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 28-JAN-2026, entry version 249. 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC 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:33795473, CC PubMed:7680771). Interacts with TAF7; the interaction is direct CC (PubMed:11592977, PubMed:25412659). 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 BACC1, 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=11; 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 --------------------------------------------------------------------------- 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_620278.2; NM_138923.4. [P21675-13] DR RefSeq; XP_047298351.1; XM_047442395.1. [P21675-14] DR RefSeq; XP_047298355.1; XM_047442399.1. [P21675-13] DR RefSeq; XP_054183607.1; XM_054327632.1. [P21675-14] DR RefSeq; XP_054183611.1; XM_054327636.1. [P21675-13] 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-37395; -. DR EMDB; EMD-37396; -. DR EMDB; EMD-37398; -. DR EMDB; EMD-37399; -. DR EMDB; EMD-37400; -. DR EMDB; EMD-37401; -. DR EMDB; EMD-37402; -. DR EMDB; EMD-37403; -. DR EMDB; EMD-9302; -. DR EMDB; EMD-9305; -. DR EMDB; EMD-9306; -. DR SASBDB; P21675; -. DR SMR; P21675; -. DR BioGRID; 112735; 258. 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 FunCoup; P21675; 3231. DR IntAct; P21675; 83. 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; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P21675; -. DR PhosphoSitePlus; P21675; -. DR BioMuta; TAF1; -. DR DMDM; 115942; -. DR jPOST; P21675; -. DR MassIVE; 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; 301 antibodies from 39 providers. DR DNASU; 6872; -. DR Ensembl; ENST00000373790.9; ENSP00000362895.5; ENSG00000147133.19. [P21675-13] DR Ensembl; ENST00000423759.6; ENSP00000406549.2; ENSG00000147133.19. [P21675-14] DR Ensembl; ENST00000715246.1; ENSP00000520427.1; ENSG00000147133.19. [P21675-2] 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 ClinPGx; PA36310; -. 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 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 VEuPathDB; HostDB:ENSG00000147133; -. DR eggNOG; KOG0008; Eukaryota. DR GeneTree; ENSGT00940000155242; -. DR HOGENOM; CLU_000572_3_0_1; -. DR InParanoid; P21675; -. DR OMA; PARIWYD; -. DR OrthoDB; 5752at2759; -. DR PAN-GO; P21675; 4 GO annotations based on evolutionary models. DR PhylomeDB; P21675; -. 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 Agora; ENSG00000147133; -. 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 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:0140046; F:histone H4K16ac reader activity; IDA:BHF-UCL. DR GO; GO:0016301; F:kinase activity; IDA:ParkinsonsUK-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: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:1901797; P:negative regulation of signal transduction by p53 class mediator; 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:0160207; P:positive regulation of androgen receptor signaling pathway; IDA:ParkinsonsUK-UCL. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-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; TAS:UniProtKB. 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 DisProt; DP03451; -. [P21675-1] DR FunFam; 1.10.1100.10:FF:000001; Transcription initiation factor TFIID subunit; 1. DR FunFam; 1.20.920.10:FF:000019; Transcription initiation factor TFIID subunit; 1. DR FunFam; 1.20.920.10:FF:000020; Transcription initiation factor TFIID subunit; 1. 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; Proteomics identification; KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription; KW Transcription regulation; 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 1397..1505 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1446..1893 FT /note="Protein kinase 2" FT DOMAIN 1519..1628 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 156..165 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..208 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 995..1004 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1139..1148 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1254..1270 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1659..1668 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1709..1723 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1741..1756 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1830..1840 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1846..1857 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1860..1869 FT /note="Polar 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; dbSNP:rs2148297629)" 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 dbSNP:rs2148488251)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076399" FT VARIANT 1517 FT /note="N -> H (in MRXS33; uncertain significance; FT dbSNP:rs1602624914)" 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 363..365 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 368..374 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 420..423 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 431..434 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 494..498 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 501..504 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 591..594 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 614..617 FT /evidence="ECO:0007829|PDB:4RGW" FT TURN 621..623 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 630..634 FT /evidence="ECO:0007829|PDB:4RGW" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 645..647 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 648..650 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 651..653 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 655..659 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 661..676 FT /evidence="ECO:0007829|PDB:4RGW" FT TURN 677..679 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 689..692 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 696..706 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 718..725 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 729..731 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 739..745 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 750..753 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 760..777 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 782..788 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 791..795 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 799..803 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 818..838 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 841..843 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 845..847 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 848..854 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 860..868 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 871..874 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 877..879 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 882..885 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 894..900 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 903..921 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 926..928 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 946..949 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 952..963 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 968..973 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 979..983 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 985..989 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 1014..1018 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1020..1031 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1035..1039 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1043..1055 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1076..1099 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 1186..1191 FT /evidence="ECO:0007829|PDB:7EGH" FT TURN 1195..1197 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 1201..1206 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1209..1224 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1238..1262 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1402..1418 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1424..1426 FT /evidence="ECO:0007829|PDB:7LB1" FT STRAND 1427..1429 FT /evidence="ECO:0007829|PDB:3AAD" FT TURN 1432..1434 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1438..1441 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1448..1456 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1463..1480 FT /evidence="ECO:0007829|PDB:7LB1" FT STRAND 1483..1485 FT /evidence="ECO:0007829|PDB:3AAD" FT HELIX 1486..1504 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1506..1516 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1518..1521 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1523..1538 FT /evidence="ECO:0007829|PDB:5I29" FT TURN 1539..1542 FT /evidence="ECO:0007829|PDB:5I29" FT HELIX 1547..1549 FT /evidence="ECO:0007829|PDB:5I29" FT TURN 1555..1557 FT /evidence="ECO:0007829|PDB:5I29" FT STRAND 1558..1560 FT /evidence="ECO:0007829|PDB:6P3A" FT HELIX 1561..1564 FT /evidence="ECO:0007829|PDB:5I29" FT STRAND 1565..1567 FT /evidence="ECO:0007829|PDB:6P3A" FT HELIX 1571..1579 FT /evidence="ECO:0007829|PDB:5I29" FT HELIX 1586..1604 FT /evidence="ECO:0007829|PDB:5I29" FT STRAND 1606..1608 FT /evidence="ECO:0007829|PDB:7K6F" FT HELIX 1609..1627 FT /evidence="ECO:0007829|PDB:5I29" FT HELIX 1629..1655 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 //