TAF3_HUMAN
ID TAF3_HUMAN Reviewed; 929 AA.
AC Q5VWG9; Q05DA0; Q6GMS5; Q6P6B5; Q86VY6; Q9BQS9; Q9UFI8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transcription initiation factor TFIID subunit 3;
DE AltName: Full=140 kDa TATA box-binding protein-associated factor;
DE AltName: Full=TBP-associated factor 3;
DE AltName: Full=Transcription initiation factor TFIID 140 kDa subunit;
DE Short=TAF(II)140;
DE Short=TAF140;
DE Short=TAFII-140;
DE Short=TAFII140;
GN Name=TAF3;
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], SUBCELLULAR LOCATION, INTERACTION WITH TAF10;
RP TAF13; TBP; SAP130 AND GCN5L2, AND MUTAGENESIS OF TRP-23.
RC TISSUE=Cervix carcinoma;
RX PubMed=11438666; DOI=10.1128/mcb.21.15.5109-5121.2001;
RA Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are
RT novel metazoan homologues of yeast TAFII47 containing a histone fold and a
RT PHD finger.";
RL Mol. Cell. Biol. 21:5109-5121(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-714, AND VARIANT SER-442.
RC TISSUE=Bone, Skin, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-703, AND VARIANT ALA-696.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-229; SER-243;
RP SER-297; SER-301 AND THR-501, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-266 AND LYS-776, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-199; SER-291;
RP SER-297; SER-301; SER-667 AND SER-755, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-291, AND
RP IDENTIFICATION BY 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-746, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-581 AND LYS-746, 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 [14] {ECO:0007744|PDB:5C13}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 855-915.
RA Zhao S., Zhang B., Li H.;
RT "Crystal Structure of TAF3 PHD finger bound to histone H3C4me3 peptide.";
RL Submitted (NOV-2015) to the PDB data bank.
RN [15] {ECO:0007744|PDB:5XMY}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 853-915.
RA Zhao S., Zhang B., Li H.;
RT "Crystal structure of TAF3 PHD finger bound to H3K4me3Q5ser.";
RL Submitted (MAY-2017) to the PDB data bank.
RN [16] {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:7EGF}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.16 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).
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). The TFIID
CC complex structure can be divided into 3 modules TFIID-A, TFIID-B, and
CC TFIID-C (PubMed:33795473). TAF3 forms the TFIID-A module together with
CC TAF5 and TBP (PubMed:33795473). Required in complex with TBPL2 for the
CC differentiation of myoblasts into myocytes (PubMed:11438666). The TAF3-
CC TBPL2 complex replaces TFIID at specific promoters at an early stage in
CC the differentiation process (PubMed:11438666).
CC {ECO:0000269|PubMed:11438666, ECO:0000269|PubMed:33795473}.
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
CC (PubMed:33795473). Interacts with TAF10 via the histone fold
CC (PubMed:11438666). Interacts with TAF13, TBP, SAP130 and GCN5L2
CC (PubMed:11438666). Interacts with TBPL2 (PubMed:11438666).
CC {ECO:0000269|PubMed:11438666, ECO:0000269|PubMed:33795473}.
CC -!- INTERACTION:
CC Q5VWG9; P84243: H3-3B; NbExp=3; IntAct=EBI-1560087, EBI-120658;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11438666}.
CC -!- DOMAIN: The PHD-type zinc finger mediates binding to histone H3
CC methyllysine at position 4 (H3K4me3). {ECO:0000250|UniProtKB:Q5HZG4}.
CC -!- SIMILARITY: Belongs to the TAF3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH45106.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH62352.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH73884.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ292190; CAC34475.1; -; mRNA.
DR EMBL; AL390294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL159172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017320; AAH17320.1; -; mRNA.
DR EMBL; BC045106; AAH45106.1; ALT_SEQ; mRNA.
DR EMBL; BC073884; AAH73884.1; ALT_INIT; mRNA.
DR EMBL; BC062352; AAH62352.1; ALT_INIT; mRNA.
DR EMBL; AL117661; CAB56032.1; -; mRNA.
DR CCDS; CCDS41487.1; -.
DR PIR; T17342; T17342.
DR RefSeq; NP_114129.1; NM_031923.3.
DR PDB; 5C13; X-ray; 2.10 A; A/C/E/G=855-915.
DR PDB; 5WXG; X-ray; 1.70 A; A=853-915.
DR PDB; 5WXH; X-ray; 1.30 A; A/C=853-915.
DR PDB; 5XMY; X-ray; 1.70 A; A/C=853-915.
DR PDB; 6MZD; EM; 9.80 A; C=1-929.
DR PDB; 6MZL; EM; 23.00 A; C=1-929.
DR PDB; 7EDX; EM; 4.50 A; c=1-929.
DR PDB; 7EG7; EM; 6.20 A; c=1-929.
DR PDB; 7EG8; EM; 7.40 A; c=1-929.
DR PDB; 7EG9; EM; 3.70 A; c=1-929.
DR PDB; 7EGA; EM; 4.10 A; c=1-929.
DR PDB; 7EGB; EM; 3.30 A; c=1-929.
DR PDB; 7EGC; EM; 3.90 A; c=1-929.
DR PDB; 7EGD; EM; 6.75 A; c=1-929.
DR PDB; 7EGE; EM; 9.00 A; c=1-929.
DR PDB; 7EGF; EM; 3.16 A; c=1-929.
DR PDB; 7EGI; EM; 9.82 A; c=1-929.
DR PDB; 7EGJ; EM; 8.64 A; c=1-929.
DR PDB; 7ENA; EM; 4.07 A; Dc=1-929.
DR PDB; 7ENC; EM; 4.13 A; Dc=1-929.
DR PDBsum; 5C13; -.
DR PDBsum; 5WXG; -.
DR PDBsum; 5WXH; -.
DR PDBsum; 5XMY; -.
DR PDBsum; 6MZD; -.
DR PDBsum; 6MZL; -.
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; 7EGF; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR AlphaFoldDB; Q5VWG9; -.
DR BMRB; Q5VWG9; -.
DR SMR; Q5VWG9; -.
DR BioGRID; 123775; 74.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR CORUM; Q5VWG9; -.
DR DIP; DIP-38920N; -.
DR IntAct; Q5VWG9; 22.
DR MINT; Q5VWG9; -.
DR STRING; 9606.ENSP00000340271; -.
DR ChEMBL; CHEMBL4523329; -.
DR iPTMnet; Q5VWG9; -.
DR MetOSite; Q5VWG9; -.
DR PhosphoSitePlus; Q5VWG9; -.
DR BioMuta; TAF3; -.
DR DMDM; 74747393; -.
DR EPD; Q5VWG9; -.
DR jPOST; Q5VWG9; -.
DR MassIVE; Q5VWG9; -.
DR MaxQB; Q5VWG9; -.
DR PaxDb; Q5VWG9; -.
DR PeptideAtlas; Q5VWG9; -.
DR PRIDE; Q5VWG9; -.
DR ProteomicsDB; 65526; -.
DR Antibodypedia; 24519; 138 antibodies from 26 providers.
DR DNASU; 83860; -.
DR Ensembl; ENST00000344293.6; ENSP00000340271.5; ENSG00000165632.9.
DR GeneID; 83860; -.
DR KEGG; hsa:83860; -.
DR MANE-Select; ENST00000344293.6; ENSP00000340271.5; NM_031923.4; NP_114129.1.
DR UCSC; uc010qbd.4; human.
DR CTD; 83860; -.
DR DisGeNET; 83860; -.
DR GeneCards; TAF3; -.
DR HGNC; HGNC:17303; TAF3.
DR HPA; ENSG00000165632; Low tissue specificity.
DR MIM; 606576; gene.
DR neXtProt; NX_Q5VWG9; -.
DR OpenTargets; ENSG00000165632; -.
DR PharmGKB; PA38222; -.
DR VEuPathDB; HostDB:ENSG00000165632; -.
DR eggNOG; KOG1973; Eukaryota.
DR eggNOG; KOG2389; Eukaryota.
DR GeneTree; ENSGT00710000106806; -.
DR HOGENOM; CLU_014486_0_0_1; -.
DR InParanoid; Q5VWG9; -.
DR OMA; FPQPGAR; -.
DR OrthoDB; 826756at2759; -.
DR PhylomeDB; Q5VWG9; -.
DR TreeFam; TF316513; -.
DR PathwayCommons; Q5VWG9; -.
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; Q5VWG9; -.
DR SIGNOR; Q5VWG9; -.
DR BioGRID-ORCS; 83860; 186 hits in 1098 CRISPR screens.
DR ChiTaRS; TAF3; human.
DR GeneWiki; TAF3; -.
DR GenomeRNAi; 83860; -.
DR Pharos; Q5VWG9; Tbio.
DR PRO; PR:Q5VWG9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VWG9; protein.
DR Bgee; ENSG00000165632; Expressed in tendon of biceps brachii and 192 other tissues.
DR Genevisible; Q5VWG9; HS.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:ARUK-UCL.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IEA:Ensembl.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:HGNC-UCL.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00576; BTP; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..929
FT /note="Transcription initiation factor TFIID subunit 3"
FT /id="PRO_0000245528"
FT ZN_FING 865..915
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 131..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5C13"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5C13"
FT BINDING 883
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5C13"
FT BINDING 886
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5C13"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5C13"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:5C13"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5C13"
FT BINDING 912
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:5C13"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 776
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 581
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 746
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VARIANT 349
FT /note="S -> T (in dbSNP:rs17366712)"
FT /id="VAR_052254"
FT VARIANT 442
FT /note="N -> S (in dbSNP:rs4747647)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052255"
FT VARIANT 696
FT /note="V -> A (in dbSNP:rs1244229)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_052256"
FT VARIANT 696
FT /note="V -> L (in dbSNP:rs10795583)"
FT /id="VAR_052257"
FT MUTAGEN 23
FT /note="W->R: Loss of interaction with TAF10."
FT /evidence="ECO:0000269|PubMed:11438666"
FT CONFLICT 23..25
FT /note="WDS -> TRP (in Ref. 4; CAB56032)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="M -> K (in Ref. 3; AAH73884)"
FT /evidence="ECO:0000305"
FT CONFLICT 537..539
FT /note="EKQ -> KKK (in Ref. 3; AAH17320)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="V -> P (in Ref. 3; AAH62352)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="E -> K (in Ref. 4; CAB56032)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="E -> K (in Ref. 3; AAH62352)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="E -> K (in Ref. 3; AAH62352)"
FT /evidence="ECO:0000305"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:7EGF"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:7EGF"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:7EGF"
FT HELIX 28..55
FT /evidence="ECO:0007829|PDB:7EGF"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:7EGF"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:7EGF"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7EGF"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:5WXH"
FT STRAND 864..867
FT /evidence="ECO:0007829|PDB:5WXH"
FT TURN 869..871
FT /evidence="ECO:0007829|PDB:5WXH"
FT STRAND 880..882
FT /evidence="ECO:0007829|PDB:5WXH"
FT TURN 884..886
FT /evidence="ECO:0007829|PDB:5WXH"
FT STRAND 889..891
FT /evidence="ECO:0007829|PDB:5WXH"
FT HELIX 892..895
FT /evidence="ECO:0007829|PDB:5WXH"
FT HELIX 910..913
FT /evidence="ECO:0007829|PDB:5WXH"
SQ SEQUENCE 929 AA; 103582 MW; C951754B5B532E72 CRC64;
MCESYSRSLL RVSVAQICQA LGWDSVQLSA CHLLTDVLQR YLQQLGRGCH RYSELYGRTD
PILDDVGEAF QLMGVSLHEL EDYIHNIEPV TFPHQIPSFP VSKNNVLQFP QPGSKDAEER
KEYIPDYLPP IVSSQEEEEE EQVPTDGGTS AEAMQVPLEE DDELEEEEII NDENFLGKRP
LDSPEAEELP AMKRPRLLST KGDTLDVVLL EAREPLSSIN TQKIPPMLSP VHVQDSTDLA
PPSPEPPMLA PVAKSQMPTA KPLETKSFTP KTKTKTSSPG QKTKSPKTAQ SPAMVGSPIR
SPKTVSKEKK SPGRSKSPKS PKSPKVTTHI PQTPVRPETP NRTPSATLSE KISKETIQVK
QIQTPPDAGK LNSENQPKKA VVADKTIEAS IDAVIARACA EREPDPFEFS SGSESEGDIF
TSPKRISGPE CTTPKASTSA NNFTKSGSTP LPLSGGTSSS DNSWTMDASI DEVVRKAKLG
TPSNMPPNFP YISSPSVSPP TPEPLHKVYE EKTKLPSSVE VKKKLKKELK TKMKKKEKQR
DREREKDKNK DKSKEKDKVK EKEKDKETGR ETKYPWKEFL KEEEADPYKF KIKEFEDVDP
KVKLKDGLVR KEKEKHKDKK KDREKGKKDK DKREKEKVKD KGREDKMKAP APPLVLPPKE
LALPLFSPAT ASRVPAMLPS LLPVLPEKLF EEKEKVKEKE KKKDKKEKKK KKEKEKEKKE
KEREKEKRER EKREKEKEKH KHEKIKVEPV ALAPSPVIPR LTLRVGAGQD KIVISKVVPA
PEAKPAPSQN RPKTPPPAPA PAPGPMLVSP APVPLPLLAQ AAAGPALLPS PGPAASGASA
KAPVRSVVTE TVSTYVIRDE WGNQIWICPG CNKPDDGSPM IGCDDCDDWY HWPCVGIMTA
PPEEMQWFCP KCANKKKDKK HKKRKHRAH
