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P38129

- TAF5_YEAST

UniProt

P38129 - TAF5_YEAST

Protein

Transcription initiation factor TFIID subunit 5

Gene

TAF5

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 146 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      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) complexes SAGA, SALSA 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). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. 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.6 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
    5. ubiquitin binding 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-29139-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription initiation factor TFIID subunit 5
    Alternative name(s):
    TAFII-90
    TBP-associated factor 5
    TBP-associated factor 90 kDa
    Gene namesi
    Name:TAF5
    Synonyms:TAF90
    Ordered Locus Names:YBR198C
    ORF Names:YBR1410
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR198c.
    SGDiS000000402. TAF5.

    Subcellular locationi

    Nucleus Curated

    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 – 798798Transcription initiation factor TFIID subunit 5PRO_0000051260Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei299 – 2991Phosphoserine1 Publication
    Modified residuei411 – 4111Phosphoserine1 Publication
    Modified residuei415 – 4151Phosphoserine1 Publication
    Modified residuei787 – 7871Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38129.
    PaxDbiP38129.
    PeptideAtlasiP38129.

    Expressioni

    Gene expression databases

    GenevestigatoriP38129.

    Interactioni

    Subunit structurei

    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 SALSA complex, which consists of at least TRA1, SPT7 (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1, GCN5, ADA2 and SPT3. 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 TAF9.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself9EBI-18868,EBI-18868
    HFI1Q1206015EBI-18868,EBI-8287
    TAF2P2325510EBI-18868,EBI-18862
    TAF4P5010512EBI-18868,EBI-11231
    TAF6P5304013EBI-18868,EBI-18876

    Protein-protein interaction databases

    BioGridi32895. 304 interactions.
    DIPiDIP-740N.
    IntActiP38129. 197 interactions.
    MINTiMINT-475651.
    STRINGi4932.YBR198C.

    Structurei

    Secondary structure

    1
    798
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi152 – 16413
    Turni168 – 1703
    Helixi171 – 19222
    Helixi194 – 20411
    Helixi205 – 2084
    Helixi209 – 2179
    Turni218 – 2214
    Helixi225 – 2306
    Helixi232 – 2387
    Beta strandi242 – 2465
    Helixi248 – 26013
    Helixi262 – 2643
    Helixi266 – 27611
    Beta strandi277 – 2815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J49X-ray2.30A147-290[»]
    ProteinModelPortaliP38129.
    SMRiP38129. Positions 149-282, 422-794.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38129.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 8833LisHPROSITE-ProRule annotationAdd
    BLAST
    Repeati464 – 50340WD 1Add
    BLAST
    Repeati523 – 56240WD 2Add
    BLAST
    Repeati565 – 60440WD 3Add
    BLAST
    Repeati607 – 64640WD 4Add
    BLAST
    Repeati649 – 68840WD 5Add
    BLAST
    Repeati692 – 73140WD 6Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili329 – 34921Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 4846Gln-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat TAF5 family.Curated
    Contains 1 LisH domain.PROSITE-ProRule annotation
    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00740000114860.
    HOGENOMiHOG000212424.
    KOiK03130.
    OMAiRFRIEGR.
    OrthoDBiEOG7KQ29H.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR006594. LisH_dimerisation.
    IPR013720. LisH_dimerisation_subgr.
    IPR007582. TFIID-su_WD40-assoc_reg.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF08513. LisH. 1 hit.
    PF04494. TFIID_90kDa. 1 hit.
    PF00400. WD40. 6 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00667. LisH. 1 hit.
    SM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 2 hits.
    PROSITEiPS50896. LISH. 1 hit.
    PS00678. WD_REPEATS_1. 3 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38129-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQKQSTNQN QNGTHQPQPV KNQRTNNAAG ANSGQQPQQQ SQGQSQQQGR    50
    SNGPFSASDL NRIVLEYLNK KGYHRTEAML RAESGRTLTP QNKQSPANTK 100
    TGKFPEQSSI PPNPGKTAKP ISNPTNLSSK RDAEGGIVSS GRLEGLNAPE 150
    NYIRAYSMLK NWVDSSLEIY KPELSYIMYP IFIYLFLNLV AKNPVYARRF 200
    FDRFSPDFKD FHGSEINRLF SVNSIDHIKE NEVASAFQSH KYRITMSKTT 250
    LNLLLYFLNE NESIGGSLII SVINQHLDPN IVESVTAREK LADGIKVLSD 300
    SENGNGKQNL EMNSVPVKLG PFPKDEEFVK EIETELKIKD DQEKQLNQQT 350
    AGDNYSGANN RTLLQEYKAM NNEKFKDNTG DDDKDKIKDK IAKDEEKKES 400
    ELKVDGEKKD SNLSSPARDI LPLPPKTALD LKLEIQKVKE SRDAIKLDNL 450
    QLALPSVCMY TFQNTNKDMS CLDFSDDCRI AAAGFQDSYI KIWSLDGSSL 500
    NNPNIALNNN DKDEDPTCKT LVGHSGTVYS TSFSPDNKYL LSGSEDKTVR 550
    LWSMDTHTAL VSYKGHNHPV WDVSFSPLGH YFATASHDQT ARLWSCDHIY 600
    PLRIFAGHLN DVDCVSFHPN GCYVFTGSSD KTCRMWDVST GDSVRLFLGH 650
    TAPVISIAVC PDGRWLSTGS EDGIINVWDI GTGKRLKQMR GHGKNAIYSL 700
    SYSKEGNVLI SGGADHTVRV WDLKKATTEP SAEPDEPFIG YLGDVTASIN 750
    QDIKEYGRRR TVIPTSDLVA SFYTKKTPVF KVKFSRSNLA LAGGAFRP 798
    Length:798
    Mass (Da):88,968
    Last modified:October 1, 1994 - v1
    Checksum:iB42315B8C752D0B6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21487 Genomic DNA. Translation: CAA79685.1.
    Z36067 Genomic DNA. Translation: CAA85160.1.
    AY692890 Genomic DNA. Translation: AAT92909.1.
    BK006936 Genomic DNA. Translation: DAA07314.1.
    PIRiS34023.
    RefSeqiNP_009757.1. NM_001178546.1.

    Genome annotation databases

    EnsemblFungiiYBR198C; YBR198C; YBR198C.
    GeneIDi852497.
    KEGGisce:YBR198C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21487 Genomic DNA. Translation: CAA79685.1 .
    Z36067 Genomic DNA. Translation: CAA85160.1 .
    AY692890 Genomic DNA. Translation: AAT92909.1 .
    BK006936 Genomic DNA. Translation: DAA07314.1 .
    PIRi S34023.
    RefSeqi NP_009757.1. NM_001178546.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2J49 X-ray 2.30 A 147-290 [» ]
    ProteinModelPortali P38129.
    SMRi P38129. Positions 149-282, 422-794.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32895. 304 interactions.
    DIPi DIP-740N.
    IntActi P38129. 197 interactions.
    MINTi MINT-475651.
    STRINGi 4932.YBR198C.

    Proteomic databases

    MaxQBi P38129.
    PaxDbi P38129.
    PeptideAtlasi P38129.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR198C ; YBR198C ; YBR198C .
    GeneIDi 852497.
    KEGGi sce:YBR198C.

    Organism-specific databases

    CYGDi YBR198c.
    SGDi S000000402. TAF5.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00740000114860.
    HOGENOMi HOG000212424.
    KOi K03130.
    OMAi RFRIEGR.
    OrthoDBi EOG7KQ29H.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29139-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P38129.
    NextBioi 971495.
    PROi P38129.

    Gene expression databases

    Genevestigatori P38129.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR006594. LisH_dimerisation.
    IPR013720. LisH_dimerisation_subgr.
    IPR007582. TFIID-su_WD40-assoc_reg.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF08513. LisH. 1 hit.
    PF04494. TFIID_90kDa. 1 hit.
    PF00400. WD40. 6 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00667. LisH. 1 hit.
    SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 2 hits.
    PROSITEi PS50896. LISH. 1 hit.
    PS00678. WD_REPEATS_1. 3 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence analysis of an 11.7 kb fragment of yeast chromosome II including BEM1, a new gene of the WD-40 repeat family and a new member of the KRE2/MNT1 family."
      Mallet L., Bussereau F., Jacquet M.
      Yeast 10:819-831(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Yeast TAFIIS in a multisubunit complex required for activated transcription."
      Reese J.C., Apone L., Walker S.S., Griffin L.A., Green M.R.
      Nature 371:523-527(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 726-747, CHARACTERIZATION.
      Strain: Y57.
    6. "Identification and characterization of a TFIID-like multiprotein complex from Saccharomyces cerevisiae."
      Poon D., Bai Y., Campbell A.M., Bjorklund S., Kim Y.-J., Zhou S., Kornberg R.D., Weil P.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:8224-8228(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-63 AND 726-752, CHARACTERIZATION.
      Strain: ATCC 76621 / YPH252.
    7. "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 IN SAGA COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "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.
    9. "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 TFIID COMPLEX.
    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 IN SAGA COMPLEX.
    11. "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.
    12. "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription."
      Sterner D.E., Belotserkovskaya R., Berger S.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SALSA COMPLEX.
    13. Cited for: 3D-STRUCTURE, ELECTRON MICROSCOPY OF TFIID.
    14. "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.
    15. "Multi-protein complexes in eukaryotic gene transcription."
      Martinez E.
      Plant Mol. Biol. 50:925-947(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    17. "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.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-411 AND SER-787, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, 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 nameiTAF5_YEAST
    AccessioniPrimary (citable) accession number: P38129
    Secondary accession number(s): D6VQJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 146 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 14834 (+/-203) molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3