ID TAF10_YEAST STANDARD; PRT; 206 AA. AC Q12030; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 24-JAN-2006 (Rel. 49, Last annotation update) DE Transcription initiation factor TFIID subunit 10 (TBP-associated DE factor 10) (TBP-associated factor 25 kDa) (TAFII-23) (TAFII23) (TAFII- DE 25) (TAFII25) (p25). GN Name=TAF10; Synonyms=TAF23, TAF25; OrderedLocusNames=YDR167W; GN ORFNames=YD9489.02; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96278804; PubMed=8662725; DOI=10.1074/jbc.271.23.13706; RA Klebanow E.R., Poon D., Zhou S., Weil P.A.; RT "Isolation and characterization of TAF25, an essential yeast gene that RT encodes an RNA polymerase II-specific TATA-binding protein-associated RT factor."; RL J. Biol. Chem. 271:13706-13715(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=97313263; PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [3] RP FUNCTION, AND TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN. RX PubMed=9695952; DOI=10.1016/S0092-8674(00)81423-3; RA Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C., RA Davidson I., Moras D.; RT "Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded RT by atypical evolutionary conserved motifs also found in the SPT3 RT family."; RL Cell 94:239-249(1998). RN [4] RP FUNCTION, AND SUBUNIT. RX PubMed=9674426; DOI=10.1016/S0092-8674(00)81220-9; RA Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C., RA Yates J.R. III, Workman J.L.; RT "A subset of TAF(II)s are integral components of the SAGA complex RT required for nucleosome acetylation and transcriptional stimulation."; RL Cell 94:45-53(1998). RN [5] RP FUNCTION, AND SUBUNIT. RX PubMed=10788514; DOI=10.1074/jbc.275.18.13895; RA Sanders S.L., Weil P.A.; RT "Identification of two novel TAF subunits of the yeast Saccharomyces RT cerevisiae TFIID complex."; RL J. Biol. Chem. 275:13895-13900(2000). RN [6] RP FUNCTION, AND INTERACTION IN TFIID AND SAGA. RX PubMed=11238921; DOI=10.1128/MCB.21.5.1841-1853.2001; RA Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A., RA Tora L., Davidson I.; RT "Histone folds mediate selective heterodimerization of yeast TAF(II)25 RT with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA RT component ySPT7."; RL Mol. Cell. Biol. 21:1841-1853(2001). RN [7] RP FUNCTION, AND HISTONE-FOLD DOMAIN CHARACTERIZATION. RX PubMed=11295558; DOI=10.1016/S0968-0004(00)01741-2; RA Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.; RT "The histone fold is a key structural motif of transcription factor RT TFIID."; RL Trends Biochem. Sci. 26:250-257(2001). RN [8] RP FUNCTION, AND SAGA COMPLEX COMPOSITION. RX PubMed=12052880; DOI=10.1128/MCB.22.13.4723-4738.2002; RA Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.; RT "Proteomics of the eukaryotic transcription machinery: identification RT of proteins associated with components of yeast TFIID by RT multidimensional mass spectrometry."; RL Mol. Cell. Biol. 22:4723-4738(2002). RN [9] RP 3D-STRUCTURE, AND ELECTRON MICROSCOPY OF TFIID. RX PubMed=12093743; DOI=10.1093/emboj/cdf342; RA Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A., RA Kirschner D.B., Tora L., Schultz P.; RT "Mapping histone fold TAFs within yeast TFIID."; RL EMBO J. 21:3424-3433(2002). RN [10] RP FUNCTION, AND TFIID STOICHIOMETRY. RX PubMed=12138208; DOI=10.1128/MCB.22.16.6000-6013.2002; RA Sanders S.L., Garbett K.A., Weil P.A.; RT "Molecular characterization of Saccharomyces cerevisiae TFIID."; RL Mol. Cell. Biol. 22:6000-6013(2002). RN [11] RP FUNCTION. RX PubMed=12516863; DOI=10.1023/A:1021258713850; RA Martinez E.; RT "Multi-protein complexes in eukaryotic gene transcription."; RL Plant Mol. Biol. 50:925-947(2002). RN [12] RP LEVEL OF PROTEIN EXPRESSION. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Functions as a component of the DNA-binding general CC transcription factor complex TFIID and the regulatory CC transcription complex SAGA. Binding of TFIID to a promoter (with CC or without TATA element) is the initial step in pre-initiation CC complex (PIC) formation. TFIID plays a key role in the regulation CC of gene expression by RNA polymerase II through different CC activities such as transcription activator interaction, core CC promoter recognition and selectivity, TFIIA and TFIIB interaction, CC chromatin modification (histone acetylation by TAF1), facilitation CC of DNA opening and initiation of transcription. SAGA influences CC RNA polymerase II transcriptional activity through different CC activities such as TBP interaction (SPT3 and SPT8) and promoter CC selectivity, interaction with transcription activators (GCN5, CC ADA2, ADA3, and TRA1), and chromatin modification through histone CC acetylation (GCN5). CC -!- SUBUNIT: In TFIID, TAF10 heterodimerizes with TAF3 and TAF8. The CC 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) CC and the 14 TBP-associated factors. One copy of each TAF1, TAF2, CC TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, CC TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. The 1.8 MDa CC SAGA complex is composed of at least 17 subunits: TRA1, ADA1, CC SPT7, SPT20, SPT3, SPT8, GCN5, ADA2, ADA3, TAF5, TAF6, TAF9, CC TAF10, TAF12, SGF29, SGF73, and UBP8. CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-18889, EBI-18889; CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- MISCELLANEOUS: Present with 3400 molecules/cell. CC -!- SIMILARITY: Belongs to the TAF10 family. CC -!- SIMILARITY: Contains 1 histone-fold 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; U51636; AAB07766.1; -; Genomic_DNA. DR EMBL; Z47813; CAA87798.1; -; Genomic_DNA. DR PIR; S50913; S50913. DR IntAct; Q12030; -. DR GermOnline; 140658; -. DR TRANSFAC; T03124; -. DR Ensembl; YDR167W; Saccharomyces cerevisiae. DR SGD; S000002574; TAF10. DR LinkHub; Q12030; -. DR GO; GO:0000124; C:SAGA complex; IDA. DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IPI. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA. DR GO; GO:0016251; F:general RNA polymerase II transcription fac...; TAS. DR GO; GO:0042802; F:protein self binding; IPI. DR GO; GO:0016568; P:chromatin modification; TAS. DR GO; GO:0000114; P:G1-specific transcription in mitotic cell c...; IPI. DR GO; GO:0016573; P:histone acetylation; TAS. DR GO; GO:0006367; P:transcription initiation from RNA polymeras...; TAS. DR InterPro; IPR002197; HTH_Fis. DR InterPro; IPR003923; TFIID_30kD. DR Pfam; PF03540; TFIID_30kDa; 1. DR PRINTS; PR01590; HTHFIS. DR PRINTS; PR01443; TFIID30KDSUB. KW Complete proteome; Nuclear protein; Transcription; KW Transcription regulation. FT DOMAIN 47 194 Histone-fold. FT COMPBIAS 147 172 Gln-rich. SQ SEQUENCE 206 AA; 23019 MW; A472CCA10DC3B495 CRC64; MDFEEDYDAE FDDNQEGQLE TPFPSVAGAD DGDNDNDDSV AENMKKKQKR EAVVDDGSEN AFGIPEFTRK DKTLEEILEM MDSTPPIIPD AVIDYYLTKN GFNVADVRVK RLLALATQKF VSDIAKDAYE YSRIRSSVAV SNANNSQARA RQLLQGQQQP GVQQISQQQH QQNEKTTASK VVLTVNDLSS AVAEYGLNIG RPDFYR //