Aliases for PTPN11 Gene
External Ids for PTPN11 Gene
Previous HGNC Symbols for PTPN11 Gene
Previous GeneCards Identifiers for PTPN11 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. This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. This PTP is widely expressed in most tissues and plays a regulatory role in various cell signaling events that are important for a diversity of cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration. Mutations in this gene are a cause of Noonan syndrome as well as acute myeloid leukemia. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May 2012]
GeneCards Summary for PTPN11 Gene
PTPN11 (Protein Tyrosine Phosphatase, Non-Receptor Type 11) is a Protein Coding gene. Diseases associated with PTPN11 include noonan syndrome 1 and leopard syndrome 1. Among its related pathways are PI-3K cascade and PI-3K cascade. GO annotations related to this gene include protein domain specific binding and SH3/SH2 adaptor activity. An important paralog of this gene is PTPN6.
UniProtKB/Swiss-Prot for PTPN11 Gene
Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity.
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.