TAF4_HUMAN
ID TAF4_HUMAN Reviewed; 1085 AA.
AC O00268; A6NGD9; Q5TBP6; Q99721; Q9BR40; Q9BX42;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Transcription initiation factor TFIID subunit 4;
DE AltName: Full=RNA polymerase II TBP-associated factor subunit C;
DE AltName: Full=TBP-associated factor 4;
DE AltName: Full=Transcription initiation factor TFIID 130 kDa subunit;
DE Short=TAF(II)130;
DE Short=TAFII-130;
DE Short=TAFII130;
DE AltName: Full=Transcription initiation factor TFIID 135 kDa subunit;
DE Short=TAF(II)135;
DE Short=TAFII-135;
DE Short=TAFII135;
GN Name=TAF4; Synonyms=TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135;
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], AND FUNCTION.
RX PubMed=9192867; DOI=10.1101/gad.11.11.1381;
RA Mengus G., May M., Carre L., Chambon P., Davidson I.;
RT "Human TAF(II)135 potentiates transcriptional activation by the AF-2s of
RT the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian
RT cells.";
RL Genes Dev. 11:1381-1395(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-1085, PARTIAL PROTEIN SEQUENCE, AND
RP FUNCTION.
RX PubMed=8942982; DOI=10.1073/pnas.93.24.13611;
RA Tanese N., Saluja D., Vassallo M.F., Chen J.-L., Admon A.;
RT "Molecular cloning and analysis of two subunits of the human TFIID complex:
RT hTAFII130 and hTAFII100.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13611-13616(1996).
RN [6]
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 [7]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H;
RP TAF2; TAF5; TRRAP; TAF12; GCN5L2 AND TAF10.
RX PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
RA Brand M., Yamamoto K., Staub A., Tora L.;
RT "Identification of TATA-binding protein-free TAFII-containing complex
RT subunits suggests a role in nucleosome acetylation and signal
RT transduction.";
RL J. Biol. Chem. 274:18285-18289(1999).
RN [8]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12601814; DOI=10.1002/pmic.200390030;
RA Cavusoglu N., Brand M., Tora L., van Dorsselaer A.;
RT "Novel subunits of the TATA binding protein free TAFII-containing
RT transcription complex identified by matrix-assisted laser
RT desorption/ionization-time of flight mass spectrometry following one-
RT dimensional gel electrophoresis.";
RL Proteomics 3:217-223(2003).
RN [9]
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 [10]
RP INTERACTION WITH ATF7.
RX PubMed=15735663; DOI=10.1038/sj.onc.1208565;
RA Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C.,
RA Chatton B.;
RT "A functional interaction between ATF7 and TAF12 that is modulated by
RT TAF4.";
RL Oncogene 24:3472-3483(2005).
RN [11]
RP IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS 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 [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-424 AND ARG-435, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 872-920 IN COMPLEX WITH TAF12, AND
RP FUNCTION.
RX PubMed=10594036; DOI=10.1128/mcb.20.1.340-351.2000;
RA Gangloff Y.-G., Werten S., Romier C., Carre L., Poch O., Moras D.,
RA Davidson I.;
RT "The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA
RT components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.";
RL Mol. Cell. Biol. 20:340-351(2000).
RN [15] {ECO:0007744|PDB:2P6V}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 575-688, AND METHYLATION AT
RP LYS-594; LYS-595; LYS-597; LYS-605; LYS-611; LYS-621; LYS-631 AND LYS-658.
RX PubMed=17483474; DOI=10.1073/pnas.0608570104;
RA Wang X., Truckses D.M., Takada S., Matsumura T., Tanese N., Jacobson R.H.;
RT "Conserved region I of human coactivator TAF4 binds to a short hydrophobic
RT motif present in transcriptional regulators.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7839-7844(2007).
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 (2.77 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,
CC PubMed:10594036, PubMed:8942982). TAF4 may maintain an association
CC between the TFIID and TFIIA complexes, while bound to the promoter,
CC together with TBP, during PIC assembly (PubMed:33795473). Potentiates
CC transcriptional activation by the AF-2S of the retinoic acid, vitamin
CC D3 and thyroid hormone (PubMed:9192867). {ECO:0000269|PubMed:10594036,
CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:8942982,
CC ECO:0000269|PubMed:9192867}.
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:10594036). Component of the TFTC-HAT complex, at least composed
CC of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5, TAF10,
CC TAF12 and TRRAP (PubMed:10373431, PubMed:12601814). Component of some
CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1,
CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975).
CC Interacts with ATF7; the interaction inhibits ATF7-mediated
CC tranactivation (PubMed:15735663). {ECO:0000269|PubMed:10373431,
CC ECO:0000269|PubMed:10594036, ECO:0000269|PubMed:12601814,
CC ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:33795473}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 Large T antigen.
CC {ECO:0000269|PubMed:8647434}.
CC -!- INTERACTION:
CC O00268; O43889: CREB3; NbExp=2; IntAct=EBI-1034261, EBI-625002;
CC O00268; Q9NS37: CREBZF; NbExp=2; IntAct=EBI-1034261, EBI-632965;
CC O00268; Q16514-1: TAF12; NbExp=16; IntAct=EBI-1034261, EBI-1034253;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf4/";
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DR EMBL; Y11354; CAA72189.1; -; mRNA.
DR EMBL; AY623115; AAT38111.1; -; Genomic_DNA.
DR EMBL; AL109911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75407.1; -; Genomic_DNA.
DR EMBL; U75308; AAC50901.1; -; mRNA.
DR CCDS; CCDS33500.1; -.
DR RefSeq; NP_003176.2; NM_003185.3.
DR PDB; 1H3O; X-ray; 2.30 A; A/C=872-945.
DR PDB; 2P6V; X-ray; 2.00 A; A=575-688.
DR PDB; 6MZC; EM; 4.50 A; E=1-1085.
DR PDB; 6MZD; EM; 9.80 A; D=1-1085.
DR PDB; 6MZL; EM; 23.00 A; D/E=1-1085.
DR PDB; 6MZM; EM; 7.50 A; D=61-1085.
DR PDB; 7EDX; EM; 4.50 A; D/d=1-1085.
DR PDB; 7EG7; EM; 6.20 A; D/d=1-1085.
DR PDB; 7EG8; EM; 7.40 A; D/d=1-1085.
DR PDB; 7EG9; EM; 3.70 A; D/d=1-1085.
DR PDB; 7EGA; EM; 4.10 A; D/d=1-1085.
DR PDB; 7EGB; EM; 3.30 A; D/d=1-1085.
DR PDB; 7EGC; EM; 3.90 A; D/d=1-1085.
DR PDB; 7EGD; EM; 6.75 A; D/d=1-1085.
DR PDB; 7EGE; EM; 9.00 A; D/d=1-1085.
DR PDB; 7EGF; EM; 3.16 A; d=1-1085.
DR PDB; 7EGG; EM; 2.77 A; D=1-1085.
DR PDB; 7EGI; EM; 9.82 A; D/d=1-1085.
DR PDB; 7EGJ; EM; 8.64 A; D/d=1-1085.
DR PDB; 7ENA; EM; 4.07 A; DD/Dd=1-1085.
DR PDB; 7ENC; EM; 4.13 A; DD/Dd=1-1085.
DR PDBsum; 1H3O; -.
DR PDBsum; 2P6V; -.
DR PDBsum; 6MZC; -.
DR PDBsum; 6MZD; -.
DR PDBsum; 6MZL; -.
DR PDBsum; 6MZM; -.
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; 7EGG; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR AlphaFoldDB; O00268; -.
DR SMR; O00268; -.
DR BioGRID; 112737; 108.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR CORUM; O00268; -.
DR DIP; DIP-35350N; -.
DR ELM; O00268; -.
DR IntAct; O00268; 40.
DR MINT; O00268; -.
DR STRING; 9606.ENSP00000252996; -.
DR GlyConnect; 2870; 1 O-Linked glycan (1 site).
DR GlyGen; O00268; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; O00268; -.
DR PhosphoSitePlus; O00268; -.
DR BioMuta; TAF4; -.
DR EPD; O00268; -.
DR jPOST; O00268; -.
DR MassIVE; O00268; -.
DR MaxQB; O00268; -.
DR PaxDb; O00268; -.
DR PeptideAtlas; O00268; -.
DR PRIDE; O00268; -.
DR ProteomicsDB; 47818; -.
DR Antibodypedia; 1785; 97 antibodies from 25 providers.
DR DNASU; 6874; -.
DR Ensembl; ENST00000252996.9; ENSP00000252996.3; ENSG00000130699.20.
DR GeneID; 6874; -.
DR KEGG; hsa:6874; -.
DR MANE-Select; ENST00000252996.9; ENSP00000252996.3; NM_003185.4; NP_003176.2.
DR UCSC; uc002ybs.3; human.
DR CTD; 6874; -.
DR DisGeNET; 6874; -.
DR GeneCards; TAF4; -.
DR HGNC; HGNC:11537; TAF4.
DR HPA; ENSG00000130699; Low tissue specificity.
DR MIM; 601796; gene.
DR neXtProt; NX_O00268; -.
DR OpenTargets; ENSG00000130699; -.
DR PharmGKB; PA36312; -.
DR VEuPathDB; HostDB:ENSG00000130699; -.
DR eggNOG; KOG2341; Eukaryota.
DR GeneTree; ENSGT00390000011620; -.
DR HOGENOM; CLU_010576_0_0_1; -.
DR InParanoid; O00268; -.
DR OMA; PHRTPEI; -.
DR OrthoDB; 735381at2759; -.
DR PhylomeDB; O00268; -.
DR TreeFam; TF316520; -.
DR PathwayCommons; O00268; -.
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; O00268; -.
DR SIGNOR; O00268; -.
DR BioGRID-ORCS; 6874; 127 hits in 1090 CRISPR screens.
DR ChiTaRS; TAF4; human.
DR EvolutionaryTrace; O00268; -.
DR GeneWiki; TAF4; -.
DR GenomeRNAi; 6874; -.
DR Pharos; O00268; Tbio.
DR PRO; PR:O00268; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O00268; protein.
DR Bgee; ENSG00000130699; Expressed in right testis and 99 other tissues.
DR ExpressionAtlas; O00268; baseline and differential.
DR Genevisible; O00268; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; EXP:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:ARUK-UCL.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd08045; TAF4; 1.
DR DisProt; DP01170; -.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 1.20.120.1110; -; 1.
DR IDEAL; IID00231; -.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR045144; TAF4.
DR InterPro; IPR007900; TAF4_C.
DR InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR InterPro; IPR003894; TAFH_NHR1.
DR PANTHER; PTHR15138; PTHR15138; 1.
DR Pfam; PF05236; TAF4; 1.
DR Pfam; PF07531; TAFH; 1.
DR SMART; SM00549; TAFH; 1.
DR SUPFAM; SSF158553; SSF158553; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS51119; TAFH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Host-virus interaction;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1085
FT /note="Transcription initiation factor TFIID subunit 4"
FT /id="PRO_0000118869"
FT DOMAIN 590..687
FT /note="TAFH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT REGION 66..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..913
FT /note="Minimal region required to interact with TAF12"
FT /evidence="ECO:0000269|PubMed:10594036"
FT REGION 1015..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 424
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 435
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 594
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT MOD_RES 595
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT MOD_RES 597
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT MOD_RES 605
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT MOD_RES 611
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT MOD_RES 621
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT MOD_RES 631
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT MOD_RES 658
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0007744|PDB:2P6V"
FT VARIANT 651
FT /note="P -> L (in dbSNP:rs6089604)"
FT /id="VAR_052258"
FT CONFLICT 105..117
FT /note="PGPPSPRRPLVPA -> GRGLLQQRGGRES (in Ref. 5;
FT AAC50901)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="S -> A (in Ref. 1; CAA72189 and 5; AAC50901)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..187
FT /note="Missing (in Ref. 1; CAA72189 and 5; AAC50901)"
FT /evidence="ECO:0000305"
FT CONFLICT 235..266
FT /note="Missing (in Ref. 5; AAC50901)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="P -> L (in Ref. 5; AAC50901)"
FT /evidence="ECO:0000305"
FT HELIX 585..593
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 599..604
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 614..620
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 623..628
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 634..644
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 653..657
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 661..666
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 671..677
FT /evidence="ECO:0007829|PDB:2P6V"
FT HELIX 843..856
FT /evidence="ECO:0007829|PDB:7EGG"
FT HELIX 875..887
FT /evidence="ECO:0007829|PDB:1H3O"
FT TURN 888..890
FT /evidence="ECO:0007829|PDB:1H3O"
FT HELIX 898..918
FT /evidence="ECO:0007829|PDB:1H3O"
FT HELIX 923..925
FT /evidence="ECO:0007829|PDB:7EGF"
FT TURN 928..930
FT /evidence="ECO:0007829|PDB:7EGG"
FT STRAND 932..936
FT /evidence="ECO:0007829|PDB:7EGG"
FT HELIX 940..969
FT /evidence="ECO:0007829|PDB:7EGG"
FT STRAND 1056..1058
FT /evidence="ECO:0007829|PDB:7EGG"
FT HELIX 1060..1065
FT /evidence="ECO:0007829|PDB:7EGG"
FT STRAND 1068..1071
FT /evidence="ECO:0007829|PDB:7EGG"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:7EGG"
FT HELIX 1077..1082
FT /evidence="ECO:0007829|PDB:7EGG"
SQ SEQUENCE 1085 AA; 110114 MW; BC2F5B5F143DB145 CRC64;
MAAGSDLLDE VFFNSEVDEK VVSDLVGSLE SQLAASAAHH HHLAPRTPEV RAAAAGALGN
HVVSGSPAGA AGAGPAAPAE GAPGAAPEPP PAGRARPGGG GPQRPGPPSP RRPLVPAGPA
PPAAKLRPPP EGSAGSCAPV PAAAAVAAGP EPAPAGPAKP AGPAALAARA GPGPGPGPGP
GPGPGPGKPA GPGAAQTLNG SAALLNSHHA AAPAVSLVNN GPAALLPLPK PAAPGTVIQT
PPFVGAAAPP APAAPSPPAA PAPAAPAAAP PPPPPAPATL ARPPGHPAGP PTAAPAVPPP
AAAQNGGSAG AAPAPAPAAG GPAGVSGQPG PGAAAAAPAP GVKAESPKRV VQAAPPAAQT
LAASGPASTA ASMVIGPTMQ GALPSPAAVP PPAPGTPTGL PKGAAGAVTQ SLSRTPTATT
SGIRATLTPT VLAPRLPQPP QNPTNIQNFQ LPPGMVLVRS ENGQLLMIPQ QALAQMQAQA
HAQPQTTMAP RPATPTSAPP VQISTVQAPG TPIIARQVTP TTIIKQVSQA QTTVQPSATL
QRSPGVQPQL VLGGAAQTAS LGTATAVQTG TPQRTVPGAT TTSSAATETM ENVKKCKNFL
STLIKLASSG KQSTETAANV KELVQNLLDG KIEAEDFTSR LYRELNSSPQ PYLVPFLKRS
LPALRQLTPD SAAFIQQSQQ QPPPPTSQAT TALTAVVLSS SVQRTAGKTA ATVTSALQPP
VLSLTQPTQV GVGKQGQPTP LVIQQPPKPG ALIRPPQVTL TQTPMVALRQ PHNRIMLTTP
QQIQLNPLQP VPVVKPAVLP GTKALSAVSA QAAAAQKNKL KEPGGGSFRD DDDINDVASM
AGVNLSEESA RILATNSELV GTLTRSCKDE TFLLQAPLQR RILEIGKKHG ITELHPDVVS
YVSHATQQRL QNLVEKISET AQQKNFSYKD DDRYEQASDV RAQLKFFEQL DQIEKQRKDE
QEREILMRAA KSRSRQEDPE QLRLKQKAKE MQQQELAQMR QRDANLTALA AIGPRKKRKV
DCPGPGSGAE GSGPGSVVPG SSGVGTPRQF TRQRITRVNL RDLIFCLENE RETSHSLLLY
KAFLK
