Cyclin A2

Cyclin A2
PDB rendering based on 1e9h.
Available structures PDB 1E9H, 1FIN, 1FVV, 1GY3, 1H1P, 1H1Q, 1H1R, 1H1S, 1H24, 1H25, 1H26, 1H27, 1H28, 1JST, 1JSU, 1OGU, 1OI9, 1OIU, 1OIY, 1OKV, 1OKW, 1OL1, 1OL2, 1P5E, 1PKD, 1QMZ, 1URC, 1VYW, 2BKZ, 2BPM, 2C4G, 2C5N, 2C5O, 2C5V, 2C5X, 2C6T, 2CCH, 2CCI, 2CJM, 2I40, 2IW6, 2IW8, 2IW9, 2UUE, 2UZB, 2UZD, 2UZE, 2UZL, 2V22, 2WEV, 2WFY, 2WHB, 2WIH, 2WIP, 2WMA, 2WMB, 2WPA, 2WXV, 2X1N, 3EID, 3EJ1, 3EOC, 3F5X
Identifiers
Symbols	CCNA2; CCN1; CCNA
External IDs	OMIM: 123835 MGI: 108069 HomoloGene: 55562 GeneCards: CCNA2 Gene
Gene Ontology Molecular function • protein binding • protein kinase binding Cellular component • female pronucleus • male pronucleus • nucleus • nucleoplasm • cytoplasm Biological process • regulation of cyclin-dependent protein kinase activity • G2/M transition of mitotic cell cycle • mitotic cell cycle • mitosis • mitotic cell cycle G2/M transition DNA damage checkpoint • Ras protein signal transduction • organ regeneration • response to estradiol stimulus • response to glucagon stimulus • positive regulation of fibroblast proliferation • cell division Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	890	12428
Ensembl	ENSG00000145386	ENSMUSG00000027715
UniProt	P20248	Q8BRG1
RefSeq (mRNA)	NM_001237	NM_009828.2
RefSeq (protein)	NP_001228	NP_033958.2
Location (UCSC)	Chr 4: 122.74 – 122.75 Mb	Chr 3: 36.46 – 36.47 Mb
PubMed search	[1]	[2]

Cyclin-A2 is a protein that in humans is encoded by the CCNA2 gene.^[1]

The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. In contrast to cyclin A1, which is present only in germ cells, this cyclin is expressed in all tissues tested. This cyclin binds and activates CDC2 or CDK2 kinases, and thus promotes both cell cycle G1/S and G2/M transitions.^[2]

See also

• Cyclin A

Interactions

Cyclin A2 has been shown to interact with ITGB3BP,^[3] Retinoblastoma-like protein 1,^[4][5] E2F1,^[6] CDC6,^[7][8] SKP2^[9][10] and Flap structure-specific endonuclease 1.^[11]

References

1. ^ Paterlini P, De Mitri MS, Martin C, Munnich A, Brechot C (July 1991). "A Taql polymorphism in the human cyclin A gene". Nucleic Acids Res 19 (9): 2516. doi:10.1093/nar/19.9.2516. PMC 329485. PMID 1675006. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=329485. 
2. ^ "Entrez Gene: CCNA2 cyclin A2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=890. 
3. ^ Ohtoshi, A; Maeda T, Higashi H, Ashizawa S, Yamada M, Hatakeyama M (January 2000). "beta3-endonexin as a novel inhibitor of cyclin A-associated kinase". Biochem. Biophys. Res. Commun. (UNITED STATES) 267 (3): 947–52. doi:10.1006/bbrc.1999.2007. ISSN 0006-291X. PMID 10673397. 
4. ^ Dyson, N; Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (December 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". J. Virol. (UNITED STATES) 67 (12): 7641–7. ISSN 0022-538X. PMC 238233. PMID 8230483. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=238233. 
5. ^ Joaquin, Manel; Bessa Maria, Saville Mark K, Watson Roger J (November 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene (England) 21 (52): 7923–32. doi:10.1038/sj.onc.1206001. ISSN 0950-9232. PMID 12439743. 
6. ^ Xu, M; Sheppard K A, Peng C Y, Yee A S, Piwnica-Worms H (December 1994). "Cyclin A/CDK2 binds directly to E2F-1 and inhibits the DNA-binding activity of E2F-1/DP-1 by phosphorylation". Mol. Cell. Biol. (UNITED STATES) 14 (12): 8420–31. ISSN 0270-7306. PMC 359381. PMID 7969176. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=359381. 
7. ^ Petersen, B O; Lukas J, Sørensen C S, Bartek J, Helin K (January 1999). "Phosphorylation of mammalian CDC6 by cyclin A/CDK2 regulates its subcellular localization". EMBO J. (ENGLAND) 18 (2): 396–410. doi:10.1093/emboj/18.2.396. ISSN 0261-4189. PMC 1171134. PMID 9889196. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171134. 
8. ^ Saha, P; Chen J, Thome K C, Lawlis S J, Hou Z H, Hendricks M, Parvin J D, Dutta A (May 1998). "Human CDC6/Cdc18 Associates with Orc1 and Cyclin-cdk and Is Selectively Eliminated from the Nucleus at the Onset of S Phase". Mol. Cell. Biol. (UNITED STATES) 18 (5): 2758–67. ISSN 0270-7306. PMC 110655. PMID 9566895. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=110655. 
9. ^ Rosner, Margit; Hengstschläger Markus (November 2004). "Tuberin binds p27 and negatively regulates its interaction with the SCF component Skp2". J. Biol. Chem. (United States) 279 (47): 48707–15. doi:10.1074/jbc.M405528200. ISSN 0021-9258. PMID 15355997. 
10. ^ Marti, A; Wirbelauer C, Scheffner M, Krek W (May 1999). "Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation". Nat. Cell Biol. (ENGLAND) 1 (1): 14–9. doi:10.1038/8984. ISSN 1465-7392. PMID 10559858. 
11. ^ Henneke, Ghislaine; Koundrioukoff Stéphane, Hübscher Ulrich (July 2003). "Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation". Oncogene (England) 22 (28): 4301–13. doi:10.1038/sj.onc.1206606. ISSN 0950-9232. PMID 12853968. 

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