title: SAM as a protein interaction domain involved in developmental regulation.
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.
authors.affiliation: EMBL, Heidelberg, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Schultz
authors.forename: C P
authors.initials: CP
authors.lastname: Ponting
authors.forename: K
authors.initials: K
authors.lastname: Hofmann
authors.forename: P
authors.initials: P
authors.lastname: Bork
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018507:Gene Expression Regulation, Developmental; D006801:Humans; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid