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Reviewed, UniProtKB/Swiss-Prot P16649 (TUP1_YEAST)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    General transcriptional corepressor TUP1
Alternative name(s):
    Glucose repression regulatory protein TUP1
    Flocculation suppressor protein
    Repressor AER2
Gene names
Name: TUP1
Synonyms: AAR1, AER2, AMM1, CYC9, FLK1, SFL2, UMR7
Ordered Locus Names: YCR084C
ORF Names: YCR84C
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length713 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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. Ref.1 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16

Subunit structure

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. Ref.10 Ref.11 Ref.14 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.13 Ref.17

Subcellular location

Nucleus. Ref.18

Miscellaneous

Present with 5840 molecules/cell in log phase SD medium. Ref.19

Sequence similarities

Belongs to the WD repeat TUP1 family.

Contains 7 WD repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 713713General transcriptional corepressor TUP1
PRO_0000051312

Regions

Repeat342 – 37130WD 1
Repeat441 – 47131WD 2
Repeat483 – 51331WD 3
Repeat524 – 55532WD 4
Repeat574 – 60431WD 5
Repeat628 – 65831WD 6
Repeat670 – 70637WD 7
Compositional bias97 – 11822Gln-rich
Compositional bias181 – 19818Poly-Gln
Compositional bias399 – 40911Thr-rich

Amino acid modifications

Modified residue1501Phosphoserine Ref.21
Modified residue2161Phosphoserine Ref.21
Modified residue2181Phosphothreonine Ref.21
Modified residue2531Phosphoserine Ref.21
Modified residue4371Phosphoserine Ref.21
Modified residue4381Phosphoserine Ref.21
Modified residue4391Phosphoserine Ref.21 Ref.20
Modified residue4411Phosphoserine Ref.21
Modified residue4421Phosphoserine Ref.21

Experimental info

Sequence conflict751E → A in AAA35182. Ref.1
Sequence conflict1001R → Q in AAA35182. Ref.1
Sequence conflict6851P → S in AAA35182. Ref.1
Sequence conflict6851P → S in AAA34413. Ref.2

Secondary structure

........................................................................ 713
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16649-1 [UniParc].

Last modified May 1, 1991. Version 2.
Checksum: 444104AAD63CB944

FASTA71378,308
        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 

« Hide

References

« Hide 'large scale' references
[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: 2247069] [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: 1900249] [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: 2197185] [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. expand/collapse author list , 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: 1574125] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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: 1901558] [Abstract]
Cited for: SIMILARITY TO BETA SUBUNIT OF G-PROTEINS.
[6]"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: 7995523] [Abstract]
Cited for: INTERACTION WITH MATALPHA2.
[7]"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: 8675011] [Abstract]
Cited for: INTERACTION WITH HISTONE H3 AND HISTONE H4.
[8]"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: 8943325] [Abstract]
Cited for: SUBUNIT.
[9]"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: 9741624] [Abstract]
Cited for: INTERACTION WITH RFX1.
[10]"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: 11069890] [Abstract]
Cited for: INTERACTION WITH CYC8 AND RPD3, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[11]"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: 10722672] [Abstract]
Cited for: INTERACTION WITH PGD1, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[12]"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: 11230135] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[13]"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: 11500510] [Abstract]
Cited for: INTERACTION WITH SKO1.
[14]"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: 11172717] [Abstract]
Cited for: INTERACTION WITH HDA1 AND HDA2, FUNCTION OF THE CYC8-TUP1 COMPLEX.
[15]"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: 11784848] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[16]"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: 14665463] [Abstract]
Cited for: FUNCTION OF THE CYC8-TUP1 COMPLEX.
[17]"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: 14525981] [Abstract]
Cited for: INTERACTION WITH HOS1; HOS2 AND RPD3.
[18]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[19]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, MASS SPECTROMETRY.
[21]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-216; THR-218; SER-253; SER-437; SER-438; SER-439; SER-441 AND SER-442, MASS SPECTROMETRY.
[22]"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: 10856245] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 282-713.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
PIRJN0133.
RefSeqNP_010007.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ERJX-ray2.30A/B/C282-713[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:512N.
IntActP16649. 26 interactions.

Proteomic databases

PeptideAtlasP16649.
PRIDEP16649.

Genome annotation databases

EnsemblYCR084C. Saccharomyces cerevisiae. [Contig view]
GeneID850445.
GenomeReviewsGene locus YCR084C in contig X59720_GR.
KEGGsce:YCR084C.
NMPDRfig|4932.3.peg.736.

Organism-specific databases

CYGDYCR084c.
SGDS000000680. TUP1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP16649.
OMAP16649. VTYIGHK.

Gene expression databases

ArrayExpressP16649.
GermOnlineYCR084C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013890. Transcrip_repressor_Tup1_N.
IPR015943. WD40/YVTN_repeat-like.
IPR001680. WD40_repeat.
IPR019782. WD40_repeat_2.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_region.
IPR019781. WD40_repeat_sg.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF08581. Tup_N. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
ProDomPD000018. WD40. 6 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00320. WD40. 7 hits.
[Graphical view]
PROSITEPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio966057.

Entry information

Entry nameTUP1_YEAST
AccessionPrimary (citable) accession number: P16649
Secondary accession number(s): P17995, P18323
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents