Reviewed, UniProtKB/Swiss-Prot P14635 (CCNB1_HUMAN)

Names and origin

Protein names

Recommended name:
    G2/mitotic-specific cyclin-B1

Gene names

Name:	CCNB1
Synonyms:	CCNB

Organism

Homo sapiens (Human) [Complete proteome]

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.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. Cytoplasm › cytoskeleton › centrosome 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.

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
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Non-traceable author statement. Source: UniProtKB anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from Experiment. Source: Reactome microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC2	P06493	1	EBI-495332,EBI-444308
CDKN1B	P46527	1	EBI-495332,EBI-519280
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

9

Interaction with CDK2

Region

258 – 261

4

Interaction with CDK2

Compositional bias

51 – 85

35

Lys-rich

Amino acid modifications

Modified residue

9

1

Phosphoserine Ref.9

Modified residue

35

1

Phosphoserine Ref.9

Modified residue

69

1

Phosphoserine Ref.9

Modified residue

73

1

N6-acetyllysine Ref.12

Modified residue

321

1

Phosphothreonine Ref.9

Secondary structure

1

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433

Helix Strand Turn

Details...

Turn

173 – 177

5

Helix

178 – 183

6

Turn

189 – 192

4

Beta strand

193 – 197

5

Helix

199 – 215

17

Helix

220 – 234

15

Helix

241 – 243

3

Helix

244 – 259

16

Helix

266 – 272

7

Beta strand

275 – 277

3

Helix

279 – 292

14

Helix

302 – 311

10

Helix

317 – 329

13

Helix

330 – 332

3

Helix

334 – 336

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P14635-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: E2C4767AE8A11EC0	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

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]	"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.

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.

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	[»]

DisProt

DP00223.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59N.

IntAct

P14635. 6 interactions.

STRING

P14635.

PTM databases

PhosphoSite

P14635.

Proteomic databases

PRIDE

P14635.

Genome annotation databases

Ensembl

ENST00000256442; ENSP00000256442; ENSG00000134057; Homo sapiens. [Genome view]

GeneID

891.

KEGG

hsa:891.

UCSC

uc003jvl.1. human.

Organism-specific databases

CTD

891.

GeneCards

GC05P068498.

H-InvDB

HIX0004916.

HGNC

HGNC:1579. CCNB1.

HPA

CAB000115.
CAB003804.

MIM

123836. gene.

PharmGKB

PA95.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12100.

HOGENOM

HBG750484.

HOVERGEN

P14635.

InParanoid

P14635.

OMA

NIVMVNR.

OrthoDB

EOG9CZF19.

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

IPR015454. CycB.
IPR006670. Cyclin.
IPR011028. Cyclin-like.
IPR014400. Cyclin_A_B_D_E.
IPR004367. Cyclin_C.
IPR006671. Cyclin_N.
IPR013763. Cyclin_related.
[Graphical view]

Gene3D

G3DSA:1.10.472.10. Cyclin_related. 1 hit.

PANTHER

PTHR10177:SF27. CycB. 1 hit.

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]

PROSITE

PS00292. CYCLINS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	February 9, 2010
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.