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 15-MAR-2017, entry version 179. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 RT of the retinoic acid, vitamin D3, and thyroid hormone receptors in RT mammalian 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-1085, AND PARTIAL PROTEIN SEQUENCE. 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 RT complex: hTAFII130 and hTAFII100."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13611-13616(1996). RN [6] RP INTERACTION WITH SV40 LARGE T ANTIGEN. 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; RP SUPT3H; TAF2; TAF5; TRRAP; 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 RP BY 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., RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., RA Vemulapalli V., 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 RP TAF12. 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 RT SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like RT pairs."; RL Mol. Cell. Biol. 20:340-351(2000). CC -!- FUNCTION: Part of the TFIID complex, a multimeric protein complex CC that plays a central role in mediating promoter responses to CC various activators and repressors. Potentiates transcriptional CC activation by the AF-2S of the retinoic acid, vitamin D3 and CC thyroid hormone. CC -!- SUBUNIT: TFIID is composed of TATA binding protein (TBP) and a CC number of TBP-associated factors (TAFs). Component of the TFTC-HAT CC complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, CC TAF4, TAF5, GCN5L2/GCN5, TAF10 and TRRAP. Component of some CC MLL1/MLL complex, at least composed of the core components CC KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the CC facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 CC and TEX10. Interacts with ATF7; the interaction inhibits ATF7- CC mediated tranactivation. Interacts with SV40 Large T antigen. CC {ECO:0000269|PubMed:10373431, ECO:0000269|PubMed:10594036, CC ECO:0000269|PubMed:12601814, ECO:0000269|PubMed:15735663, CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:8647434}. 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/"; 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; Y11354; CAA72189.1; -; mRNA. DR EMBL; AY623115; AAT38111.1; -; Genomic_DNA. DR EMBL; AL109911; CAI19182.1; -; Genomic_DNA. DR EMBL; AL137077; CAI19182.1; JOINED; Genomic_DNA. DR EMBL; AL137077; CAI11045.1; -; Genomic_DNA. DR EMBL; AL109911; CAI11045.1; JOINED; 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 UniGene; Hs.18857; -. DR PDB; 1H3O; X-ray; 2.30 A; A/C=872-945. DR PDB; 2P6V; X-ray; 2.00 A; A=575-679. DR PDBsum; 1H3O; -. DR PDBsum; 2P6V; -. DR ProteinModelPortal; O00268; -. DR SMR; O00268; -. DR BioGrid; 112737; 51. DR DIP; DIP-35350N; -. DR IntAct; O00268; 13. DR MINT; MINT-236922; -. DR STRING; 9606.ENSP00000252996; -. DR iPTMnet; O00268; -. DR PhosphoSitePlus; O00268; -. DR BioMuta; TAF4; -. DR EPD; O00268; -. DR MaxQB; O00268; -. DR PaxDb; O00268; -. DR PeptideAtlas; O00268; -. DR PRIDE; O00268; -. DR DNASU; 6874; -. DR Ensembl; ENST00000252996; ENSP00000252996; ENSG00000130699. DR GeneID; 6874; -. DR KEGG; hsa:6874; -. DR UCSC; uc002ybs.3; human. DR CTD; 6874; -. DR DisGeNET; 6874; -. DR GeneCards; MIR1257; -. DR GeneCards; TAF4; -. DR H-InvDB; HIX0015971; -. DR H-InvDB; HIX0174705; -. DR HGNC; HGNC:11537; TAF4. DR HPA; CAB031484; -. DR HPA; HPA008599; -. DR MIM; 601796; gene. DR neXtProt; NX_O00268; -. DR OpenTargets; ENSG00000130699; -. DR PharmGKB; PA36312; -. DR eggNOG; KOG2341; Eukaryota. DR eggNOG; ENOG410XQS6; LUCA. DR GeneTree; ENSGT00390000011620; -. DR HOGENOM; HOG000154502; -. DR HOVERGEN; HBG058585; -. DR InParanoid; O00268; -. DR KO; K03129; -. DR OMA; RPPIHTA; -. DR OrthoDB; EOG091G0GOS; -. DR PhylomeDB; O00268; -. DR TreeFam; TF316520; -. 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 SIGNOR; O00268; -. DR ChiTaRS; TAF4; human. DR EvolutionaryTrace; O00268; -. DR GeneWiki; TAF4; -. DR GenomeRNAi; 6874; -. DR PRO; PR:O00268; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000130699; -. DR CleanEx; HS_TAF4; -. DR ExpressionAtlas; O00268; baseline and differential. DR Genevisible; O00268; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB. DR GO; GO:0000790; C:nuclear chromatin; IDA:ParkinsonsUK-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:MGI. DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0008134; F:transcription factor binding; IBA:GO_Central. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB. DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome. DR GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IEA:GOC. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR CDD; cd08045; TAF4; 1. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007900; TAF4. DR InterPro; IPR003894; TAFH_NHR1. DR Pfam; PF05236; TAF4; 1. DR Pfam; PF07531; TAFH; 1. DR SMART; SM00549; TAFH; 1. DR SUPFAM; SSF47113; SSF47113; 1. DR PROSITE; PS51119; TAFH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Host-virus interaction; Methylation; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 1085 Transcription initiation factor TFIID FT subunit 4. FT /FTId=PRO_0000118869. FT DOMAIN 590 687 TAFH. {ECO:0000255|PROSITE- FT ProRule:PRU00440}. FT COMPBIAS 39 42 Poly-His. FT COMPBIAS 52 57 Poly-Ala. FT COMPBIAS 98 101 Poly-Gly. FT COMPBIAS 142 148 Poly-Ala. FT COMPBIAS 270 277 Poly-Pro. FT COMPBIAS 333 339 Poly-Ala. FT COMPBIAS 682 685 Poly-Pro. FT COMPBIAS 810 815 Poly-Ala. FT COMPBIAS 830 833 Poly-Asp. FT MOD_RES 109 109 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 424 424 Asymmetric dimethylarginine. FT {ECO:0000244|PubMed:24129315}. FT MOD_RES 435 435 Asymmetric dimethylarginine. FT {ECO:0000244|PubMed:24129315}. FT VARIANT 651 651 P -> L (in dbSNP:rs6089604). FT /FTId=VAR_052258. FT CONFLICT 105 117 PGPPSPRRPLVPA -> GRGLLQQRGGRES (in Ref. FT 5; AAC50901). {ECO:0000305}. FT CONFLICT 136 136 S -> A (in Ref. 1; CAA72189 and 5; FT AAC50901). {ECO:0000305}. FT CONFLICT 186 187 Missing (in Ref. 1; CAA72189 and 5; FT AAC50901). {ECO:0000305}. FT CONFLICT 235 266 Missing (in Ref. 5; AAC50901). FT {ECO:0000305}. FT CONFLICT 295 295 P -> L (in Ref. 5; AAC50901). FT {ECO:0000305}. FT HELIX 585 607 {ECO:0000244|PDB:2P6V}. FT STRAND 609 612 {ECO:0000244|PDB:2P6V}. FT HELIX 614 628 {ECO:0000244|PDB:2P6V}. FT HELIX 634 644 {ECO:0000244|PDB:2P6V}. FT HELIX 653 666 {ECO:0000244|PDB:2P6V}. FT HELIX 671 677 {ECO:0000244|PDB:2P6V}. FT HELIX 875 887 {ECO:0000244|PDB:1H3O}. FT TURN 888 890 {ECO:0000244|PDB:1H3O}. FT HELIX 898 918 {ECO:0000244|PDB:1H3O}. 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 //