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  The SH2 Domain Interaction Landscape

Tinti, M., Kiemer, L., Costa, S., Miller, M. L., Sacco, F., Olsen, J. V., et al. (2013). The SH2 Domain Interaction Landscape. CELL REPORTS, 3(4), 1293-1305. doi:10.1016/j.celrep.2013.03.001.

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 Creators:
Tinti, Michele1, Author
Kiemer, Lars1, Author
Costa, Stefano1, Author
Miller, Martin L.1, Author
Sacco, Francesca1, Author
Olsen, Jesper V.2, Author              
Carducci, Martina1, Author
Paoluzi, Serena1, Author
Langone, Francesca1, Author
Workman, Christopher T.1, Author
Blom, Nikolaj1, Author
Machida, Kazuya1, Author
Thompson, Christopher M.1, Author
Schutkowski, Mike1, Author
Brunak, Soren1, Author
Mann, Matthias2, Author              
Mayer, Bruce J.1, Author
Castagnoli, Luisa1, Author
Cesareni, Gianni1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Free keywords: MOLECULAR INTERACTION DATABASE; PROTEIN-PROTEIN INTERACTIONS; SIGNAL-TRANSDUCTION; PHOSPHORYLATION SITES; BINDING DOMAINS; IN-VIVO; SPECIFICITY; NETWORKS; SEQUENCE; PREDICTION
 Abstract: 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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Language(s): eng - English
 Dates: 2013-04
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
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Title: CELL REPORTS
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 3 (4) Sequence Number: - Start / End Page: 1293 - 1305 Identifier: ISSN: 2211-1247