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 27-MAR-2024, entry version 188. 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; GN 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}. 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; 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 EMDB; EMD-10412; -. DR EMDB; EMD-10414; -. DR SMR; Q05027; -. DR BioGRID; 35414; 470. 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 GlyGen; Q05027; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q05027; -. DR MaxQB; Q05027; -. DR PaxDb; 4932-YMR236W; -. DR PeptideAtlas; Q05027; -. DR EnsemblFungi; YMR236W_mRNA; YMR236W; YMR236W. DR GeneID; 855276; -. DR KEGG; sce:YMR236W; -. DR AGR; SGD:S000004849; -. 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 OrthoDB; 10695at2759; -. DR BioCyc; YEAST:G3O-32917-MONOMER; -. 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 BioGRID-ORCS; 855276; 10 hits in 10 CRISPR screens. DR PRO; PR:Q05027; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q05027; Protein. DR GO; GO:0005634; C:nucleus; NAS: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: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; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR003162; TFIID-31. DR PANTHER; PTHR48068; TAF9 RNA POLYMERASE II, TATA BOX-BINDING PROTEIN (TBP)-ASSOCIATED FACTOR; 1. DR PANTHER; PTHR48068:SF4; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 9; 1. DR Pfam; PF02291; TFIID-31kDa; 1. DR SUPFAM; SSF47113; Histone-fold; 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 //