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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.
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Protein Aliases: EC 3.1.3.48; hematopoietic cell phosphatase; Hematopoietic cell protein-tyrosine phosphatase; Protein-tyrosine phosphatase 1C; Protein-tyrosine phosphatase SHP-1; PTN6; PTP-1C; SH-PTP1; Tyrosine-protein phosphatase non-receptor type 6
Gene Aliases: HCP; HCPH; HPTP1C; PTP-1C; PTP1C; PTPN6; SH-PTP1; SHP-1; SHP-1L; SHP1
UniProt ID: (Human) P29350
Entrez Gene ID: (Human) 5777
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