ID   CCNB2_XENLA             Reviewed;         392 AA.
AC   P13351; Q498K5;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=G2/mitotic-specific cyclin-B2;
GN   Name=ccnb2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=2564315; DOI=10.1016/0092-8674(89)90628-4;
RA   Minshull J., Blow J.J., Hunt T.;
RT   "Translation of cyclin mRNA is necessary for extracts of activated Xenopus
RT   eggs to enter mitosis.";
RL   Cell 56:947-956(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH NAP1L1.
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   [4]
RP   INTERACTION WITH SPDYA.
RC   TISSUE=Oocyte;
RX   PubMed=10465793; DOI=10.1101/gad.13.16.2177;
RA   Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R.;
RT   "A novel p34cdc2 binding and activating protein that is necessary and
RT   sufficient to trigger G2/M progression in Xenopus oocytes.";
RL   Genes Dev. 13:2177-2189(1999).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition. {ECO:0000269|PubMed:2564315}.
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. When not in a complex with cdk1, interacts
CC       with spdya. Interacts with nap1l1. {ECO:0000269|PubMed:10465793,
CC       ECO:0000269|PubMed:7622566}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC       destroyed at mitosis. {ECO:0000269|PubMed:2564315}.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; J03167; AAA49697.1; -; mRNA.
DR   EMBL; BC100180; AAI00181.1; -; mRNA.
DR   PIR; B32370; B32370.
DR   RefSeq; NP_001081268.1; NM_001087799.1.
DR   AlphaFoldDB; P13351; -.
DR   SMR; P13351; -.
DR   BioGRID; 99082; 4.
DR   DIP; DIP-60880N; -.
DR   IntAct; P13351; 2.
DR   iPTMnet; P13351; -.
DR   DNASU; 397743; -.
DR   GeneID; 397743; -.
DR   KEGG; xla:397743; -.
DR   AGR; Xenbase:XB-GENE-1005605; -.
DR   CTD; 397743; -.
DR   Xenbase; XB-GENE-1005605; ccnb2.S.
DR   OMA; QPTKTNV; -.
DR   OrthoDB; 5474295at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 397743; Expressed in egg cell and 16 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR   CDD; cd20566; CYCLIN_CCNB2_rpt1; 1.
DR   CDD; cd20570; CYCLIN_CCNB2_rpt2; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   InterPro; IPR039361; Cyclin.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR046965; Cyclin_A/B-like.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   PANTHER; PTHR10177; CYCLINS; 1.
DR   PANTHER; PTHR10177:SF184; G2_MITOTIC-SPECIFIC CYCLIN-B2; 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; Cyclin-like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Mitosis; Reference proteome.
FT   CHAIN           1..392
FT                   /note="G2/mitotic-specific cyclin-B2"
FT                   /id="PRO_0000080371"
SQ   SEQUENCE   392 AA;  43625 MW;  87295E04C106218E CRC64;
     MATRRAAIPR EADNILGGAM RSKVQMNSRR AALGEIGNKV TVRGKPPAVK QSSNAVAKPS
     KMAATKVANV KTKHVPVKPV VAEAAPKVPS PVPMDVSLKE EELCQAFSDA LTSVEDIDAD
     DGGNPQLCSD YVMDIYNYLK QLEVQQSVHP CYLEGKEINE RMRAILVDWL VQVHSRFQLL
     QETLYMGVAI MDRFLQVQPV SRSKLQLVGV TSLLIASKYE EMYTPEVADF VYITDNAYTA
     SQIREMEMII LRLLNFDLGR PLPLHFLRRA SKSCSADAEQ HTLAKYLMEL TLIDYEMVHI
     KPSEIAAAAL CLSQKILGQG TWGTTQHYYT GYTEGDLQLI MKHMAKNITK VNQNLTKHVA
     VRNKYASSKL MKISTLPQLM APLITELAAS LS
//