The reversible tyrosine phosphorylation of proteins, modulated by the coordinated actions of
protein-tyrosine kinases and protein-tyrosine phosphatases (PTPs), regulates the cellular
response to a wide variety of stimuli. It is established that protein kinases possess discrete
sets of substrates and that substrate recognition is often dictated by the presence of
consensus phosphorylation sites. Here, we have extended this concept to the PTPs and
demonstrated that (E/D)-pY-pY-(R/K) is a consensus substrate recognition motif for PTP1B …