ID CCNB2_BOVIN Reviewed; 398 AA.
AC O77689; Q17QG1; Q5BIS1; Q5E9U8; Q5EAA0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=G2/mitotic-specific cyclin-B2;
GN Name=CCNB2; Synonyms=CYCB2;
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 [MRNA].
RA Lastro M.T., Ignotz G.G., Currie W.B.;
RT "Bovine cyclin B2 complete cds.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-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 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 (By similarity). {ECO:0000250}.
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; AF080219; AAC31953.1; -; mRNA.
DR EMBL; BT020648; AAX08665.1; -; mRNA.
DR EMBL; BT020669; AAX08686.1; -; mRNA.
DR EMBL; BT020762; AAX08779.1; -; mRNA.
DR EMBL; BT020822; AAX08839.1; -; mRNA.
DR EMBL; BT021153; AAX31335.1; -; mRNA.
DR EMBL; BC118382; AAI18383.1; -; mRNA.
DR RefSeq; NP_776689.2; NM_174264.3.
DR AlphaFoldDB; O77689; -.
DR SMR; O77689; -.
DR STRING; 9913.ENSBTAP00000006943; -.
DR PaxDb; 9913-ENSBTAP00000006943; -.
DR GeneID; 281668; -.
DR KEGG; bta:281668; -.
DR CTD; 9133; -.
DR eggNOG; KOG0653; Eukaryota.
DR HOGENOM; CLU_020695_2_1_1; -.
DR InParanoid; O77689; -.
DR OrthoDB; 5474295at2759; -.
DR TreeFam; TF101001; -.
DR Proteomes; UP000009136; Unplaced.
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:0015630; C:microtubule cytoskeleton; ISS:AgBase.
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:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR CDD; cd20570; CYCLIN_CCNB2_rpt2; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR046965; Cyclin_A/B-like.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF184; G2_MITOTIC-SPECIFIC CYCLIN-B2; 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; Cyclin-like; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 2: Evidence at transcript 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_0000080360"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 94
FT /note="Phosphothreonine"
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 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT CONFLICT 69
FT /note="N -> S (in Ref. 2; AAX08665/AAX08686/AAX08779/
FT AAX08839 and 3; AAI18383)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="R -> K (in Ref. 1; AAC31953)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="L -> A (in Ref. 1; AAC31953)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="L -> V (in Ref. 1; AAC31953)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="N -> S (in Ref. 2; AAX08779/AAX08839 and 3;
FT AAI18383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45260 MW; 74EFF696CA93DD0A CRC64;
MALLRRPTVS TDLENNDTGV NSKPKSHVTI RRAVLEEIGN RVTTRAIQVA KKAQNTKVPV
PPTKTTNVNK HPKPTASVKP VQMDVLAPKG PSPTPQDISM KEENLCQAFS DALLCKIEDI
DTEDWENPQL CSDYVKDIYQ YLRQLEVLQS INPHFLDGRD INGRMRAILV DWLVQVHSKF
RLLQETLYMC VAVMDRYLQV QPVSRKKLQL VGITALLLAS KYEEMFSPNI EDFVYITDNA
YTSSQIREME TLILKELKFE LGRPLPLHFL RRASKAGEVD VEQHTLAKYL MELTLVDYDM
VHYHPSKVAA AASCLSQKVL GQGKWNLKQQ YYTGYTESEV LEVMRHMAKN VVRVNENMTK
FTAIKNKYAS SKLLKISTIP QLNSKAIQEL ASPLLGRS
//
