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The ABL1 proto-oncogene encodes a cytoplasmic and nuclear protein tyrosine kinase that has been implicated in processes of cell differentiation, cell division, cell adhesion, and stress response. Activity of c-Abl protein is negatively regulated by its SH3 domain, and deletion of the SH3 domain turns c-Abl into an oncogene. The DNA-binding activity of the ubiquitously expressed ABL1 tyrosine kinase is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function for c-Abl. In chronic myelogenous leukemia and a subset of acute lymphoblastic leukemias, the c-Abl proto oncogene undergoes a (9;22) chromosomal translocation producing a novel rearranged chromosome (the Philadelphia chromosome). As the result of the fusion of c-Abl sequences from chromosome 9 to the Bcr gene on chromosome 22. The c-Abl oncogene was initially identified as the viral transforming gene of Abelson murine leukemia virus (A-MuLV). c-ABL potentially regulates DNA repair by activating the proapoptotic pathway when the DNA damage is too severe to be repaired.
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