Journal
MOLECULAR CELL
Volume 22, Issue 6, Pages 851-868Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2006.06.001
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SH2 domains are interaction modules uniquely dedicated to the recognition of phosphotyrosine sites and are embedded in proteins that couple protein-tyrosine kinases to intracellular signaling pathways. Here, we report a comprehensive bioinformatics, structural, and functional view of the human and mouse complement of SH2 domain proteins. This information delimits the set of SH2-containing effectors available for PTK signaling and will facilitate the systems-level analysis of pTyr-dependent protein-protein interactions and PTK-mediated signal transduction. The domain-based architecture of SH2-containing proteins is of more general relevance for understanding the large family of protein interaction domains and the modular organization of the majority of human proteins.
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