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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains.

The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not catalytically active; however, they resemble protein tyrosine phosphatase ( PTP) domains and, like PTPs, contain core sequences that recognize phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation.[1]

References

  1. Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains. Wishart, M.J., Dixon, J.E. Trends Biochem. Sci. (1998) [Pubmed]
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