TAF3_YEAST
ID TAF3_YEAST Reviewed; 353 AA.
AC Q12297; D6W401;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcription initiation factor TFIID subunit 3;
DE AltName: Full=TAFII-47;
DE Short=TAFII47;
DE AltName: Full=TBP-associated factor 3;
DE AltName: Full=TBP-associated factor 47 kDa;
GN Name=TAF3; Synonyms=TAF47; OrderedLocusNames=YPL011C; ORFNames=LPA6C;
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].
RX PubMed=2265610; DOI=10.1002/j.1460-2075.1990.tb07884.x;
RA Gerring S.L., Spencer F., Hieter P.;
RT "The CHL 1 (CTF 1) gene product of Saccharomyces cerevisiae is important
RT for chromosome transmission and normal cell cycle progression in G2/M.";
RL EMBO J. 9:4347-4358(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3143101; DOI=10.1093/nar/16.21.10153;
RA O'Hara P.J., Horowitz H., Eichinger G., Young E.T.;
RT "The yeast ADR6 gene encodes homopolymeric amino acid sequences and a
RT potential metal-binding domain.";
RL Nucleic Acids Res. 16:10153-10169(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 [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 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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237 AND SER-310, AND
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-346, AND
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).
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:11238921, ECO:0000269|PubMed:11295558,
CC ECO:0000269|PubMed:12138208, ECO:0000269|PubMed:12516863,
CC ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: TAF3 heterodimerizes with TAF10. The 1.2 MDa TFIID complex is
CC composed of TATA binding protein (TBP) and the 14 TBP-associated
CC factors. One copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13,
CC two copies of each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three
CC copies of TAF14. {ECO:0000269|PubMed:10788514}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF3 family. {ECO:0000305}.
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DR EMBL; U33335; AAB68094.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95030.1; -; Genomic_DNA.
DR EMBL; Z48483; CAA88375.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11417.1; -; Genomic_DNA.
DR PIR; S52520; S52520.
DR RefSeq; NP_015314.1; NM_001183825.1.
DR AlphaFoldDB; Q12297; -.
DR SMR; Q12297; -.
DR BioGRID; 36166; 265.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-5328N; -.
DR IntAct; Q12297; 18.
DR MINT; Q12297; -.
DR STRING; 4932.YPL011C; -.
DR iPTMnet; Q12297; -.
DR MaxQB; Q12297; -.
DR PaxDb; Q12297; -.
DR PRIDE; Q12297; -.
DR EnsemblFungi; YPL011C_mRNA; YPL011C; YPL011C.
DR GeneID; 856096; -.
DR KEGG; sce:YPL011C; -.
DR SGD; S000005932; TAF3.
DR VEuPathDB; FungiDB:YPL011C; -.
DR eggNOG; ENOG502S96D; Eukaryota.
DR HOGENOM; CLU_704112_0_0_1; -.
DR InParanoid; Q12297; -.
DR OMA; MDNTFQR; -.
DR BioCyc; YEAST:G3O-33930-MON; -.
DR PRO; PR:Q12297; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12297; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
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; IC:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF07524; Bromo_TP; 1.
DR SMART; SM00576; BTP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..353
FT /note="Transcription initiation factor TFIID subunit 3"
FT /id="PRO_0000118868"
FT DOMAIN 11..78
FT /note="Histone-fold"
FT REGION 279..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..309
FT /evidence="ECO:0000255"
FT COMPBIAS 295..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 353 AA; 40296 MW; 98A6B7813A29978F CRC64;
MTTNNDFYFA LLRISILQLL KAQGFDRARP SLVDVMTDLY AKFLSLLASE VSSIAQARCD
QDDTIALQDI TLALENLGIV KPTNVLDVYD ENSELSSSRG MEKFKDWCIY STQLTDARIT
ALPTVELLQS EEKESDPLSA IPDYLNQLLQ NKGAKQKLET KNRKTELIED LINNNGLDDW
IKLVIARQRI NMIERASKKE SQNVPALPHI AGYKSSILSR HHHTTITNED RMPSAMTPRD
EDALTEIQEN PFVTSKLPIM RKENRLENIT LSFEDEELES LGEVEGPNQK SQENNNEESF
KENNKSLTES PHGDDRDISM FQFDSNVDTK WAEQEDMDST FQRRTSLDYG GYF
