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The protein encoded by PTPN9 is a member of the protein tyrosine phosphatase (PTP) family.
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this study highlights an important role for miR (show MLXIP Antibodies)-96 in the regulation of PTPN9 in breast cancer cells and may provide insight into the molecular mechanisms of breast carcinogenesis.
Expression of MEG2 is reversely correlated with that of miR (show MLXIP Antibodies)-181a-5p in gastric cancer.
PTPN9 inhibited cell proliferation in HepG2 cells.
PTPMeg2 is an important phosphatase for the dephosphorylation of STAT3 (show STAT3 Antibodies) and plays a critical role in breast cancer development.
This study indentified VEGFR2 (show KDR Antibodies) as a PTPN9 substrate, and indicated that PTPN9 is a negative regulator of VEGFR2 (show KDR Antibodies) signaling and function in endothelial cells.
data suggest PTPN9 as a negative regulator of breast cancer cells by targeting ErbB2 (show ERBB2 Antibodies) and EGFR (show EGFR Antibodies) and inhibiting STAT (show STAT1 Antibodies) activation
Purification and characterization of protein tyrosine phosphatase (show ACP1 Antibodies) PTP (show SLC25A3 Antibodies)-MEG2
PTP (show SLC25A3 Antibodies)-MEG2 has an important role in the development of erythroid cells.
PTPase-MEG2 through its Sec14p homology domain couples inositide phosphorylation to tyrosine dephosphorylation and the regulation of intracellular traffic of the secretory pathway in T cells.
PTP (show SLC25A3 Antibodies)-MEG2 reduced the phosphotyrosine content of NSF (show NSF Antibodies) and co-localized with NSF (show NSF Antibodies) and syntaxin 6 (show STX6 Antibodies) in intact cells, the first demonstrated role for a protein tyrosine phosphatase (show ACP1 Antibodies) in the regulated secretory pathway
As a result, overexpression of PTP (show SLC25A3 Antibodies)-MEG2 down-regulates NGF (show NGFB Antibodies)/TrkA (show NTRK1 Antibodies) signaling and blocks neurite outgrowth and differentiation
role in the negative regulation of hepatic insulin (show INS Antibodies) signaling
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the Golgi complex in yeast. This PTP was found to be activated by polyphosphoinositide, and is thought to be involved in signaling events regulating phagocytosis.
protein tyrosine phosphatase, non-receptor type 9
, PTPase MEG2
, protein-tyrosine phosphatase MEG2
, tyrosine-protein phosphatase non-receptor type 9
, Protein-tyrosine phosphatase, non-receptor type 9 (Protein-tyrosine phosphatase MEG2) (PTPase-MEG2)