TAF13_YEAST
ID TAF13_YEAST Reviewed; 167 AA.
AC P11747; D6W0I7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Transcription initiation factor TFIID subunit 13;
DE AltName: Full=Function unknown 81 protein;
DE AltName: Full=TAFII-19;
DE Short=TAFII19;
DE AltName: Full=TBP-associated factor 13;
DE AltName: Full=TBP-associated factor 19 kDa;
GN Name=TAF13; Synonyms=FUN81, TAF19; OrderedLocusNames=YML098W;
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=3311883; DOI=10.1016/0378-1119(87)90286-1;
RA Dubois E., Bercy J., Descamps F., Messenguy F.;
RT "Characterization of two new genes essential for vegetative growth in
RT Saccharomyces cerevisiae: nucleotide sequence determination and chromosome
RT mapping.";
RL Gene 55:265-275(1987).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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 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 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-131, AND IDENTIFICATION BY
RP 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:11295558, ECO:0000269|PubMed:12138208,
CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: In TFIID, TAF13 heterodimerizes with TAF11, but they do not
CC seem to form a heterotetramer like TAF6/TAF9. The 1.2 MDa TFIID complex
CC is 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 -!- INTERACTION:
CC P11747; Q12030: TAF10; NbExp=7; IntAct=EBI-18897, EBI-18889;
CC P11747; Q04226: TAF11; NbExp=3; IntAct=EBI-18897, EBI-18884;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TAF13 family. {ECO:0000305}.
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DR EMBL; M17512; AAA34610.1; -; Genomic_DNA.
DR EMBL; Z46660; CAA86639.1; -; Genomic_DNA.
DR EMBL; AY557763; AAS56089.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09801.1; -; Genomic_DNA.
DR PIR; S49628; S49628.
DR RefSeq; NP_013611.1; NM_001182458.1.
DR AlphaFoldDB; P11747; -.
DR SMR; P11747; -.
DR BioGRID; 35045; 401.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-2054N; -.
DR IntAct; P11747; 25.
DR MINT; P11747; -.
DR STRING; 4932.YML098W; -.
DR iPTMnet; P11747; -.
DR MaxQB; P11747; -.
DR PaxDb; P11747; -.
DR PRIDE; P11747; -.
DR EnsemblFungi; YML098W_mRNA; YML098W; YML098W.
DR GeneID; 854875; -.
DR KEGG; sce:YML098W; -.
DR SGD; S000004564; TAF13.
DR VEuPathDB; FungiDB:YML098W; -.
DR eggNOG; KOG3901; Eukaryota.
DR GeneTree; ENSGT00390000012981; -.
DR HOGENOM; CLU_076665_0_2_1; -.
DR InParanoid; P11747; -.
DR OMA; EDFEFAM; -.
DR BioCyc; YEAST:G3O-32683-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
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:P11747; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P11747; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005669; C:transcription factor TFIID complex; 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; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR CDD; cd07978; TAF13; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003195; TFIID_TAF13.
DR PANTHER; PTHR11380; PTHR11380; 1.
DR Pfam; PF02269; TFIID-18kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..167
FT /note="Transcription initiation factor TFIID subunit 13"
FT /id="PRO_0000118912"
FT DOMAIN 10..74
FT /note="Histone-fold"
FT REGION 97..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..129
FT /evidence="ECO:0000255"
FT COMPBIAS 116..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 137..138
FT /note="AA -> GV (in Ref. 1; AAA34610)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> A (in Ref. 1; AAA34610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 19132 MW; F54E639C0A59C506 CRC64;
MSRKLKKTNL FNKDVSSLLY AYGDVPQPLQ ATVQCLDELV SGYLVDVCTN AFHTAQNSQR
NKLRLEDFKF ALRKDPIKLG RAEELIATNK LITEAKKQFN ETDNQNSLKR YREEDEEGDE
MEEDEDEQQV TDDDEEAAGR NSAKQSTDSK ATKIRKQGPK NLKKTKK
