TAF1_YEAST
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 03-AUG-2022, entry version 185.
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; 958.
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 iPTMnet; P46677; -.
DR MaxQB; P46677; -.
DR PaxDb; P46677; -.
DR PRIDE; P46677; -.
DR EnsemblFungi; YGR274C_mRNA; YGR274C; YGR274C.
DR GeneID; 853191; -.
DR KEGG; sce:YGR274C; -.
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 BioCyc; YEAST:G3O-30939-MON; -.
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 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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; PTHR13900; 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
