Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cyclin-dependent protein kinase PHO85 (EC 2.7.11.22) (Negative regulator of the PHO system) (Serine/threonine-protein kinase PHO85)

 PHO85_YEAST             Reviewed;         305 AA.
P17157; D6W3Y2; Q03089; Q06888;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 179.
RecName: Full=Cyclin-dependent protein kinase PHO85;
EC=2.7.11.22;
AltName: Full=Negative regulator of the PHO system;
AltName: Full=Serine/threonine-protein kinase PHO85;
Name=PHO85; Synonyms=SSG3; OrderedLocusNames=YPL031C;
ORFNames=P7102.18A;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 64665 / S288c / DC5;
PubMed=3320965; DOI=10.1093/nar/15.24.10299;
Uesono Y., Tanaka K., Toh-e A.;
"Negative regulators of the PHO system in Saccharomyces cerevisiae:
isolation and structural characterization of PHO85.";
Nucleic Acids Res. 15:10299-10309(1987).
[2]
SEQUENCE REVISION TO 1-6, AND FUNCTION.
PubMed=3067079; DOI=10.1007/BF00340196;
Toh-e A., Tanaka K., Uesono Y., Wickner R.B.;
"PHO85, a negative regulator of the PHO system, is a homolog of the
protein kinase gene, CDC28, of Saccharomyces cerevisiae.";
Mol. Gen. Genet. 214:162-164(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION IN PHOSPHORYLATION OF PHO4, AND INTERACTION WITH PHO80.
PubMed=8108735; DOI=10.1126/science.8108735;
Kaffman A., Herskowitz I., Tjian R., O'Shea E.K.;
"Phosphorylation of the transcription factor PHO4 by a cyclin-CDK
complex, PHO80-PHO85.";
Science 263:1153-1156(1994).
[6]
ENZYME REGULATION.
PubMed=7939631; DOI=10.1126/science.7939631;
Schneider K.R., Smith R.L., O'Shea E.K.;
"Phosphate-regulated inactivation of the kinase PHO80-PHO85 by the CDK
inhibitor PHO81.";
Science 266:122-126(1994).
[7]
FUNCTION, AND INTERACTION WITH PCL1.
PubMed=7973730; DOI=10.1126/science.7973730;
Espinoza F.H., Ogas J., Herskowitz I., Morgan D.O.;
"Cell cycle control by a complex of the cyclin HCS26 (PCL1) and the
kinase PHO85.";
Science 266:1388-1391(1994).
[8]
INTERACTION WITH PCL2.
PubMed=7973731; DOI=10.1126/science.7973731;
Measday V., Moore L., Ogas J., Tyers M., Andrews B.J.;
"The PCL2 (ORFD)-PHO85 cyclin-dependent kinase complex: a cell cycle
regulator in yeast.";
Science 266:1391-1395(1994).
[9]
FUNCTION IN PHOSPHORYLATION OF PHO4.
PubMed=8539622; DOI=10.1126/science.271.5246.209;
O'Neill E.M., Kaffman A., Jolly E.R., O'Shea E.K.;
"Regulation of PHO4 nuclear localization by the PHO80-PHO85 cyclin-CDK
complex.";
Science 271:209-212(1996).
[10]
INTERACTION WITH CLG1; PCL1; PCL2; PCL5; PCL6; PCL7; PCL8; PCL9 AND
PCL10.
PubMed=9032248; DOI=10.1128/MCB.17.3.1212;
Measday V., Moore L., Retnakaran R., Lee J., Donoviel M., Neiman A.M.,
Andrews B.J.;
"A family of cyclin-like proteins that interact with the Pho85 cyclin-
dependent kinase.";
Mol. Cell. Biol. 17:1212-1223(1997).
[11]
FUNCTION IN PHOSPHORYLATION OF RVS167.
PubMed=9843683; DOI=10.1016/S0960-9822(07)00561-1;
Lee J., Colwill K., Aneliunas V., Tennyson C.N., Moore L., Ho Y.,
Andrews B.J.;
"Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase
complexes may link the cell cycle to the actin cytoskeleton.";
Curr. Biol. 8:1310-1321(1998).
[12]
FUNCTION IN PHOSPHORYLATION OF SIC1.
PubMed=9725902; DOI=10.1091/mbc.9.9.2393;
Nishizawa M., Kawasumi M., Fujino M., Toh-e A.;
"Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor,
by Cdk including Pho85 kinase is required for its prompt
degradation.";
Mol. Biol. Cell 9:2393-2405(1998).
[13]
FUNCTION IN PHOSPHORYLATION OF GSY2.
PubMed=9584169; DOI=10.1128/MCB.18.6.3289;
Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J.,
Andrews B.J.;
"Cyclin partners determine Pho85 protein kinase substrate specificity
in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and
Pcl10.";
Mol. Cell. Biol. 18:3289-3299(1998).
[14]
FUNCTION, AND INTERACTION WITH PCL9.
PubMed=9593297; DOI=10.1046/j.1365-2958.1998.00773.x;
Tennyson C.N., Lee J., Andrews B.J.;
"A role for the Pcl9-Pho85 cyclin-cdk complex at the M/G1 boundary in
Saccharomyces cerevisiae.";
Mol. Microbiol. 28:69-79(1998).
[15]
CHARACTERIZATION, PHOSPHORYLATION AT TYR-18, AND MUTAGENESIS OF
GLU-53.
PubMed=10620010; DOI=10.1046/j.1365-2443.1999.00290.x;
Nishizawa M., Suzuki K., Fujino M., Oguchi T., Toh-e A.;
"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.";
Genes Cells 4:627-642(1999).
[16]
FUNCTION, INTERACTION WITH PCL10, BIOPHYSICOCHEMICAL PROPERTIES, AND
LACK OF PHOSPHORYLATION.
PubMed=10490639; DOI=10.1128/MCB.19.10.7020;
Wilson W.A., Mahrenholz A.M., Roach P.J.;
"Substrate targeting of the yeast cyclin-dependent kinase Pho85p by
the cyclin Pcl10p.";
Mol. Cell. Biol. 19:7020-7030(1999).
[17]
FUNCTION IN PHOSPHORYLATION OF SWI5.
PubMed=10692159; DOI=10.1046/j.1365-2958.2000.01754.x;
Measday V., McBride H., Moffat J., Stillman D., Andrews B.J.;
"Interactions between Pho85 cyclin-dependent kinase complexes and the
Swi5 transcription factor in budding yeast.";
Mol. Microbiol. 35:825-834(2000).
[18]
ENZYME REGULATION, AND INTERACTION WITH PCL6 AND PCL7.
PubMed=11069666; DOI=10.1046/j.1365-2958.2000.02140.x;
Lee M., O'Regan S., Moreau J.-L., Johnson A.L., Johnston L.H.,
Goding C.R.;
"Regulation of the Pcl7-Pho85 cyclin-cdk complex by Pho81.";
Mol. Microbiol. 38:411-422(2000).
[19]
FUNCTION.
PubMed=11602261; DOI=10.1016/S0014-5793(01)02914-3;
Wang Z., Wilson W.A., Fujino M.A., Roach P.J.;
"The yeast cyclins Pcl6p and Pcl7p are involved in the control of
glycogen storage by the cyclin-dependent protein kinase Pho85p.";
FEBS Lett. 506:277-280(2001).
[20]
MUTAGENESIS OF PHE-82.
PubMed=11675494; DOI=10.1073/pnas.211195798;
Carroll A.S., Bishop A.C., DeRisi J.L., Shokat K.M., O'Shea E.K.;
"Chemical inhibition of the Pho85 cyclin-dependent kinase reveals a
role in the environmental stress response.";
Proc. Natl. Acad. Sci. U.S.A. 98:12578-12583(2001).
[21]
FUNCTION IN PHOSPHORYLATION OF MMR1.
PubMed=12006994;
Shi X.Z., Ao S.Z.;
"Phosphorylation of YLR190w by PAP1 PHO85 kinase complex.";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:187-192(2002).
[22]
FUNCTION IN PHOSPHORYLATION OF YJL084C.
PubMed=12098764;
Shi X.Z., Ao S.Z.;
"Analysis of phosphorylation of YJL084c, a yeast protein.";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:433-438(2002).
[23]
FUNCTION IN PHOSPHORYLATION OF GCN4.
PubMed=12101234; DOI=10.1128/MCB.22.15.5395-5404.2002;
Shemer R., Meimoun A., Holtzman T., Kornitzer D.;
"Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5.";
Mol. Cell. Biol. 22:5395-5404(2002).
[24]
FUNCTION IN PHOSPHORYLATION OF GLC8, AND INTERACTION WITH GLC8.
PubMed=12407105; DOI=10.1074/jbc.M208058200;
Tan Y.S.H., Morcos P.A., Cannon J.F.;
"Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in
vivo.";
J. Biol. Chem. 278:147-153(2003).
[25]
FUNCTION IN PHOSPHORYLATION OF RVS167.
PubMed=12857883; DOI=10.1091/mbc.E02-09-0613;
Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J.;
"Regulation of the yeast amphiphysin homologue Rvs167p by
phosphorylation.";
Mol. Biol. Cell 14:3027-3040(2003).
[26]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[27]
FUNCTION IN PHOSPHORYLATION OF PHO80 AND PHO81, AND MUTAGENESIS OF
LYS-36.
PubMed=15057567; DOI=10.1007/s00294-004-0501-0;
Waters N.C., Knight J.P., Creasy C.L., Bergman L.W.;
"The yeast Pho80-Pho85 cyclin-CDK complex has multiple substrates.";
Curr. Genet. 46:1-9(2004).
[28]
FUNCTION IN PHOSPHORYLATION OF HMS1; NCP1 AND NPA3.
PubMed=15082539; DOI=10.1534/genetics.166.3.1177;
Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.;
"The identification of Pcl1-interacting proteins that genetically
interact with Cla4 may indicate a link between G1 progression and
mitotic exit.";
Genetics 166:1177-1186(2004).
[29]
FUNCTION.
PubMed=15721288; DOI=10.1016/j.bbrc.2005.01.106;
Wilson W.A., Wang Z., Roach P.J.;
"Regulation of yeast glycogen phosphorylase by the cyclin-dependent
protein kinase Pho85p.";
Biochem. Biophys. Res. Commun. 329:161-167(2005).
[30]
FUNCTION IN PHOSPHORYLATION OF RIM15, AND INTERACTION WITH RIM15.
PubMed=16308562; DOI=10.1038/sj.emboj.7600889;
Wanke V., Pedruzzi I., Cameroni E., Dubouloz F., De Virgilio C.;
"Regulation of G0 entry by the Pho80-Pho85 cyclin-CDK complex.";
EMBO J. 24:4271-4278(2005).
[31]
FUNCTION IN PHOSPHORYLATION OF LCB4.
PubMed=15598647; DOI=10.1074/jbc.M410908200;
Iwaki S., Kihara A., Sano T., Igarashi Y.;
"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.";
J. Biol. Chem. 280:6520-6527(2005).
[32]
FUNCTION IN PHOSPHORYLATION OF CRZ1.
PubMed=16455487; DOI=10.1016/j.molcel.2005.12.011;
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.;
"Mapping pathways and phenotypes by systematic gene overexpression.";
Mol. Cell 21:319-330(2006).
[33]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-289, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- 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. {ECO:0000269|PubMed:10490639,
ECO:0000269|PubMed:10692159, ECO:0000269|PubMed:11602261,
ECO:0000269|PubMed:12006994, ECO:0000269|PubMed:12098764,
ECO:0000269|PubMed:12101234, ECO:0000269|PubMed:12407105,
ECO:0000269|PubMed:12857883, ECO:0000269|PubMed:15057567,
ECO:0000269|PubMed:15082539, ECO:0000269|PubMed:15598647,
ECO:0000269|PubMed:15721288, ECO:0000269|PubMed:16308562,
ECO:0000269|PubMed:16455487, ECO:0000269|PubMed:3067079,
ECO:0000269|PubMed:7973730, ECO:0000269|PubMed:8108735,
ECO:0000269|PubMed:8539622, ECO:0000269|PubMed:9584169,
ECO:0000269|PubMed:9593297, ECO:0000269|PubMed:9725902,
ECO:0000269|PubMed:9843683}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Inhibited by the CDK inhibitor (CKI) PHO81 in
response to phosphate starvation. {ECO:0000269|PubMed:11069666,
ECO:0000269|PubMed:7939631}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.5 uM for substrate protein GSY2 (when associated with
cyclin PCL10) {ECO:0000269|PubMed:10490639};
Vmax=11.5 umol/min/mg enzyme {ECO:0000269|PubMed:10490639};
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:10490639, ECO:0000269|PubMed:11069666,
ECO:0000269|PubMed:12407105, ECO:0000269|PubMed:16308562,
ECO:0000269|PubMed:7973730, ECO:0000269|PubMed:7973731,
ECO:0000269|PubMed:8108735, ECO:0000269|PubMed:9032248,
ECO:0000269|PubMed:9593297}.
-!- INTERACTION:
P37366:CCL1; NbExp=2; IntAct=EBI-13327, EBI-4385;
P35190:CLG1; NbExp=3; IntAct=EBI-13327, EBI-4762;
P20437:CLN1; NbExp=2; IntAct=EBI-13327, EBI-4479;
P24867:PCL1; NbExp=4; IntAct=EBI-13327, EBI-4495;
P53124:PCL10; NbExp=6; IntAct=EBI-13327, EBI-23973;
P25693:PCL2; NbExp=8; IntAct=EBI-13327, EBI-4499;
P38794:PCL5; NbExp=2; IntAct=EBI-13327, EBI-4504;
P40038:PCL6; NbExp=7; IntAct=EBI-13327, EBI-22555;
P40186:PCL7; NbExp=8; IntAct=EBI-13327, EBI-25021;
Q08966:PCL8; NbExp=8; IntAct=EBI-13327, EBI-37056;
Q12477:PCL9; NbExp=4; IntAct=EBI-13327, EBI-38090;
P20052:PHO80; NbExp=4; IntAct=EBI-13327, EBI-13310;
P17442:PHO81; NbExp=6; IntAct=EBI-13327, EBI-13314;
P10591:SSA1; NbExp=2; IntAct=EBI-13327, EBI-8591;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- PTM: Phosphorylation of Tyr-18 seems to be important to
discriminate between the different cyclin partners for binding.
{ECO:0000269|PubMed:10620010}.
-!- MISCELLANEOUS: Present with 6160 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y00867; CAA68773.1; -; Genomic_DNA.
EMBL; Y00867; CAA68774.1; ALT_SEQ; Genomic_DNA.
EMBL; U44030; AAB68188.1; -; Genomic_DNA.
EMBL; BK006949; DAA11398.1; -; Genomic_DNA.
PIR; S62043; OKBY85.
RefSeq; NP_015294.1; NM_001183845.1.
PDB; 2PK9; X-ray; 2.91 A; A/C=1-305.
PDB; 2PMI; X-ray; 2.90 A; A/C=1-305.
PDB; 4KRC; X-ray; 2.60 A; A=1-305.
PDB; 4KRD; X-ray; 1.95 A; A=1-305.
PDBsum; 2PK9; -.
PDBsum; 2PMI; -.
PDBsum; 4KRC; -.
PDBsum; 4KRD; -.
ProteinModelPortal; P17157; -.
SMR; P17157; -.
BioGrid; 36147; 634.
DIP; DIP-1493N; -.
IntAct; P17157; 58.
MINT; MINT-384508; -.
STRING; 4932.YPL031C; -.
BindingDB; P17157; -.
ChEMBL; CHEMBL5589; -.
iPTMnet; P17157; -.
MaxQB; P17157; -.
PRIDE; P17157; -.
EnsemblFungi; YPL031C; YPL031C; YPL031C.
GeneID; 856076; -.
KEGG; sce:YPL031C; -.
EuPathDB; FungiDB:YPL031C; -.
SGD; S000005952; PHO85.
GeneTree; ENSGT00900000140869; -.
HOGENOM; HOG000233024; -.
InParanoid; P17157; -.
KO; K06655; -.
OMA; SFCHLRC; -.
OrthoDB; EOG092C2FL8; -.
BioCyc; YEAST:G3O-33946-MONOMER; -.
BRENDA; 2.7.11.22; 984.
EvolutionaryTrace; P17157; -.
PRO; PR:P17157; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:SGD.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:1990860; C:Pho85-Pho80 CDK-cyclin complex; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
GO; GO:0050849; P:negative regulation of calcium-mediated signaling; IGI:SGD.
GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IMP:SGD.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:SGD.
GO; GO:0045936; P:negative regulation of phosphate metabolic process; IGI:SGD.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IMP:SGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:SGD.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IDA:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IGI:SGD.
GO; GO:0032880; P:regulation of protein localization; IDA:SGD.
GO; GO:0031647; P:regulation of protein stability; IMP:SGD.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 305 Cyclin-dependent protein kinase PHO85.
/FTId=PRO_0000086521.
DOMAIN 7 297 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 13 21 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 133 133 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 36 36 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 166 166 Not phosphorylated.
{ECO:0000269|PubMed:10490639}.
SITE 167 167 Not phosphorylated.
{ECO:0000269|PubMed:10490639}.
MOD_RES 18 18 Phosphotyrosine.
{ECO:0000269|PubMed:10620010}.
CROSSLNK 289 289 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 18 18 Y->F: Reduces kinase activity. Abolishes
interaction to PHO80 cyclin, but not to
PCL1.
MUTAGEN 36 36 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:15057567}.
MUTAGEN 53 53 E->A: Loss of kinase activity. Abolishes
interaction to PHO80 and PCL1 cyclins.
{ECO:0000269|PubMed:10620010}.
MUTAGEN 82 82 F->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).
{ECO:0000269|PubMed:11675494}.
CONFLICT 99 99 G -> A (in Ref. 1; CAA68773/CAA68774).
{ECO:0000305}.
HELIX 4 6 {ECO:0000244|PDB:4KRD}.
STRAND 7 16 {ECO:0000244|PDB:4KRD}.
STRAND 19 26 {ECO:0000244|PDB:4KRD}.
TURN 27 29 {ECO:0000244|PDB:4KRD}.
STRAND 32 39 {ECO:0000244|PDB:4KRD}.
TURN 42 44 {ECO:0000244|PDB:4KRD}.
HELIX 48 55 {ECO:0000244|PDB:4KRD}.
TURN 56 59 {ECO:0000244|PDB:4KRD}.
STRAND 68 74 {ECO:0000244|PDB:4KRD}.
STRAND 77 83 {ECO:0000244|PDB:4KRD}.
STRAND 86 88 {ECO:0000244|PDB:4KRD}.
HELIX 89 94 {ECO:0000244|PDB:4KRD}.
STRAND 98 100 {ECO:0000244|PDB:2PMI}.
HELIX 107 126 {ECO:0000244|PDB:4KRD}.
HELIX 136 138 {ECO:0000244|PDB:4KRD}.
STRAND 139 141 {ECO:0000244|PDB:4KRD}.
STRAND 147 149 {ECO:0000244|PDB:4KRD}.
HELIX 152 154 {ECO:0000244|PDB:4KRC}.
STRAND 156 160 {ECO:0000244|PDB:4KRD}.
HELIX 172 174 {ECO:0000244|PDB:4KRD}.
HELIX 177 180 {ECO:0000244|PDB:4KRD}.
HELIX 189 204 {ECO:0000244|PDB:4KRD}.
HELIX 214 225 {ECO:0000244|PDB:4KRD}.
TURN 230 232 {ECO:0000244|PDB:4KRD}.
HELIX 234 238 {ECO:0000244|PDB:4KRD}.
STRAND 244 246 {ECO:0000244|PDB:4KRC}.
HELIX 254 258 {ECO:0000244|PDB:4KRD}.
HELIX 259 261 {ECO:0000244|PDB:4KRD}.
HELIX 268 277 {ECO:0000244|PDB:4KRD}.
HELIX 282 284 {ECO:0000244|PDB:4KRD}.
HELIX 288 292 {ECO:0000244|PDB:4KRD}.
HELIX 295 300 {ECO:0000244|PDB:4KRD}.
SEQUENCE 305 AA; 34906 MW; 246A4358870B00EC CRC64;
MSSSSQFKQL EKLGNGTYAT VYKGLNKTTG VYVALKEVKL DSEEGTPSTA IREISLMKEL
KHENIVRLYD VIHTENKLTL VFEFMDNDLK KYMDSRTVGN TPRGLELNLV KYFQWQLLQG
LAFCHENKIL HRDLKPQNLL INKRGQLKLG DFGLARAFGI PVNTFSSEVV TLWYRAPDVL
MGSRTYSTSI DIWSCGCILA EMITGKPLFP GTNDEEQLKL IFDIMGTPNE SLWPSVTKLP
KYNPNIQQRP PRDLRQVLQP HTKEPLDGNL MDFLHGLLQL NPDMRLSAKQ ALHHPWFAEY
YHHAS


Related products :

Catalog number Product name Quantity
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB06524 CAK-kinase p42,CCRK,CDCH,CDK20,CDK-activating kinase p42,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protein kinase H,Cyclin-kinase-activating
EIAAB06559 CDI1,CDK2-associated dual-specificity phosphatase,CDKN3,CIP2,Cyclin-dependent kinase inhibitor 3,Cyclin-dependent kinase interactor 1,Cyclin-dependent kinase-interacting protein 2,Homo sapiens,Human,K
EIAAB06522 CDC2L6,CDC2-related protein kinase 6,CDK11,CDK19,Cell division cycle 2-like protein kinase 6,Cell division protein kinase 19,Cyclin-dependent kinase 11,Cyclin-dependent kinase 19,Death-preventing kina
EIAAB06523 CAK-kinase p42,Ccrk,Cdch,Cdk20,CDK-activating kinase p42,CDK-related protein kinase PNQLARE,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protei
E0739m ELISA Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subuni 96T
U0739m CLIA Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit 96T
E0739b ELISA kit Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein 96T
E0739m ELISA kit Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic s 96T
U0739b CLIA Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein kinas 96T
E0739b ELISA Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein kina 96T
U1880h CLIA kit 39 kDa protein kinase,CAK,CAK1,CDK7,CDK-activating kinase 1,CDKN7,Cell division protein kinase 7,Cyclin-dependent kinase 7,Homo sapiens,Human,MO15,p39 Mo15,Serine_threonine-protein kinase 1, 96T
E1880h ELISA kit 39 kDa protein kinase,CAK,CAK1,CDK7,CDK-activating kinase 1,CDKN7,Cell division protein kinase 7,Cyclin-dependent kinase 7,Homo sapiens,Human,MO15,p39 Mo15,Serine_threonine-protein kinase 1 96T
U1880h CLIA 39 kDa protein kinase,CAK,CAK1,CDK7,CDK-activating kinase 1,CDKN7,Cell division protein kinase 7,Cyclin-dependent kinase 7,Homo sapiens,Human,MO15,p39 Mo15,Serine_threonine-protein kinase 1,STK1, 96T
E1880h ELISA 39 kDa protein kinase,CAK,CAK1,CDK7,CDK-activating kinase 1,CDKN7,Cell division protein kinase 7,Cyclin-dependent kinase 7,Homo sapiens,Human,MO15,p39 Mo15,Serine_threonine-protein kinase 1,STK1 96T
31-031 Cdk7 is the catalytic subunit of the CDK-activating kinase (CAK) complex, a serine-threonine kinase. CAK activates the cyclin-associated kinases CDC2_CDK1, CDK2, CDK4 and CDK6 by threonine phosphoryla 0.1 mg
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
U1880m CLIA 39 kDa protein kinase,Cak,Cdk7,CDK-activating kinase,Cdkn7,Cell division protein kinase 7,CR4 protein kinase,CRK4,Crk4,Cyclin-dependent kinase 7,Mo15,Mouse,Mpk-7,Mus musculus,P39 Mo15,Protein-tyr 96T
E1880m ELISA 39 kDa protein kinase,Cak,Cdk7,CDK-activating kinase,Cdkn7,Cell division protein kinase 7,CR4 protein kinase,CRK4,Crk4,Cyclin-dependent kinase 7,Mo15,Mouse,Mpk-7,Mus musculus,P39 Mo15,Protein-ty 96T
E0739r ELISA kit Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic sub 96T
EIAAB06513 CDK16,Cell division protein kinase 16,Cyclin-dependent kinase 16,Homo sapiens,Human,PCTAIRE-motif protein kinase 1,PCTK1,Serine_threonine-protein kinase PCTAIRE-1
EIAAB06520 CDK18,Cell division protein kinase 18,Cyclin-dependent kinase 18,Homo sapiens,Human,PCTAIRE-motif protein kinase 3,PCTK3,Serine_threonine-protein kinase PCTAIRE-3
EIAAB06516 CDK17,Cell division protein kinase 17,Cyclin-dependent kinase 17,Homo sapiens,Human,PCTAIRE-motif protein kinase 2,PCTK2,Serine_threonine-protein kinase PCTAIRE-2


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur