ID   CCNB1_HUMAN             Reviewed;         433 AA.
AC   P14635;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   05-OCT-2010, entry version 109.
DE   RecName: Full=G2/mitotic-specific cyclin-B1;
GN   Name=CCNB1; Synonyms=CCNB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND SUBUNIT.
RX   MEDLINE=89376534; PubMed=2570636; DOI=10.1016/0092-8674(89)90936-7;
RA   Pines J., Hunter T.;
RT   "Isolation of a human cyclin cDNA: evidence for cyclin mRNA and
RT   protein regulation in the cell cycle and for interaction with
RT   p34cdc2.";
RL   Cell 58:833-846(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX   MEDLINE=95145589; PubMed=7843284; DOI=10.1006/excr.1995.1050;
RA   Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A.,
RA   Gaetano C.;
RT   "Structure and growth-dependent regulation of the human cyclin B1
RT   promoter.";
RL   Exp. Cell Res. 216:396-402(1995).
RN   [5]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH CCNF.
RX   PubMed=10716937; DOI=10.1093/emboj/19.6.1378;
RA   Kong M., Barnes E.A., Ollendorff V., Donoghue D.J.;
RT   "Cyclin F regulates the nuclear localization of cyclin B1 through a
RT   cyclin-cyclin interaction.";
RL   EMBO J. 19:1378-1388(2000).
RN   [6]
RP   INTERACTION WITH RALBP1.
RX   PubMed=12775724; DOI=10.1074/jbc.M302191200;
RA   Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
RT   "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to
RT   phosphorylate epsin during the switch off of endocytosis in mitosis.";
RL   J. Biol. Chem. 278:30597-30604(2003).
RN   [7]
RP   INTERACTION WITH HEI10.
RX   MEDLINE=22499947; PubMed=12612082;
RX   DOI=10.1128/MCB.23.6.2109-2122.2003;
RA   Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.;
RT   "A novel RING finger protein, human enhancer of invasion 10, alters
RT   mitotic progression through regulation of cyclin B levels.";
RL   Mol. Cell. Biol. 23:2109-2122(2003).
RN   [8]
RP   UBIQUITINATION.
RX   PubMed=16009132; DOI=10.1016/j.cell.2005.04.034;
RA   Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H.,
RA   Morris S.W., Peschel C., Duyster J.;
RT   "NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic
RT   entry.";
RL   Cell 122:45-57(2005).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15181148; DOI=10.1091/mbc.E03-12-0871;
RA   Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J.,
RA   Piette J., Dulic V.;
RT   "p21-mediated nuclear retention of cyclin B1-Cdk1 in response to
RT   genotoxic stress.";
RL   Mol. Biol. Cell 15:3965-3976(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-35; SER-69 AND
RP   THR-321, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH
RP   PHOSPHORYLATED CDK2, AND FUNCTION.
RX   PubMed=17495531;
RA   Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R.,
RA   Johnson L.N.;
RT   "Cyclin B and cyclin A confer different substrate recognition
RT   properties on CDK2.";
RL   Cell Cycle 6:1350-1359(2007).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, AND FUNCTION.
RX   PubMed=17495533;
RA   Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R.;
RT   "The crystal structure of human cyclin B.";
RL   Cell Cycle 6:1342-1349(2007).
CC   -!- FUNCTION: Essential for the control of the cell cycle at the G2/M
CC       (mitosis) transition.
CC   -!- SUBUNIT: Interacts with the CDC2 protein kinase to form a
CC       serine/threonine kinase holoenzyme complex also known as
CC       maturation promoting factor (MPF). The cyclin subunit imparts
CC       substrate specificity to the complex. Binds HEI10. Interacts with
CC       catalytically active RALBP1 and CDC2 during mitosis to form an
CC       endocytotic complex during interphase. Interacts with CCNF;
CC       interaction is required for nuclear localization.
CC   -!- INTERACTION:
CC       P06493:CDC2; NbExp=1; IntAct=EBI-495332, EBI-444308;
CC       P46527:CDKN1B; NbExp=1; IntAct=EBI-495332, EBI-519280;
CC       Q99640:PKMYT1; NbExp=2; IntAct=EBI-495332, EBI-495308;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC       centrosome.
CC   -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is
CC       abruptly destroyed at mitosis.
CC   -!- PTM: Ubiquitinated by the SCF(NIPA) complex during interphase,
CC       leading to its destruction. Not ubiquitinated during G2/M phases.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/CCNB1ID951ch5q13.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ccnb1/";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M25753; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AY338491; AAP88038.1; -; Genomic_DNA.
DR   EMBL; BC006510; AAH06510.1; -; mRNA.
DR   IPI; IPI00745793; -.
DR   PIR; A32992; A32992.
DR   RefSeq; NP_114172.1; -.
DR   UniGene; Hs.23960; -.
DR   PDB; 2B9R; X-ray; 2.90 A; A/B=165-433.
DR   PDB; 2JGZ; X-ray; 2.90 A; B=167-426.
DR   PDBsum; 2B9R; -.
DR   PDBsum; 2JGZ; -.
DR   ProteinModelPortal; P14635; -.
DR   DisProt; DP00223; -.
DR   DIP; DIP-59N; -.
DR   IntAct; P14635; 17.
DR   MINT; MINT-1202632; -.
DR   STRING; P14635; -.
DR   PhosphoSite; P14635; -.
DR   PRIDE; P14635; -.
DR   Ensembl; ENST00000256442; ENSP00000256442; ENSG00000134057.
DR   GeneID; 891; -.
DR   KEGG; hsa:891; -.
DR   UCSC; uc003jvl.1; human.
DR   CTD; 891; -.
DR   GeneCards; GC05P068462; -.
DR   H-InvDB; HIX0004916; -.
DR   HGNC; HGNC:1579; CCNB1.
DR   HPA; CAB000115; -.
DR   HPA; CAB003804; -.
DR   MIM; 123836; gene.
DR   PharmGKB; PA95; -.
DR   eggNOG; prNOG12100; -.
DR   HOGENOM; HBG750484; -.
DR   HOVERGEN; HBG061650; -.
DR   InParanoid; P14635; -.
DR   OMA; NIVMVNR; -.
DR   OrthoDB; EOG9CZF19; -.
DR   PhylomeDB; P14635; -.
DR   Pathway_Interaction_DB; foxm1pathway; FOXM1 transcription factor network.
DR   Pathway_Interaction_DB; foxopathway; FoxO family signaling.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   NextBio; 3686; -.
DR   ArrayExpress; P14635; -.
DR   Bgee; P14635; -.
DR   CleanEx; HS_CCNB1; -.
DR   Genevestigator; P14635; -.
DR   GermOnline; ENSG00000134057; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0000942; C:outer kinetochore of condensed nuclear chro...; IDA:BHF-UCL.
DR   GO; GO:0000922; C:spindle pole; IDA:BHF-UCL.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent protea...; EXP:Reactome.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; NAS:UniProtKB.
DR   GO; GO:0071174; P:mitotic cell cycle spindle checkpoint; IMP:BHF-UCL.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; IMP:BHF-UCL.
DR   GO; GO:0000236; P:mitotic prometaphase; IDA:BHF-UCL.
DR   GO; GO:0043148; P:mitotic spindle stabilization; IMP:BHF-UCL.
DR   GO; GO:0051987; P:positive regulation of attachment of spindl...; IMP:BHF-UCL.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:BHF-UCL.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein li...; EXP:Reactome.
DR   InterPro; IPR015454; CycB.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR014400; Cyclin_A_B_D_E.
DR   InterPro; IPR004367; Cyclin_C.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR013763; Cyclin_related.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   PANTHER; PTHR10177:SF27; CycB; 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   SUPFAM; SSF47954; Cyclin_like; 2.
DR   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Cell division;
KW   Complete proteome; Cyclin; Cytoplasm; Cytoskeleton; Mitosis; Nucleus;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    433       G2/mitotic-specific cyclin-B1.
FT                                /FTId=PRO_0000080350.
FT   REGION      169    177       Interaction with CDK2.
FT   REGION      258    261       Interaction with CDK2.
FT   COMPBIAS     51     85       Lys-rich.
FT   MOD_RES       9      9       Phosphoserine.
FT   MOD_RES      35     35       Phosphoserine.
FT   MOD_RES      69     69       Phosphoserine.
FT   MOD_RES      73     73       N6-acetyllysine.
FT   MOD_RES     321    321       Phosphothreonine.
FT   TURN        173    177
FT   HELIX       178    183
FT   TURN        189    192
FT   STRAND      193    197
FT   HELIX       199    215
FT   HELIX       220    234
FT   HELIX       241    243
FT   HELIX       244    259
FT   HELIX       266    272
FT   STRAND      275    277
FT   HELIX       279    292
FT   HELIX       302    311
FT   HELIX       317    329
FT   HELIX       330    332
FT   HELIX       334    336
FT   STRAND      337    339
FT   HELIX       343    356
FT   HELIX       365    368
FT   TURN        375    378
FT   HELIX       379    389
FT   HELIX       399    403
FT   HELIX       407    409
FT   HELIX       412    414
FT   HELIX       420    422
SQ   SEQUENCE   433 AA;  48337 MW;  E2C4767AE8A11EC0 CRC64;
     MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN KVSEQLQAKM
     PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE PEPEPEPEPV KEEKLSPEPI
     LVDTASPSPM ETSGCAPAEE DLCQAFSDVI LAVNDVDAED GADPNLCSEY VKDIYAYLRQ
     LEEEQAVRPK YLLGREVTGN MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP
     KKMLQLVGVT AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP
     LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC LALKILDNGE
     WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV KNKYATSKHA KISTLPQLNS
     ALVQDLAKAV AKV
//