true1994-10-012024-03-27217TAF5_YEASTNucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II including BEM1, a new gene of the WD-40 repeat family and a new member of the KRE2/MNT1 family.Mallet L.Bussereau F.Jacquet M.doi:10.1002/yea.3201006121994Yeast10819-831NUCLEOTIDE SEQUENCE [GENOMIC DNA]ATCC 204508 / S288cComplete DNA sequence of yeast chromosome II.Feldmann H.Aigle M.Aljinovic G.Andre B.Baclet M.C.Barthe C.Baur A.Becam A.-M.Biteau N.Boles E.Brandt T.Brendel M.Brueckner M.Bussereau F.Christiansen C.Contreras R.Crouzet M.Cziepluch C.Demolis N.Delaveau T.Doignon F.Domdey H.Duesterhus S.Dubois E.Dujon B.El Bakkoury M.Entian K.-D.Feuermann M.Fiers W.Fobo G.M.Fritz C.Gassenhuber J.Glansdorff N.Goffeau A.Grivell L.A.de Haan M.Hein C.Herbert C.J.Hollenberg C.P.Holmstroem K.Jacq C.Jacquet M.Jauniaux J.-C.Jonniaux J.-L.Kallesoee T.Kiesau P.Kirchrath L.Koetter P.Korol S.Liebl S.Logghe M.Lohan A.J.E.Louis E.J.Li Z.Y.Maat M.J.Mallet L.Mannhaupt G.Messenguy F.Miosga T.Molemans F.Mueller S.Nasr F.Obermaier B.Perea J.Pierard A.Piravandi E.Pohl F.M.Pohl T.M.Potier S.Proft M.Purnelle B.Ramezani Rad M.Rieger M.Rose M.Schaaff-Gerstenschlaeger I.Scherens B.Schwarzlose C.Skala J.Slonimski P.P.Smits P.H.M.Souciet J.-L.Steensma H.Y.Stucka R.Urrestarazu L.A.van der Aart Q.J.M.Van Dyck L.Vassarotti A.Vetter I.Vierendeels F.Vissers S.Wagner G.de Wergifosse P.Wolfe K.H.Zagulski M.Zimmermann F.K.Mewes H.-W.Kleine K.doi:10.1002/j.1460-2075.1994.tb06923.x1994EMBO J.135795-5809NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The reference genome sequence of Saccharomyces cerevisiae: Then and now.Engel S.R.Dietrich F.S.Fisk D.G.Binkley G.Balakrishnan R.Costanzo M.C.Dwight S.S.Hitz B.C.Karra K.Nash R.S.Weng S.Wong E.D.Lloyd P.Skrzypek M.S.Miyasato S.R.Simison M.Cherry J.M.doi:10.1534/g3.113.0089952014G3 (Bethesda)4389-398GENOME REANNOTATIONApproaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.Hu Y.Rolfs A.Bhullar B.Murthy T.V.S.Zhu C.Berger M.F.Camargo A.A.Kelley F.McCarron S.Jepson D.Richardson A.Raphael J.Moreira D.Taycher E.Zuo D.Mohr S.Kane M.F.Williamson J.Simpson A.J.G.Bulyk M.L.Harlow E.Marsischky G.Kolodner R.D.LaBaer J.doi:10.1101/gr.60376072007Genome Res.17536-543NUCLEOTIDE SEQUENCE [GENOMIC DNA]Yeast TAFIIS in a multisubunit complex required for activated transcription.Reese J.C.Apone L.Walker S.S.Griffin L.A.Green M.R.doi:10.1038/371523a01994Nature371523-527PROTEIN SEQUENCE OF 726-747CHARACTERIZATIONY57Identification and characterization of a TFIID-like multiprotein complex from Saccharomyces cerevisiae.Poon D.Bai Y.Campbell A.M.Bjorklund S.Kim Y.-J.Zhou S.Kornberg R.D.Weil P.A.doi:10.1073/pnas.92.18.82241995Proc. Natl. Acad. Sci. U.S.A.928224-8228PROTEIN SEQUENCE OF 22-63 AND 726-752CHARACTERIZATIONATCC 76621 / YPH252A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation.Grant P.A.Schieltz D.Pray-Grant M.G.Steger D.J.Reese J.C.Yates J.R. IIIWorkman J.L.doi:10.1016/s0092-8674(00)81220-91998Cell9445-53FUNCTIONIDENTIFICATION IN THE IN SAGA COMPLEXIDENTIFICATION BY MASS SPECTROMETRYExpanded lysine acetylation specificity of Gcn5 in native complexes.Grant P.A.Eberharter A.John S.Cook R.G.Turner B.M.Workman J.L.doi:10.1074/jbc.274.9.58951999J. Biol. Chem.2745895-5900FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEXIdentification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex.Sanders S.L.Weil P.A.doi:10.1074/jbc.275.18.138952000J. Biol. Chem.27513895-13900FUNCTIONIDENTIFICATION IN TFIID COMPLEXProteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry.Sanders S.L.Jennings J.Canutescu A.Link A.J.Weil P.A.doi:10.1128/mcb.22.13.4723-4738.20022002Mol. Cell. Biol.224723-4738FUNCTIONIDENTIFICATION IN THE IN SAGA COMPLEXThe novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.Pray-Grant M.G.Schieltz D.McMahon S.J.Wood J.M.Kennedy E.L.Cook R.G.Workman J.L.Yates J.R. IIIGrant P.A.doi:10.1128/mcb.22.24.8774-8786.20022002Mol. Cell. Biol.228774-8786IDENTIFICATION IN THE SLIK COMPLEXSALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription.Sterner D.E.Belotserkovskaya R.Berger S.L.doi:10.1073/pnas.1820211992002Proc. Natl. Acad. Sci. U.S.A.9911622-11627IDENTIFICATION IN THE SALSA COMPLEXMapping histone fold TAFs within yeast TFIID.Leurent C.Sanders S.L.Ruhlmann C.Mallouh V.Weil P.A.Kirschner D.B.Tora L.Schultz P.doi:10.1093/emboj/cdf3422002EMBO J.213424-34333D-STRUCTUREELECTRON MICROSCOPY OF TFIIDMolecular characterization of Saccharomyces cerevisiae TFIID.Sanders S.L.Garbett K.A.Weil P.A.doi:10.1128/mcb.22.16.6000-6013.20022002Mol. Cell. Biol.226000-6013FUNCTIONTFIID STOICHIOMETRYMulti-protein complexes in eukaryotic gene transcription.Martinez E.doi:10.1023/a:10212587138502002Plant Mol. Biol.50925-947FUNCTIONGlobal analysis of protein expression in yeast.Ghaemmaghami S.Huh W.-K.Bower K.Howson R.W.Belle A.Dephoure N.O'Shea E.K.Weissman J.S.doi:10.1038/nature020462003Nature425737-741LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation.Pray-Grant M.G.Daniel J.A.Schieltz D.Yates J.R. IIIGrant P.A.doi:10.1038/nature032422005Nature433434-438IDENTIFICATION IN THE SLIK COMPLEXA multidimensional chromatography technology for in-depth phosphoproteome analysis.Albuquerque C.P.Smolka M.B.Payne S.H.Bafna V.Eng J.Zhou H.doi:10.1074/mcp.m700468-mcp2002008Mol. Cell. Proteomics71389-1396PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-411 AND SER-787IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.Holt L.J.Tuch B.B.Villen J.Johnson A.D.Gygi S.P.Morgan D.O.doi:10.1126/science.11728672009Science3251682-1686PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Molecular architecture of the S. cerevisiae SAGA complex.Wu P.Y.Ruhlmann C.Winston F.Schultz P.doi:10.1016/j.molcel.2004.06.0052004Mol. Cell15199-2083D-STRUCTURE MODELING OF THE SAGA COMPLEX2.30A=147-2903.90D=1-7983.30D=1-798870General transcription factor complex TFIIDSAGA complexSLIK (SAGA-like) complex2124 sites, 1 O-linked glycan (4 sites)TAF5EukaryotaRNA Polymerase II Pre-transcription EventsRNA polymerase II transcribes snRNA genesRNA Polymerase II Promoter EscapeRNA Polymerase II Transcription Pre-Initiation And Promoter OpeningRNA Polymerase II Transcription InitiationRNA Polymerase II Transcription Initiation And Promoter Clearance0 hits in 10 CRISPR screensProteinTAF5_NTD2WD40TFIID subunit TAF5, NTD2 domainYVTN repeat-like/Quinoprotein amine dehydrogenaseG-protein_beta_WD-40_repLisHTFIID_NTD2TFIID_NTD2_sfWD40/YVTN_repeat-like_dom_sfWD40_repeat_CSWD40_repeat_dom_sfWD40_rptCANNONBALL-RELATEDTRANSCRIPTION INITIATION FACTOR TFIIDLisHTFIID_NTD2WD40GPROTEINBRPTLisHWD40Taf5 N-terminal domain-likeWD40 repeat-likeLISHWD_REPEATS_1WD_REPEATS_2WD_REPEATS_REGIONTranscription initiation factor TFIID subunit 5TAFII-90TBP-associated factor 5TBP-associated factor 90 kDaTAF5TAF90YBR198CYBR1410Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Component of the SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9.Present with 14834 (+/-203) molecules/cell in log phase SD medium.Belongs to the WD repeat TAF5 family.Transcription initiation factor TFIID subunit 5889681798LisH5688WD 1464503WD 2523562WD 3565604WD 4607646WD 5649688WD 6692731Disordered57Disordered82134Disordered371421329349Polar residues85133Basic and acidic residues414Phosphoserine299Phosphoserine411Phosphoserine415Phosphoserine78770758699101120123152164168170171192194204205208209217218221225230232238242246248260262264266276277281432443456462469474476478480485490494504506517521528533537547549553554556558563570574577580583586589595598606612617621628629631632637638640643648654659661670675679680682684689704706708712714728747749768773781784788795false15false9false12false8false12TAF5HFI1TAF2TAF4TAF61994-10-0118896872da8a73015e8cdbf21a7e6c994529b4MSQKQSTNQNQNGTHQPQPVKNQRTNNAAGANSGQQPQQQSQGQSQQQGRSNGPFSASDLNRIVLEYLNKKGYHRTEAMLRAESGRTLTPQNKQSPANTKTGKFPEQSSIPPNPGKTAKPISNPTNLSSKRDAEGGIVSSGRLEGLNAPENYIRAYSMLKNWVDSSLEIYKPELSYIMYPIFIYLFLNLVAKNPVYARRFFDRFSPDFKDFHGSEINRLFSVNSIDHIKENEVASAFQSHKYRITMSKTTLNLLLYFLNENESIGGSLIISVINQHLDPNIVESVTAREKLADGIKVLSDSENGNGKQNLEMNSVPVKLGPFPKDEEFVKEIETELKIKDDQEKQLNQQTAGDNYSGANNRTLLQEYKAMNNEKFKDNTGDDDKDKIKDKIAKDEEKKESELKVDGEKKDSNLSSPARDILPLPPKTALDLKLEIQKVKESRDAIKLDNLQLALPSVCMYTFQNTNKDMSCLDFSDDCRIAAAGFQDSYIKIWSLDGSSLNNPNIALNNNDKDEDPTCKTLVGHSGTVYSTSFSPDNKYLLSGSEDKTVRLWSMDTHTALVSYKGHNHPVWDVSFSPLGHYFATASHDQTARLWSCDHIYPLRIFAGHLNDVDCVSFHPNGCYVFTGSSDKTCRMWDVSTGDSVRLFLGHTAPVISIAVCPDGRWLSTGSEDGIINVWDIGTGKRLKQMRGHGKNAIYSLSYSKEGNVLISGGADHTVRVWDLKKATTEPSAEPDEPFIGYLGDVTASINQDIKEYGRRRTVIPTSDLVASFYTKKTPVFKVKFSRSNLALAGGAFRPtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue