PCL1_YEAST
ID PCL1_YEAST Reviewed; 279 AA.
AC P24867; D6W0Q4;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=PHO85 cyclin-1 {ECO:0000305|PubMed:7973730};
DE AltName: Full=Cyclin HCS26 {ECO:0000303|PubMed:1832336};
DE AltName: Full=G1/S-specific cyclin PCL1 {ECO:0000303|PubMed:7973730};
GN Name=PCL1 {ECO:0000303|PubMed:7973730};
GN Synonyms=HCS26 {ECO:0000303|PubMed:1832336};
GN OrderedLocusNames=YNL289W {ECO:0000312|SGD:S000005233}; ORFNames=N0536;
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 [GENOMIC DNA], AND INDUCTION.
RX PubMed=1832336; DOI=10.1016/0092-8674(91)90445-5;
RA Ogas J., Andrews B.J., Herskowitz I.;
RT "Transcriptional activation of CLN1, CLN2, and a putative new G1 cyclin
RT (HCS26) by SWI4, a positive regulator of G1-specific transcription.";
RL Cell 66:1015-1026(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP CHARACTERIZATION, AND INTERACTION WITH PHO85.
RX PubMed=7973730; DOI=10.1126/science.7973730;
RA Espinoza F.H., Ogas J., Herskowitz I., Morgan D.O.;
RT "Cell cycle control by a complex of the cyclin HCS26 (PCL1) and the kinase
RT PHO85.";
RL Science 266:1388-1391(1994).
RN [5]
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 [6]
RP FUNCTION, AND PHOSPHORYLATION OF SIC1.
RX PubMed=9725902; DOI=10.1091/mbc.9.9.2393;
RA Nishizawa M., Kawasumi M., Fujino M., Toh-e A.;
RT "Phosphorylation of Sic1, a cyclin-dependent kinase (Cdk) inhibitor, by Cdk
RT including Pho85 kinase is required for its prompt degradation.";
RL Mol. Biol. Cell 9:2393-2405(1998).
RN [7]
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 [8]
RP FUNCTION, INTERACTION WITH HMS1; NCP1 AND NPA3, AND PHOSPHORYLATION OF
RP HMS1; NCP1 AND NPA3.
RX PubMed=15082539; DOI=10.1534/genetics.166.3.1177;
RA Keniry M.E., Kemp H.A., Rivers D.M., Sprague G.F. Jr.;
RT "The identification of Pcl1-interacting proteins that genetically interact
RT with Cla4 may indicate a link between G1 progression and mitotic exit.";
RL Genetics 166:1177-1186(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14688790; DOI=10.1038/ncb1078;
RA Moffat J., Andrews B.J.;
RT "Late-G1 cyclin-CDK activity is essential for control of cell morphogenesis
RT in budding yeast.";
RL Nat. Cell Biol. 6:59-66(2004).
RN [10]
RP FUNCTION, AND PHOSPHORYLATION OF LCB4.
RX PubMed=15598647; DOI=10.1074/jbc.m410908200;
RA Iwaki S., Kihara A., Sano T., Igarashi Y.;
RT "Phosphorylation by Pho85 cyclin-dependent kinase acts as a signal for the
RT down-regulation of the yeast sphingoid long-chain base kinase Lcb4 during
RT the stationary phase.";
RL J. Biol. Chem. 280:6520-6527(2005).
RN [11]
RP UBIQUITINATION AT LYS-82 AND LYS-121, PHOSPHORYLATION AT THR-39 AND SER-43,
RP INTERACTION WITH DMA1, AND MUTAGENESIS OF PRO-33; THR-39 AND SER-43.
RX PubMed=23264631; DOI=10.1074/jbc.m112.426593;
RA Hernandez-Ortega S., Bru S., Ricco N., Ramirez S., Casals N., Jimenez J.,
RA Isasa M., Crosas B., Clotet J.;
RT "Defective in mitotic arrest 1 (Dma1) ubiquitin ligase controls G1 cyclin
RT degradation.";
RL J. Biol. Chem. 288:4704-4714(2013).
CC -!- FUNCTION: G1/S-specific cyclin partner of the cyclin-dependent kinase
CC (CDK) PHO85. Essential for the control of the cell cycle at the G1/S
CC (start) transition. The PCL1-PHO85 cyclin-CDK holoenzyme is involved in
CC phosphorylation of the CDK inhibitor (CKI) SIC1, which is required for
CC its ubiquitination and degradation, releasing repression of b-type
CC cyclins and promoting exit from mitosis. Together with cyclin PCL2,
CC positively controls degradation of sphingoid long chain base kinase
CC LCB4. PCL1-PHO85 phosphorylates LCB4, which is required for its
CC ubiquitination and degradation. PCL1-PHO85 also phosphorylates HMS1,
CC NCP1 and NPA3, which may all have a role in mitotic exit.
CC {ECO:0000269|PubMed:14688790, ECO:0000269|PubMed:15082539,
CC ECO:0000269|PubMed:15598647, ECO:0000269|PubMed:9725902}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85 (PubMed:7973730,
CC PubMed:9032248). Interacts with HMS1, NCP1 and NPA3 (PubMed:15082539,
CC PubMed:9032248). Interacts with DMA1 (PubMed:23264631).
CC {ECO:0000269|PubMed:15082539, ECO:0000269|PubMed:23264631,
CC ECO:0000269|PubMed:7973730, ECO:0000269|PubMed:9032248}.
CC -!- INTERACTION:
CC P24867; P17157: PHO85; NbExp=4; IntAct=EBI-4495, EBI-13327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14688790}. Nucleus
CC {ECO:0000269|PubMed:14688790}. Note=Localizes to the incipient bud
CC site.
CC -!- INDUCTION: By transcription factor SBF (SWI4-SWI6 cell-cycle box
CC binding factor) in a cell cycle-regulated manner. Peaks in G1 phase.
CC {ECO:0000269|PubMed:1832336}.
CC -!- PTM: Phosphorylated by PHO85; necessary for interaction with DMA1 and
CC subsequent degradation. {ECO:0000269|PubMed:23264631}.
CC -!- PTM: Ubiquitinated by E3 ubiquitin ligase DMA1 in response to nutrient
CC condition; this targets PCL1 for destruction.
CC {ECO:0000269|PubMed:23264631}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. PCL1,2 subfamily.
CC {ECO:0000305}.
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DR EMBL; M73966; AAA34617.1; -; Genomic_DNA.
DR EMBL; Z71565; CAA96206.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10270.1; -; Genomic_DNA.
DR PIR; A40027; A40027.
DR RefSeq; NP_014110.1; NM_001183127.1.
DR AlphaFoldDB; P24867; -.
DR SMR; P24867; -.
DR BioGRID; 35548; 89.
DR ComplexPortal; CPX-1695; PCL1-PHO85 kinase complex.
DR DIP; DIP-5803N; -.
DR IntAct; P24867; 3.
DR MINT; P24867; -.
DR STRING; 4932.YNL289W; -.
DR iPTMnet; P24867; -.
DR PaxDb; P24867; -.
DR PRIDE; P24867; -.
DR EnsemblFungi; YNL289W_mRNA; YNL289W; YNL289W.
DR GeneID; 855427; -.
DR KEGG; sce:YNL289W; -.
DR SGD; S000005233; PCL1.
DR VEuPathDB; FungiDB:YNL289W; -.
DR eggNOG; KOG1674; Eukaryota.
DR GeneTree; ENSGT00390000000862; -.
DR HOGENOM; CLU_018149_0_2_1; -.
DR InParanoid; P24867; -.
DR OMA; LTTVCYL; -.
DR BioCyc; YEAST:G3O-33279-MON; -.
DR PRO; PR:P24867; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P24867; protein.
DR GO; GO:0005935; C:cellular bud neck; IC:ComplexPortal.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IC:ComplexPortal.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IGI:SGD.
DR GO; GO:0031106; P:septin ring organization; IGI:SGD.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR InterPro; IPR012104; PHO85_cyclin_1/2/9.
DR PANTHER; PTHR15615; PTHR15615; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF016511; Cyclin_Pcl; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..279
FT /note="PHO85 cyclin-1"
FT /id="PRO_0000080499"
FT DOMAIN 19..152
FT /note="Cyclin N-terminal"
FT REGION 29..36
FT /note="Required for degradation by DMA1"
FT /evidence="ECO:0000269|PubMed:23264631"
FT MOD_RES 39
FT /note="Phosphothreonine; by PHO85"
FT /evidence="ECO:0000305|PubMed:23264631"
FT MOD_RES 43
FT /note="Phosphoserine; by PHO85"
FT /evidence="ECO:0000305|PubMed:23264631"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:23264631"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:23264631"
FT MUTAGEN 33
FT /note="P->N: Stabilizes PCL1."
FT /evidence="ECO:0000269|PubMed:23264631"
FT MUTAGEN 39
FT /note="T->A: In pcl1-2A; stabilizes PCL1; when associated
FT with A-43."
FT /evidence="ECO:0000269|PubMed:23264631"
FT MUTAGEN 43
FT /note="S->A: In pcl1-2A; stabilizes PCL1; when associated
FT with A-39."
FT /evidence="ECO:0000269|PubMed:23264631"
SQ SEQUENCE 279 AA; 32095 MW; DC9E05C3C2EBD0F6 CRC64;
MCEYSKALHI LLKSPVTDDI IKFLTDTTLR VVPSSNYPTP PGSPGEKHLT RLPSLMTFIT
RLVRYTNVYT PTLLTAACYL NKLKRILPRD ATGLPSTIHR IFLACLILSA KFHNDSSPLN
KHWARYTDGL FTLEDINLME RQLLQLLNWD LRVNTEDLIL DLQPLLEPIK QDLARSSDQR
KRINMMMSMN RRTCAGTSPI RSNNRFKLYE KQRNVSIASD LSSATLVDSC NDLRRLKDVT
NIANNTVANT NYVRTVEKWN DNVNRQSWDL EQIMSQHGF
