位置:首页 > 蛋白库 > TAF1_MOUSE
TAF1_MOUSE
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   03-AUG-2022, entry version 138.
DE   RecName: Full=Transcription initiation factor TFIID subunit 1;
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; 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; Named isoforms=3;
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   -!- 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};
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; 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. [Q80UV9-1]
DR   RefSeq; XP_006528115.1; XM_006528052.3. [Q80UV9-3]
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; 1.
DR   STRING; 10090.ENSMUSP00000098895; -.
DR   iPTMnet; Q80UV9; -.
DR   PhosphoSitePlus; Q80UV9; -.
DR   EPD; Q80UV9; -.
DR   MaxQB; Q80UV9; -.
DR   PaxDb; Q80UV9; -.
DR   PeptideAtlas; Q80UV9; -.
DR   PRIDE; Q80UV9; -.
DR   ProteomicsDB; 259347; -. [Q80UV9-1]
DR   ProteomicsDB; 259348; -. [Q80UV9-2]
DR   ProteomicsDB; 259349; -. [Q80UV9-3]
DR   Antibodypedia; 25077; 68 antibodies from 22 providers.
DR   DNASU; 270627; -.
DR   Ensembl; ENSMUST00000118878; ENSMUSP00000112772; ENSMUSG00000031314. [Q80UV9-3]
DR   GeneID; 270627; -.
DR   KEGG; mmu:270627; -.
DR   UCSC; uc009txy.1; mouse. [Q80UV9-2]
DR   CTD; 6872; -.
DR   MGI; MGI:1336878; Taf1.
DR   VEuPathDB; HostDB:ENSMUSG00000031314; -.
DR   eggNOG; KOG0008; Eukaryota.
DR   GeneTree; ENSGT00940000155242; -.
DR   InParanoid; Q80UV9; -.
DR   OrthoDB; 103411at2759; -.
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 37 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 228 other 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:0005730; C:nucleolus; ISO:MGI.
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:0061628; F:H3K27me3 modified histone binding; ISO: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:0016573; P:histone acetylation; IDA:UniProtKB.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:ComplexPortal.
DR   GO; GO:0006468; P:protein phosphorylation; IC:ComplexPortal.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR   Gene3D; 1.10.1100.10; -; 1.
DR   Gene3D; 1.20.920.10; -; 2.
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; PTHR13900; 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; SSF47055; SSF47055; 1.
DR   SUPFAM; SSF47370; SSF47370; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Alternative splicing; ATP-binding;
KW   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         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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024