Vaccinia H1-related phosphatase (VHR) is classified as a dual-specificity phosphatase (DUSP), and the other name is dual-specificity phosphatase 3 (DUSP3). DUSPs are a heterogeneous group of protein phosphatases that can dephosphorylate both phosphotyrosine and phosphoserine / phosphothreonine residues within the one substrate. Unlike typical DUSPs, DUSP3 lacks mitogen-activated protein kinase (MAPK)-binding domain, and shows poor activity against MAPKs. DUSP3 often act on bisphosphorylated protein substrates, it displays a strong preference for dephosphorylating phosphotyrosine residues over phosphothreonine residues. DUSP3 has been identified as a novel regulator of extracellular regulated kinases (ERKs). DUSP3 is responsible for the rapid inactivation of ERK following stimulation and for its repression in quiescent cells. DUSP3 is a negative regulator of the Erk and Jnk pathways in T cells and, therefore, may play a role in aspects of T lymphocyte physiology that depend on these kinases.
DUSP3 ELISA Pair sets
DUSP3 cDNA Clones
Signal Transduction>>Phosphatase & Regulator>>DUSP3/VHR
DUSP3, VHR [Homo sapiens]
Dusp3, VHR, RP23-398F7.3, 2210015O03Rik, 5031436O03Rik, T-DSP11 [Mus musculus]
Entrez Gene summary for DUSP3:
The protein encoded by this DUSP3 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 maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1. [provided by RefSeq, Jul 2008]
OMIM - description for DUSP3:
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP3 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see 600714). DUSP3 was originally designated VHR because of its close similarity to VH1, a key gene in vaccinia virus (summary by Patterson et al., 2009).
Wikipedia summary for DUSP3:
Dual specificity protein phosphatase 3 is an enzyme that in humans is encoded by the DUSP3 gene.
Dual specificity protein phosphatase 3
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
DUSP3 belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. DUSP3 contains 1 tyrosine-protein phosphatase domain.
DUSP3 interacts with VRK3, which seems to activate it's phosphatase activity
General information above from UniProt
DUSP3 shows activity both for tyrosine-protein phosphate and serine-protein phosphate, but displays a strong preference toward phosphotyrosines. DUSP3 specifically dephosphorylates and inactivates ERK1 and ERK2.
- DUSP3 has activity both toward tyrosine-protein phosphate as well as with serine-protein phosphate
- DUSP3 inactivates the mitogen-activated kinases ERK2 and MAPK8
- homolog to vaccinia virus phosphatase VH1