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Protein

General transcriptional corepressor TUP1

Gene

TUP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

GO - Molecular functioni

  • histone binding Source: SGD
  • histone deacetylase binding Source: SGD
  • mediator complex binding Source: SGD
  • phosphatidylinositol-3,5-bisphosphate binding Source: SGD
  • transcriptional repressor activity, RNA polymerase II transcription factor binding Source: SGD

GO - Biological processi

  • carbon catabolite repression of transcription from RNA polymerase II promoter by glucose Source: SGD
  • histone exchange Source: SGD
  • negative regulation of dipeptide transport by negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • negative regulation of mating-type specific transcription from RNA polymerase II promoter Source: SGD
  • negative regulation of transcription by RNA polymerase II Source: SGD
  • nucleosome positioning Source: SGD
  • positive regulation of transcription by RNA polymerase II Source: SGD
  • regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of invasive growth in response to glucose limitation Source: SGD
  • regulation of response to DNA damage stimulus Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionRepressor
Biological processTranscription, 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
Proteomesi

Organism-specific databases

EuPathDBiFungiDB:YCR084C
SGDiS000000680 TUP1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000513121 – 713General transcriptional corepressor TUP1Add BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei439PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16649
PaxDbiP16649
PRIDEiP16649

PTM databases

iPTMnetiP16649

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

Show more details

GO - Molecular functioni

  • histone binding Source: SGD
  • histone deacetylase binding Source: SGD

Protein-protein interaction databases

BioGridi31057, 106 interactors
DIPiDIP-512N
IntActiP16649, 27 interactors
MINTiP16649
STRINGi4932.YCR084C

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni19 – 26Combined sources8
Helixi27 – 84Combined sources58
Beta strandi290 – 292Combined sources3
Helixi300 – 303Combined sources4
Beta strandi307 – 310Combined sources4
Beta strandi314 – 317Combined sources4
Beta strandi322 – 325Combined sources4
Beta strandi333 – 339Combined sources7
Beta strandi415 – 417Combined sources3
Beta strandi424 – 427Combined sources4
Beta strandi431 – 437Combined sources7
Beta strandi442 – 446Combined sources5
Beta strandi457 – 461Combined sources5
Beta strandi489 – 493Combined sources5
Beta strandi497 – 504Combined sources8
Beta strandi509 – 513Combined sources5
Turni514 – 517Combined sources4
Beta strandi518 – 523Combined sources6
Beta strandi529 – 534Combined sources6
Beta strandi539 – 546Combined sources8
Beta strandi549 – 555Combined sources7
Turni556 – 559Combined sources4
Beta strandi561 – 566Combined sources6
Beta strandi579 – 584Combined sources6
Beta strandi590 – 595Combined sources6
Beta strandi600 – 604Combined sources5
Turni605 – 607Combined sources3
Beta strandi609 – 612Combined sources4
Beta strandi633 – 638Combined sources6
Beta strandi642 – 649Combined sources8
Beta strandi652 – 657Combined sources6
Beta strandi664 – 669Combined sources6
Beta strandi675 – 680Combined sources6
Beta strandi690 – 697Combined sources8
Beta strandi700 – 708Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16649

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati342 – 371WD 1Add BLAST30
Repeati441 – 471WD 2Add BLAST31
Repeati483 – 513WD 3Add BLAST31
Repeati524 – 555WD 4Add BLAST32
Repeati574 – 604WD 5Add BLAST31
Repeati628 – 658WD 6Add BLAST31
Repeati670 – 706WD 7Add BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi97 – 118Gln-richAdd BLAST22
Compositional biasi181 – 198Poly-GlnAdd BLAST18
Compositional biasi399 – 409Thr-richAdd BLAST11

Sequence similaritiesi

Belongs to the WD repeat TUP1 family.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00910000144205
HOGENOMiHOG000200558
InParanoidiP16649
KOiK06666
OMAiWFMNEKS
OrthoDBiEOG092C21A7

Family and domain databases

Gene3Di2.130.10.10, 2 hits
InterProiView protein in InterPro
IPR020472 G-protein_beta_WD-40_rep
IPR013890 Tscrpt_rep_Tup1_N
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PfamiView protein in Pfam
PF08581 Tup_N, 1 hit
PF00400 WD40, 7 hits
PRINTSiPR00320 GPROTEINBRPT
ProDomiView protein in ProDom or Entries sharing at least one domain
PD010558 Transcrip_repressor_Tup1_N, 1 hit
SMARTiView protein in SMART
SM00320 WD40, 7 hits
SUPFAMiSSF50978 SSF50978, 2 hits
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 4 hits
PS50082 WD_REPEATS_2, 5 hits
PS50294 WD_REPEATS_REGION, 1 hit

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti75E → A in AAA35182 (PubMed:2247069).Curated1
Sequence conflicti100R → Q in AAA35182 (PubMed:2247069).Curated1
Sequence conflicti685P → S in AAA35182 (PubMed:2247069).Curated1
Sequence conflicti685P → S in AAA34413 (PubMed:1900249).Curated1

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

EnsemblFungiiCAA42259; CAA42259; CAA42259
YCR084C; YCR084C; YCR084C
GeneIDi850445
KEGGisce:YCR084C

Similar proteinsi

Entry informationi

Entry nameiTUP1_YEAST
AccessioniPrimary (citable) accession number: P16649
Secondary accession number(s): D6VR85, P17995, P18323
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 1, 1991
Last modified: May 23, 2018
This is version 195 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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