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SAM as a protein interaction domain involved in developmental regulation
Author(s) -
Schultz Jörg,
Bork Peer,
Ponting Christopher P.,
Hofmann Kay
Publication year - 1997
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560060128
Subject(s) - erythropoietin producing hepatocellular (eph) receptor , sh2 domain , biology , receptor tyrosine kinase , ephrin , microbiology and biotechnology , signal transduction , gene isoform , phosphotyrosine binding domain , genetics , receptor protein tyrosine kinases , tyrosine kinase , sh3 domain , conserved sequence , protein domain , protein kinase domain , peptide sequence , gene , mutant
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 diacylglycerol‐kinase isoform δ. 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.