CCNB1_BOVIN
ID CCNB1_BOVIN Reviewed; 427 AA.
AC Q1LZG6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=G2/mitotic-specific cyclin-B1;
GN Name=CCNB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition. {ECO:0000250}.
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-127 on centrosomes during prophase:
CC phosphorylation by PLK1 does not cause nuclear import. Phosphorylation
CC at Ser-141 was also reported to be mediated by PLK1 but Ser-127 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; BC116011; AAI16012.1; -; mRNA.
DR RefSeq; NP_001039337.1; NM_001045872.1.
DR AlphaFoldDB; Q1LZG6; -.
DR SMR; Q1LZG6; -.
DR STRING; 9913.ENSBTAP00000025670; -.
DR PaxDb; Q1LZG6; -.
DR PRIDE; Q1LZG6; -.
DR Ensembl; ENSBTAT00000025670; ENSBTAP00000025670; ENSBTAG00000014239.
DR GeneID; 327679; -.
DR KEGG; bta:327679; -.
DR CTD; 891; -.
DR VEuPathDB; HostDB:ENSBTAG00000014239; -.
DR VGNC; VGNC:26958; CCNB1.
DR eggNOG; KOG0653; Eukaryota.
DR GeneTree; ENSGT00940000154586; -.
DR HOGENOM; CLU_020695_2_1_1; -.
DR InParanoid; Q1LZG6; -.
DR OMA; GQTKHMA; -.
DR OrthoDB; 993640at2759; -.
DR TreeFam; TF101001; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000014239; Expressed in oocyte and 95 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097125; C:cyclin B1-CDK1 complex; IBA:GO_Central.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
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..427
FT /note="G2/mitotic-specific cyclin-B1"
FT /id="PRO_0000282330"
FT REGION 33..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..171
FT /note="Interaction with CDK2"
FT /evidence="ECO:0000250"
FT REGION 252..255
FT /note="Interaction with CDK2"
FT /evidence="ECO:0000250"
FT COMPBIAS 96..112
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 120
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 127
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
FT MOD_RES 315
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14635"
SQ SEQUENCE 427 AA; 47658 MW; D74D586F0FCD610D CRC64;
MALRITRNTK ISAENKAKIS MAGAKRVPVA AVATSKPGLR PRTALGDIGN KVSEQPQAKL
PLKKEAKTLA SGKVTAKKVP KPLEKAPVPV PEPQPEPEPE PEHVKEDKLS PEPILVDTPS
PSPMETSGCA PAEEYLCQAF SDVILAVSDV DAEDGADPNL CSEYVKDIYA YLRQLEEEQA
VKPKYLMGRE VTGNMRAILI DWLVQVQIKF RLLQETMYMT VSIIDRFMQD TYVPKKMLQL
VGVTAMFVAS KYEEMYPPEI GDFAFVTDNT YTKFQIRQME MKILRALNFS LGRPLPLHFL
RRASKIGEVD VELHTLAKYL MELTMLDYDM VHFPPSQIAA GAFCLALKVL DNGEWTPTLQ
HYLSYTEESL LVVMQHLAKN VVMVNRGLTK HMTIKNKYAT SKHAKISTLA QLNSALVQDL
AKAVAKV
