Biology:Cyclin A1

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A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Cyclin-A1 is a protein that in humans is encoded by the CCNA1 gene.[1]

Function

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 division cycle. Cyclins function as activating subunits of enzymatic complex together with cyclin-dependent kinases (CDKs). Different cyclins exhibit distinct expression and degradation patterns that contribute to the temporal coordination of cell cycle events. Cyclin A1 was shown to be expressed in testis and brain, as well as in several leukemic cell lines, and is thought to primarily function in the control of meiosis. This cyclin binds both Cdk1 and Cdk2 kinases, which give two distinct kinase activities, one appearing in S phase, the other in G2, and thus regulate separate functions in cell cycle. This cyclin was found to bind to important cell cycle regulators, such as Rb family proteins, transcription factor E2F1, and the Kip/Cip family of CDK-inhibitor proteins.[2]

Interactions

Cyclin-A1 interacts with:


References

  1. 1.0 1.1 "Characterization of a second human cyclin A that is highly expressed in testis and in several leukemic cell lines". Cancer Res. 57 (5): 913–920. March 1997. PMID 9041194. 
  2. "Entrez Gene: CCNA1 cyclin A1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8900. 
  3. "Human p55(CDC)/Cdc20 associates with cyclin A and is phosphorylated by the cyclin A-Cdk2 complex". Biochem. Biophys. Res. Commun. 268 (2): 530–534. February 2000. doi:10.1006/bbrc.2000.2167. PMID 10679238. 
  4. "A distinct cyclin A is expressed in germ cells in the mouse". Development 122 (1): 53–64. January 1996. doi:10.1242/dev.122.1.53. PMID 8565853. 
  5. 5.0 5.1 "Cyclin A1 directly interacts with B-myb and cyclin A1/cdk2 phosphorylate B-myb at functionally important serine and threonine residues: tissue-specific regulation of B-myb function". Blood 97 (7): 2091–2097. April 2001. doi:10.1182/blood.v97.7.2091. PMID 11264176. 
  6. "The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases". Nat. Cell Biol. 1 (7): 438–443. November 1999. doi:10.1038/15674. PMID 10559988. 
  7. 7.0 7.1 "Functions of cyclin A1 in the cell cycle and its interactions with transcription factor E2F-1 and the Rb family of proteins". Mol. Cell. Biol. 19 (3): 2400–2407. March 1999. doi:10.1128/mcb.19.3.2400. PMID 10022926. 
  8. 8.0 8.1 "Identification of interaction partners and substrates of the cyclin A1-CDK2 complex". J. Biol. Chem. 279 (32): 33727–33741. August 2004. doi:10.1074/jbc.M401708200. PMID 15159402. 

Further reading