; 7JJG; X-ray; 1.60 A; A=1522-1656.
DR PDB; 7JJH; X-ray; 2.10 A; A=1394-1656.
DR PDB; 7JSP; X-ray; 1.70 A; A=1522-1656.
DR PDB; 7JTC; X-ray; 2.05 A; A=1522-1656.
DR PDB; 7K03; X-ray; 1.60 A; A=1394-1656.
DR PDB; 7K0D; X-ray; 2.20 A; A=1394-1656.
DR PDB; 7K0U; X-ray; 2.52 A; A/B=1522-1656.
DR PDB; 7K1P; X-ray; 2.45 A; A=1522-1656.
DR PDB; 7K27; X-ray; 1.50 A; A=1394-1656.
DR PDB; 7K3O; X-ray; 1.70 A; A/B=1522-1656.
DR PDB; 7K42; X-ray; 1.70 A; A/B=1522-1656.
DR PDB; 7K6F; X-ray; 1.86 A; A=1394-1656.
DR PDB; 7L6X; X-ray; 2.75 A; A=1394-1656.
DR PDB; 7LB0; X-ray; 2.33 A; A=1394-1656.
DR PDB; 7LB1; X-ray; 1.35 A; A=1394-1656.
DR PDB; 7LB2; X-ray; 1.70 A; A=1394-1656.
DR PDB; 7LB3; X-ray; 1.90 A; A=1522-1656.
DR PDB; 7N42; X-ray; 1.90 A; A=1394-1656.
DR PDB; 7P4S; X-ray; 2.17 A; A=1522-1656.
DR PDB; 7T2I; X-ray; 1.89 A; A=1394-1656.
DR PDB; 7T36; X-ray; 1.65 A; A=1394-1656.
DR PDB; 8GXQ; EM; 5.04 A; DA=1-1893.
DR PDB; 8GXS; EM; 4.16 A; DA=1-1893.
DR PDB; 8WAK; EM; 5.47 A; A=1-1872.
DR PDB; 8WAL; EM; 8.52 A; A=1-1872.
DR PDB; 8WAN; EM; 6.07 A; A=1-1872.
DR PDB; 8WAO; EM; 6.40 A; A=1-1872.
DR PDB; 8WAP; EM; 5.85 A; A=1-1872.
DR PDB; 8WAQ; EM; 6.29 A; A=1-1872.
DR PDB; 8WAR; EM; 7.20 A; A=1-1872.
DR PDB; 8WAS; EM; 6.13 A; A=1-1872.
DR PDBsum; 1EQF; -.
DR PDBsum; 3AAD; -.
DR PDBsum; 3UV4; -.
DR PDBsum; 3UV5; -.
DR PDBsum; 4RGW; -.
DR PDBsum; 4YYM; -.
DR PDBsum; 4YYN; -.
DR PDBsum; 5FUR; -.
DR PDBsum; 5I1Q; -.
DR PDBsum; 5I29; -.
DR PDBsum; 5MG2; -.
DR PDBsum; 6BQD; -.
DR PDBsum; 6FIC; -.
DR PDBsum; 6MZD; -.
DR PDBsum; 6MZL; -.
DR PDBsum; 6MZM; -.
DR PDBsum; 6P38; -.
DR PDBsum; 6P39; -.
DR PDBsum; 6P3A; -.
DR PDBsum; 7EDX; -.
DR PDBsum; 7EG7; -.
DR PDBsum; 7EG8; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7EGD; -.
DR PDBsum; 7EGE; -.
DR PDBsum; 7EGH; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7JJG; -.
DR PDBsum; 7JJH; -.
DR PDBsum; 7JSP; -.
DR PDBsum; 7JTC; -.
DR PDBsum; 7K03; -.
DR PDBsum; 7K0D; -.
DR PDBsum; 7K0U; -.
DR PDBsum; 7K1P; -.
DR PDBsum; 7K27; -.
DR PDBsum; 7K3O; -.
DR PDBsum; 7K42; -.
DR PDBsum; 7K6F; -.
DR PDBsum; 7L6X; -.
DR PDBsum; 7LB0; -.
DR PDBsum; 7LB1; -.
DR PDBsum; 7LB2; -.
DR PDBsum; 7LB3; -.
DR PDBsum; 7N42; -.
DR PDBsum; 7P4S; -.
DR PDBsum; 7T2I; -.
DR PDBsum; 7T36; -.
DR PDBsum; 8GXQ; -.
DR PDBsum; 8GXS; -.
DR PDBsum; 8WAK; -.
DR PDBsum; 8WAL; -.
DR PDBsum; 8WAN; -.
DR PDBsum; 8WAO; -.
DR PDBsum; 8WAP; -.
DR PDBsum; 8WAQ; -.
DR PDBsum; 8WAR; -.
DR PDBsum; 8WAS; -.
DR AlphaFoldDB; P21675; -.
DR EMDB; EMD-31075; -.
DR EMDB; EMD-31107; -.
DR EMDB; EMD-31108; -.
DR EMDB; EMD-31109; -.
DR EMDB; EMD-31110; -.
DR EMDB; EMD-31111; -.
DR EMDB; EMD-31112; -.
DR EMDB; EMD-31113; -.
DR EMDB; EMD-31114; -.
DR EMDB; EMD-31117; -.
DR EMDB; EMD-31118; -.
DR EMDB; EMD-31119; -.
DR EMDB; EMD-31204; -.
DR EMDB; EMD-31207; -.
DR EMDB; EMD-34359; -.
DR EMDB; EMD-34360; -.
DR EMDB; EMD-9302; -.
DR EMDB; EMD-9305; -.
DR EMDB; EMD-9306; -.
DR SASBDB; P21675; -.
DR SMR; P21675; -.
DR BioGRID; 112735; 238.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR CORUM; P21675; -.
DR DIP; DIP-147N; -.
DR IntAct; P21675; 62.
DR MINT; P21675; -.
DR STRING; 9606.ENSP00000406549; -.
DR BindingDB; P21675; -.
DR ChEMBL; CHEMBL3217390; -.
DR GuidetoPHARMACOLOGY; 2231; -.
DR GlyCosmos; P21675; 1 site, 1 glycan.
DR GlyGen; P21675; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P21675; -.
DR PhosphoSitePlus; P21675; -.
DR BioMuta; TAF1; -.
DR DMDM; 115942; -.
DR EPD; P21675; -.
DR jPOST; P21675; -.
DR MassIVE; P21675; -.
DR MaxQB; P21675; -.
DR PaxDb; 9606-ENSP00000406549; -.
DR PeptideAtlas; P21675; -.
DR ProteomicsDB; 3401; -.
DR ProteomicsDB; 53886; -. [P21675-1]
DR ProteomicsDB; 53887; -. [P21675-2]
DR Pumba; P21675; -.
DR ABCD; P21675; 1 sequenced antibody.
DR Antibodypedia; 346; 341 antibodies from 37 providers.
DR DNASU; 6872; -.
DR Ensembl; ENST00000373790.9; ENSP00000362895.5; ENSG00000147133.17. [P21675-13]
DR Ensembl; ENST00000423759.6; ENSP00000406549.2; ENSG00000147133.17. [P21675-14]
DR GeneID; 6872; -.
DR KEGG; hsa:6872; -.
DR MANE-Select; ENST00000423759.6; ENSP00000406549.2; NM_004606.5; NP_004597.3. [P21675-14]
DR UCSC; uc004dzt.6; human. [P21675-2]
DR AGR; HGNC:11535; -.
DR CTD; 6872; -.
DR DisGeNET; 6872; -.
DR GeneCards; TAF1; -.
DR GeneReviews; TAF1; -.
DR HGNC; HGNC:11535; TAF1.
DR HPA; ENSG00000147133; Low tissue specificity.
DR MalaCards; TAF1; -.
DR MIM; 300966; phenotype.
DR MIM; 313650; gene.
DR MIM; 314250; phenotype.
DR neXtProt; NX_P21675; -.
DR OpenTargets; ENSG00000147133; -.
DR Orphanet; 53351; X-linked dystonia-parkinsonism.
DR Orphanet; 480907; X-linked intellectual disability-global development delay-facial dysmorphism-sacral caudal remnant syndrome.
DR PharmGKB; PA36310; -.
DR VEuPathDB; HostDB:ENSG00000147133; -.
DR eggNOG; KOG0008; Eukaryota.
DR GeneTree; ENSGT00940000155242; -.
DR HOGENOM; CLU_000572_3_0_1; -.
DR InParanoid; P21675; -.
DR OrthoDB; 5482320at2759; -.
DR PhylomeDB; P21675; -.
DR TreeFam; TF313573; -.
DR BRENDA; 2.3.1.48; 2681.
DR PathwayCommons; P21675; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; P21675; -.
DR SIGNOR; P21675; -.
DR BioGRID-ORCS; 6872; 343 hits in 821 CRISPR screens.
DR ChiTaRS; TAF1; human.
DR EvolutionaryTrace; P21675; -.
DR GeneWiki; TAF1; -.
DR GenomeRNAi; 6872; -.
DR Pharos; P21675; Tchem.
DR PRO; PR:P21675; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P21675; Protein.
DR Bgee; ENSG00000147133; Expressed in sural nerve and 182 other cell types or tissues.
DR ExpressionAtlas; P21675; baseline and differential.
DR Genevisible; P21675; HS.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:BHF-UCL.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0004672; F:protein kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:BHF-UCL.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IPI:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:BHF-UCL.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:BHF-UCL.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071318; P:cellular response to ATP; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034644; P:cellular response to UV; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006974; P:DNA damage response; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030901; P:midbrain development; IGI:ParkinsonsUK-UCL.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR GO; GO:1905524; P:negative regulation of protein autoubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
DR GO; GO:2000825; P:positive regulation of androgen receptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; TAS:ParkinsonsUK-UCL.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0006361; P:transcription initiation at RNA polymerase I promoter; IGI:ParkinsonsUK-UCL.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:BHF-UCL.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
DR CDD; cd05511; Bromo_TFIID; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR Gene3D; 1.10.1100.10; TAFII-230 TBP-binding domain; 1.
DR IDEAL; IID00545; -.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR040240; TAF1.
DR InterPro; IPR011177; TAF1_animal.
DR InterPro; IPR022591; TAF1_HAT_dom.
DR InterPro; IPR009067; TAF_II_230-bd.
DR InterPro; IPR036741; TAFII-230_TBP-bd_sf.
DR InterPro; IPR041670; Znf-CCHC_6.
DR PANTHER; PTHR13900; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR PANTHER; PTHR13900:SF0; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF12157; DUF3591; 1.
DR Pfam; PF09247; TBP-binding; 1.
DR Pfam; PF15288; zf-CCHC_6; 1.
DR PIRSF; PIRSF003047; TAF1_animal; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR SUPFAM; SSF47055; TAF(II)230 TBP-binding fragment; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative initiation;
KW Alternative splicing; ATP-binding; Bromodomain; Cell cycle;
KW Disease variant; DNA-binding; Dystonia; Host-virus interaction;
KW Intellectual disability; Isopeptide bond; Kinase; Nucleotide-binding;
KW Nucleus; Parkinsonism; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..1893
FT /note="Transcription initiation factor TFIID subunit 1"
FT /id="PRO_0000211215"
FT DOMAIN 1..435
FT /note="Protein kinase 1"
FT DOMAIN 1418..1488
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1446..1893
FT /note="Protein kinase 2"
FT DOMAIN 1541..1611
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DNA_BIND 1216..1294
FT /note="HMG box; involved in promoter binding"
FT /evidence="ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7,
FT ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9,
FT ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB,
FT ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD,
FT ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGH,
FT ECO:0007744|PDB:7EGI, ECO:0007744|PDB:7EGJ"
FT REGION 155..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..997
FT /note="Histone acetyltransferase (HAT)"
FT REGION 990..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1650
FT /note="Interaction with ASF1A and ASF1B"
FT /evidence="ECO:0000269|PubMed:12842904"
FT REGION 1651..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1372..1379
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 198..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1754
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 137
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8625415"
FT MOD_RES 328
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8625415,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 565
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80UV9"
FT MOD_RES 1847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 13 and isoform 14)"
FT /id="VSP_061987"
FT VAR_SEQ 178..198
FT /note="Missing (in isoform 1 and isoform 13)"
FT /id="VSP_061988"
FT VAR_SEQ 1546..1561
FT /note="SWPFHHPVNKKFVPDY -> VSCLCAKYFLAISSPS (in isoform
FT 2i)"
FT /evidence="ECO:0000303|PubMed:17952504"
FT /id="VSP_061989"
FT VAR_SEQ 1546..1549
FT /note="SWPF -> IITK (in isoform 2h)"
FT /evidence="ECO:0000303|PubMed:17952504"
FT /id="VSP_061990"
FT VAR_SEQ 1550..1893
FT /note="Missing (in isoform 2h)"
FT /evidence="ECO:0000303|PubMed:17952504"
FT /id="VSP_061991"
FT VAR_SEQ 1562..1893
FT /note="Missing (in isoform 2i)"
FT /evidence="ECO:0000303|PubMed:17952504"
FT /id="VSP_061992"
FT VAR_SEQ 1606..1613
FT /note="PESQYTKT -> YMCTTCRT (in isoform 2e)"
FT /evidence="ECO:0000303|PubMed:12928496,
FT ECO:0000303|PubMed:17952504"
FT /id="VSP_061993"
FT VAR_SEQ 1614..1893
FT /note="Missing (in isoform 2e)"
FT /evidence="ECO:0000303|PubMed:12928496,
FT ECO:0000303|PubMed:17952504"
FT /id="VSP_061994"
FT VAR_SEQ 1666
FT /note="Q -> QAK (in isoform N-TAF1, isoform 2d and isoform
FT 2g)"
FT /evidence="ECO:0000303|PubMed:12928496,
FT ECO:0000303|PubMed:17273961, ECO:0000303|PubMed:17952504"
FT /id="VSP_061995"
FT VAR_SEQ 1706..1708
FT /note="VTQ -> MRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP (in
FT isoform 16)"
FT /evidence="ECO:0000303|PubMed:12928496"
FT /id="VSP_061996"
FT VAR_SEQ 1708
FT /note="Q -> QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP (in isoform
FT 4, isoform 2a and isoform 2g)"
FT /evidence="ECO:0000303|PubMed:12928496,
FT ECO:0000303|PubMed:17952504, ECO:0000303|Ref.7"
FT /id="VSP_061997"
FT VAR_SEQ 1820..1893
FT /note="SYGSYEEPDPKSNTQDTSFSSIGGYEVSEEEEDEEEEEQRSGPSVLSQVHLS
FT EDEEDSEDFHSIAGDSDLDSDE -> RYQ (in isoform 2a, isoform 16,
FT isoform 2c, isoform 2d and isoform 2g)"
FT /evidence="ECO:0000303|PubMed:12928496,
FT ECO:0000303|PubMed:17952504"
FT /id="VSP_061998"
FT VAR_SEQ 1820
FT /note="S -> R (in isoform 15)"
FT /id="VSP_061999"
FT VAR_SEQ 1821..1893
FT /note="Missing (in isoform 15)"
FT /id="VSP_062000"
FT VARIANT 290
FT /note="L -> V (in dbSNP:rs28382158)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4"
FT /id="VAR_020678"
FT VARIANT 318
FT /note="A -> G (in dbSNP:rs35317750)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041930"
FT VARIANT 474
FT /note="G -> D (in a colorectal adenocarcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041931"
FT VARIANT 493
FT /note="N -> D (found in a patient with X-linked
FT intellectual disability; uncertain significance;
FT dbSNP:rs200177996)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077838"
FT VARIANT 596
FT /note="P -> S (in MRXS33; dbSNP:rs864321630)"
FT /evidence="ECO:0000269|PubMed:26637982"
FT /id="VAR_076394"
FT VARIANT 672
FT /note="E -> K (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041932"
FT VARIANT 712
FT /note="M -> I (in a lung bronchoalveolar carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041933"
FT VARIANT 807
FT /note="C -> R (in MRXS33; dbSNP:rs864321628)"
FT /evidence="ECO:0000269|PubMed:26637982"
FT /id="VAR_076395"
FT VARIANT 976
FT /note="D -> H (in MRXS33; dbSNP:rs864321631)"
FT /evidence="ECO:0000269|PubMed:26637982"
FT /id="VAR_076396"
FT VARIANT 1190
FT /note="R -> C (found in a patient with X-linked
FT intellectual disability; uncertain significance;
FT dbSNP:rs1569301036)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077839"
FT VARIANT 1246
FT /note="R -> W (in MRXS33; dbSNP:rs864321629)"
FT /evidence="ECO:0000269|PubMed:26637982"
FT /id="VAR_076397"
FT VARIANT 1337
FT /note="I -> T (in MRXS33; dbSNP:rs864321627)"
FT /evidence="ECO:0000269|PubMed:26637982"
FT /id="VAR_076398"
FT VARIANT 1404
FT /note="V -> I (in dbSNP:rs7050748)"
FT /id="VAR_048433"
FT VARIANT 1452
FT /note="R -> H (in MRXS33; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:26637982"
FT /id="VAR_076399"
FT VARIANT 1517
FT /note="N -> H (in MRXS33; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:26637982"
FT /id="VAR_076400"
FT MUTAGEN 137
FT /note="S->A: No decrease in kinase activity."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 145
FT /note="D->A: Reduces kinase activity; when associated with
FT A-147; A-149; A-150; A-152 and A-154."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 147
FT /note="D->A: Reduces kinase activity; when associated with
FT A-145; A-149; A-150; A-152 and A-154."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 149
FT /note="E->A: Reduces kinase activity; when associated with
FT A-145; A-147; A-150; A-152 and A-154."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 150
FT /note="D->A: Reduces kinase activity; when associated with
FT A-145; A-147; A-149; A-152 and A-154."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 152
FT /note="D->A: Reduces kinase activity; when associated with
FT A-145; A-147; A-149; A-150 and A-154."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 154
FT /note="K->A: Reduces kinase activity; when associated with
FT A-145; A-147; A-149; A-150 and A-152."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 326
FT /note="C->A: Reduces kinase activity; when associated with
FT A-328; A-329; A-330 and A-331."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 328
FT /note="S->A: Reduces kinase activity; when associated with
FT A-326; A-329; A-330 and A-331."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 329
FT /note="D->A: Reduces kinase activity; when associated with
FT A-326; A-328; A-330 and A-331."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 330
FT /note="D->A: Reduces kinase activity; when associated with
FT A-326; A-328; A-329 and A-331."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 331
FT /note="E->A: Reduces kinase activity; when associated with
FT A-326; A-328; A-329 and A-330."
FT /evidence="ECO:0000269|PubMed:9660973"
FT MUTAGEN 742
FT /note="E->Q: 25% decrease in histone acetylation."
FT /evidence="ECO:0000269|PubMed:15870300"
FT MUTAGEN 848..850
FT /note="Missing: Dramatic decrease in histone acetylation."
FT /evidence="ECO:0000269|PubMed:15870300"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 473..477
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:4RGW"
FT TURN 600..602
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 609..613
FT /evidence="ECO:0007829|PDB:4RGW"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 634..638
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 640..655
FT /evidence="ECO:0007829|PDB:4RGW"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 668..671
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 675..685
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 697..704
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 718..724
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 729..732
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 739..756
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 761..767
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 778..782
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 797..817
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 820..822
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 827..833
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 839..847
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 850..853
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 861..864
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 873..879
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 882..900
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 905..907
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 925..928
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 931..942
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 947..952
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 958..962
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 964..968
FT /evidence="ECO:0007829|PDB:4RGW"
FT HELIX 993..997
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 999..1010
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 1014..1018
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 1022..1034
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 1055..1078
FT /evidence="ECO:0007829|PDB:4RGW"
FT STRAND 1165..1170
FT /evidence="ECO:0007829|PDB:7EGH"
FT TURN 1174..1176
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 1180..1185
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 1188..1203
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 1217..1241
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 1381..1397
FT /evidence="ECO:0007829|PDB:7LB1"
FT HELIX 1403..1405
FT /evidence="ECO:0007829|PDB:7LB1"
FT STRAND 1406..1408
FT /evidence="ECO:0007829|PDB:3AAD"
FT TURN 1411..1413
FT /evidence="ECO:0007829|PDB:7LB1"
FT HELIX 1417..1420
FT /evidence="ECO:0007829|PDB:7LB1"
FT HELIX 1427..1435
FT /evidence="ECO:0007829|PDB:7LB1"
FT HELIX 1442..1459
FT /evidence="ECO:0007829|PDB:7LB1"
FT STRAND 1462..1464
FT /evidence="ECO:0007829|PDB:3AAD"
FT HELIX 1465..1483
FT /evidence="ECO:0007829|PDB:7LB1"
FT HELIX 1485..1495
FT /evidence="ECO:0007829|PDB:7LB1"
FT HELIX 1497..1500
FT /evidence="ECO:0007829|PDB:7LB1"
FT HELIX 1502..1517
FT /evidence="ECO:0007829|PDB:5I29"
FT TURN 1518..1521
FT /evidence="ECO:0007829|PDB:5I29"
FT HELIX 1526..1528
FT /evidence="ECO:0007829|PDB:5I29"
FT TURN 1534..1536
FT /evidence="ECO:0007829|PDB:5I29"
FT STRAND 1537..1539
FT /evidence="ECO:0007829|PDB:6P3A"
FT HELIX 1540..1543
FT /evidence="ECO:0007829|PDB:5I29"
FT STRAND 1544..1546
FT /evidence="ECO:0007829|PDB:6P3A"
FT HELIX 1550..1558
FT /evidence="ECO:0007829|PDB:5I29"
FT HELIX 1565..1583
FT /evidence="ECO:0007829|PDB:5I29"
FT STRAND 1585..1587
FT /evidence="ECO:0007829|PDB:7K6F"
FT HELIX 1588..1606
FT /evidence="ECO:0007829|PDB:5I29"
FT HELIX 1608..1634
FT /evidence="ECO:0007829|PDB:5I29"
FT MOD_RES P21675-16:1718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES P21675-18:1721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES P21675-22:1723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES P21675-25:1721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
SQ SEQUENCE 1893 AA; 214714 MW; AE148C222B418BB4 CRC64;
MGPGCDLLLR TAATITAAAI MSDTDSDEDS AGGGPFSLAG FLFGNINGAG QLEGESVLDD
ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW VRSTEDAVDY SDINEVAEDE
SRRYQQTMGS LQPLCHSDYD EDDYDADCED IDCKLMPPPP PPPGPMKKDK DQDSITGVSE
NGEGIILPSI IAPSSLASEK VDFSSSSDSE SEMGPQEATQ AESEDGKLTL PLAGIMQHDA
TKLLPSVTEL FPEFRPGKVL RFLRLFGPGK NVPSVWRSAR RKRKKKHREL IQEEQIQEVE
CSVESEVSQK SLWNYDYAPP PPPEQCLSDD EITMMAPVES KFSQSTGDID KVTDTKPRVA
EWRYGPARLW YDMLGVPEDG SGFDYGFKLR KTEHEPVIKS RMIEEFRKLE ENNGTDLLAD
ENFLMVTQLH WEDDIIWDGE DVKHKGTKPQ RASLAGWLPS SMTRNAMAYN VQQGFAATLD
DDKPWYSIFP IDNEDLVYGR WEDNIIWDAQ AMPRLLEPPV LTLDPNDENL ILEIPDEKEE
ATSNSPSKES KKESSLKKSR ILLGKTGVIK EEPQQNMSQP EVKDPWNLSN DEYYYPKQQG
LRGTFGGNII QHSIPAVELR QPFFPTHMGP IKLRQFHRPP LKKYSFGALS QPGPHSVQPL
LKHIKKKAKM REQERQASGG GEMFFMRTPQ DLTGKDGDLI LAEYSEENGP LMMQVGMATK
IKNYYKRKPG KDPGAPDCKY GETVYCHTSP FLGSLHPGQL LQAFENNLFR APIYLHKMPE
TDFLIIRTRQ GYYIRELVDI FVVGQQCPLF EVPGPNSKRA NTHIRDFLQV FIYRLFWKSK
DRPRRIRMED IKKAFPSHSE SSIRKRLKLC ADFKRTGMDS NWWVLKSDFR LPTEEEIRAM
VSPEQCCAYY SMIAAEQRLK DAGYGEKSFF APEEENEEDF QMKIDDEVRT APWNTTRAFI
AAMKGKCLLE VTGVADPTGC GEGFSYVKIP NKPTQQKDDK EPQPVKKTVT GTDADLRRLS
LKNAKQLLRK FGVPEEEIKK LSRWEVIDVV RTMSTEQARS GEGPMSKFAR GSRFSVAEHQ
ERYKEECQRI FDLQNKVLSS TEVLSTDTDS SSAEDSDFEE MGKNIENMLQ NKKTSSQLSR
EREEQERKEL QRMLLAAGSA ASGNNHRDDD TASVTSLNSS ATGRCLKIYR TFRDEEGKEY
VRCETVRKPA VIDAYVRIRT TKDEEFIRKF ALFDEQHREE MRKERRRIQE QLRRLKRNQE
KEKLKGPPEK KPKKMKERPD LKLKCGACGA IGHMRTNKFC PLYYQTNAPP SNPVAMTEEQ
EEELEKTVIH NDNEELIKVE GTKIVLGKQL IESADEVRRK SLVLKFPKQQ LPPKKKRRVG
TTVHCDYLNR PHKSIHRRRT DPMVTLSSIL ESIINDMRDL PNTYPFHTPV NAKVVKDYYK
IITRPMDLQT LRENVRKRLY PSREEFREHL ELIVKNSATY NGPKHSLTQI SQSMLDLCDE
KLKEKEDKLA RLEKAINPLL DDDDQVAFSF ILDNIVTQKM MAVPDSWPFH HPVNKKFVPD
YYKVIVNPMD LETIRKNISK HKYQSRESFL DDVNLILANS VKYNGPESQY TKTAQEIVNV
CYQTLTEYDE HLTQLEKDIC TAKEAALEEA ELESLDPMTP GPYTPQPPDL YDTNTSLSMS
RDASVFQDES NMSVLDIPSA TPEKQVTQEG EDGDGDLADE EEGTVQQPQA SVLYEDLLMS
EGEDDEEDAG SDEEGDNPFS AIQLSESGSD SDVGSGGIRP KQPRMLQENT RMDMENEESM
MSYEGDGGEA SHGLEDSNIS YGSYEEPDPK SNTQDTSFSS IGGYEVSEEE EDEEEEEQRS
GPSVLSQVHL SEDEEDSEDF HSIAGDSDLD SDE
//
