ID   CCNB_MARGL              Reviewed;         388 AA.
AC   P15206;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=G2/mitotic-specific cyclin-B;
OS   Marthasterias glacialis (Spiny starfish).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Forcipulatacea; Forcipulatida; Asteriidae; Marthasterias.
OX   NCBI_TaxID=7609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2531073; DOI=10.1002/j.1460-2075.1989.tb08456.x;
RA   Labbe J.-C., Capony J.-P., Caput D., Cavadore J.-C., Derancourt J.,
RA   Kaghad M., Lelias J.M., Picard A., Doree M.;
RT   "MPF from starfish oocytes at first meiotic metaphase is a heterodimer
RT   containing one molecule of cdc2 and one molecule of cyclin B.";
RL   EMBO J. 8:3053-3058(1989).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X16628; CAA34624.1; -; mRNA.
DR   PIR; S06012; S06012.
DR   AlphaFoldDB; P15206; -.
DR   SMR; P15206; -.
DR   IntAct; P15206; 1.
DR   BindingDB; P15206; -.
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.
FT   CHAIN           1..388
FT                   /note="G2/mitotic-specific cyclin-B"
FT                   /id="PRO_0000080386"
SQ   SEQUENCE   388 AA;  43787 MW;  3DAAEECA7FBDA917 CRC64;
     MLNGENVDSR IMGKVATRAS SKGVKSTLGT RGALENISNV ARNNLQAGAK KELVKAKRGM
     TKSKATSSLQ SVMGLNVEPM EKAKPQSPEP MDMSEINSAL EAFSQNLLEG VEDIDKNDFD
     NPQLCSEFVN DIYQYMRKLE REFKVRTDYM TIQEITERMR SILIDWLVQV HLRFHLLQET
     LFLTIQILDR YLEVQPVSKN KLQLVGVTSM LIAAKYEEMY PPEIGDFVYI TDNAYTKAQI
     RSMECNILRR LDFSLGKPLC IHFLRRNSKA GGVDGQKHTM AKYLMELTLP EYAFVPYDPS
     EIAAAALCLS SKILEPDMEW GTTLVHYSAY SEDHLMPIVQ KMALVLKNAP TAKFQAVRKK
     YSSAKFMNVS TISALTSSTV MDLADQMC