CCNB3_MOUSE
ID CCNB3_MOUSE Reviewed; 1396 AA.
AC Q810T2; Q810T3; Q8VDC8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=G2/mitotic-specific cyclin-B3;
GN Name=Ccnb3; Synonyms=Cycb3;
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] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ; TISSUE=Testis;
RA Lozano J.-C., Schatt P., Picard A.;
RT "Cloning of two mRNA coding for two isoforms of mouse cyclin B3.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1159-1396, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12185076; DOI=10.1074/jbc.m203951200;
RA Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y.,
RA Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.;
RT "Characterization and expression of mammalian cyclin b3, a prepachytene
RT meiotic cyclin.";
RL J. Biol. Chem. 277:41960-41969(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, 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: Cyclins are positive regulatory subunits of the cyclin-
CC dependent kinases (CDKs), and thereby play an essential role in the
CC control of the cell cycle, notably via their destruction during cell
CC division. Its tissue specificity suggest that it may be required during
CC early meiotic prophase I (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDK2 kinase. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q810T2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q810T2-2; Sequence=VSP_010516;
CC -!- TISSUE SPECIFICITY: Expressed in testis. Also expressed in the fetal
CC ovary, but not in the adult. {ECO:0000269|PubMed:12185076}.
CC -!- DEVELOPMENTAL STAGE: In testis, it is expressed during a narrow window
CC of meiosis, beginning at the onset of the first meiotic prophase and
CC ending by the pachytene stage. Expressed during leptoten and zygotene
CC stages of spermatogenesis. {ECO:0000269|PubMed:12185076}.
CC -!- DOMAIN: The N-terminal destruction box (D-box) probably acts as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway. {ECO:0000250}.
CC -!- PTM: Ubiquitinated (Probable). Ubiquitination leads to its degradation
CC during anaphase entry, after degradation of CCNB1 (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ555464; CAD88194.1; -; mRNA.
DR EMBL; AJ555465; CAD88195.1; -; mRNA.
DR EMBL; AJ416459; CAC94916.1; -; mRNA.
DR CCDS; CCDS29961.1; -. [Q810T2-1]
DR AlphaFoldDB; Q810T2; -.
DR SMR; Q810T2; -.
DR ComplexPortal; CPX-2071; Cyclin B3-CDK2 complex.
DR STRING; 10090.ENSMUSP00000111418; -.
DR iPTMnet; Q810T2; -.
DR PhosphoSitePlus; Q810T2; -.
DR PaxDb; Q810T2; -.
DR PRIDE; Q810T2; -.
DR ProteomicsDB; 280011; -. [Q810T2-1]
DR ProteomicsDB; 280012; -. [Q810T2-2]
DR UCSC; uc012hdx.1; mouse. [Q810T2-2]
DR MGI; MGI:2183443; Ccnb3.
DR eggNOG; KOG0653; Eukaryota.
DR InParanoid; Q810T2; -.
DR PhylomeDB; Q810T2; -.
DR ChiTaRS; Ccnb3; mouse.
DR PRO; PR:Q810T2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q810T2; protein.
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; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; 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:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR015452; Cyclin_B3.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF214; PTHR10177:SF214; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cyclin; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1396
FT /note="G2/mitotic-specific cyclin-B3"
FT /id="PRO_0000080374"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 54..62
FT /note="D-box"
FT COMPBIAS 9..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 206..1108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010516"
FT CONFLICT 10
FT /note="S -> P (in Ref. 1; CAD88195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="D -> G (in Ref. 1; CAD88195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1392
FT /note="C -> W (in Ref. 1; CAD88195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1396 AA; 158969 MW; 878FB226546F7FC0 CRC64;
MPPPLLPKRS KLETEKAQSN KITPREEQQS EKIGKSNHAA SSSSSSTQGA VKRRSVFEDV
TNASHSQCVQ SKEDNIELKS HVSKRTKKGV GEVTQKKIKS SKMGHVTSLS NMEKEFILDI
PNKPKTLTTE EPSVFQKTLV LNEEPATKET CLMRKTLKSC AFHQETLLME KPLTLLVETE
DYNEFDTELM TSKKKDKPED PTIIEEMTDL KKSVIRKVTL TSSPLWLKNK HVVQEEKPVI
QEKSSFKRIS LVSNVVTTKE KPPVKKPHFR KKKPTTEMKS LLQEPSLEEK YNTQEDASIL
KKPQVLQENT NNKDATLTEP VTFKGKHSAN EATHTKKPSS SKNNPDPQGK GTNLRPLRVH
PVTYENEPMS SKKSTTKKKD SHFHGPSVLP DKHSPQMEVS TVKKSLALPN PTTEEKMLHF
PVATVLEKQH NMGEAPCLKK PSPLRKQQQL PKRRRFFSNS AVQETVIRKP LFFKMSTTEK
DPPSQWPSAL PKKHISPGEL SKQKKQHVSP KHNMEEDSQC WLDSAFKKQL SREEPASTHT
PLKLEMQQAI TKETGFHLRN PLVLPTVTSE AKSLTKEPPS FREQNTSLLK RKSTTHTITL
QQAQSEWQEM TDEDRNLFSI KPGSHRKEPI PEFLQNPLPP NENCLISQKL SHSMPFASQK
TTSQERAHRK ESVASNDDKN FFSQDLFSPF SSADEDTLKF HKSLDFQEQV DRKNDSHKKM
FDSQDSVSEE ESFLRKLFCK DRCSSTEELS QERTVALEQE FLLIKILNEN TSSDVDEPLS
HQSPHIQNHS DTTKEALEAS EALEAPEALE TLEALVASED LEEPLNILEE LSTENMVALM
KMLVTEDEST KDSFSGNYTA AREAHAEKSL SLEETSINEA ATLKESLSSQ EKHRAELVTV
LKELLVLMKN PSLKRVALAF QENPSNNVET LLREVLALVE NSTADESTLQ EKPSTKTDVT
PKELLALEEN SSNKKANPMD SLSFDHKPDT EMGEIARMVL TDEEYNIDTL YERVLALSQG
LIAADQLSFT DLQNFEETKI VDEEEFFKSF LVFENKNSPN MSSNAFESRT DNSSAIMPSS
KAFNPVENSN PYVSSSKSFK STLGAKETEI TIQDDSDSLE RIEKEGQDPL LNTIYAKDVF
NYLKEREEKF LVQKYMDGQM ELTSDMRAIL VDWLVEIQGS FQMTHETLYL AVKIMDLYLM
KAQCKKNHLQ LLGSTTYMIA AKFEESYPPS LSEFLFICED MYEKSDMVSL ESSILQTLNF
DINIPTAYNF LRRYASCIHA SMKTLTLSRF ICEMTLQEYE YIEERPSKLA AASFILALYM
RNLSNCVPTL EYFTGYKMAE LHILVRKLNH LLNFRSHSIL KNVFEKYSEE TYFEVAKIPP
LSKQDLENLL NCALFH
