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SHP-1 (PTPN6) is a non-receptor protein tyrosine phosphatase that is expressed primarily in hematopoietic cells. The enzyme is composed of two SH2 domains, a tyrosine phosphatase catalytic domain, and a carboxy-terminal regulatory domain. SHP-1 removes phosphates from target proteins to downregulate several tyrosine kinase-regulated pathways. In hematopoietic cells, the amino-terminal SH2 domain of SHP-1 binds to tyrosine phosphorylated erythropoietin receptors (EpoR) to negatively regulate hematopoietic growth. Overexpression of SHP-1 in epithelial cells results in dephosphorylation of the Ros receptor tyrosine kinase and subsequent downregulation of Ros-dependent cell proliferation and transformation. Following ligand binding in myeloid cells, SHP-1 associates with the IL-3R beta chain and downregulates IL-3-induced tyrosine phosphorylation and cell proliferation.
cb244; eleven-nineteen lysine-rich leukemia gene 2; ELL2; ELL-related RNA polymerase II, elongation factor; elongation factor for RNA polymerase II 2; elongation factor RNA for polymerase II 2; elongation factor RNA polymerase II 2; elongation factor, RNA polymerase II 2; elongation factor, RNA polymerase II, 2; fb78f03; im:3814960; RNA polymerase II elongation factor ELL2; RNA polymerase II elongation factor ELL2-like protein; sb:cb244; wu:fb78f03; wu:fb78f03 protein
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