Protein tyrosine phosphatases are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity. As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation, transformation, and synaptic plasticity.[1][2][3][4] [from: Wikipedia contributors. (2018, November 4). Protein tyrosine phosphatase. In Wikipedia, The Free Encyclopedia. Retrieved 19:49, June 6, 2019, from https://en.wikipedia.org/w/index.php?title=Protein_tyrosine_phosphatase&oldid=867219916.]

SHP1 belongs to the family of protein tyrosine phosphatases (PTPs), which dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases. PTPs and protein tyrosine kinases function in a variety of cellular processes, from cell survival to proliferation, differentiation, migration, and immune responses. SHP1 (PTPN6) and SHP2 (PTPN11) are closely related non–receptor-type PTPs, each having two Src homology 2 domains N-terminal to the phosphatase catalytic domain (5–7). Although SHP2 is expressed ubiquitously, SHP1 is predominantly expressed in hematopoietic cell lineages, and it has been implicated in the regulation of a diverse range of cytokine receptors, growth factor receptors, and immunoreceptors (5, 6, 8). SHP1 has been shown to associate with ITIMs in these receptors (5, 6) and has been proposed to bind to ITIM-like motifs in various kinases, including IL-1R–associated kinase 1, ERK1/2, p38, JNK, JAK2, JAK3, TAK1, IκB kinase α, and LYN (9, 10). [from: Kanwal Z, Zakrzewska A, Hertog Jd, Spaink HP, Schaaf MJM and Meijer AH. (2013) Deficiency in Hematopoietic Phosphatase Ptpn6/Shp1 Hyperactivates the Innate Immune System and Impairs Control of Bacterial Infections in Zebrafish Embryos. J Immunol. 190:1631-1645.]

References:
1) Ozawa T, Nakata K, Mizuno K, Yakura H. (2007) Negative autoregulation of Src homology region 2-domain-containing phosphatase-1 in rat basophilic leukemia-2H3 cells. Int Immunol. (9):1049-1061.

Protein tyrosine phosphatases are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine (pTyr) phosphorylation is a common post-translational modification that can create novel recognition motifs for protein interactions and cellular localization, affect protein stability, and regulate enzyme activity. As a consequence, maintaining an appropriate level of protein tyrosine phosphorylation is essential for many cellular functions. Tyrosine-specific protein phosphatases (PTPase; EC 3.1.3.48) catalyse the removal of a phosphate group attached to a tyrosine residue, using a cysteinyl-phosphate enzyme intermediate. These enzymes are key regulatory components in signal transduction pathways (such as the MAP kinase pathway) and cell cycle control, and are important in the control of cell growth, proliferation, differentiation, transformation, and synaptic plasticity.[1][2][3][4] [from: Wikipedia contributors. (2018, November 4). Protein tyrosine phosphatase. In Wikipedia, The Free Encyclopedia. Retrieved 19:49, June 6, 2019, from https://en.wikipedia.org/w/index.php?title=Protein_tyrosine_phosphatase&oldid=867219916.]

SHP1 belongs to the family of protein tyrosine phosphatases (PTPs), which dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases. PTPs and protein tyrosine kinases function in a variety of cellular processes, from cell survival to proliferation, differentiation, migration, and immune responses. SHP1 (PTPN6) and SHP2 (PTPN11) are closely related non–receptor-type PTPs, each having two Src homology 2 domains N-terminal to the phosphatase catalytic domain (5–7). Although SHP2 is expressed ubiquitously, SHP1 is predominantly expressed in hematopoietic cell lineages, and it has been implicated in the regulation of a diverse range of cytokine receptors, growth factor receptors, and immunoreceptors (5, 6, 8). SHP1 has been shown to associate with ITIMs in these receptors (5, 6) and has been proposed to bind to ITIM-like motifs in various kinases, including IL-1R–associated kinase 1, ERK1/2, p38, JNK, JAK2, JAK3, TAK1, IκB kinase α, and LYN (9, 10). [from: Kanwal Z, Zakrzewska A, Hertog Jd, Spaink HP, Schaaf MJM and Meijer AH. (2013) Deficiency in Hematopoietic Phosphatase Ptpn6/Shp1 Hyperactivates the Innate Immune System and Impairs Control of Bacterial Infections in Zebrafish Embryos. J Immunol. 190:1631-1645.]

References:
1) Ozawa T, Nakata K, Mizuno K, Yakura H. (2007) Negative autoregulation of Src homology region 2-domain-containing phosphatase-1 in rat basophilic leukemia-2H3 cells. Int Immunol. (9):1049-1061.