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P16649

- TUP1_YEAST

UniProt

P16649 - TUP1_YEAST

Protein

General transcriptional corepressor TUP1

Gene

TUP1

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 159 (01 Oct 2014)
      Sequence version 2 (01 May 1991)
      Previous versions | rss
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    Functioni

    Acts as component of the CYC8-TUP1 corepressor complex which is involved in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex.7 Publications

    GO - Molecular functioni

    1. histone binding Source: SGD
    2. histone deacetylase binding Source: SGD
    3. mediator complex binding Source: SGD
    4. phosphatidylinositol-3,5-bisphosphate binding Source: SGD
    5. protein binding Source: IntAct
    6. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: SGD
    7. ubiquitin binding Source: SGD

    GO - Biological processi

    1. histone exchange Source: SGD
    2. negative regulation of dipeptide transport by negative regulation of transcription from RNA polymerase II promoter Source: SGD
    3. negative regulation of mating-type specific transcription from RNA polymerase II promoter Source: SGD
    4. negative regulation of transcription from RNA polymerase II promoter by glucose Source: SGD
    5. negative regulation of transcription from RNA polymerase II promoter during mitosis Source: SGD
    6. nucleosome positioning Source: SGD
    7. regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter Source: SGD
    8. regulation of response to DNA damage stimulus Source: SGD
    9. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: SGD
    10. regulation of transcription from RNA polymerase II promoter in response to osmotic stress Source: SGD

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29380-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    General transcriptional corepressor TUP1
    Alternative name(s):
    Flocculation suppressor protein
    Glucose repression regulatory protein TUP1
    Repressor AER2
    Gene namesi
    Name:TUP1
    Synonyms:AAR1, AER2, AMM1, CYC9, FLK1, SFL2, UMR7
    Ordered Locus Names:YCR084C
    ORF Names:YCR84C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCR084c.
    SGDiS000000680. TUP1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: SGD
    2. transcriptional repressor complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 713713General transcriptional corepressor TUP1PRO_0000051312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei439 – 4391Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP16649.
    PaxDbiP16649.
    PeptideAtlasiP16649.

    Expressioni

    Gene expression databases

    GenevestigatoriP16649.

    Interactioni

    Subunit structurei

    Associates with CYC8/SSN6 to form the CYC8-TUP1 (or TUP1-SSN6) corepressor complex that is composed of 4 copies of TUP1 and one copy of CYC8. Interacts with histone H3, histone H4, MATALPHA2, RFX1, SKO1, PGD1, HDA1, HDA2, HOS1, HOS2 AND RPD3.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CYC8P149225EBI-19654,EBI-18215
    PGD1P403563EBI-19654,EBI-13268
    RFX1P487432EBI-19654,EBI-15036
    RPD3P325612EBI-19654,EBI-15864

    Protein-protein interaction databases

    BioGridi31057. 93 interactions.
    DIPiDIP-512N.
    IntActiP16649. 16 interactions.
    MINTiMINT-648551.

    Structurei

    Secondary structure

    1
    713
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni19 – 268
    Helixi27 – 8458
    Beta strandi290 – 2923
    Helixi300 – 3034
    Beta strandi307 – 3104
    Beta strandi314 – 3174
    Beta strandi322 – 3254
    Beta strandi333 – 34210
    Beta strandi349 – 3524
    Beta strandi356 – 3627
    Beta strandi367 – 3715
    Turni372 – 3743
    Beta strandi377 – 3815
    Beta strandi445 – 4517
    Beta strandi455 – 4628
    Beta strandi467 – 4715
    Turni472 – 4754
    Beta strandi476 – 4816
    Beta strandi488 – 4936
    Beta strandi497 – 5048
    Beta strandi507 – 5137
    Turni514 – 5174
    Beta strandi518 – 5247
    Beta strandi529 – 5346
    Beta strandi541 – 5466
    Beta strandi551 – 5555
    Turni556 – 5583
    Beta strandi561 – 5655
    Beta strandi579 – 5846
    Beta strandi588 – 5958
    Beta strandi598 – 6047
    Beta strandi622 – 6276
    Beta strandi633 – 6386
    Helixi640 – 6423
    Beta strandi644 – 6496
    Beta strandi652 – 6587
    Turni659 – 6613
    Beta strandi664 – 6696
    Beta strandi675 – 6806
    Beta strandi691 – 6977
    Beta strandi700 – 70910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ERJX-ray2.30A/B/C282-388[»]
    A/B/C432-713[»]
    3VP8X-ray1.91A/B/C/D1-92[»]
    3VP9X-ray1.80A/B1-92[»]
    ProteinModelPortaliP16649.
    SMRiP16649. Positions 2-81, 283-710.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16649.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati342 – 37130WD 1Add
    BLAST
    Repeati441 – 47131WD 2Add
    BLAST
    Repeati483 – 51331WD 3Add
    BLAST
    Repeati524 – 55532WD 4Add
    BLAST
    Repeati574 – 60431WD 5Add
    BLAST
    Repeati628 – 65831WD 6Add
    BLAST
    Repeati670 – 70637WD 7Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi97 – 11822Gln-richAdd
    BLAST
    Compositional biasi181 – 19818Poly-GlnAdd
    BLAST
    Compositional biasi399 – 40911Thr-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat TUP1 family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00750000117788.
    HOGENOMiHOG000200558.
    KOiK06666.
    OMAiINEMALM.
    OrthoDBiEOG7TN01P.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR013890. Tscrpt_rep_Tup1_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF08581. Tup_N. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    ProDomiPD010558. Transcrip_repressor_Tup1_N. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 2 hits.
    PROSITEiPS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 5 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P16649-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTASVSNTQN KLNELLDAIR QEFLQVSQEA NTYRLQNQKD YDFKMNQQLA    50
    EMQQIRNTVY ELELTHRKMK DAYEEEIKHL KLGLEQRDHQ IASLTVQQQR 100
    QQQQQQQVQQ HLQQQQQQLA AASASVPVAQ QPPATTSATA TPAANTTTGS 150
    PSAFPVQASR PNLVGSQLPT TTLPVVSSNA QQQLPQQQLQ QQQLQQQQPP 200
    PQVSVAPLSN TAINGSPTSK ETTTLPSVKA PESTLKETEP ENNNTSKIND 250
    TGSATTATTT TATETEIKPK EEDATPASLH QDHYLVPYNQ RANHSKPIPP 300
    FLLDLDSQSV PDALKKQTND YYILYNPALP REIDVELHKS LDHTSVVCCV 350
    KFSNDGEYLA TGCNKTTQVY RVSDGSLVAR LSDDSAANNH RNSITENNTT 400
    TSTDNNTMTT TTTTTITTTA MTSAAELAKD VENLNTSSSP SSDLYIRSVC 450
    FSPDGKFLAT GAEDRLIRIW DIENRKIVMI LQGHEQDIYS LDYFPSGDKL 500
    VSGSGDRTVR IWDLRTGQCS LTLSIEDGVT TVAVSPGDGK YIAAGSLDRA 550
    VRVWDSETGF LVERLDSENE SGTGHKDSVY SVVFTRDGQS VVSGSLDRSV 600
    KLWNLQNANN KSDSKTPNSG TCEVTYIGHK DFVLSVATTQ NDEYILSGSK 650
    DRGVLFWDKK SGNPLLMLQG HRNSVISVAV ANGSPLGPEY NVFATGSGDC 700
    KARIWKYKKI APN 713
    Length:713
    Mass (Da):78,308
    Last modified:May 1, 1991 - v2
    Checksum:i444104AAD63CB944
    GO

    Sequence cautioni

    The sequence CAA34411.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751E → A in AAA35182. (PubMed:2247069)Curated
    Sequence conflicti100 – 1001R → Q in AAA35182. (PubMed:2247069)Curated
    Sequence conflicti685 – 6851P → S in AAA35182. (PubMed:2247069)Curated
    Sequence conflicti685 – 6851P → S in AAA34413. (PubMed:1900249)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31733 Genomic DNA. Translation: AAA35182.1.
    M35861 Genomic DNA. Translation: AAA34413.1.
    X16365 Genomic DNA. Translation: CAA34411.1. Different initiation.
    X59720 Genomic DNA. Translation: CAA42259.1.
    BK006937 Genomic DNA. Translation: DAA07554.1.
    PIRiJN0133.
    RefSeqiNP_010007.1. NM_001178790.1.

    Genome annotation databases

    EnsemblFungiiYCR084C; YCR084C; YCR084C.
    GeneIDi850445.
    KEGGisce:YCR084C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31733 Genomic DNA. Translation: AAA35182.1 .
    M35861 Genomic DNA. Translation: AAA34413.1 .
    X16365 Genomic DNA. Translation: CAA34411.1 . Different initiation.
    X59720 Genomic DNA. Translation: CAA42259.1 .
    BK006937 Genomic DNA. Translation: DAA07554.1 .
    PIRi JN0133.
    RefSeqi NP_010007.1. NM_001178790.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ERJ X-ray 2.30 A/B/C 282-388 [» ]
    A/B/C 432-713 [» ]
    3VP8 X-ray 1.91 A/B/C/D 1-92 [» ]
    3VP9 X-ray 1.80 A/B 1-92 [» ]
    ProteinModelPortali P16649.
    SMRi P16649. Positions 2-81, 283-710.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31057. 93 interactions.
    DIPi DIP-512N.
    IntActi P16649. 16 interactions.
    MINTi MINT-648551.

    Proteomic databases

    MaxQBi P16649.
    PaxDbi P16649.
    PeptideAtlasi P16649.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR084C ; YCR084C ; YCR084C .
    GeneIDi 850445.
    KEGGi sce:YCR084C.

    Organism-specific databases

    CYGDi YCR084c.
    SGDi S000000680. TUP1.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00750000117788.
    HOGENOMi HOG000200558.
    KOi K06666.
    OMAi INEMALM.
    OrthoDBi EOG7TN01P.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29380-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P16649.
    NextBioi 966057.

    Gene expression databases

    Genevestigatori P16649.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR013890. Tscrpt_rep_Tup1_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF08581. Tup_N. 1 hit.
    PF00400. WD40. 7 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    ProDomi PD010558. Transcrip_repressor_Tup1_N. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 2 hits.
    PROSITEi PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 5 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of TUP1, a mediator of glucose repression in Saccharomyces cerevisiae."
      Williams F.E., Trumbly R.J.
      Mol. Cell. Biol. 10:6500-6511(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "A yeast protein with homology to the beta-subunit of G proteins is involved in control of heme-regulated and catabolite-repressed genes."
      Zhang M., Rosenblum-Vos L.S., Lowry C.V., Boakye K., Zitomer R.S.
      Gene 97:153-161(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of the yeast SFL2 gene: its disruption results in pleiotropic phenotypes characteristic for tup1 mutants."
      Fujita A., Matsumoto S., Kuhara S., Misumi Y., Kobayashi H.
      Gene 89:93-99(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 44774 / DBY747.
    4. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "The SFL2 (TUP1?) protein of Saccharomyces cerevisiae contains a repeating motif homologous to beta subunits of G proteins."
      Kearsley S.
      Gene 98:147-148(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO BETA SUBUNIT OF G-PROTEINS.
    7. "The WD repeats of Tup1 interact with the homeo domain protein alpha 2."
      Komachi K., Redd M.J., Johnson A.D.
      Genes Dev. 8:2857-2867(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MATALPHA2.
    8. "Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4."
      Edmondson D.G., Smith M.M., Roth S.Y.
      Genes Dev. 10:1247-1259(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HISTONE H3 AND HISTONE H4.
    9. "The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits."
      Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.
      Mol. Cell. Biol. 16:6707-6714(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    10. "The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor."
      Huang M., Zhou Z., Elledge S.J.
      Cell 94:595-605(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RFX1.
    11. "Ssn6-Tup1 interacts with class I histone deacetylases required for repression."
      Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y.
      Genes Dev. 14:2737-2744(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CYC8 AND RPD3, FUNCTION OF THE CYC8-TUP1 COMPLEX.
    12. "Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme."
      Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.
      J. Biol. Chem. 275:8397-8403(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PGD1, FUNCTION OF THE CYC8-TUP1 COMPLEX.
    13. "Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress."
      Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.
      EMBO J. 20:1123-1133(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
    14. "Multiple levels of control regulate the yeast cAMP-response element-binding protein repressor Sko1p in response to stress."
      Pascual-Ahuir A., Posas F., Serrano R., Proft M.
      J. Biol. Chem. 276:37373-37378(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKO1.
    15. "TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast."
      Wu J., Suka N., Carlson M., Grunstein M.
      Mol. Cell 7:117-126(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDA1 AND HDA2, FUNCTION OF THE CYC8-TUP1 COMPLEX.
    16. "Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo."
      Davie J.K., Trumbly R.J., Dent S.Y.
      Mol. Cell. Biol. 22:693-703(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
    17. "Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein."
      Mennella T.A., Klinkenberg L.G., Zitomer R.S.
      Eukaryot. Cell 2:1288-1303(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
    18. "Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo."
      Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.
      J. Biol. Chem. 278:50158-50162(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HOS1; HOS2 AND RPD3.
    19. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    20. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    21. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    22. "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].
    23. "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-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast."
      Sprague E.R., Redd M.J., Johnson A.D., Wolberger C.
      EMBO J. 19:3016-3027(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 282-713.

    Entry informationi

    Entry nameiTUP1_YEAST
    AccessioniPrimary (citable) accession number: P16649
    Secondary accession number(s): D6VR85, P17995, P18323
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 5840 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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 III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3