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InterPro: IPR001660 Sterile alpha motif SAM
Protein matches
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UniProtKB Matches: 2424 proteins |
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Accession
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IPR001660 SAM |
Secondary
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IPR000964
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Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR013761 Sterile alpha motif-type
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Found in
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IPR016257 Tyrosine-protein kinase, ephrin receptor
IPR017239 MAP kinase kinase kinase STE11
IPR020766 Tyrosine-protein kinase, ephrin A10 receptor
IPR020767 Tyrosine-protein kinase, ephrin B6 receptor
IPR020768 Tyrosine-protein kinase, ephrin A receptor
IPR020769 Tyrosine-protein kinase, ephrin B receptor
IPR020770 Tyrosine-protein kinase, ephrin A1/A2 receptor
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InterPro annotation
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Entry Details in BioMart
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Abstract
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The sterile alpha 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-oligomerise, forming multiple self-association architectures and also binding to various non-SAM
domain-containing proteins [3], nevertheless with a
low affinity constant [4]. SAM domains also appear to possess the ability to bind RNA [5]. Smaug, a protein that helps to establish a morphogen gradient in Drosophila embryos by
repressing the translation of nanos (nos) mRNA, binds to the 3'
untranslated region (UTR) of nos mRNA via two similar hairpin structures. The 3D crystal
structure of the Smaug RNA-binding region shows a cluster of positively charged residues on the Smaug-SAM domain, which
could be the RNA-binding surface. This electropositive potential is unique among all previously
determined SAM-domain structures and is conserved among Smaug-SAM homologs. These results
suggest that the SAM domain might have a primary role in RNA binding.
Structural analyses show that the SAM domain is arranged in a small five-helix bundle with two large interfaces [3]. 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 [4].
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Structural links
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Database links
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Pfam Clan: CL0003.17
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Example proteins
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O15350 Tumor protein p73
P23561 Serine/threonine-protein kinase STE11
P39769 Polyhomeotic-proximal chromatin protein
P54763 Ephrin type-B receptor 2
Q11181 Uncharacterized protein C05D10.4
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR011510 |
Sterile alpha motif homology 2 |
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| IPR002117 |
p53 tumour antigen |
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| IPR017441 |
Protein kinase, ATP binding site |
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| IPR017442 |
Serine/threonine-protein kinase-like domain |
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| IPR013761 |
Sterile alpha motif-type |
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| IPR011009 |
Protein kinase-like domain |
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| IPR008957 |
Fibronectin, type III-like fold |
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| IPR008979 |
Galactose-binding domain-like |
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| IPR020635 |
Tyrosine-protein kinase, subgroup, catalytic domain |
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| IPR001426 |
Tyrosine-protein kinase, receptor class V, conserved site |
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| IPR000719 |
Protein kinase, catalytic domain |
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| IPR002290 |
Serine/threonine-protein kinase domain |
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| IPR015748 |
Mitogen activated protein kinase kinase kinase 3 |
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| IPR011615 |
p53, DNA-binding |
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| IPR003961 |
Fibronectin, type III |
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| IPR003962 |
Fibronectin, type III subdomain |
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| IPR012313 |
Zinc finger, FCS-type |
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| IPR015551 |
Cellular tumour antigen p53 |
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| IPR001245 |
Tyrosine-protein kinase, catalytic domain |
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| IPR001090 |
Ephrin receptor, ligand binding |
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| IPR008266 |
Tyrosine-protein kinase, active site |
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| IPR020685 |
Tyrosine-protein kinase |
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| IPR012346 |
p53/RUNT-type transcription factor, DNA-binding domain |
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| IPR008271 |
Serine/threonine-protein kinase, active site |
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| IPR001660 |
Sterile alpha motif SAM |
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| IPR008967 |
p53-like transcription factor, DNA-binding |
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| IPR016257 |
Tyrosine-protein kinase, ephrin receptor |
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| IPR010991 |
p53, tetramerisation |
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| IPR010993 |
Sterile alpha motif homology |
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ModBase |
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SWISS-MODEL |
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PDB Chain |
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CATH Domain |
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SCOP Domain |
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Publications
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1.
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Schultz J, Ponting CP, Hofmann K, Bork P.
SAM as a protein interaction domain involved in developmental regulation.
Protein Sci. 6 249-53 1997
[PubMed: 9007998]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=9007998&action=stream&blobtype=pdf
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2.
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Stapleton D, Balan I, Pawson T, Sicheri F.
The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization.
Nat. Struct. Biol. 6 44-9 1999
[PubMed: 9886291]
http://dx.doi.org/10.1038/4917
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3.
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Peterson AJ, Kyba M, Bornemann D, Morgan K, Brock HW, Simon J.
A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions.
Mol. Cell. Biol. 17 6683-92 1997
[PubMed: 9343432]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=9343432&action=stream&blobtype=pdf
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4.
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Thanos CD, Goodwill KE, Bowie JU.
Oligomeric structure of the human EphB2 receptor SAM domain.
Science 283 833-6 1999
[PubMed: 9933164]
http://dx.doi.org/10.1126/science.283.5403.833
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5.
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Kim CA, Bowie JU.
SAM domains: uniform structure, diversity of function.
Trends Biochem. Sci. 28 625-8 2003
[PubMed: 14659692]
http://dx.doi.org/10.1016/j.tibs.2003.11.001
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Additional Reading
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Kim CA, Sawaya MR, Cascio D, Kim W, Bowie JU.
Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.
J. Biol. Chem. 280 2005 27769-75
[PubMed: 15905166]
http://dx.doi.org/10.1074/jbc.M503055200
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Baron MK, Boeckers TM, Vaida B, Faham S, Gingery M, Sawaya MR, Salyer D, Gundelfinger ED, Bowie JU.
An architectural framework that may lie at the core of the postsynaptic density.
Science 311 2006 531-5
[PubMed: 16439662]
http://dx.doi.org/10.1126/science.1118995
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Bhattacharjya S, Xu P, Gingras R, Shaykhutdinov R, Wu C, Whiteway M, Ni F.
Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex.
J. Mol. Biol. 344 2004 1071-87
[PubMed: 15544813]
http://dx.doi.org/10.1016/j.jmb.2004.09.018
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Kwan JJ, Warner N, Pawson T, Donaldson LW.
The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50.
J. Mol. Biol. 342 2004 681-93
[PubMed: 15327964]
http://dx.doi.org/10.1016/j.jmb.2004.06.064
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Green JB, Gardner CD, Wharton RP, Aggarwal AK.
RNA recognition via the SAM domain of Smaug.
Mol. Cell 11 2003 1537-48
[PubMed: 12820967]
http://dx.doi.org/10.1016/S1097-2765(03)00178-3
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Ponting CP.
SAM: a novel motif in yeast sterile and Drosophila polyhomeotic proteins.
Protein Sci. 4 1995 1928-30
[PubMed: 8528090]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8528090&action=stream&blobtype=pdf
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InterPro 23.1
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