CCNB1_MOUSE
ID CCNB1_MOUSE Reviewed; 430 AA.
AC P24860;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=G2/mitotic-specific cyclin-B1;
GN Name=Ccnb1; Synonyms=Ccn-2, Ccnb1-rs13, Cycb, Cycb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster; TISSUE=Testis;
RX PubMed=1280449; DOI=10.1002/mrd.1080330305;
RA Chapman D.L., Wolgemuth D.J.;
RT "Identification of a mouse B-type cyclin which exhibits developmentally
RT regulated expression in the germ line.";
RL Mol. Reprod. Dev. 33:259-269(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/He;
RX PubMed=1836195; DOI=10.1016/0378-1119(91)90454-j;
RA Paterno G.D., Downs K.M.;
RT "Sequence of a cDNA encoding a mouse cyclin B protein.";
RL Gene 108:315-316(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1387105; DOI=10.1016/0888-7543(92)90015-k;
RA Hanley-Hyde J., Mushinski J.F., Sadofsky M., Huppi K., Krall M.,
RA Kozak C.A., Mock B.;
RT "Expression of murine cyclin B1 mRNAs and genetic mapping of related
RT genomic sequences.";
RL Genomics 13:1018-1030(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium;
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).
RN [5]
RP INTERACTION WITH RFPL4A AND UBE2A.
RX PubMed=12525704; DOI=10.1073/pnas.0234474100;
RA Suzumori N., Burns K.H., Yan W., Matzuk M.M.;
RT "RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome
RT degradation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:550-555(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC Interacts with RFPL4A and UBE2A (PubMed:12525704). Interacts with INCA1
CC (By similarity). {ECO:0000250|UniProtKB:P14635,
CC ECO:0000269|PubMed:12525704}.
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-130 on centrosomes during prophase:
CC phosphorylation by PLK1 does not cause nuclear import. Phosphorylation
CC at Ser-144 was also reported to be mediated by PLK1 but Ser-130 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; X64713; CAA45968.1; -; mRNA.
DR EMBL; X58708; CAA41545.1; -; mRNA.
DR EMBL; S43105; AAB22970.1; -; mRNA.
DR EMBL; BC011478; AAH11478.1; -; mRNA.
DR EMBL; BC085238; AAH85238.1; -; mRNA.
DR CCDS; CCDS36768.1; -.
DR PIR; A43285; A43285.
DR PIR; I48316; I48316.
DR PIR; JH0509; JH0509.
DR RefSeq; NP_758505.2; NM_172301.3.
DR AlphaFoldDB; P24860; -.
DR SMR; P24860; -.
DR BioGRID; 234538; 11.
DR ComplexPortal; CPX-2069; Cyclin B1-CDK1 complex.
DR CORUM; P24860; -.
DR IntAct; P24860; 2.
DR MINT; P24860; -.
DR STRING; 10090.ENSMUSP00000071989; -.
DR iPTMnet; P24860; -.
DR PhosphoSitePlus; P24860; -.
DR EPD; P24860; -.
DR PaxDb; P24860; -.
DR PeptideAtlas; P24860; -.
DR PRIDE; P24860; -.
DR ProteomicsDB; 281126; -.
DR Antibodypedia; 3537; 1897 antibodies from 46 providers.
DR DNASU; 268697; -.
DR Ensembl; ENSMUST00000072119; ENSMUSP00000071989; ENSMUSG00000041431.
DR GeneID; 268697; -.
DR KEGG; mmu:268697; -.
DR UCSC; uc007rro.1; mouse.
DR CTD; 891; -.
DR MGI; MGI:88302; Ccnb1.
DR VEuPathDB; HostDB:ENSMUSG00000041431; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154586; -.
DR InParanoid; P24860; -.
DR OMA; GQTKHMA; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; P24860; -.
DR TreeFam; TF101001; -.
DR Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR Reactome; R-MMU-176417; Phosphorylation of Emi1.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
DR Reactome; R-MMU-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-MMU-68875; Mitotic Prophase.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-69478; G2/M DNA replication checkpoint.
DR Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8878166; Transcriptional regulation by RUNX2.
DR BioGRID-ORCS; 268697; 24 hits in 75 CRISPR screens.
DR ChiTaRS; Ccnb1; mouse.
DR PRO; PR:P24860; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P24860; protein.
DR Bgee; ENSMUSG00000041431; Expressed in secondary oocyte and 168 other tissues.
DR ExpressionAtlas; P24860; baseline and differential.
DR Genevisible; P24860; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097125; C:cyclin B1-CDK1 complex; ISO:MGI.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000940; C:outer kinetochore; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0005113; F:patched binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0001556; P:oocyte maturation; ISO:MGI.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; ISO:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; IDA:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0060623; P:regulation of chromosome condensation; ISO:MGI.
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:MGI.
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 Acetylation; Cell cycle; Cell division; Cyclin; Cytoplasm; Cytoskeleton;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..430
FT /note="G2/mitotic-specific cyclin-B1"
FT /id="PRO_0000080352"
FT REGION 166..174
FT /note="Interaction with CDK2"
FT /evidence="ECO:0000250"
FT REGION 255..258
FT /note="Interaction with CDK2"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 123
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 130
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT CONFLICT 25
FT /note="K -> M (in Ref. 1; CAA45968)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="R -> T (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="S -> C (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="L -> P (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> S (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="L -> I (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="E -> D (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="E -> R (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="Y -> C (in Ref. 1; CAA45968)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..343
FT /note="QIAA -> RAFS (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="K -> E (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="L -> H (in Ref. 2; CAA41545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 48052 MW; F3BC9C856F66986E CRC64;
MALRVTRNTK INAENKAKVS MAGAKRVPVT VTAASKPGLR PRTALGDIGN KVSEELQARV
PLKREAKTLG TGKGTVKALP KPVEKVPVCE PEVELAEPEP EPELEHVREE KLSPEPILVD
NPSPSPMETS GCAPAEEYLC QAFSDVILAV SDVDADDGAD PNLCSEYVKD IYAYLRQLEE
EQSVRPKYLQ GREVTGNMRA ILIDWLIQVQ MKFRLLQETM YMTVSIIDRF MQNSCVPKKM
LQLVGVTAMF IASKYEEMYP PEIGDFAFVT NNTYTKHQIR QMEMKILRVL NFSLGRPLPL
HFLRRASKVG EVDVEQHTLA KYLMELSMLD YDMVHFAPSQ IAAGAFCLAL KILDNGEWTP
TLQHYLSYSE DSLLPVMQHL AKNVVMVNCG LTKHMTVKNK YAASKHAKIS TLAQLNCTLV
QNLSKAVTKA
