TAF11_YEAST
ID TAF11_YEAST Reviewed; 346 AA.
AC Q04226; D6VZF9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Transcription initiation factor TFIID subunit 11;
DE AltName: Full=TAFII-40;
DE Short=TAFII40;
DE AltName: Full=TBP-associated factor 11;
DE AltName: Full=TBP-associated factor 40 kDa;
DE Short=P40;
GN Name=TAF11; Synonyms=TAF40; OrderedLocusNames=YML015C; ORFNames=YM9571.03C;
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 29-46; 125-144;
RP 255-267 AND 323-335.
RX PubMed=9083082; DOI=10.1074/jbc.272.14.9436;
RA Klebanow E.R., Poon D., Zhou S., Weil P.A.;
RT "Cloning and characterization of an essential Saccharomyces cerevisiae
RT gene, TAF40, which encodes yTAFII40, an RNA polymerase II-specific TATA-
RT binding protein-associated factor.";
RL J. Biol. Chem. 272:9436-9442(1997).
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 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236 AND SER-238, 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:11295558, ECO:0000269|PubMed:12138208,
CC ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9695952}.
CC -!- SUBUNIT: TAF11 heterodimerizes with TAF13, but they do not seem to form
CC a heterotetramer like TAF6/TAF9. The 1.2 MDa TFIID complex is composed
CC of TATA binding protein (TBP) and the 14 TBP-associated factors (one
CC copy of each TAF1, TAF2, TAF3, TAF7, TAF8, TAF11, TAF13, two copies of
CC each TAF4, TAF5, TAF6, TAF9, TAF10, TAF12, and three copies of TAF14),
CC ranging in size from 17 to 150 kDa. {ECO:0000269|PubMed:10788514}.
CC -!- INTERACTION:
CC Q04226; Q12030: TAF10; NbExp=5; IntAct=EBI-18884, EBI-18889;
CC Q04226; P11747: TAF13; NbExp=3; IntAct=EBI-18884, EBI-18897;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TAF11 family. {ECO:0000305}.
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DR EMBL; U85960; AAB46715.1; -; Genomic_DNA.
DR EMBL; Z49810; CAA89937.1; -; Genomic_DNA.
DR EMBL; AY692911; AAT92930.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09883.1; -; Genomic_DNA.
DR PIR; S55104; S55104.
DR RefSeq; NP_013697.1; NM_001182373.1.
DR AlphaFoldDB; Q04226; -.
DR SMR; Q04226; -.
DR BioGRID; 35154; 283.
DR ComplexPortal; CPX-1642; General transcription factor complex TFIID.
DR DIP; DIP-1686N; -.
DR IntAct; Q04226; 17.
DR MINT; Q04226; -.
DR STRING; 4932.YML015C; -.
DR iPTMnet; Q04226; -.
DR MaxQB; Q04226; -.
DR PaxDb; Q04226; -.
DR PRIDE; Q04226; -.
DR EnsemblFungi; YML015C_mRNA; YML015C; YML015C.
DR GeneID; 854993; -.
DR KEGG; sce:YML015C; -.
DR SGD; S000004477; TAF11.
DR VEuPathDB; FungiDB:YML015C; -.
DR eggNOG; KOG3219; Eukaryota.
DR GeneTree; ENSGT00390000013228; -.
DR HOGENOM; CLU_048787_0_0_1; -.
DR InParanoid; Q04226; -.
DR OMA; GNGWMFR; -.
DR BioCyc; YEAST:G3O-32619-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:Q04226; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04226; 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:0003713; F:transcription coactivator activity; IBA:GO_Central.
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; cd08048; TAF11; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR045127; TAF11-like.
DR InterPro; IPR006809; TAFII28_dom.
DR PANTHER; PTHR13218; PTHR13218; 1.
DR Pfam; PF04719; TAFII28; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..346
FT /note="Transcription initiation factor TFIID subunit 11"
FT /id="PRO_0000118907"
FT DOMAIN 131..329
FT /note="Histone-fold"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 346 AA; 40624 MW; E9A538EE89488F46 CRC64;
MTEPQGPLDT IPKVNYPPIL TIANYFSTKQ MIDQVISEDQ DYVTWKLQNL RTGGTSINNQ
LNKYPKYKYQ KTRINQQDPD SINKVPENLI FPQDILQQQT QNSNYEDTNT NEDENEKLAQ
DEQFKLLVTN LDKDQTNRFE VFHRTSLNKT QVKKLASTVA NQTISENIRV FLQAVGKIYA
GEIIELAMIV KNKWLTSQMC IEFDKRTKIG YKLKKYLKKL TFSIIENQQY KQDYQSDSVP
EDEPDFYFDD EEVDKRETTL GNSLLQSKSL QQSDHNSQDL KLQLIEQYNK LVLQFNKLDV
SIEKYNNSPL LPEHIREAWR LYRLQSDTLP NAYWRTQGEG QGSMFR
