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 27-MAR-2024, entry version 176. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 286. 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; 4932-YMR199W; -. DR PeptideAtlas; P20437; -. DR TopDownProteomics; P20437; -. DR EnsemblFungi; YMR199W_mRNA; YMR199W; YMR199W. DR GeneID; 855239; -. DR KEGG; sce:YMR199W; -. DR AGR; SGD:S000004812; -. 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 OrthoDB; 1966232at2759; -. DR BioCyc; YEAST:G3O-32886-MONOMER; -. 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 BioGRID-ORCS; 855239; 0 hits in 10 CRISPR screens. 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:0005816; C:spindle pole body; IBA:GO_Central. 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; NAS:ComplexPortal. DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:SGD. DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IGI:SGD. DR CDD; cd20559; CYCLIN_ScCLN_like; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 1. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR014399; Cyclin_CLN. DR InterPro; IPR006671; Cyclin_N. DR InterPro; IPR048258; Cyclins_cyclin-box. DR PANTHER; PTHR21615:SF2; CYCLIN N-TERMINAL DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR21615; UNCHARACTERIZED; 1. DR Pfam; PF00134; Cyclin_N; 1. DR PIRSF; PIRSF001770; Cyclin_CLN; 1. DR SMART; SM00385; CYCLIN; 1. DR SUPFAM; SSF47954; Cyclin-like; 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 //