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SAM domain

[sterile alpha motif] The SAM domain (approximately 70 amino acids) occurs in a wide range of proteins and has been described originally as a sequence domain present in a small group of yeast sexual differentiation and Drosophila melanogaster polyhomeotic proteins (Ponting). This domain has been identified also in a Drosophila melanogaster zinc finger protein, where it has been termed SPM domain (Bornemann et al, 1996). The domain is known also as PNT domain (pointed domain), so named after a Drosophila melanogaster gene involved in the development of the midline glial cells (Klambt), and has been found in a number of ets transcription factors (Slupsky et al, 1998). Another synonym for this protein-protein interaction motif is HLH domain (helix-loop-helix domain) (see: Kim et al, 2002; Ledent and Vervoort, 2001).

Proteins containing SAM domains include the Eph family of receptor tyrosine kinases (Hirai et al, 1987; Tessier-Lavigne et al, 1995), serine/threonine kinases (Tu et al, 1997), SH2 domain containing adaptor proteins (Schultz et al, 1997), ETS transcription factors (Kyba et al, 1998), p53 (Schultz et al, 1997) and many other proteins that allows the formation of homo and hetero-typic oligomers. The domain is evolutionally conserved and functions as a protein-protein interaction motif. As such, it is involved in the regulation of numerous eukaryotic developmental processes.

For information on other protein domains and sequence motifs see also the Protein domains Dictionary section of this encyclopedia.


Copyright 2012 by H IBELGAUFTS. All rights reserved.
ENTRY LAST MODIFIED: August 2003



 

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