Mj. Wishart et Je. Dixon, GATHERING STYX - PHOSPHATASE LIKE FORM PREDICTS FUNCTIONS FOR UNIQUE PROTEIN-INTERACTION DOMAINS, Trends in biochemical sciences, 23(8), 1998, pp. 301-306
The effects of tyrosine phosphorylation are manifested and regulated t
hrough protein domains that bind to specific phosphotyrosine motifs. S
TYX is a unique modular domain found within proteins implicated in med
iating the effects of tyrosine phosphorylation in vivo. Individual STY
X domains are not catalytically active; however, they resemble protein
tyrosine phosphatase (PTP) domains and, like PTPs, contain core seque
nces that recognize phosphorylated substrates. Thus, the STYX domain a
dds to the repertoire of modular domains that can mediate intracellula
r signaling in response to protein phosphorylation.