TAF10_YEAST
ID TAF10_YEAST Reviewed; 206 AA.
AC Q12030; D6VSE7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transcription initiation factor TFIID subunit 10;
DE AltName: Full=TAFII-23;
DE Short=TAFII23;
DE AltName: Full=TAFII-25;
DE Short=TAFII25;
DE AltName: Full=TBP-associated factor 10;
DE AltName: Full=TBP-associated factor 25 kDa;
DE AltName: Full=p25;
GN Name=TAF10; Synonyms=TAF23, TAF25; OrderedLocusNames=YDR167W;
GN ORFNames=YD9489.02;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX 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].
RC STRAIN=ATCC 204508 / S288c;
RX 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
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 by
RT atypical evolutionary conserved motifs also found in the SPT3 family.";
RL Cell 94:239-249(1998).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 required
RT for nucleosome acetylation and transcriptional stimulation.";
RL Cell 94:45-53(1998).
RN [6]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE TFIID COMPLEX.
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 [8]
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., Tora L.,
RA Davidson I.;
RT "Histone folds mediate selective heterodimerization of yeast TAF(II)25 with
RT TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7.";
RL Mol. Cell. Biol. 21:1841-1853(2001).
RN [9]
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 [10]
RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
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 of
RT proteins associated with components of yeast TFIID by multidimensional mass
RT spectrometry.";
RL Mol. Cell. Biol. 22:4723-4738(2002).
RN [11]
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 [12]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [13]
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 [14]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [15]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-146, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [19]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Functions as a component of the DNA-binding general
CC transcription factor complex TFIID and the transcription regulatory
CC histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to
CC a promoter (with or without TATA element) is the initial step in
CC preinitiation complex (PIC) formation. TFIID plays a key role in the
CC regulation of gene expression by RNA polymerase II through different
CC activities such as transcription activator interaction, core promoter
CC recognition and selectivity, TFIIA and TFIIB interaction, chromatin
CC modification (histone acetylation by TAF1), facilitation of DNA opening
CC and initiation of transcription. SAGA is involved in RNA polymerase II-
CC dependent transcriptional regulation of approximately 10% of yeast
CC genes. At the promoters, SAGA is required for recruitment of the basal
CC transcription machinery. It influences RNA polymerase II
CC transcriptional activity through different activities such as TBP
CC interaction (SPT3, SPT8 and SPT20) and promoter selectivity,
CC interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1),
CC and chromatin modification through histone acetylation (GCN5) and
CC deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some
CC extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts
CC with DNA via upstream activating sequences (UASs). SLIK is proposed to
CC have partly overlapping functions with SAGA. It preferentially
CC acetylates methylated histone H3, at least after activation at the
CC GAL1-10 locus. {ECO:0000269|PubMed:10026213,
CC ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:11238921,
CC ECO:0000269|PubMed:11295558, ECO:0000269|PubMed:12052880,
CC ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863,
CC ECO:0000269|PubMed:9674426, ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: In TFIID, TAF10 heterodimerizes with TAF3 and TAF8. The 1.2
CC MDa TFIID complex is composed of TATA binding protein (TBP) and the 14
CC TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8,
CC TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12,
CC and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which
CC consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5,
CC SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10,
CC TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to
CC be present in 2 copies. SAGA is built of 5 distinct domains with
CC specialized functions. Domain I (containing TRA1) probably represents
CC the activator interaction surface. Domain II (containing TAF5 and TAF6,
CC and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7,
CC TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV
CC (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play
CC primarily an architectural role. Domain III also harbors the HAT
CC activity. Domain V (containing SPT3 and SPT20, and probably SPT8)
CC represents the TBP-interacting module, which may be associated
CC transiently with SAGA. Component of the SLIK complex, which consists of
CC at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1,
CC UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.
CC {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12052880,
CC ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
CC ECO:0000269|PubMed:9674426}.
CC -!- INTERACTION:
CC Q12030; Q12060: HFI1; NbExp=7; IntAct=EBI-18889, EBI-8287;
CC Q12030; Q12030: TAF10; NbExp=2; IntAct=EBI-18889, EBI-18889;
CC Q12030; Q04226: TAF11; NbExp=5; IntAct=EBI-18889, EBI-18884;
CC Q12030; Q03761: TAF12; NbExp=10; IntAct=EBI-18889, EBI-35097;
CC Q12030; P11747: TAF13; NbExp=7; IntAct=EBI-18889, EBI-18897;
CC Q12030; P53040: TAF6; NbExp=8; IntAct=EBI-18889, EBI-18876;
CC Q12030; Q03750: TAF8; NbExp=7; IntAct=EBI-18889, EBI-27947;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 3400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF10 family. {ECO:0000305}.
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DR EMBL; U51636; AAB07766.1; -; Genomic_DNA.
DR EMBL; Z47813; CAA87798.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12007.1; -; Genomic_DNA.
DR PIR; S50913; S50913.
DR RefSeq; NP_010451.3; NM_001180474.3.
DR PDB; 6T9I; EM; 3.90 A; G=1-206.
DR PDB; 6T9K; EM; 3.30 A; G=1-206.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; Q12030; -.
DR SMR; Q12030; -.
DR BioGRID; 32218; 291.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-855N; -.
DR IntAct; Q12030; 44.
DR MINT; Q12030; -.
DR STRING; 4932.YDR167W; -.
DR iPTMnet; Q12030; -.
DR MaxQB; Q12030; -.
DR PaxDb; Q12030; -.
DR PRIDE; Q12030; -.
DR EnsemblFungi; YDR167W_mRNA; YDR167W; YDR167W.
DR GeneID; 851745; -.
DR KEGG; sce:YDR167W; -.
DR SGD; S000002574; TAF10.
DR VEuPathDB; FungiDB:YDR167W; -.
DR eggNOG; KOG3423; Eukaryota.
DR GeneTree; ENSGT00390000009368; -.
DR HOGENOM; CLU_064104_0_0_1; -.
DR InParanoid; Q12030; -.
DR OMA; ATDAYEY; -.
DR BioCyc; YEAST:G3O-29756-MON; -.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR PRO; PR:Q12030; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12030; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd07982; TAF10; 1.
DR InterPro; IPR003923; TFIID_30kDa.
DR PANTHER; PTHR21242; PTHR21242; 1.
DR Pfam; PF03540; TFIID_30kDa; 1.
DR PIRSF; PIRSF017246; TFIID_TAF10; 1.
DR PRINTS; PR01443; TFIID30KDSUB.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..206
FT /note="Transcription initiation factor TFIID subunit 10"
FT /id="PRO_0000118901"
FT DOMAIN 47..194
FT /note="Histone-fold"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 107..134
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:6T9K"
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
