CCNB1_RAT
ID CCNB1_RAT Reviewed; 423 AA.
AC P30277;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=G2/mitotic-specific cyclin-B1;
GN Name=Ccnb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kanaoka Y., Nojima H., Okayama H.;
RT "Nucleotide sequences of cDNAs encoding rat cdc2 + and cyclin 2.";
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Fibroblast;
RX PubMed=8270434; DOI=10.1016/0360-3016(94)90151-1;
RA Markiewicz D.A., McKenna W.G., Flick M.B., Maity A., Muschel R.J.;
RT "The effects of radiation on the expression of a newly cloned and
RT characterized rat cyclin B mRNA.";
RL Int. J. Radiat. Oncol. Biol. Phys. 28:135-144(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8123599;
RA Trembley J.H., Kren B.T., Steer C.J.;
RT "Posttranscriptional regulation of cyclin B messenger RNA expression in the
RT regenerating rat liver.";
RL Cell Growth Differ. 5:99-108(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition.
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. Binds HEI10. Interacts with catalytically
CC active RALBP1 and CDC2 during mitosis to form an endocytotic complex
CC during interphase. Interacts with CCNF; interaction is required for
CC nuclear localization. Interacts with CDK5RAP3. Interacts with RFPL4A
CC and UBE2A. Interacts with INCA1. {ECO:0000250|UniProtKB:P14635,
CC ECO:0000250|UniProtKB:P24860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC destroyed at mitosis.
CC -!- PTM: Ubiquitinated by the SCF(NIPA) complex during interphase, leading
CC to its destruction. Not ubiquitinated during G2/M phases (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by PLK1 at Ser-123 on centrosomes during prophase:
CC phosphorylation by PLK1 does not cause nuclear import. Phosphorylation
CC at Ser-137 was also reported to be mediated by PLK1 but Ser-123 seems
CC to be the primary phosphorylation site (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; X60768; CAA43178.1; -; mRNA.
DR EMBL; X64589; CAA45877.1; -; mRNA.
DR EMBL; L11995; AAC00032.1; -; mRNA.
DR EMBL; BC059113; AAH59113.1; -; mRNA.
DR PIR; S34226; S34226.
DR RefSeq; NP_741988.1; NM_171991.3.
DR AlphaFoldDB; P30277; -.
DR SMR; P30277; -.
DR ComplexPortal; CPX-2072; Cyclin B1-CDK1 complex.
DR CORUM; P30277; -.
DR IntAct; P30277; 1.
DR STRING; 10116.ENSRNOP00000025297; -.
DR BindingDB; P30277; -.
DR ChEMBL; CHEMBL2093; -.
DR iPTMnet; P30277; -.
DR PhosphoSitePlus; P30277; -.
DR PaxDb; P30277; -.
DR Ensembl; ENSRNOT00000103969; ENSRNOP00000095719; ENSRNOG00000058539.
DR GeneID; 25203; -.
DR KEGG; rno:25203; -.
DR UCSC; RGD:2291; rat.
DR CTD; 891; -.
DR RGD; 2291; Ccnb1.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154586; -.
DR HOGENOM; CLU_020695_2_1_1; -.
DR InParanoid; P30277; -.
DR OMA; GQTKHMA; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; P30277; -.
DR TreeFam; TF101001; -.
DR Reactome; R-RNO-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-RNO-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-RNO-176412; Phosphorylation of the APC/C.
DR Reactome; R-RNO-176417; Phosphorylation of Emi1.
DR Reactome; R-RNO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
DR Reactome; R-RNO-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-RNO-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-RNO-68875; Mitotic Prophase.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-RNO-69478; G2/M DNA replication checkpoint.
DR Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR PRO; PR:P30277; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000058539; Expressed in thymus and 18 other tissues.
DR Genevisible; P30277; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097125; C:cyclin B1-CDK1 complex; ISO:RGD.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0000940; C:outer kinetochore; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; ISO:RGD.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; ISO:RGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0005113; F:patched binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071283; P:cellular response to iron(III) ion; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; IEP:RGD.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0001556; P:oocyte maturation; IMP:RGD.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; ISO:RGD.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IDA:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; IMP:RGD.
DR GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; ISO:RGD.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; IMP:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; IEP:RGD.
DR GO; GO:0060623; P:regulation of chromosome condensation; IMP:RGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISO:RGD.
DR GO; GO:0046680; P:response to DDT; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0042246; P:tissue regeneration; IEP:RGD.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IEP:RGD.
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; Cytoplasm; Cytoskeleton; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..423
FT /note="G2/mitotic-specific cyclin-B1"
FT /id="PRO_0000080353"
FT REGION 159..167
FT /note="Interaction with CDK2"
FT /evidence="ECO:0000250"
FT REGION 248..251
FT /note="Interaction with CDK2"
FT /evidence="ECO:0000250"
FT MOD_RES 116
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 123
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
SQ SEQUENCE 423 AA; 47391 MW; 4223CF71F144B279 CRC64;
MALRVTRNTK INTENKAKVS MAGAKRVPVA VAASKPLLRS RTALGDIGNK VSEQSRIPLK
KETKKLGSGT VTVKALPKPV DKVPVCEPEV ELDEPEPEPV MEVKHSPEPI LVDTPSPSPM
ETSGCAPAEE YLCQAFSDVI LAVSDVDADD GGDPNLCSEY VKDIYAYLRQ LEEEQSVRPK
YLLGREVTGN MRAILIDWLI QVQMKFRLLQ ETMYMTVSII DRFMQDSCVP KKMLQLVGVT
AMFIASKYEE MYPPEIGDFA FVTNNTYTKH QIRQMEMKIL RVLNFSLGRP LPLHFLRRAS
KIGEVDVEQH TLAKYLMELS MLDYDMVHFA PSQIAAGAFC LALKILDNGE WTPTLQHYLS
HTEESLLPVM QHLAKNIVMV NRGLTKHMTI KNKYATSKHA KISTLAQLNC TLVQNLSKAV
TKA
