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Q12030

- TAF10_YEAST

UniProt

Q12030 - TAF10_YEAST

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Protein

Transcription initiation factor TFIID subunit 10

Gene
TAF10, TAF23, TAF25, YDR167W, YD9489.02
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.9 Publications

GO - Molecular functioni

  1. chromatin binding Source: SGD
  2. identical protein binding Source: IntAct
  3. protein binding Source: IntAct
  4. protein complex scaffold Source: SGD

GO - Biological processi

  1. chromatin modification Source: SGD
  2. histone acetylation Source: SGD
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  5. transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29756-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TAF10
Synonyms:TAF23, TAF25
Ordered Locus Names:YDR167W
ORF Names:YD9489.02
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR167w.
SGDiS000002574. TAF10.

Subcellular locationi

GO - Cellular componenti

  1. SAGA complex Source: SGD
  2. SLIK (SAGA-like) complex Source: SGD
  3. transcription factor TFIID complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Transcription initiation factor TFIID subunit 10PRO_0000118901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei58 – 581Phosphoserine2 Publications
Modified residuei146 – 1461Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12030.
PaxDbiQ12030.

Expressioni

Gene expression databases

GenevestigatoriQ12030.

Interactioni

Subunit structurei

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 TAF9.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-18889,EBI-18889
HFI1Q120607EBI-18889,EBI-8287
TAF11Q042265EBI-18889,EBI-18884
TAF12Q0376111EBI-18889,EBI-35097
TAF13P117478EBI-18889,EBI-18897
TAF6P5304010EBI-18889,EBI-18876
TAF8Q037507EBI-18889,EBI-27947

Protein-protein interaction databases

BioGridi32218. 73 interactions.
DIPiDIP-855N.
IntActiQ12030. 44 interactions.
MINTiMINT-405873.
STRINGi4932.YDR167W.

Structurei

3D structure databases

ProteinModelPortaliQ12030.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 194148Histone-foldAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi147 – 17226Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the TAF10 family.

Phylogenomic databases

eggNOGiCOG5162.
GeneTreeiENSGT00390000009368.
HOGENOMiHOG000175811.
KOiK03134.
OMAiFECADIR.
OrthoDBiEOG7PGF3B.

Family and domain databases

InterProiIPR003923. TFIID_30kDa.
[Graphical view]
PANTHERiPTHR21242. PTHR21242. 1 hit.
PfamiPF03540. TFIID_30kDa. 1 hit.
[Graphical view]
PIRSFiPIRSF017246. TFIID_TAF10. 1 hit.
PRINTSiPR01443. TFIID30KDSUB.

Sequencei

Sequence statusi: Complete.

Q12030-1 [UniParc]FASTAAdd to Basket

« Hide

MDFEEDYDAE FDDNQEGQLE TPFPSVAGAD DGDNDNDDSV AENMKKKQKR    50
EAVVDDGSEN AFGIPEFTRK DKTLEEILEM MDSTPPIIPD AVIDYYLTKN 100
GFNVADVRVK RLLALATQKF VSDIAKDAYE YSRIRSSVAV SNANNSQARA 150
RQLLQGQQQP GVQQISQQQH QQNEKTTASK VVLTVNDLSS AVAEYGLNIG 200
RPDFYR 206
Length:206
Mass (Da):23,019
Last modified:November 1, 1996 - v1
Checksum:iA472CCA10DC3B495
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51636 Genomic DNA. Translation: AAB07766.1.
Z47813 Genomic DNA. Translation: CAA87798.1.
BK006938 Genomic DNA. Translation: DAA12007.1.
PIRiS50913.
RefSeqiNP_010451.3. NM_001180474.3.

Genome annotation databases

EnsemblFungiiYDR167W; YDR167W; YDR167W.
GeneIDi851745.
KEGGisce:YDR167W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51636 Genomic DNA. Translation: AAB07766.1 .
Z47813 Genomic DNA. Translation: CAA87798.1 .
BK006938 Genomic DNA. Translation: DAA12007.1 .
PIRi S50913.
RefSeqi NP_010451.3. NM_001180474.3.

3D structure databases

ProteinModelPortali Q12030.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32218. 73 interactions.
DIPi DIP-855N.
IntActi Q12030. 44 interactions.
MINTi MINT-405873.
STRINGi 4932.YDR167W.

Proteomic databases

MaxQBi Q12030.
PaxDbi Q12030.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR167W ; YDR167W ; YDR167W .
GeneIDi 851745.
KEGGi sce:YDR167W.

Organism-specific databases

CYGDi YDR167w.
SGDi S000002574. TAF10.

Phylogenomic databases

eggNOGi COG5162.
GeneTreei ENSGT00390000009368.
HOGENOMi HOG000175811.
KOi K03134.
OMAi FECADIR.
OrthoDBi EOG7PGF3B.

Enzyme and pathway databases

BioCyci YEAST:G3O-29756-MONOMER.

Miscellaneous databases

NextBioi 969490.
PROi Q12030.

Gene expression databases

Genevestigatori Q12030.

Family and domain databases

InterProi IPR003923. TFIID_30kDa.
[Graphical view ]
PANTHERi PTHR21242. PTHR21242. 1 hit.
Pfami PF03540. TFIID_30kDa. 1 hit.
[Graphical view ]
PIRSFi PIRSF017246. TFIID_TAF10. 1 hit.
PRINTSi PR01443. TFIID30KDSUB.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiTAF10_YEAST
AccessioniPrimary (citable) accession number: Q12030
Secondary accession number(s): D6VSE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi