The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

Khdrbs2  -  KH domain containing, RNA binding, signal...

Mus musculus

Synonyms: 6330586C16Rik, KH domain-containing, RNA-binding, signal transduction-associated protein 2, SLM-1, Sam68-like mammalian protein 1, Slim1, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on Khdrbs2

  • SLM-1 is an RNA-binding protein that is tyrosine phosphorylated by Src during mitosis [1].
  • Together, our data suggest that Slm1 and Slm2 define a molecular link between phosphoinositide and sphingolipid signaling and thereby regulate actin cytoskeleton organization [2].
  • The phosphorylation of SLM-1 and SLM-2 has functional relevance and leads to inhibition of their RNA-binding abilities [3].

References

  1. Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis. Di Fruscio, M., Chen, T., Richard, S. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. The phosphatidylinositol 4,5-biphosphate and TORC2 binding proteins Slm1 and Slm2 function in sphingolipid regulation. Tabuchi, M., Audhya, A., Parsons, A.B., Boone, C., Emr, S.D. Mol. Cell. Biol. (2006) [Pubmed]
  3. The nuclear tyrosine kinase BRK/Sik phosphorylates and inhibits the RNA-binding activities of the Sam68-like mammalian proteins SLM-1 and SLM-2. Haegebarth, A., Heap, D., Bie, W., Derry, J.J., Richard, S., Tyner, A.L. J. Biol. Chem. (2004) [Pubmed]
 
WikiGenes - Universities