ID   CCNB1_CARAU             Reviewed;         397 AA.
AC   Q92162;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=G2/mitotic-specific cyclin-B1;
GN   Name=ccnb1;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=1418982; DOI=10.1002/mrd.1080330204;
RA   Hirai T., Yamashita M., Yoshikuni M., Lou Y.H., Nagahama Y.;
RT   "Cyclin B in fish oocytes: its cDNA and amino acid sequences, appearance
RT   during maturation, and induction of p34cdc2 activation.";
RL   Mol. Reprod. Dev. 33:131-140(1992).
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; S48758; AAB24163.1; -; mRNA.
DR   AlphaFoldDB; Q92162; -.
DR   SMR; Q92162; -.
DR   Proteomes; UP000515129; Genome assembly.
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; Reference proteome.
FT   CHAIN           1..397
FT                   /note="G2/mitotic-specific cyclin-B1"
FT                   /id="PRO_0000080379"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   397 AA;  44764 MW;  7FA825BEC12841E5 CRC64;
     MALRVTRNTR LASSENQGAL PGKAAVANKP GLRPRAALGE IGNNPQTRQA LRKKEVKVAP
     KVEAVAEKAP VVQQPKKESP KVQHDVQILS EPSSPVPMET SGCASDDLCQ AFSDVMLNIK
     DVDADDYDNP MLCSEYVKDI YLYLRQLEIE QAVRPKYLEG SEVTGNMRAI LIDWLVQVQI
     KFKLLQETMY MTVAVIDRFL QDHPVPKKQL QLVGVTAMFI ASKYEEMYPP EIADFAFVTD
     RAYTTGQIRD MEMKILRVLD FSFGKPLPLQ FLRRASKIGD VTAEHHTLAK YFLELTMVDY
     DMVHFPPSQV ASARYALTLK VFNCGDWTPT LQHYMGYTED SLVPVMQHIA RNVVRVNEGL
     SKHLAVKNKY SSQKQMRIAS ISQLKSSLIK DLAKQIS