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Q05027

- TAF9_YEAST

UniProt

Q05027 - TAF9_YEAST

Protein

Transcription initiation factor TFIID subunit 9

Gene

TAF9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    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. 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

    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

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 157157Transcription initiation factor TFIID subunit 9PRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the TAF9 family.Curated
    Contains 1 histone-fold domain.Curated

    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

    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: October 1, 2014
    This is version 123 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.1 Publication

    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