CG11_YEAST
ID CG11_YEAST Reviewed; 546 AA.
AC P20437; D6W024;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=G1/S-specific cyclin CLN1;
GN Name=CLN1; OrderedLocusNames=YMR199W; ORFNames=YM9646.13;
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].
RX PubMed=2569741; DOI=10.1073/pnas.86.16.6255;
RA Hadwiger J.A., Wittenberg C., Richardson H.E., de Barros Lopes M.,
RA Reed S.I.;
RT "A family of cyclin homologs that control the G1 phase in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6255-6259(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2197605; DOI=10.1093/nar/18.13.4025;
RA Hadwiger J.A., Reed S.I.;
RT "Nucleotide sequence of the Saccharomyces cerevisiae CLN1 and CLN2 genes.";
RL Nucleic Acids Res. 18:4025-4025(1990).
RN [3]
RP SEQUENCE REVISION.
RA Wittenberg C., Chapman-Shimshoni D.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G1/S
CC (start) transition. Interacts with the CDC28 protein kinase to form
CC MPF.
CC -!- INTERACTION:
CC P20437; P00546: CDC28; NbExp=7; IntAct=EBI-4479, EBI-4253;
CC P20437; P17157: PHO85; NbExp=2; IntAct=EBI-4479, EBI-13327;
CC -!- DEVELOPMENTAL STAGE: CLN1 and CLN2 mRNAs fluctuate periodically in the
CC cell cycle, peaking in G1 phase.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR EMBL; M33264; AAA65724.1; -; Genomic_DNA.
DR EMBL; Z47815; CAA87822.1; -; Genomic_DNA.
DR EMBL; AY723855; AAU09772.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10098.1; -; Genomic_DNA.
DR PIR; S50929; COBYC1.
DR RefSeq; NP_013926.1; NM_001182706.1.
DR AlphaFoldDB; P20437; -.
DR SMR; P20437; -.
DR BioGRID; 35377; 281.
DR ComplexPortal; CPX-1699; CLN1-CDC28 kinase complex.
DR DIP; DIP-2269N; -.
DR IntAct; P20437; 9.
DR MINT; P20437; -.
DR STRING; 4932.YMR199W; -.
DR iPTMnet; P20437; -.
DR PaxDb; P20437; -.
DR PRIDE; P20437; -.
DR TopDownProteomics; P20437; -.
DR EnsemblFungi; YMR199W_mRNA; YMR199W; YMR199W.
DR GeneID; 855239; -.
DR KEGG; sce:YMR199W; -.
DR SGD; S000004812; CLN1.
DR VEuPathDB; FungiDB:YMR199W; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000176526; -.
DR HOGENOM; CLU_536434_0_0_1; -.
DR InParanoid; P20437; -.
DR OMA; WDVYEPM; -.
DR BioCyc; YEAST:G3O-32886-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SCE-69231; Cyclin D associated events in G1.
DR Reactome; R-SCE-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P20437; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P20437; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IC:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IGI:SGD.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR014399; Cyclin_CLN.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF001770; Cyclin_CLN; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Reference proteome.
FT CHAIN 1..546
FT /note="G1/S-specific cyclin CLN1"
FT /id="PRO_0000080411"
FT REGION 224..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 62050 MW; 4D7189B83D7A2B34 CRC64;
MNHSEVKTGL IVTAKQTYYP IELSNAELLT HYETIQEYHE EISQNVLVQS SKTKPDIKLI
DQQPEMNPHQ TREAIVTFLY QLSVMTRVSN GIFFHAVRFY DRYCSKRVVL KDQAKLVVGT
CLWLAAKTWG GCNHIINNVS IPTGGRFYGP NPRARIPRLS ELVHYCGGSD LFDESMFIQM
ERHILDTLNW DVYEPMINDY ILNVDENCLI QYELYKNQLQ NNNSNGKEWS CKRKSQSSDD
SDATVEEHIS SSPQSTGLDG DTTTMDEDEE LNSKIKLINL KRFLIDLSCW QYNLLKFELY
EICNGMFSII NKFTNQDQGP FLSMPIGNDI NSNTQTQVFS IIINGIVNSP PSLVEVYKEQ
YGIVPFILQV KDYNLELQKK LQLASTIDLT RKIAVNSRYF DQNASSSSVS SPSTYSSGTN
YTPMRNFSAQ SDNSVFSTTN IDHSSPITPH MYTFNQFKNE SACDSAISVS SLPNQTQNGN
MPLSSNYQNM MLEERNKENR IPNSSSAEIP QRAKFMTTGI FQNTGELTNR ASSISLSLRN
HNSSQL
