phosphoprotein phosphatase (phosphotyrosine)
mutant F513S, deletion 528-593, phosphorylated Y542/Y580
Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras.
Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase.
Interaction of SH2-containing protein tyrosine phosphatase 2 with the insulin receptor and the insulin-like growth factor-I receptor: studies of the domains involved using the yeast two-hybrid system.
Involvement of Src-homology-2-domain-containing protein-tyrosine phosphatase 2 in T cell activation.
Characterization of two SHP-2-associated binding proteins and potential substrates in hematopoietic cells.
Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2.
Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera.
A family of proteins that inhibit signalling through tyrosine kinase receptors.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-526.
Crystal structure of the tyrosine phosphatase SHP-2.
Protein tyrosine phosphatases: mechanisms of catalysis and regulation.
SHP-2, SH2-containing protein tyrosine phosphatase-2.
A new tyrosine-phosphorylated 97-kDa adaptor protein mediates interleukin-2-induced association of SHP-2 with p85-phosphatidylinositol 3-kinase in human T lymphocytes.
Roles of the complex formation of SHPS-1 with SHP-2 in insulin-stimulated mitogen-activated protein kinase activation.
Enhancing leptin response by preventing SH2-containing phosphatase 2 interaction with Ob receptor.
Regulation of B cell signal transduction by SH2-containing protein-tyrosine phosphatases.
Revealing mechanisms for SH2 domain mediated regulation of the protein tyrosine phosphatase SHP-2.
Tyrosine phosphatase SHP-2 dephosphorylates the platelet-derived growth factor receptor but enhances its downstream signalling.
Immune signalling: SHP-2 docks at multiple ports.
Shp-2 tyrosine phosphatase: signaling one cell or many.
Cytoplasmic protein tyrosine phosphatases SHP-1 and SHP-2: regulators of B cell signal transduction.
Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family protein containing immunoreceptor tyrosine-based inhibitory motifs.
Role of the SHP-2 tyrosine phosphatase in cytokine-induced signaling and cellular response.
Chemical dissection of the effects of tyrosine phosphorylation of SHP-2.
Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2) can play a direct role in the inhibitory function of killer cell Ig-like receptors in human NK cells.
This enzyme is composed of two SH2 domains, and the C-terminal catalytic domain. According to the literature [9], the N-terminal SH2 domain seems to inhibit the catalytic reaction by interacting directly with the active site. As the catalytic domain is homologous to other phosphatase domains (S00458, D00154, M00149, M00169 in EzCatDB) and the catalytic residues are conserved, the mechanism must be similar to those of the counterparts. The literature [10] confirmed that Cys459, Asp425 and Arg465 act as nucleophile, acid-base, and stabilizer for the phosphate group, respectively, and that loop 460-465 also stabilizes the phosphate group during the catalysis.