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Q05027

- TAF9_YEAST

UniProt

Q05027 - TAF9_YEAST

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Protein
Transcription initiation factor TFIID subunit 9
Gene
TAF9, TAF17, YMR236W, YM9959.18
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) complex 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.10 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. RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  2. chromatin modification Source: SGD
  3. histone acetylation Source: SGD
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-32917-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 9
Alternative name(s):
TAFII-17
TAFII20
TBP-associated factor 17 kDa
TBP-associated factor 9
Gene namesi
Name:TAF9
Synonyms:TAF17
Ordered Locus Names:YMR236W
ORF Names:YM9959.18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR236w.
SGDiS000004849. TAF9.

Subcellular locationi

Nucleus 1 Publication

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 – 157157Transcription initiation factor TFIID subunit 9
PRO_0000118896Add
BLAST

Proteomic databases

MaxQBiQ05027.
PaxDbiQ05027.
PeptideAtlasiQ05027.

Expressioni

Gene expression databases

GenevestigatoriQ05027.

Interactioni

Subunit structurei

In TFIID, TAF9 heterodimerizes with TAF6, forming ultimately an octamer consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12 dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer. 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
itself6EBI-27500,EBI-27500
TAF4P5010510EBI-27500,EBI-11231
TAF6P5304010EBI-27500,EBI-18876

Protein-protein interaction databases

BioGridi35414. 268 interactions.
DIPiDIP-925N.
IntActiQ05027. 153 interactions.
MINTiMINT-406129.
STRINGi4932.YMR236W.

Structurei

3D structure databases

ProteinModelPortaliQ05027.
SMRiQ05027. Positions 30-101.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 9768Histone-fold
Add
BLAST

Sequence similaritiesi

Belongs to the TAF9 family.

Phylogenomic databases

eggNOGiCOG5094.
GeneTreeiENSGT00390000001626.
HOGENOMiHOG000204913.
KOiK03133.
OMAiWEFGGRI.
OrthoDBiEOG7DZ8XZ.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR003162. TFIID-31.
[Graphical view]
PANTHERiPTHR12075. PTHR12075. 1 hit.
PfamiPF02291. TFIID-31kDa. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Q05027-1 [UniParc]FASTAAdd to Basket

« Hide

MNGGGKNVLN KNSVGSVSEV GPDSTQEETP RDVRLLHLLL ASQSIHQYED    50
QVPLQLMDFA HRYTQGVLKD ALVYNDYAGS GNSAGSGLGV EDIRLAIAAR 100
TQYQFKPTAP KELMLQLAAE RNKKALPQVM GTWGVRLPPE KYCLTAKEWD 150
LEDPKSM 157
Length:157
Mass (Da):17,315
Last modified:November 1, 1997 - v1
Checksum:iD1C97EDDCA468EC5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49939 Genomic DNA. Translation: CAA90207.1.
BK006946 Genomic DNA. Translation: DAA10136.1.
PIRiS57603.
RefSeqiNP_013963.1. NM_001182743.1.

Genome annotation databases

EnsemblFungiiYMR236W; YMR236W; YMR236W.
GeneIDi855276.
KEGGisce:YMR236W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49939 Genomic DNA. Translation: CAA90207.1 .
BK006946 Genomic DNA. Translation: DAA10136.1 .
PIRi S57603.
RefSeqi NP_013963.1. NM_001182743.1.

3D structure databases

ProteinModelPortali Q05027.
SMRi Q05027. Positions 30-101.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35414. 268 interactions.
DIPi DIP-925N.
IntActi Q05027. 153 interactions.
MINTi MINT-406129.
STRINGi 4932.YMR236W.

Proteomic databases

MaxQBi Q05027.
PaxDbi Q05027.
PeptideAtlasi Q05027.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YMR236W ; YMR236W ; YMR236W .
GeneIDi 855276.
KEGGi sce:YMR236W.

Organism-specific databases

CYGDi YMR236w.
SGDi S000004849. TAF9.

Phylogenomic databases

eggNOGi COG5094.
GeneTreei ENSGT00390000001626.
HOGENOMi HOG000204913.
KOi K03133.
OMAi WEFGGRI.
OrthoDBi EOG7DZ8XZ.

Enzyme and pathway databases

BioCyci YEAST:G3O-32917-MONOMER.

Miscellaneous databases

NextBioi 978900.
PROi Q05027.

Gene expression databases

Genevestigatori Q05027.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR003162. TFIID-31.
[Graphical view ]
PANTHERi PTHR12075. PTHR12075. 1 hit.
Pfami PF02291. TFIID-31kDa. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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.
  4. "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.
  5. "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.
  6. "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, SUBUNIT.
  7. "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.
  8. "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.
  9. "A histone fold TAF octamer within the yeast TFIID transcriptional coactivator."
    Selleck W., Howley R., Fang Q., Podolny V., Fried M.G., Buratowski S., Tan S.
    Nat. Struct. Biol. 8:695-700(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TAF OCTAMER FORMATION.
  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: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  16. "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.
  17. Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
  18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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 nameiTAF9_YEAST
AccessioniPrimary (citable) accession number: Q05027
Secondary accession number(s): D6W062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 122 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 7000 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

Similar proteinsi