ID   CCNB2_MESAU             Reviewed;         397 AA.
AC   P37883;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=G2/mitotic-specific cyclin-B2;
GN   Name=CCNB2;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shiraki T., Yamashita K., Nishitani H., Nishimoto T.;
RT   "Nucleotide sequence of hamster cyclin B1 and B2 cDNA.";
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition.
CC   -!- SUBUNIT: Interacts with the CDK1 protein kinase to form a
CC       serine/threonine kinase holoenzyme complex also known as maturation
CC       promoting factor (MPF). The cyclin subunit imparts substrate
CC       specificity to the complex.
CC   -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC       destroyed at mitosis.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; D17294; BAA04127.1; -; mRNA.
DR   RefSeq; NP_001268312.1; NM_001281383.1.
DR   AlphaFoldDB; P37883; -.
DR   SMR; P37883; -.
DR   STRING; 10036.XP_005075532.1; -.
DR   GeneID; 101833257; -.
DR   CTD; 9133; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Mitosis; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..397
FT                   /note="G2/mitotic-specific cyclin-B2"
FT                   /id="PRO_0000080362"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O95067"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95067"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95067"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95067"
FT   MOD_RES         391
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95067"
SQ   SEQUENCE   397 AA;  45279 MW;  247DBAA412E6CBBD CRC64;
     MALLRRPTVS SDLKNIDTGV NPKAKSHVTI RRAVLEEIGN KVRSRAAPVA KKPQNTKIPV
     QPTKVTHVNK QPKPTASVKP VQMETLAPKD PPAPEDVSMK EENLCQAFSD ALLCKIEDID
     NEDWENPQLC SDYVKDIYQY LRQLEVLQSI NPHFLDGRDI NGRMRAILVD WLVQVHSKFR
     LLQETLYMCI AIMDRFLQAQ PVCRKKLQLV GITALLLASK YEEMFSPNIE DFVYITDNAY
     TSSQIREMET LILKELKFEL GRPLPLHFLR RASKAGEVDV EQHTLAKYLM ELTLIDYDMV
     HYHPSQVAAA ASCLSQKVLG QGKWNLKQQY YTGYMETEVL EVMQHMAKNV VKVNENLTKF
     IAVKNKYASS RLLKISTIPQ LNSKTIKDLA SPLMGRL