ID   CG22_YEAST              Reviewed;         491 AA.
AC   P24869; D6W4B8;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=G2/mitotic-specific cyclin-2;
GN   Name=CLB2; OrderedLocusNames=YPR119W; ORFNames=P9642.6;
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=1849457; DOI=10.1016/0092-8674(91)90416-v;
RA   Surana U., Robitsch H., Price C., Schuster T., Fitch I., Futcher A.B.,
RA   Nasmyth K.;
RT   "The role of CDC28 and cyclins during mitosis in the budding yeast S.
RT   cerevisiae.";
RL   Cell 65:145-161(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1427070; DOI=10.1101/gad.6.11.2021;
RA   Richardson H., Lew D.J., Henze M., Sugimoto K., Reed S.I.;
RT   "Cyclin-B homologs in Saccharomyces cerevisiae function in S phase and in
RT   G2.";
RL   Genes Dev. 6:2021-2034(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [4]
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   [5]
RP   INTERACTION WITH NAP1.
RX   PubMed=7622566; DOI=10.1083/jcb.130.3.661;
RA   Kellogg D.R., Kikuchi A., Fujii-Nakata T., Turck C.W., Murray A.W.;
RT   "Members of the NAP/SET family of proteins interact specifically with B-
RT   type cyclins.";
RL   J. Cell Biol. 130:661-673(1995).
RN   [6]
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   [7]
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).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. Interacts with the CDC2 protein kinase to form
CC       MPF. G2/M cyclins accumulate steadily during G2 and are abruptly
CC       destroyed at mitosis.
CC   -!- SUBUNIT: Interacts with NAP1. {ECO:0000269|PubMed:7622566}.
CC   -!- INTERACTION:
CC       P24869; P35734: ASK1; NbExp=2; IntAct=EBI-4515, EBI-26682;
CC       P24869; Q03898: FIN1; NbExp=2; IntAct=EBI-4515, EBI-32941;
CC       P24869; P38826: ORC6; NbExp=2; IntAct=EBI-4515, EBI-12588;
CC       P24869; P38283: SLI15; NbExp=2; IntAct=EBI-4515, EBI-20842;
CC   -!- DEVELOPMENTAL STAGE: Maximally expressed before mitosis. The levels
CC       peak late in the G2 phase of the cell cycle and are at a minimum in G1
CC       phase.
CC   -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M65070; AAA34502.1; -; Genomic_DNA.
DR   EMBL; X62319; CAA44195.1; -; Genomic_DNA.
DR   EMBL; U40828; AAB68060.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11534.1; -; Genomic_DNA.
DR   PIR; S14166; S14166.
DR   RefSeq; NP_015444.1; NM_001184216.1.
DR   AlphaFoldDB; P24869; -.
DR   SMR; P24869; -.
DR   BioGRID; 36287; 304.
DR   ComplexPortal; CPX-1701; CLB2-CDC28 kinase complex.
DR   DIP; DIP-658N; -.
DR   ELM; P24869; -.
DR   IntAct; P24869; 27.
DR   MINT; P24869; -.
DR   STRING; 4932.YPR119W; -.
DR   iPTMnet; P24869; -.
DR   MaxQB; P24869; -.
DR   PaxDb; 4932-YPR119W; -.
DR   PeptideAtlas; P24869; -.
DR   EnsemblFungi; YPR119W_mRNA; YPR119W; YPR119W.
DR   GeneID; 856236; -.
DR   KEGG; sce:YPR119W; -.
DR   AGR; SGD:S000006323; -.
DR   SGD; S000006323; CLB2.
DR   VEuPathDB; FungiDB:YPR119W; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   GeneTree; ENSGT00940000176520; -.
DR   HOGENOM; CLU_020695_10_4_1; -.
DR   InParanoid; P24869; -.
DR   OMA; ANDPFMV; -.
DR   OrthoDB; 5474295at2759; -.
DR   BioCyc; YEAST:G3O-34258-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; 856236; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P24869; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P24869; Protein.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISS:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005819; C:spindle; IDA:SGD.
DR   GO; GO:0005816; C:spindle pole body; 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:0006974; P:DNA damage response; IDA:ComplexPortal.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:SGD.
DR   GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IGI:SGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:SGD.
DR   GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:SGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IMP:SGD.
DR   CDD; cd20568; CYCLIN_CLBs_yeast_rpt1; 1.
DR   CDD; cd20512; CYCLIN_CLBs_yeast_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR046965; Cyclin_A/B-like.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF520; G2_MITOTIC-SPECIFIC CYCLIN-1-RELATED; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF001771; Cyclin_A_B_D_E; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Cyclin; Mitosis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..491
FT                   /note="G2/mitotic-specific cyclin-2"
FT                   /id="PRO_0000080404"
FT   REGION          59..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   491 AA;  56247 MW;  B68FF888871022A0 CRC64;
     MSNPIENTEN SQNTSSSRFL RNVQRLALNN VTNTTFQKSN ANNPALTNFK STLNSVKKEG
     SRIPQFTRES VSRSTAAQEE KRTLKENGIQ LPKNNLLDDK ENQDPSSQQF GALTSIKEGR
     AELPANISLQ ESSSAKEIIQ HDPLKGVGSS TEVVHNSVEN EKLHPARSQL QVRNTESETD
     SGKKRPISTI VEQELPKKFK VCDENGKEEY EWEDLDAEDV NDPFMVSEYV NDIFEYLHQL
     EVITLPKKED LYQHRNIHQN RDILVNWLVK IHNKFGLLPE TLYLAINIMD RFLGKELVQL
     DKLQLVGTSC LFIASKYEEV YSPSIKHFAS ETDGACTEDE IKEGEKFILK TLKFNLNYPN
     PMNFLRRISK ADDYDIQSRT LAKFLLEISL VDFRFIGILP SLCAAAAMFM SRKMLGKGKW
     DGNLIHYSGG YTKEELAPVC HMIMDYLVSP IVHDEFHRKY QSRRFMKASI ISVQWALKVR
     KNGYDIMTLH E
//