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CG21_YEAST
ID   CG21_YEAST              Reviewed;         471 AA.
AC   P24868; D6VUN9;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=G2/mitotic-specific cyclin-1;
GN   Name=CLB1; Synonyms=SCB1; OrderedLocusNames=YGR108W; ORFNames=G5967;
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].
RX   PubMed=1849458; DOI=10.1016/0092-8674(91)90417-w;
RA   Ghiara J.B., Richardson H.E., Sugimoto K., Henze M., Lew D.J.,
RA   Wittenberg C., Reed S.I.;
RT   "A cyclin B homolog in S. cerevisiae: chronic activation of the Cdc28
RT   protein kinase by cyclin prevents exit from mitosis.";
RL   Cell 65:163-174(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   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 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   -!- INTERACTION:
CC       P24868; P20486: CKS1; NbExp=3; IntAct=EBI-4508, EBI-4746;
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 300 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; M65069; AAA34501.1; -; Genomic_DNA.
DR   EMBL; M62389; AAA35019.1; -; Genomic_DNA.
DR   EMBL; Z72893; CAA97112.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08200.1; -; Genomic_DNA.
DR   PIR; S14165; S14165.
DR   RefSeq; NP_011622.1; NM_001181237.1.
DR   AlphaFoldDB; P24868; -.
DR   SMR; P24868; -.
DR   BioGRID; 33352; 94.
DR   ComplexPortal; CPX-335; CLB1-CDC28 kinase complex.
DR   DIP; DIP-1261N; -.
DR   IntAct; P24868; 5.
DR   MINT; P24868; -.
DR   STRING; 4932.YGR108W; -.
DR   iPTMnet; P24868; -.
DR   PaxDb; P24868; -.
DR   PRIDE; P24868; -.
DR   EnsemblFungi; YGR108W_mRNA; YGR108W; YGR108W.
DR   GeneID; 853002; -.
DR   KEGG; sce:YGR108W; -.
DR   SGD; S000003340; CLB1.
DR   VEuPathDB; FungiDB:YGR108W; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   GeneTree; ENSGT00940000176520; -.
DR   HOGENOM; CLU_020695_10_4_1; -.
DR   InParanoid; P24868; -.
DR   BioCyc; YEAST:G3O-30817-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:P24868; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P24868; protein.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IDA:SGD.
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; IMP:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0008315; P:G2/MI transition of meiotic cell cycle; IMP:SGD.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP: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:0060631; P:regulation of meiosis I; IDA: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   Cell cycle; Cell division; Cyclin; Mitosis; Reference proteome.
FT   CHAIN           1..471
FT                   /note="G2/mitotic-specific cyclin-1"
FT                   /id="PRO_0000080403"
SQ   SEQUENCE   471 AA;  54871 MW;  4B347E96DD188735 CRC64;
     MSRSLLVENS RTINSNEEKG VNESQYILQK RNVPRTILGN VTNNANILQE ISMNRKIGMK
     NFSKLNNFFP LKDDVSRADD FTSSFNDSRQ GVKQEVLNNK ENIPEYGYSE QEKQQCSNDD
     SFHTNSTALS CNRLIYSENK SISTQMEWQK KIMREDSKKK RPISTLVEQD DQKKFKLHEL
     TTEEEVLEEY EWDDLDEEDC DDPLMVSEEV NDIFDYLHHL EIITLPNKAN LYKHKNIKQN
     RDILVNWIIK IHNKFGLLPE TLYLAINIMD RFLCEEVVQL NRLQLVGTSC LFIASKYEEI
     YSPSIKHFAY ETDGACSVED IKEGERFILE KLDFQISFAN PMNFLRRISK ADDYDIQSRT
     LAKFLMEISI VDFKFIGILP SLCASAAMFL SRKMLGKGTW DGNLIHYSGG YTKAKLYPVC
     QLLMDYLVGS TIHDEFLKKY QSRRFLKASI ISIEWALKVR KNGYDIMTLH E
 
 
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