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Protein

PHO85 cyclin PHO80

Gene

PHO80

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Negatively regulates the expression of phosphate-starvation-responsive genes under phosphate-rich conditions. The PHO80-PHO85 cyclin-CDK holoenzyme phosphorylates and inactivates the transcription factor PHO4, by preventing its association with the transcription factor PHO2 and the nuclear import receptor PSE1, and by promoting association with the nuclear export receptor MSN5, excluding PHO4 from the nucleus. PHO80-PHO85 phosphorylates and inactivates protein kinase RIM15 by retaining it in the cytoplasm, antagonizing RIM15-induced entry into stationary phase. PHO80-PHO85 also phosphorylates and inactivates the calcineurin-responsive transcription factor CRZ1, linking PHO85 to calcium signaling.6 Publications

Enzyme regulationi

Inhibited by the CDK inhibitor (CKI) PHO81 in response to phosphate starvation.1 Publication

GO - Molecular functioni

  • cyclin-dependent protein serine/threonine kinase regulator activity Source: SGD

GO - Biological processi

  • cellular metal ion homeostasis Source: SGD
  • negative regulation of calcium-mediated signaling Source: SGD
  • negative regulation of macroautophagy Source: SGD
  • negative regulation of phosphate metabolic process Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • regulation of cyclin-dependent protein serine/threonine kinase activity Source: SGD
  • regulation of protein localization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Enzyme and pathway databases

BioCyciYEAST:G3O-33418-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
PHO85 cyclin PHO80
Alternative name(s):
Aminoglycoside antibiotic sensitivity protein 3
Phosphate system cyclin PHO80
Gene namesi
Name:PHO80
Synonyms:AGS3, TUP7, VAC5
Ordered Locus Names:YOL001W
ORF Names:O2505, UNB293
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL001W.
SGDiS000005361. PHO80.

Subcellular locationi

GO - Cellular componenti

  • cyclin-dependent protein kinase holoenzyme complex Source: SGD
  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: SGD
  • Pho85-Pho80 CDK-cyclin complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi163 – 1631L → S: Temperature-sensitive allele. 1 Publication
Mutagenesisi229 – 2291G → D in PHO80-1. 1 Publication

Chemistry

ChEMBLiCHEMBL2111355.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293PHO85 cyclin PHO80PRO_0000080502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei234 – 2341Phosphoserine; by PHO851 Publication
Modified residuei267 – 2671Phosphoserine; by PHO851 Publication

Post-translational modificationi

Phosphorylation of Ser-267 by PHO85 is required to form an active cyclin-kinase complex and for function.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20052.

PTM databases

iPTMnetiP20052.

Interactioni

Subunit structurei

Forms a cyclin-CDK complex with PHO85. PHO80-PHO85 forms a stable complex with its inhibitor PHO81 under both high- and low-phosphate conditions, but PHO81 only inhibits the kinase upon phosphate starvation. Interacts with transcription factor PHO4.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PHO85P171574EBI-13310,EBI-13327

Protein-protein interaction databases

BioGridi34403. 288 interactions.
DIPiDIP-2479N.
IntActiP20052. 8 interactions.
MINTiMINT-2786576.

Chemistry

BindingDBiP20052.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 223Combined sources
Helixi27 – 293Combined sources
Helixi32 – 5120Combined sources
Helixi77 – 8610Combined sources
Turni87 – 893Combined sources
Helixi92 – 10817Combined sources
Turni116 – 1183Combined sources
Helixi119 – 13416Combined sources
Helixi141 – 1488Combined sources
Helixi152 – 16413Combined sources
Turni165 – 1684Combined sources
Helixi176 – 1838Combined sources
Helixi210 – 2134Combined sources
Helixi216 – 22712Combined sources
Helixi235 – 2373Combined sources
Beta strandi242 – 2443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PK9X-ray2.91B/D1-293[»]
2PMIX-ray2.90B/D1-293[»]
ProteinModelPortaliP20052.
SMRiP20052. Positions 17-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20052.

Family & Domainsi

Sequence similaritiesi

Belongs to the cyclin family. PHO80 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00530000066532.
HOGENOMiHOG000000777.
InParanoidiP20052.
KOiK06654.
OMAiSSLEHCV.
OrthoDBiEOG7SFJ7H.

Family and domain databases

InterProiIPR013922. Cyclin_PHO80-like.
[Graphical view]
PfamiPF08613. Cyclin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20052-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESTSGERSE NIHEDQGIPK VILPADFNKC SRTDLVVLIS RMLVSLIAIN
60 70 80 90 100
ENSATKKSDD QITLTRYHSK IPPNISIFNY FIRLTKFSSL EHCVLMTSLY
110 120 130 140 150
YIDLLQTVYP DFTLNSLTAH RFLLTATTVA TKGLCDSFST NAHYAKVGGV
160 170 180 190 200
RCHELNILEN DFLKRVNYRI IPRDHNITLC SIEQKQKKFV IDKNALGSLD
210 220 230 240 250
LDSYSYVNRP KSGYNVLDKY YRRIVQLVGS FNASPDKSRK VDYVLPPNID
260 270 280 290
IVSESGSQTT QLKGSSSPNS HSSQKRYSEA KDAHIYNKRS KPD
Length:293
Mass (Da):33,227
Last modified:July 5, 2005 - v3
Checksum:i72918CAF845AE74C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651T → S in CAA30347 (PubMed:3283704).Curated
Sequence conflicti247 – 2471P → S in AAA34869 (PubMed:2269431).Curated
Sequence conflicti247 – 2471P → S in AAA34870 (PubMed:2269431).Curated
Sequence conflicti254 – 2541E → K in AAA34869 (PubMed:2269431).Curated
Sequence conflicti254 – 2541E → K in AAA34870 (PubMed:2269431).Curated
Sequence conflicti292 – 2921P → A in CAA30347 (PubMed:3283704).Curated
Sequence conflicti292 – 2921P → A no nucleotide entry (PubMed:3333302).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07464 Genomic DNA. Translation: CAA30347.1.
U43491 Genomic DNA. Translation: AAC49479.1.
Z74743 Genomic DNA. Translation: CAA99000.1.
Y00382 Genomic DNA. Translation: CAA68454.1.
M60624 Genomic DNA. Translation: AAA34869.1.
M60625 Genomic DNA. Translation: AAA34870.1.
BK006948 Genomic DNA. Translation: DAA10782.1.
PIRiS61983.
RefSeqiNP_014642.1. NM_001183255.1.

Genome annotation databases

EnsemblFungiiYOL001W; YOL001W; YOL001W.
GeneIDi854161.
KEGGisce:YOL001W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07464 Genomic DNA. Translation: CAA30347.1.
U43491 Genomic DNA. Translation: AAC49479.1.
Z74743 Genomic DNA. Translation: CAA99000.1.
Y00382 Genomic DNA. Translation: CAA68454.1.
M60624 Genomic DNA. Translation: AAA34869.1.
M60625 Genomic DNA. Translation: AAA34870.1.
BK006948 Genomic DNA. Translation: DAA10782.1.
PIRiS61983.
RefSeqiNP_014642.1. NM_001183255.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PK9X-ray2.91B/D1-293[»]
2PMIX-ray2.90B/D1-293[»]
ProteinModelPortaliP20052.
SMRiP20052. Positions 17-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34403. 288 interactions.
DIPiDIP-2479N.
IntActiP20052. 8 interactions.
MINTiMINT-2786576.

Chemistry

BindingDBiP20052.
ChEMBLiCHEMBL2111355.

PTM databases

iPTMnetiP20052.

Proteomic databases

MaxQBiP20052.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL001W; YOL001W; YOL001W.
GeneIDi854161.
KEGGisce:YOL001W.

Organism-specific databases

EuPathDBiFungiDB:YOL001W.
SGDiS000005361. PHO80.

Phylogenomic databases

GeneTreeiENSGT00530000066532.
HOGENOMiHOG000000777.
InParanoidiP20052.
KOiK06654.
OMAiSSLEHCV.
OrthoDBiEOG7SFJ7H.

Enzyme and pathway databases

BioCyciYEAST:G3O-33418-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP20052.
NextBioi975935.
PROiP20052.

Family and domain databases

InterProiIPR013922. Cyclin_PHO80-like.
[Graphical view]
PfamiPF08613. Cyclin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the PHO80 gene of Saccharomyces cerevisiae."
    Madden S.L., Creasy C.L., Srinivas V., Fawcett W., Bergman L.W.
    Nucleic Acids Res. 16:2625-2637(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LEU-163.
  2. "Cloning and sequencing of the PHO80 gene and CEN15 of Saccharomyces cerevisiae."
    Toh-e A., Shimauchi T.
    Yeast 2:129-139(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The sequence of a 30 kb fragment on the left arm of chromosome XV from Saccharomyces cerevisiae reveals 15 open reading frames, five of which correspond to previously identified genes."
    Sterky F., Holmberg A., Pettersson B., Uhlen M.
    Yeast 12:1091-1095(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [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. "Sequence of the region 5' to the negative regulatory gene PHO80 of Saccharomyces cerevisiae."
    Gilliquet V., Legrain M., Hilger F.
    Nucleic Acids Res. 15:5893-5893(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    Strain: S288c / GRF88.
  7. "Negative regulatory elements of the Saccharomyces cerevisiae PHO system: interaction between PHO80 and PHO85 proteins."
    Gilliquet V., Legrain M., Berben G.H.F., Hilger F.
    Gene 96:181-188(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-293, MUTAGENESIS OF GLY-229.
  8. "The activation domain of a basic helix-loop-helix protein is masked by repressor interaction with domains distinct from that required for transcription regulation."
    Jayaraman P.-S., Hirst K., Goding C.R.
    EMBO J. 13:2192-2199(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHO4.
  9. "The transcription factor, the Cdk, its cyclin and their regulator: directing the transcriptional response to a nutritional signal."
    Hirst K., Fisher F., McAndrew P.C., Goding C.R.
    EMBO J. 13:5410-5420(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHO4 AND PHO81.
  10. "Phosphorylation of the transcription factor PHO4 by a cyclin-CDK complex, PHO80-PHO85."
    Kaffman A., Herskowitz I., Tjian R., O'Shea E.K.
    Science 263:1153-1156(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHO85, PHOSPHORYLATION OF PHO4.
  11. "Phosphate-regulated inactivation of the kinase PHO80-PHO85 by the CDK inhibitor PHO81."
    Schneider K.R., Smith R.L., O'Shea E.K.
    Science 266:122-126(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH PHO81.
  12. "Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK complex."
    O'Neill E.M., Kaffman A., Jolly E.R., O'Shea E.K.
    Science 271:209-212(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF PHO4.
  13. "Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121."
    Kaffman A., Rank N.M., O'Shea E.K.
    Genes Dev. 12:2673-2683(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus."
    Kaffman A., Rank N.M., O'Neill E.M., Huang L.S., O'Shea E.K.
    Nature 396:482-486(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "The yeast Pho80-Pho85 cyclin-CDK complex has multiple substrates."
    Waters N.C., Knight J.P., Creasy C.L., Bergman L.W.
    Curr. Genet. 46:1-9(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-234 AND SER-267, PHOSPHORYLATION OF PHO4 AND PHO81.
  16. "Regulation of G0 entry by the Pho80-Pho85 cyclin-CDK complex."
    Wanke V., Pedruzzi I., Cameroni E., Dubouloz F., De Virgilio C.
    EMBO J. 24:4271-4278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION OF RIM15.
  17. Cited for: PHOSPHORYLATION OF CRZ1.

Entry informationi

Entry nameiPHO80_YEAST
AccessioniPrimary (citable) accession number: P20052
Secondary accession number(s): D6W266, Q06882, Q06883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 5, 2005
Last modified: May 11, 2016
This is version 129 of the entry and version 3 of the sequence. [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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.