Cyclin A2


Cyclin A2
Cyclin A2

PDB rendering based on 1e9h.
Identifiers
Symbols CCNA2; CCN1; CCNA
External IDs OMIM123835 MGI108069 HomoloGene55562 GeneCards: CCNA2 Gene
RNA expression pattern
PBB GE CCNA2 203418 at tn.png
PBB GE CCNA2 213226 at tn.png
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

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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