CCNB1_CAEEL
ID CCNB1_CAEEL Reviewed; 361 AA.
AC Q10653;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=G2/mitotic-specific cyclin-B1;
GN Name=cyb-1; ORFNames=ZC168.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=7545687; DOI=10.1242/jcs.108.6.2415;
RA Kreutzer M.A., Richards J.P., de Silva-Udawatta M.N., Temenak J.J.,
RA Knoblich J.A., Lehner C.F., Bennett K.L.;
RT "Caenorhabditis elegans cyclin A- and B-type genes: a cyclin A multigene
RT family, an ancestral cyclin B3 and differential germline expression.";
RL J. Cell Sci. 108:2415-2424(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP INTERACTION WITH ETC-1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP UBIQUITINATION.
RX PubMed=23578927; DOI=10.1242/dev.090688;
RA Wang R., Kaul Z., Ambardekar C., Yamamoto T.G., Kavdia K., Kodali K.,
RA High A.A., Kitagawa R.;
RT "HECT-E3 ligase ETC-1 regulates securin and cyclin B1 cytoplasmic abundance
RT to promote timely anaphase during meiosis in C. elegans.";
RL Development 140:2149-2159(2013).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition. {ECO:0000250|UniProtKB:P14635}.
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) (By similarity). The cyclin subunit imparts
CC substrate specificity to the complex (By similarity). Interacts with E3
CC ubiquitin-protein ligase etc-1 (PubMed:23578927).
CC {ECO:0000250|UniProtKB:P14635, ECO:0000269|PubMed:23578927}.
CC -!- INTERACTION:
CC Q10653; Q9U2G4: puf-3; NbExp=3; IntAct=EBI-330851, EBI-330810;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23578927}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mature oocytes followed by a severe
CC reduction in protein levels as meiotic division progresses
CC (PubMed:23578927). {ECO:0000269|PubMed:23578927}.
CC -!- PTM: Ubiquitinated by etc-1 likely during meiosis, resulting in its
CC degradation. {ECO:0000269|PubMed:23578927}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; U20903; AAA84394.1; -; mRNA.
DR EMBL; Z70312; CAA94384.1; -; Genomic_DNA.
DR PIR; T27504; T27504.
DR RefSeq; NP_501987.1; NM_069586.5.
DR AlphaFoldDB; Q10653; -.
DR SMR; Q10653; -.
DR BioGRID; 43066; 4.
DR IntAct; Q10653; 2.
DR STRING; 6239.ZC168.4.2; -.
DR EPD; Q10653; -.
DR PaxDb; Q10653; -.
DR PeptideAtlas; Q10653; -.
DR EnsemblMetazoa; ZC168.4.1; ZC168.4.1; WBGene00000865.
DR EnsemblMetazoa; ZC168.4.2; ZC168.4.2; WBGene00000865.
DR GeneID; 177965; -.
DR KEGG; cel:CELE_ZC168.4; -.
DR UCSC; ZC168.4.2; c. elegans.
DR CTD; 177965; -.
DR WormBase; ZC168.4; CE06570; WBGene00000865; cyb-1.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000168350; -.
DR HOGENOM; CLU_020695_2_0_1; -.
DR InParanoid; Q10653; -.
DR OMA; ASKCCSA; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; Q10653; -.
DR Reactome; R-CEL-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-CEL-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-CEL-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-CEL-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-CEL-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-CEL-69478; G2/M DNA replication checkpoint.
DR Reactome; R-CEL-8878166; Transcriptional regulation by RUNX2.
DR SignaLink; Q10653; -.
DR PRO; PR:Q10653; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000865; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:WormBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:WormBase.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0001556; P:oocyte maturation; IGI:WormBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:WormBase.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 1.
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 SMART; SM00385; CYCLIN; 1.
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; Mitosis; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..361
FT /note="G2/mitotic-specific cyclin-B1"
FT /id="PRO_0000080380"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 40519 MW; 2B76FE39E0248C9D CRC64;
MLRATNNRRT SNNVEKDSLQ MAKHGNGPLK PVNAQGLQTK REAREILALK PSNPAPVETA
QKSQRINLQD AETKCLAMAD DIYKYLVHHE KKYLLEECFM EGGEPTPKMR RILVDWLVQV
HVRFHLTPET LHLTVFILDR MLQKKVTSKA DLQLLGISAM FVASKFEEVY LPDIHDYEFI
TENTYSKKQI LAMEQTILNS LNFDLSCPSS LVFLRCLSRI LSENDASPID NQAFCYTYNI
SKCLGELALL DSVMASTPRS HIASASMIIA LEVHPVDGIE AENAVSVICK QLGASKKVIE
DAVALLAEVS YKNFKQGKLV AIKNKYQSSK LAQVSNLMTD DVLEKINRMG QNAKVDASEM
E