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UniProtKB/Swiss-Prot entry P16649


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TUP1_YEAST
Primary accession number P16649
Secondary accession numbers P17995 P18323
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on May 1, 1991 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 93)
Name and origin of the protein
Protein name General transcriptional corepressor TUP1
Synonyms Glucose repression regulatory protein TUP1
Flocculation suppressor protein
Repressor AER2
Gene name
Name: TUP1
Synonyms: AAR1, AER2, AMM1, CYC9, FLK1, SFL2, UMR7
OrderedLocusNames: YCR084C
ORFNames: YCR84C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=2247069 [NCBI, ExPASy, EBI, Israel, Japan]
Williams F.E., Trumbly R.J.;
"Characterization of TUP1, a mediator of glucose repression in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 10:6500-6511(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(91)90047-F; PubMed=1900249 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang M., Rosenblum-Vos L.S., Lowry C.V., Boakye K., Zitomer R.S.;
"A yeast protein with homology to the beta-subunit of G proteins is involved in control of heme-regulated and catabolite-repressed genes.";
Gene 97:153-161(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 44774 / DBY747;
DOI=10.1016/0378-1119(90)90210-I; PubMed=2197185 [NCBI, ExPASy, EBI, Israel, Japan]
Fujita A., Matsumoto S., Kuhara S., Misumi Y., Kobayashi H.;
"Cloning of the yeast SFL2 gene: its disruption results in pleiotropic phenotypes characteristic for tup1 mutants.";
Gene 89:93-99(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/357038a0; PubMed=1574125 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[5]
SIMILARITY TO BETA SUBUNIT OF G-PROTEINS.
DOI=10.1016/0378-1119(91)90118-U; PubMed=1901558 [NCBI, ExPASy, EBI, Israel, Japan]
Kearsley S.;
"The SFL2 (TUP1?) protein of Saccharomyces cerevisiae contains a repeating motif homologous to beta subunits of G proteins.";
Gene 98:147-148(1991).
[6]
INTERACTION WITH MATALPHA2.
PubMed=7995523 [NCBI, ExPASy, EBI, Israel, Japan]
Komachi K., Redd M.J., Johnson A.D.;
"The WD repeats of Tup1 interact with the homeo domain protein alpha 2.";
Genes Dev. 8:2857-2867(1994).
[7]
INTERACTION WITH HISTONE H3 AND HISTONE H4.
PubMed=8675011 [NCBI, ExPASy, EBI, Israel, Japan]
Edmondson D.G., Smith M.M., Roth S.Y.;
"Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4.";
Genes Dev. 10:1247-1259(1996).
[8]
SUBUNIT.
PubMed=8943325 [NCBI, ExPASy, EBI, Israel, Japan]
Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.;
"The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and four Tup1 subunits.";
Mol. Cell. Biol. 16:6707-6714(1996).
[9]
INTERACTION WITH RFX1.
DOI=10.1016/S0092-8674(00)81601-3; PubMed=9741624 [NCBI, ExPASy, EBI, Israel, Japan]
Huang M., Zhou Z., Elledge S.J.;
"The DNA replication and damage checkpoint pathways induce transcription by inhibition of the Crt1 repressor.";
Cell 94:595-605(1998).
[10]
INTERACTION WITH CYC8 AND RPD3, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
DOI=10.1101/gad.829100; PubMed=11069890 [NCBI, ExPASy, EBI, Israel, Japan]
Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W., Stillman D.J., Roth S.Y.;
"Ssn6-Tup1 interacts with class I histone deacetylases required for repression.";
Genes Dev. 14:2737-2744(2000).
[11]
INTERACTION WITH PGD1, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
DOI=10.1074/jbc.275.12.8397; PubMed=10722672 [NCBI, ExPASy, EBI, Israel, Japan]
Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T., Tzamarias D.;
"Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II holoenzyme.";
J. Biol. Chem. 275:8397-8403(2000).
[12]
FUNCTION OF THE CYC8-TUP1 COMPLEX.
DOI=10.1093/emboj/20.5.1123; PubMed=11230135 [NCBI, ExPASy, EBI, Israel, Japan]
Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R., Posas F.;
"Regulation of the Sko1 transcriptional repressor by the Hog1 MAP kinase in response to osmotic stress.";
EMBO J. 20:1123-1133(2001).
[13]
INTERACTION WITH SKO1.
DOI=10.1074/jbc.M105755200; PubMed=11500510 [NCBI, ExPASy, EBI, Israel, Japan]
Pascual-Ahuir A., Posas F., Serrano R., Proft M.;
"Multiple levels of control regulate the yeast cAMP-response element-binding protein repressor Sko1p in response to stress.";
J. Biol. Chem. 276:37373-37378(2001).
[14]
INTERACTION WITH HDA1 AND HDA2, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
DOI=10.1016/S1097-2765(01)00160-5; PubMed=11172717 [NCBI, ExPASy, EBI, Israel, Japan]
Wu J., Suka N., Carlson M., Grunstein M.;
"TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress gene activity in yeast.";
Mol. Cell 7:117-126(2001).
[15]
FUNCTION OF THE CYC8-TUP1 COMPLEX.
PubMed=11784848 [NCBI, ExPASy, EBI, Israel, Japan]
Davie J.K., Trumbly R.J., Dent S.Y.;
"Histone-dependent association of Tup1-Ssn6 with repressed genes in vivo.";
Mol. Cell. Biol. 22:693-703(2002).
[16]
FUNCTION OF THE CYC8-TUP1 COMPLEX.
DOI=10.1128/EC.2.6.1288-1303.2003; PubMed=14665463 [NCBI, ExPASy, EBI, Israel, Japan]
Mennella T.A., Klinkenberg L.G., Zitomer R.S.;
"Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-independent exclusion of TATA binding protein.";
Eukaryot. Cell 2:1288-1303(2003).
[17]
INTERACTION WITH HOS1; HOS2 AND RPD3.
DOI=10.1074/jbc.M309753200; PubMed=14525981 [NCBI, ExPASy, EBI, Israel, Japan]
Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.;
"Tup1-Ssn6 interacts with multiple class I histone deacetylases in vivo.";
J. Biol. Chem. 278:50158-50162(2003).
[18]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[19]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-216; THR-218; SER-253; SER-437; SER-438; SER-439; SER-441 AND SER-442, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 282-713.
DOI=10.1093/emboj/19.12.3016; PubMed=10856245 [NCBI, ExPASy, EBI, Israel, Japan]
Sprague E.R., Redd M.J., Johnson A.D., Wolberger C.;
"Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast.";
EMBO J. 19:3016-3027(2000).
Comments
  • FUNCTION: 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.
  • SUBUNIT: 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.
  • INTERACTION:
    P14922:CYC8; NbExp=3; IntAct=EBI-19654, EBI-18215;
    P53973:HDA1; NbExp=1; IntAct=EBI-19654, EBI-8206;
    Q06623:HDA3; NbExp=1; IntAct=EBI-19654, EBI-38663;
    Q12214:HOS1; NbExp=1; IntAct=EBI-19654, EBI-8471;
    P40356:PGD1; NbExp=1; IntAct=EBI-19654, EBI-13268;
    P48743:RFX1; NbExp=1; IntAct=EBI-19654, EBI-15036;
    P32561:RPD3; NbExp=2; IntAct=EBI-19654, EBI-15864;
  • SUBCELLULAR LOCATION: Nucleus.
  • MISCELLANEOUS: Present with 5840 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the WD repeat TUP1 family.
  • SIMILARITY: Contains 7 WD repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M31733; AAA35182.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35861; AAA34413.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16365; CAA34411.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59720; CAA42259.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JN0133; JN0133.
RefSeq NP_010007.1; -.
3D structure databases
PDB
1ERJ; X-ray; 2.30 A; A/B/C=282-713.[ExPASy / RCSB / EBI]
PDBsum 1ERJ; -.
ModBase P16649.
Protein-protein interaction databases
DIP DIP:512N; -.
IntAct P16649; -.
Organism-specific databases
CYGD YCR084c; -.
SGD S000000680; TUP1.
Yeast-GFP YCR084C.
Gene expression databases
ArrayExpress P16649; -.
GermOnline YCR084C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0017053; Cellular component: transcriptional repressor complex (inferred from direct assay from SGD).
GO:0016565; Molecular function: general transcriptional repressor activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0016481; Biological process: negative regulation of transcription (inferred from direct assay from SGD).
GO:0016584; Biological process: nucleosome positioning (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013890; Transcrip_repressor_Tup1_N.
IPR015943; WD40/YVTN_repeat-like.
IPR001680; WD40_repeat.
Graphical view of domain structure.
Gene3D G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
Pfam PF08581; Tup_N; 1.
PF00400; WD40; 7.
Pfam graphical view of domain structure.
PRINTS PR00320; GPROTEINBRPT.
ProDom PD000018; WD40; 6.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00320; WD40; 7.
SMART graphical view of domain structure.
PROSITE PS00678; WD_REPEATS_1; 4.
PS50082; WD_REPEATS_2; 5.
PS50294; WD_REPEATS_REGION; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P16649.
Proteomic databases
PeptideAtlas P16649; -.
Genome annotation databases
Ensembl YCR084C; Saccharomyces cerevisiae. [Contig view]
GeneID 850445; -.
GenomeReviews X59720_GR; YCR084C.
KEGG sce:YCR084C; -.
NMPDR fig|4932.3.peg.736; -.
Phylogenomic databases
HOGENOM P16649; -.
Other
LinkHub P16649; -.
ProtoNet P16649.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Nucleus; Phosphoprotein; Repeat; Repressor; Transcription; Transcription regulation; WD repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   713  713     General transcriptional corepressor TUP1. PRO_0000051312
REPEAT   342   371  30     WD 1. 
REPEAT   441   471  31     WD 2. 
REPEAT   483   513  31     WD 3. 
REPEAT   524   555  32     WD 4. 
REPEAT   574   604  31     WD 5. 
REPEAT   628   658  31     WD 6. 
REPEAT   670   706  37     WD 7. 
COMPBIAS   97   118  22     Gln-rich. 
COMPBIAS   181   198  18     Poly-Gln. 
COMPBIAS   399   409  11     Thr-rich. 
MOD_RES   150   150        Phosphoserine. 
MOD_RES   216   216        Phosphoserine. 
MOD_RES   218   218        Phosphothreonine. 
MOD_RES   253   253        Phosphoserine. 
MOD_RES   437   437        Phosphoserine. 
MOD_RES   438   438        Phosphoserine. 
MOD_RES   439   439        Phosphoserine. 
MOD_RES   441   441        Phosphoserine. 
MOD_RES   442   442        Phosphoserine. 
CONFLICT   75    75        E -> A (in Ref. 1; AAA35182). 
CONFLICT   100   100        R -> Q (in Ref. 1; AAA35182). 
CONFLICT   685   685        P -> S (in Ref. 1; AAA35182 and 2; AAA34413). 
STRAND   290   292  3      
HELIX   300   303  4      
STRAND   307   310  4      
STRAND   314   317  4      
STRAND   322   325  4      
STRAND   333   342  10      
STRAND   349   352  4      
STRAND   356   362  7      
STRAND   367   371  5      
TURN   372   374  3      
STRAND   377   381  5      
STRAND   445   451  7      
STRAND   455   462  8      
STRAND   467   471  5      
TURN   472   475  4      
STRAND   476   481  6      
STRAND   488   493  6      
STRAND   497   504  8      
STRAND   507   513  7      
TURN   514   517  4      
STRAND   518   524  7      
STRAND   529   534  6      
STRAND   541   546  6      
STRAND   551   555  5      
TURN   556   558  3      
STRAND   561   565  5      
STRAND   579   584  6      
STRAND   588   595  8      
STRAND   598   604  7      
STRAND   622   627  6      
STRAND   633   638  6      
HELIX   640   642  3      
STRAND   644   649  6      
STRAND   652   658  7      
TURN   659   661  3      
STRAND   664   669  6      
STRAND   675   680  6      
STRAND   691   697  7      
STRAND   700   709  10      
Sequence information
Length: 713 AA [This is the length of the unprocessed precursor] Molecular weight: 78308 Da [This is the MW of the unprocessed precursor] CRC64: 444104AAD63CB944 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTASVSNTQN KLNELLDAIR QEFLQVSQEA NTYRLQNQKD YDFKMNQQLA EMQQIRNTVY 

        70         80         90        100        110        120 
ELELTHRKMK DAYEEEIKHL KLGLEQRDHQ IASLTVQQQR QQQQQQQVQQ HLQQQQQQLA 

       130        140        150        160        170        180 
AASASVPVAQ QPPATTSATA TPAANTTTGS PSAFPVQASR PNLVGSQLPT TTLPVVSSNA 

       190        200        210        220        230        240 
QQQLPQQQLQ QQQLQQQQPP PQVSVAPLSN TAINGSPTSK ETTTLPSVKA PESTLKETEP 

       250        260        270        280        290        300 
ENNNTSKIND TGSATTATTT TATETEIKPK EEDATPASLH QDHYLVPYNQ RANHSKPIPP 

       310        320        330        340        350        360 
FLLDLDSQSV PDALKKQTND YYILYNPALP REIDVELHKS LDHTSVVCCV KFSNDGEYLA 

       370        380        390        400        410        420 
TGCNKTTQVY RVSDGSLVAR LSDDSAANNH RNSITENNTT TSTDNNTMTT TTTTTITTTA 

       430        440        450        460        470        480 
MTSAAELAKD VENLNTSSSP SSDLYIRSVC FSPDGKFLAT GAEDRLIRIW DIENRKIVMI 

       490        500        510        520        530        540 
LQGHEQDIYS LDYFPSGDKL VSGSGDRTVR IWDLRTGQCS LTLSIEDGVT TVAVSPGDGK 

       550        560        570        580        590        600 
YIAAGSLDRA VRVWDSETGF LVERLDSENE SGTGHKDSVY SVVFTRDGQS VVSGSLDRSV 

       610        620        630        640        650        660 
KLWNLQNANN KSDSKTPNSG TCEVTYIGHK DFVLSVATTQ NDEYILSGSK DRGVLFWDKK 

       670        680        690        700        710 
SGNPLLMLQG HRNSVISVAV ANGSPLGPEY NVFATGSGDC KARIWKYKKI APN 

P16649 in FASTA format

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View entry in raw text format (no links)
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