ID CCNB2_ORYJA Reviewed; 382 AA.
AC Q9DG99;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=G2/mitotic-specific cyclin-B2;
GN Name=ccnb2;
OS Oryzias javanicus (Javanese ricefish) (Aplocheilus javanicus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=123683;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Yamashita M., Mita K.;
RT "cDNA cloning of Cdc2 and cyclin B in medaka species.";
RL Submitted (OCT-2000) 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; AB050464; BAB17222.1; -; mRNA.
DR AlphaFoldDB; Q9DG99; -.
DR SMR; Q9DG99; -.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:InterPro.
DR CDD; cd20507; CYCLIN_CCNB1-like_rpt1; 1.
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.
FT CHAIN 1..382
FT /note="G2/mitotic-specific cyclin-B2"
FT /id="PRO_0000080367"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 42995 MW; 992F7F0EE2816366 CRC64;
MSSVEAVTQQ QLLAAENPVR MGKGAADPRR AALGEITNRN AAAAANRKMG PSKKQPKPSC
AQKPQPVVHT SAGDPAPISA DMSMKVEQDL SQAFSEVLML AVQDVDEQDA DQPQLCSQYV
KDIYKYLHTL EEQQAIRPNY MQGYSVTEHM RALLVDWLVQ VHSRFQLLQE TLYLTVAILD
RFLQVHPVSR RKLQLVGVTA MLVACKYEEM YPPEVGDFAY ITDDAFTKFQ IVEMEQVILR
SLGFQLGRPL PLHFLRRASK VADADVEKHT LAKYLLELTL LDYHMVHYRP SEAAAAALCL
SQLLLDGLPW SLEQQHYSTY DEQHLKPIMQ LMAKNVVQVT EGRTKFLAVK KKYSSSKLMK
ISLIPQLNSS TIKVMAEALQ NP
//
