ID CCNB_ARBPU Reviewed; 409 AA.
AC P07818;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=G2/mitotic-specific cyclin-B;
OS Arbacia punctulata (Punctuate sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Arbacioida; Arbaciidae; Arbacia.
OX NCBI_TaxID=7641;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2826125; DOI=10.1002/j.1460-2075.1987.tb02604.x;
RA Pines J., Hunt T.;
RT "Molecular cloning and characterization of the mRNA for cyclin from sea
RT urchin eggs.";
RL EMBO J. 6:2987-2995(1987).
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}.
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DR EMBL; Y00608; CAA68650.1; -; mRNA.
DR PIR; S00662; S00662.
DR PDB; 6EF0; EM; 4.43 A; s=26-37.
DR PDB; 6EF1; EM; 4.73 A; s=22-36.
DR PDB; 6EF2; EM; 4.27 A; s=21-36.
DR PDB; 6EF3; EM; 4.17 A; s=16-41.
DR PDBsum; 6EF0; -.
DR PDBsum; 6EF1; -.
DR PDBsum; 6EF2; -.
DR PDBsum; 6EF3; -.
DR AlphaFoldDB; P07818; -.
DR SMR; P07818; -.
DR ELM; P07818; -.
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; 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; 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:SF615; G2_MITOTIC-SPECIFIC CYCLIN-B; 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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cyclin; Mitosis.
FT CHAIN 1..409
FT /note="G2/mitotic-specific cyclin-B"
FT /id="PRO_0000080377"
SQ SEQUENCE 409 AA; 46086 MW; FAE254110567C618 CRC64;
MALGTRNMNM NLHGESKHTF NNENVSARLG GKSIAVQKPA QRAALGNISN VVRTAQAGSK
KVVKKDTRQK AMTKTKATSS LHAVVGLPVE DLPTEMRSTS PDVLDAMEVD QAIEAFSQQL
IALQVEDIDK DDGDNPQLCS EYAKDIYLYL RRLEVEMMVP ANYLDRQETQ ITGRMRLILV
DWLVQVHLRF HLLQETLFLT VQLIDRFLAE HSVSKGKLQL VGVTAMFIAS KYEEMYPPEI
NDFVYITDNA YTKAQIRQME IAMLKGLKYK LGKPLCLHFL RRNSKAAGVD AQKHTLAKYL
MEITLPEYSM VQYSPSEIAA AAIYLSMTLL DPETHSSWCP KMTHYSMYSE DHLRPIVQKI
VQILLRDDSA SQKYSAVKTK YGSSKFMKIS GIAQLDSSLL KQIAQGSNE
//
