DUSP5
DUSP5 (dual specificity phosphatase 5, also known as HVH3) is a nuclear dual specificity phosphatase that dephosphorylates serine, threonine and tyrosine residues. It negatively regulates MAP kinase signalling, with its highest relative activity directed toward ERK1. Browse Assay Genie's current range of DUSP5 research reagents below, or read on for the biology behind the target.
DUSP5 is a dual specificity protein phosphatase that is active against phosphotyrosine, phosphoserine and phosphothreonine residues. Like other members of the subfamily, it inactivates its target kinases by removing phosphate groups from both the serine/threonine and tyrosine residues. It negatively regulates members of the mitogen-activated protein (MAP) kinase superfamily, namely MAPK/ERK, SAPK/JNK and p38, which are associated with cellular proliferation and differentiation. Among its substrates, DUSP5 shows the highest relative activity toward ERK1, and the gene product is described as inactivating ERK1.
The DUSP5 gene encodes a protein that belongs to the protein-tyrosine phosphatase family, in the non-receptor class dual specificity subfamily. HGNC places it in the MAP kinase phosphatases gene group. The protein is localised to the nucleus and is expressed in a variety of tissues, with the highest levels in pancreas and brain. Researchers studying the DUSP5 protein therefore often focus on nuclear control of ERK signalling.
Different dual specificity phosphatases show distinct substrate specificities for various MAP kinases, as well as different tissue distribution, subcellular localisation and modes of inducibility by extracellular stimuli. This makes DUSP5 one of several related enzymes that tune MAP kinase output in a context-specific manner. HVH3 is a previous symbol for the gene, and a rat ortholog, Dusp5, is recorded.
DUSP5 shows its highest relative activity toward ERK1, making it a relevant phosphatase for dissecting how ERK pathway activity is switched off.
It negatively regulates the MAPK/ERK, SAPK/JNK and p38 branches, which are linked to cellular proliferation and differentiation.
DUSP5 is localised to the nucleus, offering a model for how compartment-specific phosphatases shape kinase signalling.
Expression across many tissues, with the highest levels in pancreas and brain, supports comparative studies of dual specificity phosphatase distribution.
DUSP5 is a dual specificity phosphatase that removes phosphate from phosphoserine, phosphothreonine and phosphotyrosine residues. It negatively regulates MAP kinases, and its highest relative activity is toward ERK1. By inactivating these kinases it limits signalling linked to cellular proliferation and differentiation.
The approved HGNC name is dual specificity phosphatase 5, and UniProt lists it as dual specificity protein phosphatase 5. HVH3 is an alias or previous symbol. The enzyme carries EC numbers 3.1.3.16 and 3.1.3.48, reflecting its serine/threonine and tyrosine phosphatase activities.
DUSP5 is expressed in a variety of tissues, with the highest levels in pancreas and brain, and the protein is found in the nucleus. A rat ortholog, Dusp5, is recorded in the data; check the datasheet of any product for its validated reactivity.
Other dual specificity phosphatases and MAP kinase phosphatases that regulate ERK, JNK and p38 signalling.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q16690; product specifications from Assay Genie datasheets.