ID Q9IB44_DANRE Unreviewed; 398 AA. AC Q9IB44; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 04-FEB-2015, entry version 91. DE SubName: Full=Cyclin B1 {ECO:0000313|EMBL:BAA92876.1}; DE SubName: Full=Cyclin-B {ECO:0000313|EMBL:AAP47013.1}; GN Name=ccnb1 {ECO:0000313|EMBL:AAI53627.1, GN ECO:0000313|ZFIN:ZDB-GENE-000406-10}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:BAA92876.1}; RN [1] {ECO:0000313|EMBL:AAP47013.1} RP NUCLEOTIDE SEQUENCE. RA Bauer M.P., Goetz F.W.; RT "The isolation and characterization of cyclin B from the zebrafish."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAA92876.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Ovary {ECO:0000313|EMBL:BAA92876.1}; RX PubMed=11283000; DOI=10.1074/jbc.M010528200; RA Nakahata S., Katsu Y., Mita K., Inoue K., Nagahama Y., Yamashita M.; RT "Biochemical identification of Xenopus Pumilio as a sequence-specific RT cyclin B1 mRNA-binding protein that physically interacts with a Nanos RT homolog, Xcat-2, and a cytoplasmic polyadenylation element-binding RT protein."; RL J. Biol. Chem. 276:20945-20953(2001). RN [3] {ECO:0000313|EMBL:AAI53627.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Activated eggs {ECO:0000313|EMBL:AAI53627.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the cyclin family. CC {ECO:0000256|RuleBase:RU000383}. 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; BC153626; AAI53627.1; -; mRNA. DR EMBL; AF268043; AAP47013.1; -; mRNA. DR EMBL; AB040435; BAA92876.1; -; mRNA. DR RefSeq; NP_571588.1; NM_131513.1. DR UniGene; Dr.121261; -. DR ProteinModelPortal; Q9IB44; -. DR SMR; Q9IB44; 134-393. DR STRING; 7955.ENSDARP00000063356; -. DR GeneID; 58025; -. DR KEGG; dre:58025; -. DR CTD; 891; -. DR ZFIN; ZDB-GENE-000406-10; ccnb1. DR HOGENOM; HOG000167672; -. DR HOVERGEN; HBG061650; -. DR KO; K05868; -. DR PhylomeDB; Q9IB44; -. DR Reactome; REACT_209285; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; REACT_210283; Resolution of Sister Chromatid Cohesion. DR Reactome; REACT_213851; Condensation of Prometaphase Chromosomes. DR Reactome; REACT_216095; Recruitment of NuMA to mitotic centrosomes. DR Reactome; REACT_216685; MASTL Facilitates Mitotic Progression. DR Reactome; REACT_223777; Condensation of Prophase Chromosomes. DR Reactome; REACT_226028; Depolymerisation of the Nuclear Lamina. DR Reactome; REACT_226328; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; REACT_227128; Nuclear Pore Complex (NPC) Disassembly. DR Reactome; REACT_241009; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex. DR Reactome; REACT_241526; E2F-enabled inhibition of pre-replication complex formation. DR Reactome; REACT_242489; Activation of NIMA Kinases NEK9, NEK6, NEK7. DR Reactome; REACT_244204; Regulation of APC/C activators between G1/S and early anaphase. DR Reactome; REACT_245050; Cyclin A/B1 associated events during G2/M transition. DR Reactome; REACT_246075; G2/M DNA replication checkpoint. DR Reactome; REACT_251772; APC/C:Cdc20 mediated degradation of Cyclin B. DR Reactome; REACT_253492; Phosphorylation of the APC/C. DR Reactome; REACT_259952; Phosphorylation of Emi1. DR NextBio; 20892002; -. DR GO; GO:0005634; C:nucleus; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro. DR Gene3D; 1.10.472.10; -; 2. DR InterPro; IPR013763; Cyclin-like. DR InterPro; IPR014400; Cyclin_A/B/D/E/F. DR InterPro; IPR004367; Cyclin_C-dom. DR InterPro; IPR006671; Cyclin_N. 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 SUPFAM; SSF47954; SSF47954; 2. DR PROSITE; PS00292; CYCLINS; 1. PE 2: Evidence at transcript level; KW Cell cycle {ECO:0000256|SAAS:SAAS00043797}; KW Cell division {ECO:0000256|SAAS:SAAS00043785}; KW Cyclin {ECO:0000256|RuleBase:RU000383, ECO:0000256|SAAS:SAAS00043802}. SQ SEQUENCE 398 AA; 44836 MW; 8A26971453F5907A CRC64; MMALRVTRNT RLASSENQNA LPGKAVVANK PGLRPRAALG EIGNNPQTRQ ALKKKEVKVA PAAEVVVEKA PVVQQPKKDS PKVQHGVKVV SEPSSPVPME TSGCASDDLC QAFSDVLLNI KDVDADDYDN PMLCSEYVKD IYLYLRQLET EQAVRPKYLA GKEVTGNMRA ILIDWLVQVQ IKFRLLQETM YMTVAIIDRF LQDHPVPKKQ LQLVGVTAMF IASKYEEMYP PEIADFAFVT DRAYTTSQIR EMEMKVLRVL NFGFGRPLPL QFLRRASKIG DVTAEHHTLA KYFLELTMVD YDMVHYPPSQ MASAAYALTL KVFNCGDWTP TLQHYMGYTE DELVPVMQHI AKNVVRVNEG LSKHLAVKNK YSSQKQMRIA TISQLKSSLI KDLAKQIS //