TAF4_YEAST
ID TAF4_YEAST Reviewed; 388 AA.
AC P50105; D6VZI0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Transcription initiation factor TFIID subunit 4;
DE AltName: Full=MPT-1;
DE AltName: Full=TAF suppressor gene 2 protein;
DE AltName: Full=TAFII-48;
DE AltName: Full=TBP-associated factor 4;
DE AltName: Full=TBP-associated factor 48 kDa;
GN Name=TAF4; Synonyms=MPT1, TAF48, TSG2; OrderedLocusNames=YMR005W;
GN ORFNames=YM8270.07;
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].
RC STRAIN=DBY939;
RA Estey L.A., Douglas M.G.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, AND SUBUNIT.
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP 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 SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-49 AND SER-80, 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).
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:11473260, ECO:0000269|PubMed:12138208,
CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: TAF4 heterodimerizes with TAF12, forming ultimately an octamer
CC consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12
CC dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer.
CC The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and
CC the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7,
CC TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10,
CC TAF12, and three copies of TAF14. {ECO:0000269|PubMed:10788514,
CC ECO:0000269|PubMed:11473260}.
CC -!- INTERACTION:
CC P50105; P46677: TAF1; NbExp=6; IntAct=EBI-11231, EBI-18855;
CC P50105; Q03761: TAF12; NbExp=13; IntAct=EBI-11231, EBI-35097;
CC P50105; P38129: TAF5; NbExp=12; IntAct=EBI-11231, EBI-18868;
CC P50105; Q05027: TAF9; NbExp=10; IntAct=EBI-11231, EBI-27500;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}.
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DR EMBL; X79240; CAA55822.1; -; Genomic_DNA.
DR EMBL; Z48613; CAA88520.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09904.1; -; Genomic_DNA.
DR PIR; S45013; S45013.
DR RefSeq; NP_013718.1; NM_001182501.1.
DR AlphaFoldDB; P50105; -.
DR SMR; P50105; -.
DR BioGRID; 35175; 257.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-789N; -.
DR IntAct; P50105; 34.
DR MINT; P50105; -.
DR STRING; 4932.YMR005W; -.
DR iPTMnet; P50105; -.
DR MaxQB; P50105; -.
DR PaxDb; P50105; -.
DR PRIDE; P50105; -.
DR EnsemblFungi; YMR005W_mRNA; YMR005W; YMR005W.
DR GeneID; 855017; -.
DR KEGG; sce:YMR005W; -.
DR SGD; S000004607; TAF4.
DR VEuPathDB; FungiDB:YMR005W; -.
DR eggNOG; KOG2341; Eukaryota.
DR GeneTree; ENSGT00390000011620; -.
DR HOGENOM; CLU_036634_0_0_1; -.
DR InParanoid; P50105; -.
DR OMA; YGWLTSS; -.
DR BioCyc; YEAST:G3O-32716-MON; -.
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:P50105; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P50105; 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:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor 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; IC:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd08045; TAF4; 1.
DR InterPro; IPR045144; TAF4.
DR InterPro; IPR007900; TAF4_C.
DR PANTHER; PTHR15138; PTHR15138; 1.
DR Pfam; PF05236; TAF4; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..388
FT /note="Transcription initiation factor TFIID subunit 4"
FT /id="PRO_0000118871"
FT DOMAIN 193..261
FT /note="Histone-fold"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 279..297
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 388 AA; 42336 MW; 7DFAC01C7AF07189 CRC64;
MANSPKKPSD GTGVSASDTP KYQHTVPETK PAFNLSPGKA SELSHSLPSP SQIKSTAHVS
STHNDAAGNT DDSVLPKNVS PTTNLRVESN GDTNNMFSSP AGLALPKKDD KKKNKGTSKA
DSKDGKASNS SGQNAQQQSD PNKMQDVLFS AGIDVREEEA LLNSSINASK SQVQTNNVKI
PNHLPFLHPE QVSNYMRKVG KEQNFNLTPT KNPEILDMMS SACENYMRDI LTNAIVISRH
RRKAVKINSG RRSEVSAALR AIALIQKKEE ERRVKKRIAL GLEKEDYENK IDSEETLHRA
SNVTAGLRAG SKKQYGWLTS SVNKPTSLGA KSSGKVASDI TARGESGLKF REAREEPGIV
MRDLLFALEN RRNSVQTIIS KGYAKIRD
