Homology between phosphotyrosine acceptor site of human c-abl and viral oncogene products.
The human homologues of several independent viral oncogenes, each of which encodes tyrosine-specific protein kinases, have been identified. Of these, three (v-src, v-yes and v-fes/fps) are known to exhibit considerable sequence homology, particularly in the regions of their phosphorylation acceptor sites. In the present study, sequences encoding the tyrosine phosphorylation acceptor sites of the Abelson murine leukaemia virus oncogene, v-abl, and its human cellular homologue, c-abl, have been identified and their nucleic acid sequences determined. Our results establish extensive homology between this region of c-abl and acceptor domains of the v-src, v-yes and v-fes/fps family of viral oncogenes, as well as more distant relatedness to the catalytic chain of the mammalian cyclic AMP-dependent protein kinase. These findings suggest that, of the homologues of retroviral oncogenes with tyrosine protein kinase activity examined to date, all were probably derived from a common progenitor and may represent members of a diverse family of cellular protein kinases.
D000595:Amino Acid Sequence; D001483:Base Sequence; D004262:DNA Restriction Enzymes; D005796:Genes; D005814:Genes, Viral; D006801:Humans; D009857:Oncogenes; D019000:Phosphotyrosine; D011494:Protein Kinases / Q000235:genetics*; D011505:Protein-Tyrosine Kinases; D014443:Tyrosine / Q000031:analogs & derivatives*
D019000:Phosphotyrosine; D014443:Tyrosine; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases; D004262:DNA Restriction Enzymes