Aliases for PTPN6 Gene
External Ids for PTPN6 Gene
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. N-terminal part of this PTP contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling. Multiple alternatively spliced variants of this gene, which encode distinct isoforms, have been reported. [provided by RefSeq, Jul 2008]
GeneCards Summary for PTPN6 Gene
PTPN6 (Protein Tyrosine Phosphatase, Non-Receptor Type 6) is a Protein Coding gene. Diseases associated with PTPN6 include cd45 deficiency and polycythemia. Among its related pathways are PI-3K cascade and Signaling by GPCR. GO annotations related to this gene include protein kinase binding and protein tyrosine phosphatase activity. An important paralog of this gene is PTPRN.
UniProtKB/Swiss-Prot for PTPN6 Gene
Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis.
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.