Description
Product Characteristics:
Dual specificity phosphatases (DSPs) are a subclass of the protein tyrosine phosphatase (PTP) gene superfamily, which are selective for dephosphorylating critical phosphothreonine and phosphotyrosine residues within MAP kinases. DSP gene expression is induced by a host of growth factors and/or cellular stresses, thereby negatively regulating MAP kinase superfamily members including MAPK/ERK, SAPK/JNK and p38. The members of the dual-specificity phosphatase protein family include MKP-1/CL100 (3CH134), MKP-2, MKP-3, MKP-4, MKP-5, MKP-6, MKP-7, MKP-X, VHR, VHY, PAC1, hVH-3 (B23), hVH-5, PYST2, DUSP1, DUSP5, DUSP8, PIR1 and SKRP1. DUSP5 is a nuclear phosphoprotein that displays phosphatase activity toward several different substrates. It shows the highest relative activity toward ERK1.
Subcellular location: Nucleus
Synonyms: Dual specicity protein phosphatase 5, Dual specicity protein phosphatase hVH 3, Dual specicity protein phosphatase hVH3, DUSP 5, DUSP, HVH 3, HVH3, Serine/threonine specic protein phosphatase, VH 3, VH1 like phosphatase 3, VH3, DUS5_HUMAN.
Target Information: The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1, is expressed in a variety of tissues with the highest levels in pancreas and brain, and is localized in the nucleus. [provided by RefSeq, Jul 2008]