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P17157

- PHO85_YEAST

UniProt

P17157 - PHO85_YEAST

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
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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
    3. protein binding Source: IntAct

    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

    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-SubCell
    3. nucleus Source: SGD

    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. 590 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.
    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_dom.
    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

    MSSSSQFKQL EKLGNGTYAT VYKGLNKTTG VYVALKEVKL DSEEGTPSTA    50
    IREISLMKEL KHENIVRLYD VIHTENKLTL VFEFMDNDLK KYMDSRTVGN 100
    TPRGLELNLV KYFQWQLLQG LAFCHENKIL HRDLKPQNLL INKRGQLKLG 150
    DFGLARAFGI PVNTFSSEVV TLWYRAPDVL MGSRTYSTSI DIWSCGCILA 200
    EMITGKPLFP GTNDEEQLKL IFDIMGTPNE SLWPSVTKLP KYNPNIQQRP 250
    PRDLRQVLQP HTKEPLDGNL MDFLHGLLQL NPDMRLSAKQ ALHHPWFAEY 300
    YHHAS 305
    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. 590 interactions.
    DIPi DIP-1493N.
    IntActi P17157. 30 interactions.
    MINTi MINT-384508.

    Chemistry

    BindingDBi P17157.
    ChEMBLi CHEMBL5589.

    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.
    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_dom.
    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

    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 1, 2014
    This is version 150 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