PROSITE documentation PDOC50105SAM domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC50105
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.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Schultz J. Ponting C.P. Hofmann K. Bork P. |
| Title | SAM as a protein interaction domain involved in developmental regulation. | |
| Source | Protein Sci. 6:249-253(1997). | |
| PubMed ID | 9007998 |
| 2 | Authors | Stapleton D. Balan I. Pawson T. Sicheri F. |
| Title | The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization. | |
| Source | Nat. Struct. Biol. 6:44-49(1999). | |
| PubMed ID | 9886291 | |
| DOI | 10.1038/4917 |
| 3 | Authors | Peterson A.J. Kyba M. Bornemann D. Morgan K. Brock H.W. Simon J. |
| Title | A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions. | |
| Source | Mol. Cell. Biol. 17:6683-6692(1997). | |
| PubMed ID | 9343432 |
| 4 | Authors | Thanos C.D. Goodwill K.E. Bowie J.U. |
| Title | Oligomeric structure of the human EphB2 receptor SAM domain. | |
| Source | Science 283:833-836(1999). | |
| PubMed ID | 9933164 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.