ID   CCNB1_MESAU             Reviewed;         429 AA.
AC   P37882;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=G2/mitotic-specific cyclin-B1;
GN   Name=CCNB1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shiraki T., Yamashita K., Nishitani H., Nishimoto T.;
RT   "Nucleotide sequence of hamster cyclin B1 and B2 cDNA.";
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
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-129 on centrosomes during prophase:
CC       phosphorylation by PLK1 does not cause nuclear import. Phosphorylation
CC       at Ser-143 was also reported to be mediated by PLK1 but Ser-129 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D17293; BAA04126.1; -; mRNA.
DR   RefSeq; NP_001297493.1; NM_001310564.1.
DR   AlphaFoldDB; P37882; -.
DR   SMR; P37882; -.
DR   STRING; 10036.XP_005065657.1; -.
DR   GeneID; 101836169; -.
DR   CTD; 891; -.
DR   eggNOG; KOG0653; Eukaryota.
DR   OrthoDB; 993640at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   Acetylation; Cell cycle; Cell division; Cyclin; Cytoplasm; Cytoskeleton;
KW   Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..429
FT                   /note="G2/mitotic-specific cyclin-B1"
FT                   /id="PRO_0000080351"
FT   REGION          71..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..173
FT                   /note="Interaction with CDK2"
FT                   /evidence="ECO:0000250"
FT   REGION          254..257
FT                   /note="Interaction with CDK2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        95..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P14635"
FT   MOD_RES         122
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:P14635"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14635"
FT   MOD_RES         129
FT                   /note="Phosphoserine; by PLK1"
FT                   /evidence="ECO:0000250|UniProtKB:P14635"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14635"
FT   MOD_RES         317
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P14635"
SQ   SEQUENCE   429 AA;  47901 MW;  FE6FF1016FF06253 CRC64;
     MALRVTRNTK LNTENKAKVS MAGAKAVPVT LAAASKPGLR PRTALGDIGN KVSEQAQARL
     PLKKELKTSV TGKVSAKIPP PKPLEKVPPV SEPEVELAET HEPEPVMDEK LSPEPILVDN
     PSPSPMETSG CAPAEEYLCQ AFSDVILAVS DVDADDGADP NLCSEYVKDI YAYLRQLEEE
     QSVRPKYLLG REVTGNMRAI LIDWLIQVQM KFRLLQETMY MTVSIIDRFM QDNCVPKKML
     QLVGVTAMFI ASKYEEMYPP EIGDFAFVTN NTYTKHQIRQ MEMKILRVLN FSLGRPLPLH
     FLRRTSKIGE VDVEQHTLAK YLMELTLLDY DMVDFAPSQI AAGAFCLALK ILDNGEWTPT
     LQHYLSYTEE SLLPVMQHLA KNVVMVNHGL TKHMTIKNKY ATSKHAKIST LAQLNCTLVQ
     NLSKAVAKA