G2/mitotic-specific cyclin-B1 - Homo sapiens (Human)

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P14635 (CCNB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
G2/mitotic-specific cyclin-B1

Gene names

Name:	CCNB1
Synonyms:	CCNB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for the control of the cell cycle at the G2/M (mitosis) transition. Ref.16 Ref.17
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. Interacts with CCNF; interaction is required for nuclear localization. Ref.1 Ref.5 Ref.7 Ref.8
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton › centrosome Ref.5 Ref.6 Ref.9 Ref.11.
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.10 Phosphorylated by PLK1 at Ser-133 on centrosomes during prophase: phosphorylation by PLK1 does not cause nuclear import. Phosphorylation at Ser-147 was also reported to be mediated by PLK1 but Ser-133 seems to be the primary phosphorylation site. Ref.6 Ref.9 Ref.12 Ref.13
Sequence similarities	Belongs to the cyclin family. Cyclin AB subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Molecular function	Cyclin
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome G2/M transition of mitotic cell cycle Non-traceable author statement. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Traceable author statement. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle spindle checkpoint Inferred from mutant phenotype. Source: BHF-UCL mitotic metaphase plate congression Inferred from mutant phenotype. Source: BHF-UCL mitotic prometaphase Inferred from direct assay. Source: BHF-UCL mitotic spindle stabilization Inferred from mutant phenotype. Source: BHF-UCL positive regulation of attachment of spindle microtubules to kinetochore Inferred from mutant phenotype. Source: BHF-UCL positive regulation of mitotic cell cycle Inferred from mutant phenotype. Source: BHF-UCL positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome regulation of cyclin-dependent protein kinase activity Inferred from electronic annotation. Source: InterPro
Cellular component	condensed nuclear chromosome outer kinetochore Inferred from direct assay. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome spindle pole Inferred from direct assay. Source: BHF-UCL
Molecular function	patched binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CCNB1IP1	Q9NPC3	2	EBI-495332,EBI-745269
CDK1	P06493	4	EBI-495332,EBI-444308
PKMYT1	Q99640	2	EBI-495332,EBI-495308

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 433

433

G2/mitotic-specific cyclin-B1

PRO_0000080350

Regions

Region

169 – 177

Interaction with CDK2

Region

258 – 261

Interaction with CDK2

Compositional bias

51 – 85

Lys-rich

Amino acid modifications

Modified residue

Phosphoserine Ref.12 Ref.13

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

N6-acetyllysine Ref.14

Modified residue

126

Phosphoserine; by CDK1 Ref.6 Ref.9

Modified residue

128

Phosphoserine Ref.6

Modified residue

133

Phosphoserine; by PLK1 Ref.6 Ref.9

Modified residue

147

Phosphoserine Ref.6 Ref.9

Modified residue

321

Phosphothreonine Ref.12

Experimental info

Mutagenesis

133

S → A: Strongly impairs phosphorylation by PLK1. Ref.6 Ref.9

Mutagenesis

147

S → A: Does not affect phosphorylation by PLK1. Ref.9

Secondary structure

433

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P14635 [UniParc].

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

FASTA

433

48,337

        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' referencesShow '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]	"Cyclin F regulates the nuclear localization of cyclin B1 through a cyclin-cyclin interaction." Kong M., Barnes E.A., Ollendorff V., Donoghue D.J. EMBO J. 19:1378-1388(2000) [PubMed: 10716937] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CCNF.
[6]	"Cooperative phosphorylation including the activity of polo-like kinase 1 regulates the subcellular localization of cyclin B1." Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E., Kaufmann M., Strebhardt K. Oncogene 21:8282-8292(2002) [PubMed: 12447691] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-128; SER-133 AND SER-147, MUTAGENESIS OF SER-133.
[7]	"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.
[8]	"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.
[9]	"Active cyclin B1-Cdk1 first appears on centrosomes in prophase." Jackman M., Lindon C., Nigg E.A., Pines J. Nat. Cell Biol. 5:143-148(2003) [PubMed: 12524548] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-126; SER-133 AND SER-147, MUTAGENESIS OF SER-133 AND SER-147.
[10]	"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.
[11]	"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.
[12]	"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. Tissue: Cervix carcinoma.
[13]	"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.
[14]	"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.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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.
[17]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M25753 mRNA. No translation available.
AY338491 Genomic DNA. Translation: AAP88038.1.
BC006510 mRNA. Translation: AAH06510.1.

IPI

IPI00745793.

PIR

A32992.

RefSeq

NP_114172.1. NM_031966.3.

UniGene

Hs.23960.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B9R	X-ray	2.90	A/B	165-433	[»]
2JGZ	X-ray	2.90	B	167-426	[»]

ProteinModelPortal

P14635.

SMR

P14635. Positions 167-426.

DisProt

DP00223.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59N.

IntAct

P14635. 10 interactions.

MINT

MINT-1202632.

STRING

P14635.

PTM databases

PhosphoSite

P14635.

Polymorphism databases

DMDM

116176.

Proteomic databases

PRIDE

P14635.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256442; ENSP00000256442; ENSG00000134057.

GeneID

891.

KEGG

hsa:891.

UCSC

uc003jvl.1. human.

Organism-specific databases

CTD

891.

GeneCards

GC05P068462.

H-InvDB

HIX0004916.

HGNC

HGNC:1579. CCNB1.

HPA

CAB000115.
CAB003804.

MIM

123836. gene.

neXtProt

NX_P14635.

PharmGKB

PA95.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12100.

HOGENOM

HBG750484.

HOVERGEN

HBG061650.

InParanoid

P14635.

OMA

NIVMVNR.

OrthoDB

EOG47WNP2.

PhylomeDB

P14635.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.

Gene expression databases

ArrayExpress

P14635.

Bgee

P14635.

CleanEx

HS_CCNB1.

Genevestigator

P14635.

GermOnline

ENSG00000134057. Homo sapiens.

Family and domain databases

InterPro

IPR013763. Cyclin-like.
IPR014400. Cyclin_A/B/D/E.
IPR004367. Cyclin_C.
IPR006671. Cyclin_N.
[Graphical view]

Gene3D

G3DSA:1.10.472.10. Cyclin_related. 2 hits.

K05868.

Pfam

PF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001771. Cyclin_A_B_D_E. 1 hit.

SMART

SM00385. CYCLIN. 2 hits.
[Graphical view]

SUPFAM

SSF47954. Cyclin_like. 2 hits.

PROSITE

PS00292. CYCLINS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

3686.

SOURCE

Search...

Entry information

Entry name

CCNB1_HUMAN

Accession

Primary (citable) accession number: P14635

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 5

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·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents