期刊
CELL REPORTS
卷 3, 期 4, 页码 1293-1305出版社
CELL PRESS
DOI: 10.1016/j.celrep.2013.03.001
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类别
资金
- EU FP6 Interaction Proteome integrated project
- FP7 Affinomics project
- Italian Foundation for Cancer Research (AIRC)
- Novo Nordisk Foundation
Members of the SH2 domain family modulate signal transduction by binding to short peptides containing phosphorylated tyrosines. Each domain displays a distinct preference for the sequence context of the phosphorylated residue. We have developed a high-density peptide chip technology that allows for probing of the affinity of most SH2 domains for a large fraction of the entire complement of tyrosine phosphopeptides in the human proteome. Using this technique, we have experimentally identified thousands of putative SH2-peptide interactions for more than 70 different SH2 domains. By integrating this rich data set with orthogonal context-specific information, we have assembled an SH2-mediated probabilistic interaction network, which we make available as a community resource in the PepspotDB database. A predicted dynamic interaction between the SH2 domains of the tyrosine phosphatase SHP2 and the phosphorylated tyrosine in the extracellular signal-regulated kinase activation loop was validated by experiments in living cells.
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