SH-PTP2, also known as SHP-2, is a non-receptor type protein tyrosine phosphatase (PTPN11) that contains two Src homology 2 (SH2) domains and a phosphatase domain. SHP-2 plays a crucial role in various cellular signaling pathways, including those downstream of growth factors, cytokines, and adhesion receptors. It modulates specific protein-protein interactions by binding to phosphotyrosine residues through its SH2 domains. Under normal conditions, the catalytic efficiency of SHP-2 is low due to the autoinhibition of its SH2 domains, but its catalytic activity increases when the SH2 domains are occupied by phosphotyrosine residues, possibly by inducing conformational changes in the enzyme. SHP-2 is involved in multiple signaling pathways, including the Ras-Raf-MAP kinase, Jak-Stat, and PI3 kinase pathways, and may function at multiple sites within a single signaling pathway. SHP-2 is also associated with a variety of diseases, including Noonan syndrome, LEOPARD syndrome, juvenile myelomonocytic leukemia (JMML), and cartilage development abnormalities. Gain-of-function mutations in SHP-2 lead to developmental disorders such as Noonan syndrome and are frequently found in JMML patients. Additionally, SHP-2 has antitumor activity in various cancer models, and its inhibitors are being investigated as potential therapeutic agents for cancer treatment.