CCNB2_MACFA
ID CCNB2_MACFA Reviewed; 398 AA.
AC Q4R7A8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=G2/mitotic-specific cyclin-B2;
GN Name=CCNB2; ORFNames=QtsA-15734;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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; AB168913; BAE01014.1; -; mRNA.
DR RefSeq; NP_001270393.1; NM_001283464.1.
DR AlphaFoldDB; Q4R7A8; -.
DR SMR; Q4R7A8; -.
DR STRING; 9541.XP_005559729.1; -.
DR GeneID; 101925942; -.
DR CTD; 9133; -.
DR eggNOG; KOG0653; Eukaryota.
DR OrthoDB; 993640at2759; -.
DR Proteomes; UP000233100; Unplaced.
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 Cell cycle; Cell division; Cyclin; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..398
FT /note="G2/mitotic-specific cyclin-B2"
FT /id="PRO_0000273974"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95067"
FT MOD_RES 11
FT /note="Phosphoserine"
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"
SQ SEQUENCE 398 AA; 45322 MW; 6E613D954533C5E8 CRC64;
MALLRRPTVS SDLENIDTGF NSKVKSHVTI RRTVLEEIGN KVTTRAAQVA KKAQNTKVPV
QPTKTTNVNK QLKPTASVKP VQMEMLAPKG PSPTPEDVSM KEENLCQAFS DALLCKIEDI
DNEDWENPQL CSDYVKDIYQ YLRQLEVLQS INPHFLDGRD INGRMRAILV DWLVQVHSKF
RLLQETLYMC VAIMDRFLQV QPVSRKKLQL VGITALLLAS KYEEMFSPNI EDFVYITDNA
YTSSQIREME TLILKELKFE LGRPLPLHFL RRASKAGEVD VEQHTLAKYL MELTLIDYDM
VHYHPSKVAA AASCLSQKLL GQGKWNLKQQ YYTGYTENEV LEVMQHMAKN VVKVDENLTK
FIAIKNKYAS SKLLKISTIP QLNSKAVKDL ASPLMGRS