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P17157

- PHO85_YEAST

UniProt

P17157 - PHO85_YEAST

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Protein

Cyclin-dependent protein kinase PHO85

Gene

PHO85

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

Functioni

Cyclin-dependent protein kinase (CDK) catalytic subunit that regulates multiple cell cycle and metabolic processes in response to nutrient availability. Associates with different cyclins, that control kinase activity, substrate specificity and subcellular location of the kinase. Favorable growth conditions always result in activated cyclin-CDK complexes. Regulates metabolic processes when associated with PHO80 cyclin family members (PH080, PCL6, PCL7, PCL8 and PCL10), and cell cycle and morphogenesis processes when associated with PCL1,2 cyclin family members (PCL1, PCL2, CLG1, PCL5 and PCL9). When associated with PHO80, 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 promoting its export to the cytoplasm. 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 cyclin-CDK activity to calcium signaling. Together with the cyclins PCL6/PCL7 and PCL8/PCL10, negatively controls glycogen accumulation. When associated with cyclins PCL6 and PCL7, controls glycogen phosphorylase and glycogen synthase activities. PCL6-PHO85 and PCL7-PHO85 phosphorylate and inactivate the phosphatase PP1-2 inhibitor GLC8, causing activation of PP1-2, which then dephosphorylates and activates glycogen phosphorylase. When associated with cyclins PCL8 and PCL10, has glycogen synthase kinase activity. PCL10-PHO85 phosphorylates and negatively regulates glycogen synthase GSY2. Association with PCL1 and PCL2 is required for cell cycle progression at start in the absence of the CDC28-dependent G1 cyclins CLN1 and CLN2. PCL1-PHO85 is involved in phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for its ubiquitination and degradation, releasing repression of b-type cyclins and promoting exit from mitosis. When associated with cyclins PCL1 and PCL2, positively controls degradation of sphingoid long chain base kinase LCB4 via phosphorylation of LCB4, which is required for its ubiquitination and degradation. PCL1-PHO85 also phosphorylates HMS1, NCP1 and NPA3, which may all have a role in mitotic exit. PCL2-PHO85 also phosphorylates RVS167, linking cyclin-CDK activity with organization of the actin cytoskeleton. When associated with PCL5, positively controls degradation of transcription factor GCN4 via phosphorylation of GCN4, which is required for its degradation by the E3 ubiquitin ligase complex SCF(Cdc4). When associated with PCL9, may have a role in bud site selection in G1 phase. PHO85 also phosphorylates the transcription factor SWI5.22 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inhibited by the CDK inhibitor (CKI) PHO81 in response to phosphate starvation.2 Publications

Kineticsi

  1. KM=1.5 µM for substrate protein GSY2 (when associated with cyclin PCL10)1 Publication

Vmax=11.5 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361ATPPROSITE-ProRule annotation
Active sitei133 – 1331Proton acceptorPROSITE-ProRule annotation
Sitei166 – 1661Not phosphorylated
Sitei167 – 1671Not phosphorylated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 219ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: SGD
  2. negative regulation of calcium-mediated signaling Source: SGD
  3. negative regulation of glycogen biosynthetic process Source: SGD
  4. negative regulation of macroautophagy Source: SGD
  5. negative regulation of phosphate metabolic process Source: SGD
  6. negative regulation of sequence-specific DNA binding transcription factor activity Source: SGD
  7. negative regulation of transcription from RNA polymerase II promoter Source: SGD
  8. positive regulation of macroautophagy Source: SGD
  9. protein phosphorylation Source: SGD
  10. regulation of cell cycle Source: GOC
  11. regulation of establishment or maintenance of cell polarity Source: SGD
  12. regulation of protein localization Source: SGD
  13. regulation of protein stability Source: SGD
  14. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33946-MONOMER.
BRENDAi2.7.11.22. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent protein kinase PHO85 (EC:2.7.11.22)
Alternative name(s):
Negative regulator of the PHO system
Serine/threonine-protein kinase PHO85
Gene namesi
Name:PHO85
Synonyms:SSG3
Ordered Locus Names:YPL031C
ORF Names:P7102.18A
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL031c.
SGDiS000005952. PHO85.

Subcellular locationi

GO - Cellular componenti

  1. cyclin-dependent protein kinase holoenzyme complex Source: SGD
  2. cytoplasm Source: UniProtKB-KW
  3. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181Y → F: Reduces kinase activity. Abolishes interaction to PHO80 cyclin, but not to PCL1.
Mutagenesisi36 – 361K → R: Loss of kinase activity. 1 Publication
Mutagenesisi53 – 531E → A: Loss of kinase activity. Abolishes interaction to PHO80 and PCL1 cyclins. 1 Publication
Mutagenesisi82 – 821F → G: Functional kinase, that can be rapidly inhibited by small, cell-permeable drugs like 1-Na PP1 (4-amino-1-tert-butyl-3-(1'-naphthyl)pyrazolo[3,4-d]pyrimidine). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305Cyclin-dependent protein kinase PHO85PRO_0000086521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylation of Tyr-18 seems to be important to discriminate between the different cyclin partners for binding.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP17157.
PaxDbiP17157.

Expressioni

Gene expression databases

GenevestigatoriP17157.

Interactioni

Subunit structurei

Monomer. Forms a cyclin-CDK complex with at least 10 different cyclin partners: PCL1, PCL2, PHO80, CLG1, PCL5, PCL6, PCL7, PCL8, PCL9 and PCL10. Interacts with GLC8 and RIM15.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCL1P373662EBI-13327,EBI-4385
CLG1P351903EBI-13327,EBI-4762
CLN1P204372EBI-13327,EBI-4479
PCL1P248674EBI-13327,EBI-4495
PCL10P531247EBI-13327,EBI-23973
PCL2P256938EBI-13327,EBI-4499
PCL5P387942EBI-13327,EBI-4504
PCL6P400387EBI-13327,EBI-22555
PCL7P401869EBI-13327,EBI-25021
PCL8Q089669EBI-13327,EBI-37056
PCL9Q124774EBI-13327,EBI-38090
PHO80P200524EBI-13327,EBI-13310
PHO81P174425EBI-13327,EBI-13314
SSA1P105912EBI-13327,EBI-8591

Protein-protein interaction databases

BioGridi36147. 592 interactions.
DIPiDIP-1493N.
IntActiP17157. 30 interactions.
MINTiMINT-384508.

Structurei

Secondary structure

1
305
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63
Beta strandi7 – 1610
Beta strandi19 – 268
Turni27 – 293
Beta strandi32 – 398
Turni42 – 443
Helixi48 – 558
Turni56 – 594
Beta strandi68 – 747
Beta strandi77 – 837
Beta strandi86 – 883
Helixi89 – 946
Beta strandi98 – 1003
Helixi107 – 12620
Helixi136 – 1383
Beta strandi139 – 1413
Beta strandi147 – 1493
Helixi152 – 1543
Beta strandi156 – 1605
Helixi172 – 1743
Helixi177 – 1804
Helixi189 – 20416
Helixi214 – 22512
Turni230 – 2323
Helixi234 – 2385
Beta strandi244 – 2463
Helixi254 – 2585
Helixi259 – 2613
Helixi268 – 27710
Helixi282 – 2843
Helixi288 – 2925
Helixi295 – 3006

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PK9X-ray2.91A/C1-305[»]
2PMIX-ray2.90A/C1-305[»]
4KRCX-ray2.60A1-305[»]
4KRDX-ray1.95A1-305[»]
ProteinModelPortaliP17157.
SMRiP17157. Positions 19-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 297291Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00600000083998.
HOGENOMiHOG000233024.
InParanoidiP17157.
KOiK06655.
OMAiQVPQNAY.
OrthoDBiEOG7K3TWD.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17157-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSSSQFKQL EKLGNGTYAT VYKGLNKTTG VYVALKEVKL DSEEGTPSTA
60 70 80 90 100
IREISLMKEL KHENIVRLYD VIHTENKLTL VFEFMDNDLK KYMDSRTVGN
110 120 130 140 150
TPRGLELNLV KYFQWQLLQG LAFCHENKIL HRDLKPQNLL INKRGQLKLG
160 170 180 190 200
DFGLARAFGI PVNTFSSEVV TLWYRAPDVL MGSRTYSTSI DIWSCGCILA
210 220 230 240 250
EMITGKPLFP GTNDEEQLKL IFDIMGTPNE SLWPSVTKLP KYNPNIQQRP
260 270 280 290 300
PRDLRQVLQP HTKEPLDGNL MDFLHGLLQL NPDMRLSAKQ ALHHPWFAEY

YHHAS
Length:305
Mass (Da):34,906
Last modified:November 1, 1997 - v2
Checksum:i246A4358870B00EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991G → A in CAA68773. (PubMed:3320965)Curated
Sequence conflicti99 – 991G → A in CAA68774. (PubMed:3320965)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00867 Genomic DNA. Translation: CAA68773.1.
Y00867 Genomic DNA. Translation: CAA68774.1. Sequence problems.
U44030 Genomic DNA. Translation: AAB68188.1.
BK006949 Genomic DNA. Translation: DAA11398.1.
PIRiS62043. OKBY85.
RefSeqiNP_015294.1. NM_001183845.1.

Genome annotation databases

EnsemblFungiiYPL031C; YPL031C; YPL031C.
GeneIDi856076.
KEGGisce:YPL031C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00867 Genomic DNA. Translation: CAA68773.1 .
Y00867 Genomic DNA. Translation: CAA68774.1 . Sequence problems.
U44030 Genomic DNA. Translation: AAB68188.1 .
BK006949 Genomic DNA. Translation: DAA11398.1 .
PIRi S62043. OKBY85.
RefSeqi NP_015294.1. NM_001183845.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PK9 X-ray 2.91 A/C 1-305 [» ]
2PMI X-ray 2.90 A/C 1-305 [» ]
4KRC X-ray 2.60 A 1-305 [» ]
4KRD X-ray 1.95 A 1-305 [» ]
ProteinModelPortali P17157.
SMRi P17157. Positions 19-302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36147. 592 interactions.
DIPi DIP-1493N.
IntActi P17157. 30 interactions.
MINTi MINT-384508.

Chemistry

BindingDBi P17157.
ChEMBLi CHEMBL2111410.

Proteomic databases

MaxQBi P17157.
PaxDbi P17157.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL031C ; YPL031C ; YPL031C .
GeneIDi 856076.
KEGGi sce:YPL031C.

Organism-specific databases

CYGDi YPL031c.
SGDi S000005952. PHO85.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00600000083998.
HOGENOMi HOG000233024.
InParanoidi P17157.
KOi K06655.
OMAi QVPQNAY.
OrthoDBi EOG7K3TWD.

Enzyme and pathway databases

BioCyci YEAST:G3O-33946-MONOMER.
BRENDAi 2.7.11.22. 984.

Miscellaneous databases

EvolutionaryTracei P17157.
NextBioi 981077.
PROi P17157.

Gene expression databases

Genevestigatori P17157.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Negative regulators of the PHO system in Saccharomyces cerevisiae: isolation and structural characterization of PHO85."
    Uesono Y., Tanaka K., Toh-e A.
    Nucleic Acids Res. 15:10299-10309(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 64665 / S288c / DC5.
  2. "PHO85, a negative regulator of the PHO system, is a homolog of the protein kinase gene, CDC28, of Saccharomyces cerevisiae."
    Toh-e A., Tanaka K., Uesono Y., Wickner R.B.
    Mol. Gen. Genet. 214:162-164(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 1-6, FUNCTION.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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 IN PHOSPHORYLATION OF PHO4, INTERACTION WITH PHO80.
  6. "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.
  7. "Cell cycle control by a complex of the cyclin HCS26 (PCL1) and the kinase PHO85."
    Espinoza F.H., Ogas J., Herskowitz I., Morgan D.O.
    Science 266:1388-1391(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCL1.
  8. "The PCL2 (ORFD)-PHO85 cyclin-dependent kinase complex: a cell cycle regulator in yeast."
    Measday V., Moore L., Ogas J., Tyers M., Andrews B.J.
    Science 266:1391-1395(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCL2.
  9. "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 IN PHOSPHORYLATION OF PHO4.
  10. "A family of cyclin-like proteins that interact with the Pho85 cyclin-dependent kinase."
    Measday V., Moore L., Retnakaran R., Lee J., Donoviel M., Neiman A.M., Andrews B.J.
    Mol. Cell. Biol. 17:1212-1223(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLG1; PCL1; PCL2; PCL5; PCL6; PCL7; PCL8; PCL9 AND PCL10.
  11. "Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton."
    Lee J., Colwill K., Aneliunas V., Tennyson C.N., Moore L., Ho Y., Andrews B.J.
    Curr. Biol. 8:1310-1321(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RVS167.
  12. "Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk including Pho85 kinase is required for its prompt degradation."
    Nishizawa M., Kawasumi M., Fujino M., Toh-e A.
    Mol. Biol. Cell 9:2393-2405(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SIC1.
  13. "Cyclin partners determine Pho85 protein kinase substrate specificity in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10."
    Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J., Andrews B.J.
    Mol. Cell. Biol. 18:3289-3299(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GSY2.
  14. "A role for the Pcl9-Pho85 cyclin-cdk complex at the M/G1 boundary in Saccharomyces cerevisiae."
    Tennyson C.N., Lee J., Andrews B.J.
    Mol. Microbiol. 28:69-79(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCL9.
  15. "The Pho85 kinase, a member of the yeast cyclin-dependent kinase (Cdk) family, has a regulation mechanism different from Cdks functioning throughout the cell cycle."
    Nishizawa M., Suzuki K., Fujino M., Oguchi T., Toh-e A.
    Genes Cells 4:627-642(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PHOSPHORYLATION AT TYR-18, MUTAGENESIS OF GLU-53.
  16. "Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the cyclin Pcl10p."
    Wilson W.A., Mahrenholz A.M., Roach P.J.
    Mol. Cell. Biol. 19:7020-7030(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PCL10, BIOPHYSICOCHEMICAL PROPERTIES, LACK OF PHOSPHORYLATION.
  17. "Interactions between Pho85 cyclin-dependent kinase complexes and the Swi5 transcription factor in budding yeast."
    Measday V., McBride H., Moffat J., Stillman D., Andrews B.J.
    Mol. Microbiol. 35:825-834(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SWI5.
  18. Cited for: ENZYME REGULATION, INTERACTION WITH PCL6 AND PCL7.
  19. "The yeast cyclins Pcl6p and Pcl7p are involved in the control of glycogen storage by the cyclin-dependent protein kinase Pho85p."
    Wang Z., Wilson W.A., Fujino M.A., Roach P.J.
    FEBS Lett. 506:277-280(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Chemical inhibition of the Pho85 cyclin-dependent kinase reveals a role in the environmental stress response."
    Carroll A.S., Bishop A.C., DeRisi J.L., Shokat K.M., O'Shea E.K.
    Proc. Natl. Acad. Sci. U.S.A. 98:12578-12583(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-82.
  21. "Phosphorylation of YLR190w by PAP1 PHO85 kinase complex."
    Shi X.Z., Ao S.Z.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:187-192(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MMR1.
  22. "Analysis of phosphorylation of YJL084c, a yeast protein."
    Shi X.Z., Ao S.Z.
    Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:433-438(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF YJL084C.
  23. "Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5."
    Shemer R., Meimoun A., Holtzman T., Kornitzer D.
    Mol. Cell. Biol. 22:5395-5404(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GCN4.
  24. "Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in vivo."
    Tan Y.S.H., Morcos P.A., Cannon J.F.
    J. Biol. Chem. 278:147-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GLC8, INTERACTION WITH GLC8.
  25. "Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation."
    Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J.
    Mol. Biol. Cell 14:3027-3040(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RVS167.
  26. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  27. "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: FUNCTION IN PHOSPHORYLATION OF PHO80 AND PHO81, MUTAGENESIS OF LYS-36.
  28. "The identification of Pcl1-interacting proteins that genetically interact with Cla4 may indicate a link between G1 progression and mitotic exit."
    Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.
    Genetics 166:1177-1186(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HMS1; NCP1 AND NPA3.
  29. "Regulation of yeast glycogen phosphorylase by the cyclin-dependent protein kinase Pho85p."
    Wilson W.A., Wang Z., Roach P.J.
    Biochem. Biophys. Res. Commun. 329:161-167(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "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 IN PHOSPHORYLATION OF RIM15, INTERACTION WITH RIM15.
  31. "Phosphorylation by Pho85 cyclin-dependent kinase acts as a signal for the down-regulation of the yeast sphingoid long-chain base kinase Lcb4 during the stationary phase."
    Iwaki S., Kihara A., Sano T., Igarashi Y.
    J. Biol. Chem. 280:6520-6527(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LCB4.
  32. Cited for: FUNCTION IN PHOSPHORYLATION OF CRZ1.
  33. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPHO85_YEAST
AccessioniPrimary (citable) accession number: P17157
Secondary accession number(s): D6W3Y2, Q03089, Q06888
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 151 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 6160 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3