ID   TAF1_YEAST              Reviewed;        1066 AA.
AC   P46677; D6VV51;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Transcription initiation factor TFIID subunit 1;
DE            EC=2.3.1.48;
DE   AltName: Full=TAFII-130;
DE   AltName: Full=TAFII-145;
DE   AltName: Full=TBP-associated factor 1;
DE   AltName: Full=TBP-associated factor 145 kDa;
GN   Name=TAF1; Synonyms=TAF130, TAF145; OrderedLocusNames=YGR274C;
GN   ORFNames=G9374;
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], AND PROTEIN SEQUENCE OF 583-599 AND
RP   651-671.
RC   STRAIN=Y57;
RX   PubMed=7935765; DOI=10.1038/371523a0;
RA   Reese J.C., Apone L., Walker S.S., Griffin L.A., Green M.R.;
RT   "Yeast TAFIIS in a multisubunit complex required for activated
RT   transcription.";
RL   Nature 371:523-527(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9133740;
RX   DOI=10.1002/(sici)1097-0061(19970330)13:4<365::aid-yea78>3.0.co;2-f;
RA   Ruzzi M., Marconi A., Saliola M., Fabiani L., Montebove F., Frontali L.;
RT   "The sequence of a 8 kb segment on the right arm of yeast chromosome VII
RT   identifies four new open reading frames and the genes for yTAFII145.";
RL   Yeast 13:365-368(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 368-384; 528-554 AND 752-783, AND CHARACTERIZATION.
RC   STRAIN=ATCC 76621 / YPH252;
RX   PubMed=7667272; DOI=10.1073/pnas.92.18.8224;
RA   Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S.,
RA   Kornberg R.D., Weil P.A.;
RT   "Identification and characterization of a TFIID-like multiprotein complex
RT   from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995).
RN   [6]
RP   FUNCTION, AND TAF1 ACETYLATION ACTIVITY.
RX   PubMed=8980232; DOI=10.1016/s0092-8674(00)81821-8;
RA   Mizzen C.A., Yang X.J., Kokubo T., Brownell J.E., Bannister A.J.,
RA   Owen-Hughes T., Workman J., Wang L., Berger S.L., Kouzarides T.,
RA   Nakatani Y., Allis C.D.;
RT   "The TAF(II)250 subunit of TFIID has histone acetyltransferase activity.";
RL   Cell 87:1261-1270(1996).
RN   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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   [12]
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).
CC   -!- FUNCTION: Functions as a component of the DNA-binding general
CC       transcription factor complex TFIID. Binding of TFIID to a promoter
CC       (with or without TATA element) is the initial step in pre-initiation
CC       complex (PIC) formation. TFIID plays a key role in the regulation of
CC       gene expression by RNA polymerase II through different activities such
CC       as transcription activator interaction, core promoter recognition and
CC       selectivity, TFIIA and TFIIB interaction, chromatin modification
CC       (histone acetylation by TAF1), facilitation of DNA opening and
CC       initiation of transcription. {ECO:0000269|PubMed:10788514,
CC       ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863,
CC       ECO:0000269|PubMed:8980232}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC   -!- SUBUNIT: 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.
CC       {ECO:0000269|PubMed:10788514}.
CC   -!- INTERACTION:
CC       P46677; P35817: BDF1; NbExp=3; IntAct=EBI-18855, EBI-3493;
CC       P46677; P23255: TAF2; NbExp=4; IntAct=EBI-18855, EBI-18862;
CC       P46677; P50105: TAF4; NbExp=6; IntAct=EBI-18855, EBI-11231;
CC       P46677; P53040: TAF6; NbExp=6; IntAct=EBI-18855, EBI-18876;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: Compared to higher eukaryotes TAF1, yeast TAF1 lacks the C-
CC       terminal bromodomains and C-terminal kinase activity. The TFIID
CC       interacting proteins BDF1 and BDF2 may substitute for these domains.
CC   -!- MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
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DR   EMBL; U14954; AAA79178.1; -; Genomic_DNA.
DR   EMBL; X84098; CAA58896.1; -; Genomic_DNA.
DR   EMBL; Z73059; CAA97304.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08362.1; -; Genomic_DNA.
DR   PIR; S50237; S50237.
DR   RefSeq; NP_011790.1; NM_001181403.2.
DR   PDB; 4B0A; X-ray; 1.97 A; A=8-71.
DR   PDB; 4OY2; X-ray; 2.90 A; A/C/E=455-960.
DR   PDB; 6E16; X-ray; 2.40 A; A=9-40.
DR   PDB; 6E24; X-ray; 3.00 A; A=9-40.
DR   PDBsum; 4B0A; -.
DR   PDBsum; 4OY2; -.
DR   PDBsum; 6E16; -.
DR   PDBsum; 6E24; -.
DR   AlphaFoldDB; P46677; -.
DR   SMR; P46677; -.
DR   BioGRID; 33524; 965.
DR   ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR   DIP; DIP-839N; -.
DR   IntAct; P46677; 76.
DR   MINT; P46677; -.
DR   STRING; 4932.YGR274C; -.
DR   GlyGen; P46677; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P46677; -.
DR   MaxQB; P46677; -.
DR   PaxDb; 4932-YGR274C; -.
DR   PeptideAtlas; P46677; -.
DR   EnsemblFungi; YGR274C_mRNA; YGR274C; YGR274C.
DR   GeneID; 853191; -.
DR   KEGG; sce:YGR274C; -.
DR   AGR; SGD:S000003506; -.
DR   SGD; S000003506; TAF1.
DR   VEuPathDB; FungiDB:YGR274C; -.
DR   eggNOG; KOG0008; Eukaryota.
DR   GeneTree; ENSGT00940000155242; -.
DR   HOGENOM; CLU_000572_1_0_1; -.
DR   InParanoid; P46677; -.
DR   OMA; KEFMKYQ; -.
DR   OrthoDB; 5482320at2759; -.
DR   BioCyc; YEAST:G3O-30939-MONOMER; -.
DR   BRENDA; 2.3.1.48; 984.
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   BioGRID-ORCS; 853191; 8 hits in 10 CRISPR screens.
DR   PRO; PR:P46677; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P46677; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; 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:0004402; F:histone acetyltransferase activity; IDA:SGD.
DR   GO; GO:0060090; F:molecular adaptor activity; IDA:SGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR   GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:InterPro.
DR   GO; GO:0017025; F:TBP-class protein binding; IDA:SGD.
DR   GO; GO:0045944; P:positive 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   InterPro; IPR040240; TAF1.
DR   InterPro; IPR022591; TAF1_HAT_dom.
DR   InterPro; IPR041670; Znf-CCHC_6.
DR   PANTHER; PTHR13900; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR   PANTHER; PTHR13900:SF0; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1; 1.
DR   Pfam; PF12157; DUF3591; 1.
DR   Pfam; PF15288; zf-CCHC_6; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Chromatin regulator; Coiled coil;
KW   Direct protein sequencing; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..1066
FT                   /note="Transcription initiation factor TFIID subunit 1"
FT                   /id="PRO_0000118862"
FT   REGION          836..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          989..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          409..425
FT                   /evidence="ECO:0000255"
FT   COILED          944..1000
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        989..1017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:6E24"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:4B0A"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:4B0A"
FT   HELIX           28..35
FT                   /evidence="ECO:0007829|PDB:4B0A"
FT   HELIX           471..475
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   TURN            478..480
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          481..484
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           488..491
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   TURN            492..494
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   TURN            498..501
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          507..510
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           518..521
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           526..529
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           533..536
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          538..542
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          544..553
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          563..571
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          584..591
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   TURN            598..601
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          610..615
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          617..626
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          632..640
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          643..650
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          653..658
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          662..665
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           673..694
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           702..705
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           713..720
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   TURN            721..723
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          724..726
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   TURN            731..734
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          735..738
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           747..750
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           751..753
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           756..778
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           782..790
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           793..804
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          820..824
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           859..882
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           888..891
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           900..903
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          914..922
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   STRAND          926..935
FT                   /evidence="ECO:0007829|PDB:4OY2"
FT   HELIX           938..951
FT                   /evidence="ECO:0007829|PDB:4OY2"
SQ   SEQUENCE   1066 AA;  120696 MW;  FAF1EE2A9B2A7B73 CRC64;
     MVKQQGSGKT NLANEDEAYE AIFGGEFGSL EIGSYIGGDE GANSKDYTEH LPDAVDFEDE
     DELADDDDDL PEESDANLHP AMMTMGAYDD VNENGAVLGI DSNSLNMQLP EINGDLSQQF
     ILEDDGGTPA TSNALFMGMD ANEIHLATET GVLDGSGANE IGHSQLSIGG VNGNDMSING
     GFIMEPDMSD GKHKKATKLD LINHEKYLLK KYFPDFEKGK ILKWNKLIYR RSVPYHWHSE
     ISRVKKPFMP LNLKFKVQQD DKRLFNSRTI SYVAPIYQGK NNLLQSNSSA SRRGLIHVSI
     DELFPIKEQQ KKRKIIHDEK TISEDLLIAT DDWDQEKIIN QGTSSTATLA DSSMTPNLKF
     SGGYKLKSLI EDVAEDWQWD EDMIIDAKLK ESKHAELNMN DEKLLLMIEK TNNLAQQKQQ
     LDSSNLILPL NETILQQKFN LSNDDKYQIL KKTHQTKVRS TISNLNIQHS QPAINLQSPF
     YKVAVPRYQL RHFHRENFGS HIRPGTKIVF SKLKARKRKR DKGKDVKESF STSQDLTIGD
     TAPVYLMEYS EQTPVALSKF GMANKLINYY RKANEQDTLR PKLPVGETHV LGVQDKSPFW
     NFGFVEPGHI VPTLYNNMIR APVFKHDISG TDFLLTKSSG FGISNRFYLR NINHLFTVGQ
     TFPVEEIPGP NSRKVTSMKA TRLKMIIYRI LNHNHSKAIS IDPIAKHFPD QDYGQNRQKV
     KEFMKYQRDG PEKGLWRLKD DEKLLDNEAV KSLITPEQIS QVESMSQGLQ FQEDNEAYNF
     DSKLKSLEEN LLPWNITKNF INSTQMRAMI QIHGVGDPTG CGEGFSFLKT SMKGGFVKSG
     SPSSNNNSSN KKGTNTHSYN VAQQQKAYDE EIAKTWYTHT KSLSISNPFE EMTNPDEINQ
     TNKHVKTDRD DKKILKIVRK KRDENGIIQR QTIFIRDPRV IQGYIKIKEQ DKEDVNKLLE
     EDTSKINNLE ELEKQKKLLQ LELANLEKSQ QRRAARQNSK RNGGATRTEN SVDNGSDLAG
     VTDGKAARNK GKNTTRRCAT CGQIGHIRTN KSCPMYSSKD NPASPK
//