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Reviewed, UniProtKB/Swiss-Prot P14635 (CCNB1_HUMAN)

Last modified February 9, 2010. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    G2/mitotic-specific cyclin-B1
Gene names
Name: CCNB1
Synonyms: CCNB
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Essential for the control of the cell cycle at the G2/M (mitosis) transition. Ref.13 Ref.14

Subunit structure

Interacts with the CDC2 protein kinase to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex. Binds HEI10. Interacts with catalytically active RALBP1 and CDC2 during mitosis to form an endocytotic complex during interphase. Ref.1 Ref.5 Ref.6

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeletoncentrosome Ref.8.

Developmental stage

Accumulates steadily during G2 and is abruptly destroyed at mitosis. Ref.1

Post-translational modification

Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction. Not ubiquitinated during G2/M phases. Ref.7

Sequence similarities

Belongs to the cyclin family. Cyclin AB subfamily.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 433433G2/mitotic-specific cyclin-B1
PRO_0000080350

Regions

Region169 – 1779Interaction with CDK2
Region258 – 2614Interaction with CDK2
Compositional bias51 – 8535Lys-rich

Amino acid modifications

Modified residue91Phosphoserine Ref.9
Modified residue351Phosphoserine Ref.9
Modified residue691Phosphoserine Ref.9
Modified residue731N6-acetyllysine Ref.12
Modified residue3211Phosphothreonine Ref.9

Secondary structure

........................................... 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14635-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: E2C4767AE8A11EC0

FASTA43348,337
        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 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2."
Pines J., Hunter T.
Cell 58:833-846(1989) [PubMed: 2570636] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, SUBUNIT.
[2]NIEHS SNPs program
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"Structure and growth-dependent regulation of the human cyclin B1 promoter."
Piaggio G., Farina A., Perrotti D., Manni I., Fuschi P., Sacchi A., Gaetano C.
Exp. Cell Res. 216:396-402(1995) [PubMed: 7843284] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[5]"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
J. Biol. Chem. 278:30597-30604(2003) [PubMed: 12775724] [Abstract]
Cited for: INTERACTION WITH RALBP1.
[6]"A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels."
Toby G.G., Gherraby W., Coleman T.R., Golemis E.A.
Mol. Cell. Biol. 23:2109-2122(2003) [PubMed: 12612082] [Abstract]
Cited for: INTERACTION WITH HEI10.
[7]"NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry."
Bassermann F., von Klitzing C., Munch S., Bai R.-Y., Kawaguchi H., Morris S.W., Peschel C., Duyster J.
Cell 122:45-57(2005) [PubMed: 16009132] [Abstract]
Cited for: UBIQUITINATION.
[8]"p21-mediated nuclear retention of cyclin B1-Cdk1 in response to genotoxic stress."
Baus Charrier-Savournin F., Chateau M.-T., Gire V., Sedivy J., Piette J., Dulic V.
Mol. Biol. Cell 15:3965-3976(2004) [PubMed: 15181148] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-35; SER-69 AND THR-321, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73, MASS SPECTROMETRY.
[13]"Cyclin B and cyclin A confer different substrate recognition properties on CDK2."
Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.
Cell Cycle 6:1350-1359(2007) [PubMed: 17495531] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 167-426 IN COMPLEX WITH PHOSPHORYLATED CDK2, FUNCTION.
[14]"The crystal structure of human cyclin B."
Petri E.T., Errico A., Escobedo L., Hunt T., Basavappa R.
Cell Cycle 6:1342-1349(2007) [PubMed: 17495533] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 165-433, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25753 mRNA. No translation available.
AY338491 Genomic DNA. Translation: AAP88038.1.
BC006510 mRNA. Translation: AAH06510.1.
IPIIPI00745793.
PIRA32992.
RefSeqNP_114172.1.
UniGeneHs.23960

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B9RX-ray2.90A/B165-433[»]
2JGZX-ray2.90B167-426[»]
DisProtDP00223.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-59N.
IntActP14635. 6 interactions.
STRINGP14635.

PTM databases

PhosphoSiteP14635.

Proteomic databases

PRIDEP14635.

Genome annotation databases

EnsemblENST00000256442; ENSP00000256442; ENSG00000134057; Homo sapiens. [Genome view]
GeneID891.
KEGGhsa:891.
UCSCuc003jvl.1. human.

Organism-specific databases

CTD891.
GeneCardsGC05P068498.
H-InvDBHIX0004916.
HGNCHGNC:1579. CCNB1.
HPACAB000115.
CAB003804.
MIM123836. gene.
PharmGKBPA95.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12100.
HOGENOMHBG750484.
HOVERGENP14635.
InParanoidP14635.
OMANIVMVNR.
OrthoDBEOG9CZF19.
PhylomeDBP14635.

Enzyme and pathway databases

Pathway_Interaction_DBfoxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.
ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.

Gene expression databases

ArrayExpressP14635.
BgeeP14635.
CleanExHS_CCNB1.
GenevestigatorP14635.
GermOnlineENSG00000134057. Homo sapiens.

Family and domain databases

InterProIPR015454. CycB.
IPR006670. Cyclin.
IPR011028. Cyclin-like.
IPR014400. Cyclin_A_B_D_E.
IPR004367. Cyclin_C.
IPR006671. Cyclin_N.
IPR013763. Cyclin_related.
[Graphical view]
Gene3DG3DSA:1.10.472.10. Cyclin_related. 1 hit.
PANTHERPTHR10177:SF27. CycB. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF001771. Cyclin_A_B_D_E. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
PROSITEPS00292. CYCLINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3686.
SOURCESearch...

Entry information

Entry nameCCNB1_HUMAN
AccessionPrimary (citable) accession number: P14635
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 9, 2010
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

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Human chromosome 5: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents