ID TAF4_HUMAN STANDARD; PRT; 1085 AA. AC O00268; Q99721; Q9BR40; Q9BX42; DT 15-JUL-1998 (Rel. 36, Created) DT 01-FEB-2005 (Rel. 46, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Transcription initiation factor TFIID subunit 4 (Transcription DE initiation factor TFIID 135 kDa subunit) (TAF(II)135) (TAFII-135) DE (TAFII135) (TAFII-130) (TAFII130). 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; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=97336072; PubMed=9192867; 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. RA Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., RA Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., RA Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; 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 OF 105-1085, AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=97098442; 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 [5] 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 872-920 IN COMPLEX WITH RP TAF12. RX MEDLINE=20063193; PubMed=10594036; 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: Makes part of TFIID is a multimeric protein complex that CC plays a central role in mediating promoter responses to various CC activators and repressors. Potentiates transcriptional activation CC by the AF-2S of the retinoic acid, vitamin D3 and 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/SPT3, CC TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 CC and TRRAP. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: Contains 1 TAFH/NHR1 domain. 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; -. DR EMBL; AY623115; AAT38111.1; -. DR EMBL; AL137077; CAC36006.1; -. DR EMBL; AL109911; CAC22312.2; -. DR EMBL; U75308; AAC50901.1; -. DR PDB; 1H3O; X-ray; A/C=871-945. DR TRANSFAC; T02328; -. DR Genew; HGNC:11537; TAF4. DR Reactome; O00268; -. DR MIM; 601796; -. DR GO; GO:0005669; C:transcription factor TFIID complex; TAS. DR GO; GO:0016251; F:general RNA polymerase II transcription fac...; TAS. DR GO; GO:0005515; F:protein binding; TAS. DR GO; GO:0003713; F:transcription coactivator activity; TAS. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007900; TAF4. DR InterPro; IPR003894; TAF_hom. DR Pfam; PF05236; TAF4; 1. DR Pfam; PF07531; TAFH; 1. DR SMART; SM00549; TAFH; 1. KW 3D-structure; Direct protein sequencing; Nuclear protein; KW Transcription; Transcription regulation. FT DOMAIN 592 684 TAFH/NHR1. FT DOMAIN 39 42 Poly-His. FT DOMAIN 52 57 Poly-Ala. FT DOMAIN 98 101 Poly-Gly. FT DOMAIN 142 148 Poly-Ala. FT DOMAIN 270 277 Poly-Pro. FT DOMAIN 333 339 Poly-Ala. FT DOMAIN 682 685 Poly-Pro. FT DOMAIN 810 815 Poly-Ala. FT DOMAIN 830 833 Poly-Asp. FT CONFLICT 105 117 PGPPSPRRPLVPA -> GRGLLQQRGGRES (in Ref. FT 4). FT CONFLICT 136 136 S -> A (in Ref. 1 and 4). FT CONFLICT 186 187 Missing (in Ref. 1 and 4). FT CONFLICT 235 266 Missing (in Ref. 4). FT CONFLICT 295 295 P -> L (in Ref. 4). 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 //