The carboxy-terminal sequence of p56lck can regulate p60c-src.
A chimera containing the coding region for residues 1 to 516 of p60c-src and residues 495 to 509 (the carboxy terminus) of p56lck was constructed and expressed in mouse fibroblasts. The chimeric protein appeared to be phosphorylated and regulated in the same fashion as p60c-src.
MacAuley
A
A
Department of Cell Biology, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104.
Cooper
J A
JA
D000595:Amino Acid Sequence; D001483:Base Sequence; D005796:Genes; D005814:Genes, Viral; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010748:Phosphopeptides / Q000032:analysis; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000235:genetics* / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000235:genetics* / Q000378:metabolism; D016392:Proto-Oncogene Proteins pp60(c-src); D012045:Regulatory Sequences, Nucleic Acid
D010748:Phosphopeptides; D011518:Proto-Oncogene Proteins; D011505:Protein-Tyrosine Kinases; D019860:Lymphocyte Specific Protein Tyrosine Kinase p56(lck); D016392:Proto-Oncogene Proteins pp60(c-src)