ID   CCNB2_HUMAN             Reviewed;         398 AA.
AC   O95067; Q6FI99;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   07-JUL-2009, entry version 72.
DE   RecName: Full=G2/mitotic-specific cyclin-B2;
GN   Name=CCNB2;
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].
RA   Kim D.G., Choi S.S., Kang Y.S., Lee K.H., Kim U.-J., Shin H.-S.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Saito T., Miyajima N.;
RT   "G2/mitotic-specific cyclin B2.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=21154917; PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-100 AND THR-395.
RG   NIEHS SNPs program;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; THR-94; SER-99;
RP   SER-204; SER-392 AND SER-398, AND MASS SPECTROMETRY.
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-99 AND SER-398,
RP   AND MASS SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
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.
CC   -!- INTERACTION:
CC       P24941:CDK2; NbExp=1; IntAct=EBI-375024, EBI-375096;
CC       P38936:CDKN1A; NbExp=1; IntAct=EBI-375024, EBI-375077;
CC       P49736:MCM2; NbExp=1; IntAct=EBI-375024, EBI-374819;
CC   -!- DEVELOPMENTAL STAGE: Accumulates steadily during G2 and is
CC       abruptly destroyed at mitosis.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ccnb2/";
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; AF002822; AAD09309.1; -; mRNA.
DR   EMBL; AB020981; BAA78387.1; -; mRNA.
DR   EMBL; AL080146; CAB45739.1; -; mRNA.
DR   EMBL; CR533527; CAG38558.1; -; mRNA.
DR   EMBL; AY864066; AAW34361.1; -; Genomic_DNA.
DR   EMBL; BC105086; AAI05087.1; -; mRNA.
DR   EMBL; BC105112; AAI05113.1; -; mRNA.
DR   IPI; IPI00028266; -.
DR   PIR; T12530; T12530.
DR   RefSeq; NP_004692.1; -.
DR   UniGene; Hs.194698; -.
DR   HSSP; P20248; 1H1R.
DR   IntAct; O95067; 4.
DR   PhosphoSite; O95067; -.
DR   PRIDE; O95067; -.
DR   Ensembl; ENSG00000157456; Homo sapiens.
DR   GeneID; 9133; -.
DR   KEGG; hsa:9133; -.
DR   UCSC; uc002afz.1; human.
DR   GeneCards; GC15P057184; -.
DR   HGNC; HGNC:1580; CCNB2.
DR   HPA; CAB009575; -.
DR   HPA; HPA008873; -.
DR   MIM; 602755; gene.
DR   PharmGKB; PA26148; -.
DR   HOGENOM; O95067; -.
DR   HOVERGEN; O95067; -.
DR   OMA; O95067; RPTVSTD.
DR   Pathway_Interaction_DB; foxm1pathway; FOXM1 transcription factor network.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   NextBio; 34245; -.
DR   ArrayExpress; O95067; -.
DR   Bgee; O95067; -.
DR   CleanEx; HS_CCNB2; -.
DR   GermOnline; ENSG00000157456; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR015454; CycB.
DR   InterPro; IPR006670; Cyclin.
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   PROSITE; PS00292; CYCLINS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Complete proteome; Cyclin; Mitosis;
KW   Phosphoprotein; Polymorphism.
FT   CHAIN         1    398       G2/mitotic-specific cyclin-B2.
FT                                /FTId=PRO_0000080361.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES      94     94       Phosphothreonine.
FT   MOD_RES      99     99       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     398    398       Phosphoserine.
FT   VARIANT     100    100       M -> T (in dbSNP:rs16941036).
FT                                /FTId=VAR_022221.
FT   VARIANT     135    135       V -> I (in dbSNP:rs2306785).
FT                                /FTId=VAR_053052.
FT   VARIANT     395    395       I -> T (in dbSNP:rs28383563).
FT                                /FTId=VAR_022222.
SQ   SEQUENCE   398 AA;  45282 MW;  874466E1DD68A4C4 CRC64;
     MALLRRPTVS SDLENIDTGV NSKVKSHVTI RRTVLEEIGN RVTTRAAQVA KKAQNTKVPV
     QPTKTTNVNK QLKPTASVKP VQMEKLAPKG PSPTPEDVSM KEENLCQAFS DALLCKIEDI
     DNEDWENPQL CSDYVKDIYQ YLRQLEVLQS INPHFLDGRD INGRMRAILV DWLVQVHSKF
     RLLQETLYMC VGIMDRFLQV QPVSRKKLQL VGITALLLAS KYEEMFSPNI EDFVYITDNA
     YTSSQIREME TLILKELKFE LGRPLPLHFL RRASKAGEVD VEQHTLAKYL MELTLIDYDM
     VHYHPSKVAA AASCLSQKVL GQGKWNLKQQ YYTGYTENEV LEVMQHMAKN VVKVNENLTK
     FIAIKNKYAS SKLLKISMIP QLNSKAVKDL ASPLIGRS
//