Signaling molecules are often composed of distinct modules, each with a specific binding or catalytic function. The discovery of tyrosine phosphorylation represented a major breakthrough in the study of cellular signaling pathways. It was subsequently discovered that the sequence surrounding specific phosphorylated tyro-sine residues contributes to the interaction of tyrosine-phosphorylated proteins with other signaling molecules. An appreciation that signaling molecules contain modules or domains that each have defined functions was obtained from the study of non-receptor tyrosine kinases. The cellular homologue of the transforming protein of the Rous sarcoma virus, called c-Src, is the prototype for an immunologically important family of non-receptor tyrosine kinases known as Src family kinases. c-Src contains unique domains, including Src homology 2 (SH2) and Src homology 3 (SH3) domains described later. It also
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