CCNB1_CRIGR
ID CCNB1_CRIGR Reviewed; 429 AA.
AC Q08301;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=G2/mitotic-specific cyclin-B1;
GN Name=CCNB1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
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).
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}.
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DR EMBL; X64588; CAA45876.1; -; mRNA.
DR PIR; S34224; S34224.
DR RefSeq; XP_003506318.3; XM_003506270.3.
DR AlphaFoldDB; Q08301; -.
DR SMR; Q08301; -.
DR STRING; 10029.XP_007623068.1; -.
DR Ensembl; ENSCGRT00001003708; ENSCGRP00001002713; ENSCGRG00001003079.
DR GeneID; 100770842; -.
DR KEGG; cge:100770842; -.
DR CTD; 891; -.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154586; -.
DR OMA; CAEENCQ; -.
DR OrthoDB; 993640at2759; -.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097125; C:cyclin B1-CDK1 complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0005113; F:patched binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IEA:Ensembl.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:Ensembl.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1905448; P:positive regulation of mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IEA:Ensembl.
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; Ubl conjugation.
FT CHAIN 1..429
FT /note="G2/mitotic-specific cyclin-B1"
FT /id="PRO_0000080349"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..128
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 1..19
FT /note="Polar 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; 48062 MW; 6E0BAE7511A678B7 CRC64;
MALRVTRNTK LNTENKAKVS MTGAKRVPVA IAAASKPGLR PRTALGDIGN KVSEQAQARV
PLKKELKTSV TGKVSAKIPP PKPQEKVPVS EPEVELAEPE PEPEPVMEEK LSPEPILVDN
PSPSPMETSG CAPAEEYLCQ AFSDVILAVS DVDADDGADP NLCSEYVKDI YAYLRQLEEE
QSVRPRYLLG REVTGNMRAI LIDWLIQVQM KFRLLQETMY MTVSIIDRFM QDNCVPKKML
QLVGVTAMFI ASKYEEMYPP EIGDFAFVTN NTYTKHQIRQ MEMKILRVLN FSLGRPLPLH
FLRRASKIGE VDVEQHTLAK YLMELTMLDY DMVHFAPSQI AAGAFCLALK ILDNGEWTPT
LQHYLSYTEE SLLPVMQHLA KNVVMVNRGL TKHMTIKNKY ATSKHAKIST LAQLNCTLVQ
NLSKAVSKA
