CG22_YEAST
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 03-AUG-2022, entry version 192.
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; 299.
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; P24869; -.
DR PRIDE; P24869; -.
DR EnsemblFungi; YPR119W_mRNA; YPR119W; YPR119W.
DR GeneID; 856236; -.
DR KEGG; sce:YPR119W; -.
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 BioCyc; YEAST:G3O-34258-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: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; IBA:GO_Central.
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:cellular response to DNA damage stimulus; 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:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IGI:SGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:SGD.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:SGD.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 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; SSF47954; 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
