Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16649

- TUP1_YEAST

UniProt

P16649 - TUP1_YEAST

(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)

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

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. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: SGD
  6. 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 Source: SGD
  5. negative regulation of transcription from RNA polymerase II promoter by glucose Source: SGD
  6. negative regulation of transcription from RNA polymerase II promoter during mitosis Source: SGD
  7. nucleosome positioning Source: SGD
  8. regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter Source: SGD
  9. regulation of response to DNA damage stimulus Source: SGD
Complete GO annotation...

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
Complete GO annotation...

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. 94 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 – 268Combined sources
Helixi27 – 8458Combined sources
Beta strandi290 – 2923Combined sources
Helixi300 – 3034Combined sources
Beta strandi307 – 3104Combined sources
Beta strandi314 – 3174Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi333 – 34210Combined sources
Beta strandi349 – 3524Combined sources
Beta strandi356 – 3627Combined sources
Beta strandi367 – 3715Combined sources
Turni372 – 3743Combined sources
Beta strandi377 – 3815Combined sources
Beta strandi445 – 4517Combined sources
Beta strandi455 – 4628Combined sources
Beta strandi467 – 4715Combined sources
Turni472 – 4754Combined sources
Beta strandi476 – 4816Combined sources
Beta strandi488 – 4936Combined sources
Beta strandi497 – 5048Combined sources
Beta strandi507 – 5137Combined sources
Turni514 – 5174Combined sources
Beta strandi518 – 5247Combined sources
Beta strandi529 – 5346Combined sources
Beta strandi541 – 5466Combined sources
Beta strandi551 – 5555Combined sources
Turni556 – 5583Combined sources
Beta strandi561 – 5655Combined sources
Beta strandi579 – 5846Combined sources
Beta strandi588 – 5958Combined sources
Beta strandi598 – 6047Combined sources
Beta strandi622 – 6276Combined sources
Beta strandi633 – 6386Combined sources
Helixi640 – 6423Combined sources
Beta strandi644 – 6496Combined sources
Beta strandi652 – 6587Combined sources
Turni659 – 6613Combined sources
Beta strandi664 – 6696Combined sources
Beta strandi675 – 6806Combined sources
Beta strandi691 – 6977Combined sources
Beta strandi700 – 70910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119348.
HOGENOMiHOG000200558.
InParanoidiP16649.
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

        10         20         30         40         50
MTASVSNTQN KLNELLDAIR QEFLQVSQEA NTYRLQNQKD YDFKMNQQLA
60 70 80 90 100
EMQQIRNTVY ELELTHRKMK DAYEEEIKHL KLGLEQRDHQ IASLTVQQQR
110 120 130 140 150
QQQQQQQVQQ HLQQQQQQLA AASASVPVAQ QPPATTSATA TPAANTTTGS
160 170 180 190 200
PSAFPVQASR PNLVGSQLPT TTLPVVSSNA QQQLPQQQLQ QQQLQQQQPP
210 220 230 240 250
PQVSVAPLSN TAINGSPTSK ETTTLPSVKA PESTLKETEP ENNNTSKIND
260 270 280 290 300
TGSATTATTT TATETEIKPK EEDATPASLH QDHYLVPYNQ RANHSKPIPP
310 320 330 340 350
FLLDLDSQSV PDALKKQTND YYILYNPALP REIDVELHKS LDHTSVVCCV
360 370 380 390 400
KFSNDGEYLA TGCNKTTQVY RVSDGSLVAR LSDDSAANNH RNSITENNTT
410 420 430 440 450
TSTDNNTMTT TTTTTITTTA MTSAAELAKD VENLNTSSSP SSDLYIRSVC
460 470 480 490 500
FSPDGKFLAT GAEDRLIRIW DIENRKIVMI LQGHEQDIYS LDYFPSGDKL
510 520 530 540 550
VSGSGDRTVR IWDLRTGQCS LTLSIEDGVT TVAVSPGDGK YIAAGSLDRA
560 570 580 590 600
VRVWDSETGF LVERLDSENE SGTGHKDSVY SVVFTRDGQS VVSGSLDRSV
610 620 630 640 650
KLWNLQNANN KSDSKTPNSG TCEVTYIGHK DFVLSVATTQ NDEYILSGSK
660 670 680 690 700
DRGVLFWDKK SGNPLLMLQG HRNSVISVAV ANGSPLGPEY NVFATGSGDC
710
KARIWKYKKI APN
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 94 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 ENSGT00760000119348.
HOGENOMi HOG000200558.
InParanoidi P16649.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 161 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