Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q12030

- TAF10_YEAST

UniProt

Q12030 - TAF10_YEAST

Protein

Transcription initiation factor TFIID subunit 10

Gene

TAF10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Curated
    Contains 1 histone-fold domain.Curated

    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

    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: October 1, 2014
    This is version 132 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.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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3