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Q12030 (TAF10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription initiation factor TFIID subunit 10
Alternative name(s):
TAFII-23
Short name=TAFII23
TAFII-25
Short name=TAFII25
TBP-associated factor 10
TBP-associated factor 25 kDa
p25
Gene names
Name:TAF10
Synonyms:TAF23, TAF25
Ordered Locus Names:YDR167W
ORF Names:YD9489.02
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Subunit structure

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. Ref.5 Ref.7 Ref.10 Ref.12 Ref.15

Subcellular location

Nucleus.

Miscellaneous

Present with 3400 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the TAF10 family.

Contains 1 histone-fold domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206Transcription initiation factor TFIID subunit 10
PRO_0000118901

Regions

Domain47 – 194148Histone-fold
Compositional bias147 – 17226Gln-rich

Amino acid modifications

Modified residue581Phosphoserine Ref.17 Ref.18
Modified residue1461Phosphoserine Ref.17

Sequences

Sequence LengthMass (Da)Tools
Q12030 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A472CCA10DC3B495

FASTA20623,019
        10         20         30         40         50         60 
MDFEEDYDAE FDDNQEGQLE TPFPSVAGAD DGDNDNDDSV AENMKKKQKR EAVVDDGSEN 

        70         80         90        100        110        120 
AFGIPEFTRK DKTLEEILEM MDSTPPIIPD AVIDYYLTKN GFNVADVRVK RLLALATQKF 

       130        140        150        160        170        180 
VSDIAKDAYE YSRIRSSVAV SNANNSQARA RQLLQGQQQP GVQQISQQQH QQNEKTTASK 

       190        200 
VVLTVNDLSS AVAEYGLNIG RPDFYR 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of TAF25, an essential yeast gene that encodes an RNA polymerase II-specific TATA-binding protein-associated factor."
Klebanow E.R., Poon D., Zhou S., Weil P.A.
J. Biol. Chem. 271:13706-13715(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
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. expand/collapse author list , 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.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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."
Birck C., Poch O., Romier C., Ruff M., Mengus G., Lavigne A.C., Davidson I., Moras D.
Cell 94:239-249(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TAF-TAF INTERACTION THROUGH HISTONE-FOLD DOMAIN.
[5]"A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation."
Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C., Yates J.R. III, Workman J.L.
Cell 94:45-53(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Expanded lysine acetylation specificity of Gcn5 in native complexes."
Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.
J. Biol. Chem. 274:5895-5900(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
[7]"Identification of two novel TAF subunits of the yeast Saccharomyces cerevisiae TFIID complex."
Sanders S.L., Weil P.A.
J. Biol. Chem. 275:13895-13900(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE TFIID COMPLEX.
[8]"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."
Gangloff Y.G., Sanders S.L., Romier C., Kirschner D.B., Weil P.A., Tora L., Davidson I.
Mol. Cell. Biol. 21:1841-1853(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION IN TFIID AND SAGA.
[9]"The histone fold is a key structural motif of transcription factor TFIID."
Gangloff Y.G., Romier C., Thuault S., Werten S., Davidson I.
Trends Biochem. Sci. 26:250-257(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HISTONE-FOLD DOMAIN CHARACTERIZATION.
[10]"Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry."
Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A.
Mol. Cell. Biol. 22:4723-4738(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX.
[11]"Molecular characterization of Saccharomyces cerevisiae TFIID."
Sanders S.L., Garbett K.A., Weil P.A.
Mol. Cell. Biol. 22:6000-6013(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TFIID STOICHIOMETRY.
[12]"The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway."
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.
Mol. Cell. Biol. 22:8774-8786(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
[13]"Multi-protein complexes in eukaryotic gene transcription."
Martinez E.
Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[15]"Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation."
Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.
Nature 433:434-438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SLIK COMPLEX.
[16]"Mapping histone fold TAFs within yeast TFIID."
Leurent C., Sanders S.L., Ruhlmann C., Mallouh V., Weil P.A., Kirschner D.B., Tora L., Schultz P.
EMBO J. 21:3424-3433(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
[17]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Molecular architecture of the S. cerevisiae SAGA complex."
Wu P.Y., Ruhlmann C., Winston F., Schultz P.
Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51636 Genomic DNA. Translation: AAB07766.1.
Z47813 Genomic DNA. Translation: CAA87798.1.
BK006938 Genomic DNA. Translation: DAA12007.1.
PIRS50913.
RefSeqNP_010451.3. NM_001180474.3.

3D structure databases

ProteinModelPortalQ12030.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32218. 73 interactions.
DIPDIP-855N.
IntActQ12030. 44 interactions.
MINTMINT-405873.
STRING4932.YDR167W.

Proteomic databases

PaxDbQ12030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR167W; YDR167W; YDR167W.
GeneID851745.
KEGGsce:YDR167W.

Organism-specific databases

CYGDYDR167w.
SGDS000002574. TAF10.

Phylogenomic databases

eggNOGCOG5162.
GeneTreeENSGT00390000009368.
HOGENOMHOG000175811.
KOK03134.
OMANPPIIPD.
OrthoDBEOG7PGF3B.

Enzyme and pathway databases

BioCycYEAST:G3O-29756-MONOMER.

Gene expression databases

GenevestigatorQ12030.

Family and domain databases

InterProIPR003923. TFIID_30kDa.
[Graphical view]
PANTHERPTHR21242. PTHR21242. 1 hit.
PfamPF03540. TFIID_30kDa. 1 hit.
[Graphical view]
PIRSFPIRSF017246. TFIID_TAF10. 1 hit.
PRINTSPR01443. TFIID30KDSUB.
ProtoNetSearch...

Other

NextBio969490.
PROQ12030.

Entry information

Entry nameTAF10_YEAST
AccessionPrimary (citable) accession number: Q12030
Secondary accession number(s): D6VSE7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families