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UniProtKB/Swiss-Prot entry P14635


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCNB1_HUMAN
Primary accession number P14635
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on April 1, 1990 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 84)
Name and origin of the protein
Protein name G2/mitotic-specific cyclin-B1
Synonyms None
Gene name
Name: CCNB1
Synonyms: CCNB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND SUBUNIT.
DOI=10.1016/0092-8674(89)90936-7; PubMed=2570636 [NCBI, ExPASy, EBI, Israel, Japan]
Pines J., Hunter T.;
"Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2.";
Cell 58:833-846(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
DOI=10.1006/excr.1995.1050; PubMed=7843284 [NCBI, ExPASy, EBI, Israel, Japan]
Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A., Gaetano C.;
"Structure and growth-dependent regulation of the human cyclin B1 promoter.";
Exp. Cell Res. 216:396-402(1995).
[5]
INTERACTION WITH RALBP1.
DOI=10.1074/jbc.M302191200; PubMed=12775724 [NCBI, ExPASy, EBI, Israel, Japan]
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis.";
J. Biol. Chem. 278:30597-30604(2003).
[6]
INTERACTION WITH HEI10.
DOI=10.1128/MCB.23.6.2109-2122.2003; PubMed=12612082 [NCBI, ExPASy, EBI, Israel, Japan]
Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.;
"A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels.";
Mol. Cell. Biol. 23:2109-2122(2003).
[7]
UBIQUITINATION.
DOI=10.1016/j.cell.2005.04.034; PubMed=16009132 [NCBI, ExPASy, EBI, Israel, Japan]
Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H., Morris S.W., Peschel C., Duyster J.;
"NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry.";
Cell 122:45-57(2005).
[8]
SUBCELLULAR LOCATION.
DOI=10.1091/mbc.E03-12-0871; PubMed=15181148 [NCBI, ExPASy, EBI, Israel, Japan]
Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J., Piette J., Dulic V.;
"p21-mediated nuclear retention of cyclin B1-Cdk1 in response to genotoxic stress.";
Mol. Biol. Cell 15:3965-3976(2004).
[9]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH PHOSPHORYLATED CDK2, AND FUNCTION.
PubMed=17495531 [NCBI, ExPASy, EBI, Israel, Japan]
Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.;
"Cyclin B and cyclin A confer different substrate recognition properties on CDK2.";
Cell Cycle 6:1350-1359(2007).
[10]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, AND FUNCTION.
PubMed=17495533 [NCBI, ExPASy, EBI, Israel, Japan]
Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R.;
"The crystal structure of human cyclin B.";
Cell Cycle 6:1342-1349(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M25753; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
AY338491; AAP88038.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006510; AAH06510.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32992; A32992.
RefSeq NP_114172.1; -.
UniGene Hs.23960
3D structure databases
PDB
2B9R; X-ray; 2.90 A; A/B=165-433.[ExPASy / RCSB / EBI]
2JGZ; X-ray; 2.90 A; B=167-426.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2B9R; -.
2JGZ; -.
DisProt DP00223; -.
ModBase P14635.
Protein-protein interaction databases
DIP DIP:59N; -.
IntAct P14635; -.
PTM databases
PhosphoSite P14635; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
Polymorphism databases
NIEHS-SNPs CCNB1.
Organism-specific databases
H-InvDB HIX0004916; -.
HGNC HGNC:1579; CCNB1.
GenAtlas CCNB1.
HPA CAB000115; -.
CAB003804; -.
MIM 123836; gene. [NCBI / EBI]
PharmGKB PA95; -.
GeneCards P14635.
Gene expression databases
ArrayExpress P14635; -.
CleanEx HS_CCNB1; -.
GermOnline ENSG00000134057; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0000086; Biological process: G2/M transition of mitotic cell cycle (non-traceable author statement from UniProtKB).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR015454; CycB.
IPR006670; Cyclin.
IPR014400; Cyclin_A_B_D_E.
IPR004367; Cyclin_C.
IPR006671; Cyclin_N.
IPR013763; Cyclin_related.
Graphical view of domain structure.
Gene3D G3DSA:1.10.472.10; Cyclin_related; 1.
PANTHER PTHR10177:SF27; CycB; 1.
Pfam PF02984; Cyclin_C; 1.
PF00134; Cyclin_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001771; Cyclin_A_B_D_E; 1.
SMART SM00385; CYCLIN; 2.
SMART graphical view of domain structure.
PROSITE PS00292; CYCLINS; 1.
BLOCKS P14635.
Genome annotation databases
Ensembl ENSG00000134057; Homo sapiens. [Contig view]
GeneID 891; -.
KEGG hsa:891; -.
Phylogenomic databases
HOGENOM P14635; -.
HOVERGEN P14635; -.
Other
SOURCE CCNB1; Homo sapiens.
ProtoNet P14635.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell cycle; Cell division; Cyclin; Cytoplasm; Mitosis; Nucleus; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   433  433     G2/mitotic-specific cyclin-B1. PRO_0000080350
REGION   169   177  9     Interaction with CDK2. 
REGION   258   261  4     Interaction with CDK2. 
COMPBIAS   51    85  35     Lys-rich. 
TURN   173   177  5      
HELIX   178   183  6      
TURN   189   192  4      
STRAND   193   197  5      
HELIX   199   215  17      
HELIX   220   234  15      
HELIX   241   243  3      
HELIX   244   259  16      
HELIX   266   272  7      
STRAND   275   277  3      
HELIX   279   292  14      
HELIX   302   311  10      
HELIX   317   329  13      
HELIX   330   332  3      
HELIX   334   336  3      
STRAND   337   339  3      
HELIX   343   356  14      
HELIX   365   368  4      
TURN   375   378  4      
HELIX   379   389  11      
HELIX   399   403  5      
HELIX   407   409  3      
HELIX   412   414  3      
HELIX   420   422  3      
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 48337 Da [This is the MW of the unprocessed precursor] CRC64: E2C4767AE8A11EC0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALRVTRNSK INAENKAKIN MAGAKRVPTA PAATSKPGLR PRTALGDIGN KVSEQLQAKM 

        70         80         90        100        110        120 
PMKKEAKPSA TGKVIDKKLP KPLEKVPMLV PVPVSEPVPE PEPEPEPEPV KEEKLSPEPI 

       130        140        150        160        170        180 
LVDTASPSPM ETSGCAPAEE DLCQAFSDVI LAVNDVDAED GADPNLCSEY VKDIYAYLRQ 

       190        200        210        220        230        240 
LEEEQAVRPK YLLGREVTGN MRAILIDWLV QVQMKFRLLQ ETMYMTVSII DRFMQNNCVP 

       250        260        270        280        290        300 
KKMLQLVGVT AMFIASKYEE MYPPEIGDFA FVTDNTYTKH QIRQMEMKIL RALNFGLGRP 

       310        320        330        340        350        360 
LPLHFLRRAS KIGEVDVEQH TLAKYLMELT MLDYDMVHFP PSQIAAGAFC LALKILDNGE 

       370        380        390        400        410        420 
WTPTLQHYLS YTEESLLPVM QHLAKNVVMV NQGLTKHMTV KNKYATSKHA KISTLPQLNS 

       430 
ALVQDLAKAV AKV 

P14635 in FASTA format

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