PROSITE documentation PDOC50105
SAM domain profile


The sterile α motif (SAM) domain is a putative protein interaction module present in a wide variety of proteins [1] involved in many biological processes. The SAM domain that spreads over around 70 residues is found in diverse eukaryotic organisms [2]. SAM domains have been shown to homo- and hetero-oligomerize [3], nevertheless with a low-affinity constant [4], 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 [4]. The presence of these two distinct intermonomers binding surface suggest that SAM could form extended polymeric structures [4].

Some of the proteins in which such a domain is known to exist are listed below.

  • Vertebrate Eph receptor protein tyrosine kinases. Involved in developmental regulation.
  • Yeast STE11, serine/threonine protein kinase which participates in mating pheromone response pathways.
  • Mammalian liprin α. Interacts with LAR transmembrane protein tyrosine phosphatase.
  • Mammalian Neurabin actin filament binding protein. Involved in neurite formation.
  • 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 genes.
  • 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.

Last update:

December 2001 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

SAM_DOMAIN, PS50105; SAM domain profile  (MATRIX)


1AuthorsSchultz J. Ponting C.P. Hofmann K. Bork P.
TitleSAM as a protein interaction domain involved in developmental regulation.
SourceProtein Sci. 6:249-253(1997).
PubMed ID9007998

2AuthorsStapleton D. Balan I. Pawson T. Sicheri F.
TitleThe crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization.
SourceNat. Struct. Biol. 6:44-49(1999).
PubMed ID9886291

3AuthorsPeterson A.J. Kyba M. Bornemann D. Morgan K. Brock H.W. Simon J.
TitleA domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions.
SourceMol. Cell. Biol. 17:6683-6692(1997).
PubMed ID9343432

4AuthorsThanos C.D. Goodwill K.E. Bowie J.U.
TitleOligomeric structure of the human EphB2 receptor SAM domain.
SourceScience 283:833-836(1999).
PubMed ID9933164

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