ID CCNB_PATPE Reviewed; 394 AA.
AC P18063;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=G2/mitotic-specific cyclin-B;
OS Patiria pectinifera (Starfish) (Asterina pectinifera).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Valvatacea; Valvatida; Asterinidae; Patiria.
OX NCBI_TaxID=7594;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1695583; DOI=10.1016/0012-1606(90)90074-s;
RA Tachibana K., Ishiura M., Uchida T., Kishimoto T.;
RT "The starfish egg mRNA responsible for meiosis reinitiation encodes
RT cyclin.";
RL Dev. Biol. 140:241-252(1990).
RN [2]
RP CONCEPTUAL TRANSLATION.
RA Gibson T.J.;
RL Unpublished observations (AUG-1994).
CC -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC (mitosis) transition.
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.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA29994.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M33880; AAA29994.1; ALT_FRAME; mRNA.
DR PIR; A37350; A37350.
DR BindingDB; P18063; -.
DR ChEMBL; CHEMBL2366468; -.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd20507; CYCLIN_CCNB1-like_rpt1; 1.
DR CDD; cd20509; CYCLIN_CCNB1-like_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; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR PANTHER; PTHR10177:SF615; G2_MITOTIC-SPECIFIC CYCLIN-B; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 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..394
FT /note="G2/mitotic-specific cyclin-B"
FT /id="PRO_0000080378"
FT REGION 360..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 45120 MW; E1245635CF94F64E CRC64;
MQTACSGNLC GYQLMFSLST VVTVCRSLRS RNRHWFLKLL GVRLTIAMRC ALENISNVAK
NNVQAAAKKE IKQKRGMTKS KATSSLQSVI GLHVEPVEKV QSPEPMDMSE VSNALEAFSQ
NILEMGVDDI DKDDHENPQL CSEYVNDIYL YMRHLEREFK VRTDYMAMQE ITERMRTILI
DWLVQVHLRF HLLQETLFLT IQILDRYLEG ASVSKTKLQL VGVTSMLIAA YEEMYAEIGD
FVYITDNAYS KAQIRAMECN ILRKLDFNLG KPLCIHFLRR CSKAGGVDGH KHTLSKYIME
LTLXEYSFVK YDXEIAAAAL LSTRFWDEDM EWTKSLVHYS AYSEGHLGPI VQKMAVLSQQ
SHPSPNSRLD QEEDMASSKF MSDQQATQEL KSIR
//
