ID TAF1_MOUSE Reviewed; 1891 AA.
AC Q80UV9; A2AM32; A2AM33; O35361; Q3UPF3; Q3V223; Q505F9; Q8BQH8; Q8BQQ7;
AC Q8BR59; Q8C7N8; Q9WTW9; Q9WTX0; Q9WTX1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=Transcription initiation factor TFIID subunit 1 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:P21675};
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|MGI:MGI:1336878}; Synonyms=Ccg1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 601-1891.
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-280 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 849-1237 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-401 AND 1143-1891.
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Corpora quadrigemina, Head, Hippocampus, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 217-370; 841-876 AND 1199-1488.
RC STRAIN=CD-1; TISSUE=Heart;
RX PubMed=10070062; DOI=10.1152/ajpheart.1999.276.3.h803;
RA Saadane N., Alpert L., Chalifour L.E.;
RT "TAFII250, Egr-1, and D-type cyclin expression in mice and neonatal rat
RT cardiomyocytes treated with doxorubicin.";
RL Am. J. Physiol. 276:H803-H814(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 867-1306.
RC TISSUE=Spleen;
RX PubMed=9751712; DOI=10.1073/pnas.95.20.11601;
RA Weissman J.D., Brown J.A., Howcroft T.K., Hwang J., Chawla A., Roche P.A.,
RA Schiltz L., Nakatani Y., Singer D.S.;
RT "HIV-1 tat binds TAFII250 and represses TAFII250-dependent transcription of
RT major histocompatibility class I genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11601-11606(1998).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10438527; DOI=10.1074/jbc.274.33.23480;
RA Wu S.Y., Thomas M.C., Hou S.Y., Likhite V., Chiang C.M.;
RT "Isolation of mouse TFIID and functional characterization of TBP and TFIID
RT in mediating estrogen receptor and chromatin transcription.";
RL J. Biol. Chem. 274:23480-23490(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1690; SER-1693; SER-1799;
RP SER-1802 AND SER-1820, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-565, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 (By similarity). 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) (By
CC similarity). 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 (By similarity). TAF1 is the
CC largest component and core scaffold of the TFIID complex, involved in
CC nucleating complex assembly (PubMed:10438527). TAF1 forms a promoter
CC DNA binding subcomplex of TFIID, together with TAF7 and TAF2 (By
CC similarity). Contains novel N- and C-terminal Ser/Thr kinase domains
CC which can autophosphorylate or transphosphorylate other transcription
CC factors (By similarity). Phosphorylates TP53 on 'Thr-55' which leads to
CC MDM2-mediated degradation of TP53 (By similarity). Phosphorylates
CC GTF2A1 and GTF2F1 on Ser residues (By similarity). Possesses DNA-
CC binding activity (By similarity). Exhibits histone acetyltransferase
CC activity towards histones H3 and H4 (By similarity). Essential for
CC progression of the G1 phase of the cell cycle (By similarity).
CC {ECO:0000250|UniProtKB:P21675, ECO:0000269|PubMed:10438527}.
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:0000250|UniProtKB:P21675};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Autophosphorylates on Ser residues. Inhibited by
CC retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA
CC inhibits the histone acetyltransferase activity.
CC {ECO:0000250|UniProtKB:P21675}.
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) (PubMed:10438527). TFIID consists of at least
CC TBP, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10,
CC TAF11, TAF12 and TAF13. Interacts with TAF7; the interaction is direct.
CC TAF1, when part of the TFIID complex, interacts with C-terminus of
CC TP53. Part of a TFIID-containing RNA polymerase II pre-initiation
CC complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1,
CC GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2,
CC ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10,
CC TAF11, TAF12 and TAF13. 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. RB1 interacts with the N-terminal domain of TAF1. Interacts
CC with ASF1A and ASF1B. Interacts (via bromo domains) with acetylated
CC lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4
CC (in vitro) (By similarity). {ECO:0000250|UniProtKB:P21675,
CC ECO:0000269|PubMed:10438527}.
CC -!- INTERACTION:
CC Q80UV9-1; Q15545: TAF7; Xeno; NbExp=2; IntAct=EBI-15563115, EBI-1560194;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1;
CC IsoId=Q80UV9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UV9-2; Sequence=VSP_023320;
CC Name=3;
CC IsoId=Q80UV9-3; Sequence=VSP_023321;
CC Name=4;
CC IsoId=Q80UV9-4; Sequence=VSP_062001;
CC -!- DOMAIN: The Bromo domain mediates interaction with histones that have
CC acetylated lysine residues at specific positions. The second domain
CC also recognizes and binds histones that are butyrylated and
CC crotonylated. {ECO:0000250|UniProtKB:P21675}.
CC -!- PTM: Phosphorylated by casein kinase II in vitro.
CC {ECO:0000250|UniProtKB:P21675}.
CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34383.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL806534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047418; AAH47418.1; -; mRNA.
DR EMBL; BC094568; AAH94568.1; -; mRNA.
DR EMBL; AK045586; BAC32425.1; -; mRNA.
DR EMBL; AK046668; BAC32828.1; -; mRNA.
DR EMBL; AK049826; BAC33938.1; -; mRNA.
DR EMBL; AK050691; BAC34383.1; ALT_INIT; mRNA.
DR EMBL; AK132088; BAE20976.1; -; mRNA.
DR EMBL; AK143571; BAE25442.1; -; mRNA.
DR EMBL; AF081115; AAD23349.1; -; mRNA.
DR EMBL; AF081116; AAD23348.1; -; mRNA.
DR EMBL; AF081117; AAD23350.1; -; mRNA.
DR EMBL; AF022178; AAC62118.1; -; mRNA.
DR RefSeq; NP_001277658.1; NM_001290729.1.
DR RefSeq; XP_006528113.1; XM_006528050.3.
DR RefSeq; XP_006528115.1; XM_006528052.3.
DR AlphaFoldDB; Q80UV9; -.
DR SMR; Q80UV9; -.
DR BioGRID; 234808; 14.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; Q80UV9; -.
DR DIP; DIP-61093N; -.
DR IntAct; Q80UV9; 2.
DR MINT; Q80UV9; -.
DR STRING; 10090.ENSMUSP00000114765; -.
DR GlyGen; Q80UV9; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q80UV9; -.
DR PhosphoSitePlus; Q80UV9; -.
DR EPD; Q80UV9; -.
DR MaxQB; Q80UV9; -.
DR PaxDb; 10090-ENSMUSP00000098895; -.
DR PeptideAtlas; Q80UV9; -.
DR ProteomicsDB; 259347; -. [Q80UV9-1]
DR ProteomicsDB; 259348; -. [Q80UV9-2]
DR ProteomicsDB; 259349; -. [Q80UV9-3]
DR Pumba; Q80UV9; -.
DR Antibodypedia; 25077; 83 antibodies from 22 providers.
DR DNASU; 270627; -.
DR Ensembl; ENSMUST00000118878.8; ENSMUSP00000112772.2; ENSMUSG00000031314.19. [Q80UV9-3]
DR GeneID; 270627; -.
DR KEGG; mmu:270627; -.
DR UCSC; uc009txy.1; mouse. [Q80UV9-2]
DR AGR; MGI:1336878; -.
DR CTD; 6872; -.
DR MGI; MGI:1336878; Taf1.
DR VEuPathDB; HostDB:ENSMUSG00000031314; -.
DR eggNOG; KOG0008; Eukaryota.
DR GeneTree; ENSGT00940000155242; -.
DR InParanoid; Q80UV9; -.
DR OrthoDB; 5482320at2759; -.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR BioGRID-ORCS; 270627; 12 hits in 41 CRISPR screens.
DR ChiTaRS; Taf1; mouse.
DR PRO; PR:Q80UV9; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q80UV9; Protein.
DR Bgee; ENSMUSG00000031314; Expressed in manus and 231 other cell types or tissues.
DR ExpressionAtlas; Q80UV9; baseline and differential.
DR Genevisible; Q80UV9; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045120; C:pronucleus; IDA:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:ComplexPortal.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; ISO:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:ComplexPortal.
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 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 Acetylation; Acyltransferase; Alternative initiation; Alternative splicing;
KW ATP-binding; Bromodomain; Cell cycle; DNA-binding; Isopeptide bond; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..1891
FT /note="Transcription initiation factor TFIID subunit 1"
FT /id="PRO_0000278524"
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..1891
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"
FT /evidence="ECO:0000250"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..180
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 535..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..997
FT /note="Histone acetyltransferase (HAT)"
FT /evidence="ECO:0000250"
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 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:0000250"
FT REGION 1651..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1690..1891
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..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1708
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 1762..1776
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 1867..1891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT MOD_RES 565
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1799
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT CROSSLNK 583
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P21675"
FT VAR_SEQ 1..962
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023320"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 4)"
FT /id="VSP_062001"
FT VAR_SEQ 178..198
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023321"
FT CONFLICT 217
FT /note="D -> E (in Ref. 4; AAD23348)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="S -> A (in Ref. 4; AAD23348)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> H (in Ref. 4; AAD23348)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="E -> K (in Ref. 4; AAD23348)"
FT /evidence="ECO:0000305"
FT CONFLICT 867..868
FT /note="LK -> EG (in Ref. 5; AAC62118)"
FT /evidence="ECO:0000305"
FT CONFLICT 876
FT /note="T -> Q (in Ref. 4; AAD23349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1302..1306
FT /note="LYYQT -> AFVAS (in Ref. 5; AAC62118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1358
FT /note="R -> P (in Ref. 4; AAD23350)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="L -> F (in Ref. 4; AAD23350)"
FT /evidence="ECO:0000305"
FT CONFLICT 1450
FT /note="T -> E (in Ref. 4; AAD23350)"
FT /evidence="ECO:0000305"
FT CONFLICT 1469..1470
FT /note="HL -> QM (in Ref. 4; AAD23350)"
FT /evidence="ECO:0000305"
FT CONFLICT 1736
FT /note="D -> N (in Ref. 2; AAH94568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1891 AA; 214419 MW; 9A4EA0475BB3E885 CRC64;
MGPGWAGLLQ DKGGGSPSVV MSDTDSDEES AGGGPFSLTG FLFGNINGAG QLEGESVLDD
ECKKHLAGLG ALGLGSLITE LTANEELSGS DGALVNDEGW IRSREDAVDY SDINEVAEDE
SRRYQQTMGS LQPLCHTDYD EDDYDADCED IDCKLMPPPP PPPGPLKKEK DQDDITGVSE
DGEGIILPSI IAPSSLASEK VDFSSSSDSE SEMGPQDAAQ SESKDGQLTL PLAGIMQHDA
TKLLPSVTEL FPEFRPGKVL RFLRLFGPGK NVPSVWRSAR RKRKKKHREL IQEGQVQEEE
CSVELEVNQK SLWNYDYAPP PLPDQCLSDD EITMMAPVES KFSQSTGDTD KVMDTKPRVA
EWRYGPARLW YDMLGVPEDG SGFDYGFKMK KTEHESTIKC NIMKKLRKLE ENSGVDLLAD
ENFLMVTQLH WEDDIIWDGE DVKHKGTKPQ RASLAGWLPS SMTRNAMAYN VQQGFTATLD
DDKPWYSIFP IDNEDLVYGR WEDNIIWDAQ NMPRILEPPV LTLDPNDENL ILEIPDEKEE
ATSNSPSKEN KKESSLKKSR ILLGKTGVIK EEPQQNMSQP EVKDPWNLSN DEYYYPKQQG
LRGTFGGNII QHSIPAVELR QPFFPTHMGP IKLRQFHRPP LKKYSFGALS QPGPHSVQPL
LKHIKKKAKM REQERQASGG GEMFFMRTPQ DLTGKDGDLI LAEYSEENGP LMMQVGMATK
IKNYYKRKPG KDPGAPDCKY GETVYCHTSP FLGSLHPGQL LQAFENNLFR APIYLHKMPE
SDFLIIRTRQ GYFIRELVDI 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 AAGNNHRDDD TASVTSLNSS ATGRCLKIYR TFRDEEGKEY
VRCETVRKAT 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
YYKVIVSPMD LETIRKNISK HKYQSRESFL DDVNLILANS VKYNGPESQY TKTAQEIVNV
CHQTLTEYDE HLTQLEKDIC TAKEAALEEA ELESLDPMTP GPYTPQPPDL YDNNTSLSVS
RDASVYQDES NLSVLDIPSA TSEKQLTQEG GDGDGDLADE EEGTVQQPQA SVLYEDLLMS
EGEDDEEDAG SDEEGDNPFF AIQLSESGSD SDVESGSLRP KQPRVLQENT RMGMENEESM
MSYEGDGGDA SRGLEDSNIS YGSYEEPDPK SNTQDTSFSS IGGYEVSEEE EDEEEQRSGP
SVLSQVHLSE DEEDSEDFHS IAGDTDLDSD E
//
