ID   CCNB1_XENLA             Reviewed;         397 AA.
AC   P13350; Q5HZN2;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=G2/mitotic-specific cyclin-B1;
GN   Name=ccnb1;
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=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-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).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9922449; DOI=10.1083/jcb.144.2.213;
RA   Moore J.D., Yang J., Truant R., Kornbluth S.;
RT   "Nuclear import of Cdk/cyclin complexes: identification of distinct
RT   mechanisms for import of Cdk2/cyclin E and Cdc2/cyclin B1.";
RL   J. Cell Biol. 144:213-224(1999).
RN   [6]
RP   INTERACTION WITH NANOS1.
RX   PubMed=21195170; DOI=10.1016/j.mod.2010.12.001;
RA   Lai F., Zhou Y., Luo X., Fox J., King M.L.;
RT   "Nanos1 functions as a translational repressor in the Xenopus germline.";
RL   Mech. Dev. 128:153-163(2011).
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 cdc2 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 cdc2, interacts
CC       with spdya. Interacts with nap1l1. Interacts with nanos1.
CC       {ECO:0000269|PubMed:10465793, ECO:0000269|PubMed:21195170,
CC       ECO:0000269|PubMed:7622566}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000250}. Cytoplasm
CC       {ECO:0000269|PubMed:9922449}. Nucleus {ECO:0000269|PubMed:9922449}.
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; J03166; AAA49696.1; -; mRNA.
DR   EMBL; BC088950; AAH88950.1; -; mRNA.
DR   PIR; A32370; A32370.
DR   RefSeq; NP_001081266.1; NM_001087797.1.
DR   AlphaFoldDB; P13350; -.
DR   SMR; P13350; -.
DR   BioGRID; 99081; 1.
DR   ELM; P13350; -.
DR   IntAct; P13350; 1.
DR   GeneID; 397742; -.
DR   KEGG; xla:397742; -.
DR   CTD; 397742; -.
DR   Xenbase; XB-GENE-5736929; ccnb1.2.S.
DR   OMA; GQTKHMA; -.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 397742; Expressed in egg cell and 17 other tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005113; F:patched binding; IPI:BHF-UCL.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Cytoplasm; Cytoskeleton; Mitosis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..397
FT                   /note="G2/mitotic-specific cyclin-B1"
FT                   /id="PRO_0000080354"
SQ   SEQUENCE   397 AA;  44673 MW;  FBDA648E1258D78F CRC64;
     MSLRVTRNML ANAENNVKTT LAGKRVVATK PGLRPRTALG DIGNKAEVKV PTKKELKPAV
     KAAKKAKPVD KLLEPLKVIE ENVCPKPAQV EPSSPSPMET SGCLPDELCQ AFSDVLIHVK
     DVDADDDGNP MLCSEYVKDI YAYLRSLEDA QAVRQNYLHG QEVTGNMRAI LIDWLVQVQM
     KFRLLQETMF MTVGIIDRFL QEHPVPKNQL QLVGVTAMFL AAKYEEMYPP EIGDFTFVTD
     HTYTKAQIRD MEMKILRVLK FAIGRPLPLH FLRRASKIGE VTAEQHSLAK YLMELVMVDY
     DMVHFTPSQI AAASSCLSLK ILNAGDWTPT LHHYMAYSEE DLVPVMQHMA KNIIKVNKGL
     TKHLTVKNKY ASSKQMKIST IPQLRSDVVV EMARPLM