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Wiley, Protein Science, 1(6), p. 249-253, 1997

DOI: 10.1002/pro.5560060128

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SAM as a protein interaction domain involved in developmental regulation.

Journal article published in 1997 by Jörg Schultz, Peer Bork, Kay Hofmann, Christopher P. Ponting ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

More than 60 previously undetected SAM domain-containing proteins have been identified using profile searching methods. Among these are over 40 EPH-related receptor tyrosine kinases (RPTK), Drosophila bicaudal-C, a p53 from Loligo forbesi, and diacyglycerol-kinase isoform delta. This extended dataset suggests that SAM is an evolutionary conserved protein binding domain that is involved in the regulation of numerous developmental processes among diverse eukaryotes. A conserved tyrosine in the SAM sequences of the EPH related RPTKs is likely to mediate cell-cell initiated signal transduction via the binding of SH2 containing proteins to phosphotyrosine.