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The sterile α motif (SAM) domain is a putative protein interaction module
present in a wide variety of proteins  involved in many biological
processes. The SAM domain that spreads over around 70 residues is found in
diverse eukaryotic organisms . SAM domains have been shown to homo- and
hetero-oligomerize , nevertheless with a low-affinity constant , and to
mediate specific protein-protein interactions.
Structural analyses show that the SAM domain is arranged in a small five-helix
bundle with two large interfaces [3,4]. In the case of the SAM domain of
EphB2, each of these interfaces is able to form dimers . The presence of
these two distinct intermonomers binding surface suggest that SAM could form
extended polymeric structures .
Some of the proteins in which such a domain is known to exist are listed
Vertebrate Eph receptor protein tyrosine kinases. Involved in developmental
Yeast STE11, serine/threonine protein kinase which participates in mating
pheromone response pathways.
Mammalian liprin α. Interacts with LAR transmembrane protein tyrosine
Mammalian Neurabin actin filament binding protein. Involved in neurite
Mammalian inositol phosphatase protein Ship2.
Mammalian SH2 domain-containing leukocyte Protein of 76kDa (SLP-76).
Hematopoietic cell specific molecule, critical for T cell development.
Mammalian ETS translocation variant (ETV) or TEL. Translocations which fuse
the SAM domain from ETV to Abl, PDGFB, JAK2 or AML1 have been associated
with many human leukemias.
Drosophila polyhomeotic (ph) and Sex comb on midleg (Scm), member of the
Polycomb group genes, implied in the transcriptional repression of homeotic
Mammalian Polycomb group proteins Rae-28/MPH1 and SCML1. Homologues of
drosophila ph and Scm proteins.
We developed a profile that spans the whole domain.
December 2001 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Schultz J., Ponting C.P., Hofmann K., Bork P.
SAM as a protein interaction domain involved in developmental regulation.
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