PCL6_YEAST
ID PCL6_YEAST Reviewed; 420 AA.
AC P40038; D3DLW3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=PHO85 cyclin-6;
GN Name=PCL6; OrderedLocusNames=YER059W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP INTERACTION WITH PHO85.
RX PubMed=9032248; DOI=10.1128/mcb.17.3.1212;
RA Measday V., Moore L., Retnakaran R., Lee J., Donoviel M., Neiman A.M.,
RA Andrews B.J.;
RT "A family of cyclin-like proteins that interact with the Pho85 cyclin-
RT dependent kinase.";
RL Mol. Cell. Biol. 17:1212-1223(1997).
RN [4]
RP INTERACTION WITH ELC1.
RX PubMed=10760578; DOI=10.1016/s0167-4781(00)00052-x;
RA Jackson T., Kwon E., Chachulska A.M., Hyman L.E.;
RT "Novel roles for elongin C in yeast.";
RL Biochim. Biophys. Acta 1491:161-176(2000).
RN [5]
RP ACTIVITY REGULATION, AND INTERACTION WITH PHO81 AND PHO85.
RX PubMed=11069666; DOI=10.1046/j.1365-2958.2000.02140.x;
RA Lee M., O'Regan S., Moreau J.-L., Johnson A.L., Johnston L.H., Goding C.R.;
RT "Regulation of the Pcl7-Pho85 cyclin-cdk complex by Pho81.";
RL Mol. Microbiol. 38:411-422(2000).
RN [6]
RP FUNCTION.
RX PubMed=11602261; DOI=10.1016/s0014-5793(01)02914-3;
RA Wang Z., Wilson W.A., Fujino M.A., Roach P.J.;
RT "The yeast cyclins Pcl6p and Pcl7p are involved in the control of glycogen
RT storage by the cyclin-dependent protein kinase Pho85p.";
RL FEBS Lett. 506:277-280(2001).
RN [7]
RP FUNCTION, INTERACTION WITH YJL084C, AND PHOSPHORYLATION OF YJL084C.
RX PubMed=12098764;
RA Shi X.Z., Ao S.Z.;
RT "Analysis of phosphorylation of YJL084c, a yeast protein.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:433-438(2002).
RN [8]
RP FUNCTION.
RX PubMed=11864988; DOI=10.1074/jbc.m200800200;
RA Hyman L.E., Kwon E., Ghosh S., McGee J., Chachulska A.M., Jackson T.,
RA Baricos W.H.;
RT "Binding to Elongin C inhibits degradation of interacting proteins in
RT yeast.";
RL J. Biol. Chem. 277:15586-15591(2002).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION OF GLC8.
RX PubMed=12407105; DOI=10.1074/jbc.m208058200;
RA Tan Y.S.H., Morcos P.A., Cannon J.F.;
RT "Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in
RT vivo.";
RL J. Biol. Chem. 278:147-153(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP FUNCTION.
RX PubMed=15721288; DOI=10.1016/j.bbrc.2005.01.106;
RA Wilson W.A., Wang Z., Roach P.J.;
RT "Regulation of yeast glycogen phosphorylase by the cyclin-dependent protein
RT kinase Pho85p.";
RL Biochem. Biophys. Res. Commun. 329:161-167(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-281 AND SER-312, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND THR-317, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85.
CC Together with cyclin PCL7, controls glycogen phosphorylase and glycogen
CC synthase activities in response to nutrient availablility. The PCL6-
CC PHO85 cyclin-CDK holoenzyme has GLC8 kinase activity and phosphorylates
CC and inactivates the phosphatase PP1-2 inhibitor GLC8, causing
CC activation of PP1-2, which then dephosphorylates and activates glycogen
CC phosphorylase. PCL6-PHO85 also phosphorylates YJL084C.
CC {ECO:0000269|PubMed:11602261, ECO:0000269|PubMed:11864988,
CC ECO:0000269|PubMed:12098764, ECO:0000269|PubMed:12407105,
CC ECO:0000269|PubMed:15721288}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85. Interacts with the
CC substrate protein YJL084C. Interacts with elongin-C, which stabilizes
CC PCL6. Interacts with the CDK inhibitor (CKI) PHO81.
CC {ECO:0000269|PubMed:10760578, ECO:0000269|PubMed:11069666,
CC ECO:0000269|PubMed:12098764, ECO:0000269|PubMed:9032248}.
CC -!- INTERACTION:
CC P40038; P17157: PHO85; NbExp=7; IntAct=EBI-22555, EBI-13327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. PHO80 subfamily.
CC {ECO:0000305}.
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DR EMBL; U18813; AAB64595.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07717.1; -; Genomic_DNA.
DR PIR; S50562; S50562.
DR RefSeq; NP_010980.1; NM_001178950.1.
DR AlphaFoldDB; P40038; -.
DR SMR; P40038; -.
DR BioGRID; 36800; 79.
DR ComplexPortal; CPX-1689; PCL6-PHO85 kinase complex.
DR DIP; DIP-1496N; -.
DR IntAct; P40038; 24.
DR MINT; P40038; -.
DR STRING; 4932.YER059W; -.
DR iPTMnet; P40038; -.
DR MaxQB; P40038; -.
DR PaxDb; P40038; -.
DR PRIDE; P40038; -.
DR EnsemblFungi; YER059W_mRNA; YER059W; YER059W.
DR GeneID; 856787; -.
DR KEGG; sce:YER059W; -.
DR SGD; S000000861; PCL6.
DR VEuPathDB; FungiDB:YER059W; -.
DR eggNOG; KOG1674; Eukaryota.
DR GeneTree; ENSGT00390000000862; -.
DR HOGENOM; CLU_048130_1_0_1; -.
DR InParanoid; P40038; -.
DR OMA; QSSTQXD; -.
DR BioCyc; YEAST:G3O-30236-MON; -.
DR PRO; PR:P40038; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40038; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IGI:SGD.
DR GO; GO:0005981; P:regulation of glycogen catabolic process; IGI:SGD.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR PANTHER; PTHR15615; PTHR15615; 1.
DR Pfam; PF08613; Cyclin; 2.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cyclin; Cytoplasm; Glycogen metabolism; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..420
FT /note="PHO85 cyclin-6"
FT /id="PRO_0000202631"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 420 AA; 47007 MW; BD8A0C7A501C94E5 CRC64;
MSIKGDSPSS TNASSSPKST YSIQSDDKAN LGSGNVDIRT DNSQQDSNNR RDIVVVTRVA
SEETLESQSS TSSMGIRPES SFNYEDASNQ ARVEMNNRVH GSNMNTINKY YPVRFPKNNE
RQLSDTNNLN EKVQGTHTVQ SSTQEDKILD GDTSNSQVTP SLNIAEFPTD KLLKMLTALL
TKIIKSNDRT AATNPSLTQE IENGRCLALS DNEKKYLSPV LGFRGKHVPQ IGLDQYFQRI
QKYCPTTNDV FLSLLVYFDR ISKRCNSVTT TPKTNTAKHE SPSNESSLDK ANRGADKMSA
CNSNENNEND DSDDENTGVQ RDSRAHPQMF VMDSHNIHRL IIAGITVSTK FLSDFFYSNS
RYSRVGGISL QELNHLELQF LVLCDFELLI SVNELQRYAD LLYRFWNNAK AQSQALVTGM
