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Transcription initiation factor TFIID subunit 10 (TAFII-23) (TAFII23) (TAFII-25) (TAFII25) (TBP-associated factor 10) (TBP-associated factor 25 kDa) (p25)

 TAF10_YEAST             Reviewed;         206 AA.
Q12030; D6VSE7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 159.
RecName: Full=Transcription initiation factor TFIID subunit 10;
AltName: Full=TAFII-23;
Short=TAFII23;
AltName: Full=TAFII-25;
Short=TAFII25;
AltName: Full=TBP-associated factor 10;
AltName: Full=TBP-associated factor 25 kDa;
AltName: Full=p25;
Name=TAF10; Synonyms=TAF23, TAF25; OrderedLocusNames=YDR167W;
ORFNames=YD9489.02;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8662725; DOI=10.1074/jbc.271.23.13706;
Klebanow E.R., Poon D., Zhou S., Weil P.A.;
"Isolation and characterization of TAF25, an essential yeast gene that
encodes an RNA polymerase II-specific TATA-binding protein-associated
factor.";
J. Biol. Chem. 271:13706-13715(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, AND TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
PubMed=9695952; DOI=10.1016/S0092-8674(00)81423-3;
Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C.,
Davidson I., Moras D.;
"Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded
by atypical evolutionary conserved motifs also found in the SPT3
family.";
Cell 94:239-249(1998).
[5]
FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=9674426; DOI=10.1016/S0092-8674(00)81220-9;
Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
Yates J.R. III, Workman J.L.;
"A subset of TAF(II)s are integral components of the SAGA complex
required for nucleosome acetylation and transcriptional stimulation.";
Cell 94:45-53(1998).
[6]
FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M.,
Workman J.L.;
"Expanded lysine acetylation specificity of Gcn5 in native
complexes.";
J. Biol. Chem. 274:5895-5900(1999).
[7]
FUNCTION, AND IDENTIFICATION IN THE TFIID COMPLEX.
PubMed=10788514; DOI=10.1074/jbc.275.18.13895;
Sanders S.L., Weil P.A.;
"Identification of two novel TAF subunits of the yeast Saccharomyces
cerevisiae TFIID complex.";
J. Biol. Chem. 275:13895-13900(2000).
[8]
FUNCTION, AND INTERACTION IN TFIID AND SAGA.
PubMed=11238921; DOI=10.1128/MCB.21.5.1841-1853.2001;
Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A.,
Tora L., Davidson I.;
"Histone folds mediate selective heterodimerization of yeast TAF(II)25
with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA
component ySPT7.";
Mol. Cell. Biol. 21:1841-1853(2001).
[9]
FUNCTION, AND HISTONE-FOLD DOMAIN CHARACTERIZATION.
PubMed=11295558; DOI=10.1016/S0968-0004(00)01741-2;
Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.;
"The histone fold is a key structural motif of transcription factor
TFIID.";
Trends Biochem. Sci. 26:250-257(2001).
[10]
FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
PubMed=12052880; DOI=10.1128/MCB.22.13.4723-4738.2002;
Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.;
"Proteomics of the eukaryotic transcription machinery: identification
of proteins associated with components of yeast TFIID by
multidimensional mass spectrometry.";
Mol. Cell. Biol. 22:4723-4738(2002).
[11]
FUNCTION, AND TFIID STOICHIOMETRY.
PubMed=12138208; DOI=10.1128/MCB.22.16.6000-6013.2002;
Sanders S.L., Garbett K.A., Weil P.A.;
"Molecular characterization of Saccharomyces cerevisiae TFIID.";
Mol. Cell. Biol. 22:6000-6013(2002).
[12]
IDENTIFICATION IN THE SLIK COMPLEX.
PubMed=12446794; DOI=10.1128/MCB.22.24.8774-8786.2002;
Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
"The novel SLIK histone acetyltransferase complex functions in the
yeast retrograde response pathway.";
Mol. Cell. Biol. 22:8774-8786(2002).
[13]
FUNCTION.
PubMed=12516863; DOI=10.1023/A:1021258713850;
Martinez E.;
"Multi-protein complexes in eukaryotic gene transcription.";
Plant Mol. Biol. 50:925-947(2002).
[14]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[15]
IDENTIFICATION IN THE SLIK COMPLEX.
PubMed=15647753; DOI=10.1038/nature03242;
Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
"Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
dependent acetylation.";
Nature 433:434-438(2005).
[16]
3D-STRUCTURE, AND ELECTRON MICROSCOPY OF TFIID.
PubMed=12093743; DOI=10.1093/emboj/cdf342;
Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A.,
Kirschner D.B., Tora L., Schultz P.;
"Mapping histone fold TAFs within yeast TFIID.";
EMBO J. 21:3424-3433(2002).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-146, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[19]
3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
"Molecular architecture of the S. cerevisiae SAGA complex.";
Mol. Cell 15:199-208(2004).
-!- FUNCTION: Functions as a component of the DNA-binding general
transcription factor complex TFIID and the transcription
regulatory histone acetylation (HAT) complexes SAGA and SLIK.
Binding of TFIID to a promoter (with or without TATA element) is
the initial step in preinitiation complex (PIC) formation. TFIID
plays a key role in the regulation of gene expression by RNA
polymerase II through different activities such as transcription
activator interaction, core promoter recognition and selectivity,
TFIIA and TFIIB interaction, chromatin modification (histone
acetylation by TAF1), facilitation of DNA opening and initiation
of transcription. SAGA is involved in RNA polymerase II-dependent
transcriptional regulation of approximately 10% of yeast genes. At
the promoters, SAGA is required for recruitment of the basal
transcription machinery. It influences RNA polymerase II
transcriptional activity through different activities such as TBP
interaction (SPT3, SPT8 and SPT20) and promoter selectivity,
interaction with transcription activators (GCN5, ADA2, ADA3 and
TRA1), and chromatin modification through histone acetylation
(GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal
histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and
H3K23ac). SAGA interacts with DNA via upstream activating
sequences (UASs). SLIK is proposed to have partly overlapping
functions with SAGA. It preferentially acetylates methylated
histone H3, at least after activation at the GAL1-10 locus.
{ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:10788514,
ECO:0000269|PubMed:11238921, ECO:0000269|PubMed:11295558,
ECO:0000269|PubMed:12052880, ECO:0000269|PubMed:12138208,
ECO:0000269|PubMed:12516863, ECO:0000269|PubMed:9674426,
ECO:0000269|PubMed:9695952}.
-!- SUBUNIT: In TFIID, TAF10 heterodimerizes with TAF3 and TAF8. The
1.2 MDa TFIID complex is composed of TATA binding protein (TBP)
and the 14 TBP-associated factors. One copy of each TAF1, TAF2,
TAF3, TAF7, TAF8, TAF11, TAF13, two copies of each TAF4, TAF5,
TAF6, TAF9, TAF10, TAF12, and three copies of TAF14. Component of
the 1.8 MDa SAGA complex, which consists of at least TRA1, CHD1,
SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1,
UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5,
TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies.
SAGA is built of 5 distinct domains with specialized functions.
Domain I (containing TRA1) probably represents the activator
interaction surface. Domain II (containing TAF5 and TAF6, and
probably TAF9 and TAF10), domain III (containing GCN5, TAF10,
SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and
domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are
believed to play primarily an architectural role. Domain III also
harbors the HAT activity. Domain V (containing SPT3 and SPT20, and
probably SPT8) represents the TBP-interacting module, which may be
associated transiently with SAGA. Component of the SLIK complex,
which consists of at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20,
RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and
TAF9. {ECO:0000269|PubMed:10788514, ECO:0000269|PubMed:12052880,
ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:15647753,
ECO:0000269|PubMed:9674426}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-18889, EBI-18889;
Q12060:HFI1; NbExp=7; IntAct=EBI-18889, EBI-8287;
Q04226:TAF11; NbExp=5; IntAct=EBI-18889, EBI-18884;
Q03761:TAF12; NbExp=10; IntAct=EBI-18889, EBI-35097;
P11747:TAF13; NbExp=7; IntAct=EBI-18889, EBI-18897;
P53040:TAF6; NbExp=8; IntAct=EBI-18889, EBI-18876;
Q03750:TAF8; NbExp=7; IntAct=EBI-18889, EBI-27947;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 3400 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TAF10 family. {ECO:0000305}.
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EMBL; U51636; AAB07766.1; -; Genomic_DNA.
EMBL; Z47813; CAA87798.1; -; Genomic_DNA.
EMBL; BK006938; DAA12007.1; -; Genomic_DNA.
PIR; S50913; S50913.
RefSeq; NP_010451.3; NM_001180474.3.
ProteinModelPortal; Q12030; -.
SMR; Q12030; -.
BioGrid; 32218; 279.
DIP; DIP-855N; -.
IntAct; Q12030; 44.
MINT; MINT-405873; -.
STRING; 4932.YDR167W; -.
iPTMnet; Q12030; -.
MaxQB; Q12030; -.
PRIDE; Q12030; -.
EnsemblFungi; YDR167W; YDR167W; YDR167W.
GeneID; 851745; -.
KEGG; sce:YDR167W; -.
EuPathDB; FungiDB:YDR167W; -.
SGD; S000002574; TAF10.
GeneTree; ENSGT00390000009368; -.
HOGENOM; HOG000175811; -.
InParanoid; Q12030; -.
KO; K03134; -.
OMA; QGGSQNR; -.
OrthoDB; EOG092C3BLF; -.
BioCyc; YEAST:G3O-29756-MONOMER; -.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape.
Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
PRO; PR:Q12030; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000124; C:SAGA complex; IDA:SGD.
GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:SGD.
GO; GO:0003682; F:chromatin binding; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0032947; F:protein complex scaffold activity; IMP:SGD.
GO; GO:0006325; P:chromatin organization; IDA:SGD.
GO; GO:0016573; P:histone acetylation; IDA:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IMP:SGD.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:SGD.
CDD; cd07982; TAF10; 1.
InterPro; IPR003923; TFIID_30kDa.
PANTHER; PTHR21242; PTHR21242; 1.
Pfam; PF03540; TFIID_30kDa; 1.
PIRSF; PIRSF017246; TFIID_TAF10; 1.
PRINTS; PR01443; TFIID30KDSUB.
1: Evidence at protein level;
Complete proteome; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 206 Transcription initiation factor TFIID
subunit 10.
/FTId=PRO_0000118901.
DOMAIN 47 194 Histone-fold.
COMPBIAS 147 172 Gln-rich.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
SEQUENCE 206 AA; 23019 MW; A472CCA10DC3B495 CRC64;
MDFEEDYDAE FDDNQEGQLE TPFPSVAGAD DGDNDNDDSV AENMKKKQKR EAVVDDGSEN
AFGIPEFTRK DKTLEEILEM MDSTPPIIPD AVIDYYLTKN GFNVADVRVK RLLALATQKF
VSDIAKDAYE YSRIRSSVAV SNANNSQARA RQLLQGQQQP GVQQISQQQH QQNEKTTASK
VVLTVNDLSS AVAEYGLNIG RPDFYR


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