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P17157 (PHO85_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PHO85
Synonyms:SSG3
Ordered Locus Names:YPL031C
ORF Names:P7102.18A
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.5 Ref.7 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Inhibited by the CDK inhibitor (CKI) PHO81 in response to phosphate starvation. Ref.6 Ref.18

Subunit structure

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. Ref.5 Ref.7 Ref.8 Ref.10 Ref.14 Ref.16 Ref.18 Ref.24 Ref.30

Subcellular location

Cytoplasm. Nucleus.

Post-translational modification

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

Miscellaneous

Present with 6160 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Biophysicochemical properties

Kinetic parameters:

KM=1.5 µM for substrate protein GSY2 (when associated with cyclin PCL10) Ref.16

Vmax=11.5 µmol/min/mg enzyme

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 16964260. Source: SGD

negative regulation of calcium-mediated signaling

Inferred from genetic interaction Ref.32. Source: SGD

negative regulation of glycogen biosynthetic process

Inferred from mutant phenotype Ref.13. Source: SGD

negative regulation of macroautophagy

Inferred from mutant phenotype PubMed 20417603. Source: SGD

negative regulation of phosphate metabolic process

Inferred from genetic interaction PubMed 3915785. Source: SGD

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype Ref.32. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 3915785. Source: SGD

positive regulation of macroautophagy

Inferred from mutant phenotype PubMed 20417603. Source: SGD

protein phosphorylation

Inferred from direct assay PubMed 19823668Ref.8Ref.5. Source: SGD

regulation of establishment or maintenance of cell polarity

Inferred from genetic interaction PubMed 17853895. Source: SGD

regulation of protein localization

Inferred from direct assay Ref.9. Source: SGD

regulation of protein stability

Inferred from mutant phenotype PubMed 16508019. Source: SGD

regulation of transcription involved in G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 19823668. Source: SGD

   Cellular_componentcyclin-dependent protein kinase holoenzyme complex

Inferred from physical interaction PubMed 16611745Ref.7Ref.8Ref.5Ref.13. Source: SGD

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 9853758. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.24PubMed 19823668Ref.7Ref.8Ref.5Ref.13. Source: SGD

protein binding

Inferred from physical interaction PubMed 10688190PubMed 11283351PubMed 16429126PubMed 18719252PubMed 20489023PubMed 23217712Ref.8Ref.10. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Cyclin-dependent protein kinase PHO85
PRO_0000086521

Regions

Domain7 – 297291Protein kinase
Nucleotide binding13 – 219ATP By similarity

Sites

Active site1331Proton acceptor By similarity
Binding site361ATP By similarity
Site1661Not phosphorylated
Site1671Not phosphorylated

Amino acid modifications

Modified residue181Phosphotyrosine Ref.15

Experimental info

Mutagenesis181Y → F: Reduces kinase activity. Abolishes interaction to PHO80 cyclin, but not to PCL1.
Mutagenesis361K → R: Loss of kinase activity. Ref.27
Mutagenesis531E → A: Loss of kinase activity. Abolishes interaction to PHO80 and PCL1 cyclins. Ref.15
Mutagenesis821F → 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). Ref.20
Sequence conflict991G → A in CAA68773. Ref.1
Sequence conflict991G → A in CAA68774. Ref.1

Secondary structure

........................................................... 305
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17157 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 246A4358870B00EC

FASTA30534,906
        10         20         30         40         50         60 
MSSSSQFKQL EKLGNGTYAT VYKGLNKTTG VYVALKEVKL DSEEGTPSTA IREISLMKEL 

        70         80         90        100        110        120 
KHENIVRLYD VIHTENKLTL VFEFMDNDLK KYMDSRTVGN TPRGLELNLV KYFQWQLLQG 

       130        140        150        160        170        180 
LAFCHENKIL HRDLKPQNLL INKRGQLKLG DFGLARAFGI PVNTFSSEVV TLWYRAPDVL 

       190        200        210        220        230        240 
MGSRTYSTSI DIWSCGCILA EMITGKPLFP GTNDEEQLKL IFDIMGTPNE SLWPSVTKLP 

       250        260        270        280        290        300 
KYNPNIQQRP PRDLRQVLQP HTKEPLDGNL MDFLHGLLQL NPDMRLSAKQ ALHHPWFAEY 


YHHAS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Regulation of the Pcl7-Pho85 cyclin-cdk complex by Pho81."
Lee M., O'Regan S., Moreau J.-L., Johnson A.L., Johnston L.H., Goding C.R.
Mol. Microbiol. 38:411-422(2000) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"Mapping pathways and phenotypes by systematic gene overexpression."
Sopko R., Huang D., Preston N., Chua G., Papp B., Kafadar K., Snyder M., Oliver S.G., Cyert M., Hughes T.R., Boone C., Andrews B.J.
Mol. Cell 21:319-330(2006) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIROKBY85. S62043.
RefSeqNP_015294.1. NM_001183845.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PK9X-ray2.91A/C1-305[»]
2PMIX-ray2.90A/C1-305[»]
4KRCX-ray2.60A1-305[»]
4KRDX-ray1.95A1-305[»]
ProteinModelPortalP17157.
SMRP17157. Positions 19-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36147. 590 interactions.
DIPDIP-1493N.
IntActP17157. 30 interactions.
MINTMINT-384508.

Chemistry

BindingDBP17157.
ChEMBLCHEMBL5589.

Proteomic databases

MaxQBP17157.
PaxDbP17157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL031C; YPL031C; YPL031C.
GeneID856076.
KEGGsce:YPL031C.

Organism-specific databases

CYGDYPL031c.
SGDS000005952. PHO85.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00600000083998.
HOGENOMHOG000233024.
KOK06655.
OMAQVPQNAY.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BioCycYEAST:G3O-33946-MONOMER.
BRENDA2.7.11.22. 984.

Gene expression databases

GenevestigatorP17157.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17157.
NextBio981077.
PROP17157.

Entry information

Entry namePHO85_YEAST
AccessionPrimary (citable) accession number: P17157
Secondary accession number(s): D6W3Y2, Q03089, Q06888
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references