Aliases for PTPN1 Gene
External Ids for PTPN1 Gene
Previous Symbols for PTPN1 Gene
The protein encoded by this gene is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. 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 has been shown to act as a negative regulator of insulin signaling by dephosphorylating the phosphotryosine residues of insulin receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to interferon stimulation. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2013]
GeneCards Summary for PTPN1 Gene
PTPN1 (Protein Tyrosine Phosphatase, Non-Receptor Type 1) is a Protein Coding gene. Diseases associated with PTPN1 include bubonic plague and plague. Among its related pathways are Signaling by GPCR and PAK Pathway. GO annotations related to this gene include protein kinase binding and protein tyrosine phosphatase activity. An important paralog of this gene is PTPN6.
UniProtKB/Swiss-Prot for PTPN1 Gene
Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.
Protein tyrosine phosphatases (PTPs) are a group of enzymes that catalyze the removal of phosphate groups from tyrosine residues by the hydrolysis of phosphoric acid monoesters. They directly oppose the actions of kinases and phosphorylases and therefore play an integral role in many signal transduction pathways. PTPs are cysteine-dependent phosphatases that contain a conserved C[X]5R motif essential for enzymatic activity. PTPs are currently divided into five subtypes; tyrosine-specific phosphatases (e.g. PTP1B), dual specificity phosphatases (DSPs) (e.g. DUSP1), Cdc25 phosphatases (e.g. Cdc25A), myotubularin-related phosphatases (e.g. MTMR13) and low molecular weight phosphatases (e.g. PTPase A). Perturbations in PTP activity has been implicated in human diseases, including type II diabetes. PTPs have been identified as a negative regulator of the insulin signaling by dephosphorylating phosphotyrosine residues of insulin receptor kinase. In cancers, PTPs dephosphorylate EGFR, JAK2 and TYK2 kinases, promoting oncogenic transformation.