TAF9_YEAST
ID TAF9_YEAST Reviewed; 157 AA.
AC Q05027; D6W062;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Transcription initiation factor TFIID subunit 9;
DE AltName: Full=TAFII-17;
DE AltName: Full=TAFII20;
DE AltName: Full=TBP-associated factor 17 kDa;
DE AltName: Full=TBP-associated factor 9;
GN Name=TAF9; Synonyms=TAF17; OrderedLocusNames=YMR236W; ORFNames=YM9959.18;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [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 by
RT atypical evolutionary conserved motifs also found in the SPT3 family.";
RL Cell 94:239-249(1998).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND TAF OCTAMER FORMATION.
RX PubMed=11473260; DOI=10.1038/90408;
RA Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S.,
RA Tan S.;
RT "A histone fold TAF octamer within the yeast TFIID transcriptional
RT coactivator.";
RL Nat. Struct. Biol. 8:695-700(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [15]
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 [16]
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 [17]
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 [18]
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 [19]
RP IDENTIFICATION BY 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 [20]
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) complex SAGA and SLIK. Binding of TFIID to a
CC 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:11473260,
CC ECO:0000269|PubMed:12052880, ECO:0000269|PubMed:12138208,
CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9674426,
CC ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: In TFIID, TAF9 heterodimerizes with TAF6, forming ultimately
CC an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by
CC TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4
CC octamer. The 1.2 MDa TFIID complex is composed of TATA binding protein
CC (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2,
CC TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6,
CC TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa
CC SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3,
CC SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2,
CC SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19,
CC TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5
CC distinct domains with specialized functions. Domain I (containing TRA1)
CC probably represents the activator interaction surface. Domain II
CC (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III
CC (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3
CC and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably
CC TAF9) are believed to play primarily an architectural role. Domain III
CC also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and
CC probably SPT8) represents the TBP-interacting module, which may be
CC associated transiently with SAGA. Component of the SLIK complex, which
CC consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12,
CC TAF6, HFI1, 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 Q05027; P50105: TAF4; NbExp=10; IntAct=EBI-27500, EBI-11231;
CC Q05027; P53040: TAF6; NbExp=11; IntAct=EBI-27500, EBI-18876;
CC Q05027; Q05027: TAF9; NbExp=6; IntAct=EBI-27500, EBI-27500;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000305}.
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DR EMBL; Z49939; CAA90207.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10136.1; -; Genomic_DNA.
DR PIR; S57603; S57603.
DR RefSeq; NP_013963.1; NM_001182743.1.
DR PDB; 6T9I; EM; 3.90 A; F=1-157.
DR PDB; 6T9K; EM; 3.30 A; F=1-157.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; Q05027; -.
DR SMR; Q05027; -.
DR BioGRID; 35414; 465.
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-925N; -.
DR IntAct; Q05027; 154.
DR MINT; Q05027; -.
DR STRING; 4932.YMR236W; -.
DR iPTMnet; Q05027; -.
DR MaxQB; Q05027; -.
DR PaxDb; Q05027; -.
DR PRIDE; Q05027; -.
DR EnsemblFungi; YMR236W_mRNA; YMR236W; YMR236W.
DR GeneID; 855276; -.
DR KEGG; sce:YMR236W; -.
DR SGD; S000004849; TAF9.
DR VEuPathDB; FungiDB:YMR236W; -.
DR eggNOG; KOG3334; Eukaryota.
DR GeneTree; ENSGT00940000169542; -.
DR HOGENOM; CLU_068315_3_0_1; -.
DR InParanoid; Q05027; -.
DR OMA; PHDAQVM; -.
DR BioCyc; YEAST:G3O-32917-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-6807505; RNA polymerase II transcribes snRNA genes.
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:Q05027; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05027; 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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; 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:0043966; P:histone H3 acetylation; IBA:GO_Central.
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 CDD; cd07979; TAF9; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003162; TFIID-31.
DR Pfam; PF02291; TFIID-31kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..157
FT /note="Transcription initiation factor TFIID subunit 9"
FT /id="PRO_0000118896"
FT DOMAIN 30..97
FT /note="Histone-fold"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 51..77
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 99..103
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6T9K"
SQ SEQUENCE 157 AA; 17315 MW; D1C97EDDCA468EC5 CRC64;
MNGGGKNVLN KNSVGSVSEV GPDSTQEETP RDVRLLHLLL ASQSIHQYED QVPLQLMDFA
HRYTQGVLKD ALVYNDYAGS GNSAGSGLGV EDIRLAIAAR TQYQFKPTAP KELMLQLAAE
RNKKALPQVM GTWGVRLPPE KYCLTAKEWD LEDPKSM
