CCNB2_MOUSE
ID CCNB2_MOUSE Reviewed; 398 AA.
AC P30276; Q922E9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=G2/mitotic-specific cyclin-B2;
GN Name=Ccnb2; Synonyms=Cycb2;
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 TISSUE=Testis;
RX PubMed=8375336; DOI=10.1242/dev.118.1.229;
RA Chapman D.L., Wolgemuth D.J.;
RT "Isolation of the murine cyclin B2 cDNA and characterization of the lineage
RT and temporal specificity of expression of the B1 and B2 cyclins during
RT oogenesis, spermatogenesis and early embryogenesis.";
RL Development 118:229-240(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 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.
CC -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is abruptly
CC destroyed at mitosis.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; X66032; CAA46831.1; -; mRNA.
DR EMBL; AK076122; BAC36200.1; -; mRNA.
DR EMBL; CT010286; CAJ18494.1; -; mRNA.
DR EMBL; CH466522; EDL26195.1; -; Genomic_DNA.
DR EMBL; BC008247; AAH08247.1; -; mRNA.
DR CCDS; CCDS23320.1; -.
DR PIR; I48315; S21529.
DR RefSeq; NP_031656.2; NM_007630.2.
DR AlphaFoldDB; P30276; -.
DR SMR; P30276; -.
DR ComplexPortal; CPX-2070; Cyclin B2-CDK1 complex.
DR STRING; 10090.ENSMUSP00000034742; -.
DR iPTMnet; P30276; -.
DR PhosphoSitePlus; P30276; -.
DR EPD; P30276; -.
DR jPOST; P30276; -.
DR MaxQB; P30276; -.
DR PaxDb; P30276; -.
DR PeptideAtlas; P30276; -.
DR PRIDE; P30276; -.
DR ProteomicsDB; 281336; -.
DR Antibodypedia; 1393; 627 antibodies from 37 providers.
DR DNASU; 12442; -.
DR Ensembl; ENSMUST00000034742; ENSMUSP00000034742; ENSMUSG00000032218.
DR GeneID; 12442; -.
DR KEGG; mmu:12442; -.
DR UCSC; uc009qny.1; mouse.
DR CTD; 9133; -.
DR MGI; MGI:88311; Ccnb2.
DR VEuPathDB; HostDB:ENSMUSG00000032218; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000155405; -.
DR HOGENOM; CLU_020695_2_1_1; -.
DR InParanoid; P30276; -.
DR OMA; QPTKTNV; -.
DR OrthoDB; 993640at2759; -.
DR PhylomeDB; P30276; -.
DR TreeFam; TF101001; -.
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-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-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR BioGRID-ORCS; 12442; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ccnb2; mouse.
DR PRO; PR:P30276; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P30276; protein.
DR Bgee; ENSMUSG00000032218; Expressed in fetal liver hematopoietic progenitor cell and 194 other tissues.
DR Genevisible; P30276; MM.
DR GO; GO:0005813; C:centrosome; 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:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008315; P:G2/MI transition of meiotic cell cycle; IDA:MGI.
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:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR GO; GO:0007057; P:spindle assembly involved in female meiosis I; IDA:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP: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 Cell cycle; Cell division; Cyclin; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..398
FT /note="G2/mitotic-specific cyclin-B2"
FT /id="PRO_0000080363"
FT REGION 65..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 62
FT /note="P -> S (in Ref. 1; CAA46831)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> G (in Ref. 1; CAA46831)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="L -> V (in Ref. 1; CAA46831)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..379
FT /note="STI -> KHD (in Ref. 1; CAA46831)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> V (in Ref. 1; CAA46831)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45383 MW; 8AB8F569550BE32C CRC64;
MALLRRPTVS SDLKNIDTEV IPKAKSHVTI RRAVLEEIGN KVRNRTTQVA KKPQNTKVPA
LPTKVTNVNK QPKPTASVKP VQMEALAPKD RPPAPEDVSM KEESLCQAFS DALLCKIEDI
DNEDRENPQL CSDYVKDIYQ YLRQLEVLQS INPHFLDGRD INGRMRAILV DWLVQVHSKF
RLLQETLYMC IAIMDRFLQA QLVCRKKLQL VGITALLLAS KYEEMFSPNI EDFVYITDNA
YTSSQIREME TLILKELKFE LGRPLPLHFL RRASKAGEVD VEQHTLAKYL MELTLVDYDM
VHYHPSQVAA AASCLSQKVL GQGKWNLKQQ YYTGYMESEV LEVMQHMAKN VVKVNDNRTK
FIAVKNKYAS SRLLKISTIP QLNSKIIKDL ASPLLGSP
