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The Journal of Neuroscience, July 2, 2003, ():

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Barentsz, a New Component of the Staufen-Containing Ribonucleoprotein Particles in Mammalian Cells, Interacts with Staufen in an RNA-Dependent Manner
J. Neurosci. Macchi et al. 23 (13): 5778.

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  • Supplementary Figure 1 - Alignment of a conserved domain in MLN51 and TRAP150 proteins. The domain is located toward the N terminal of MLN51 proteins and at the very C terminal of TRAP150 proteins. Whereas MLN51 and its homologs are widely distributed in animals and plants, the only fungal sequence that could be identified is from Neurospora crassa. TRAP150 homologs appear to be present in all vertebrates, but not in other organisms. Humans contain two paralogs of TRAP150; the phylogenetic depth of this paralogy is unclear. Residues highly conserved in MLN51 proteins from animals are colored red. Gly-Arg-rich regions are colored blue.




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