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Human DUSP3 Protein expressed in Escherichia coli (E. coli) - ABIN667577
Keyse: An emerging family of dual specificity MAP kinase phosphatases. in Biochimica et biophysica acta 1995
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Human DUSP3 Protein expressed in Baculovirus infected Insect Cells - ABIN2002103
Todd, Tanner, Denu: Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway. in The Journal of biological chemistry 1999
Show all 2 references for ABIN2002103
Human DUSP3 Protein expressed in Baculovirus infected Insect Cells - ABIN2002101
Henkens, Delvenne, Arafa, Moutschen, Zeddou, Tautz, Boniver, Mustelin, Rahmouni: Cervix carcinoma is associated with an up-regulation and nuclear localization of the dual-specificity protein phosphatase VHR. in BMC cancer 2008
Show all 2 references for ABIN2002101
Data suggest levels of gene expression of both DUSP3 (dual specificity phosphatase 3) and PSME3 (proteasome activator subunit 3 (show PSME3 Proteins)) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model.
Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses
VHR can dimerize inside cells, and that VHR catalytic activity is reduced upon dimerization.
DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase.
DUSP3 interacting partners are nucleolar proteins involved in processes related to DNA repair and senescence.
we report the first successful site-specific incorporation of sulfotyrisine into VHR through the use of expanding genetic code
Proteins containing the class II motifs are efficient VHR substrates in vitro, suggesting that VHR may act on a novel class of yet unidentified Tyr (show TYR Proteins)(P) proteins in vivo.
VHR expression enhances the signaling of ErbB (show EGFR Proteins) receptors and may be involved in NSCLC pathogenesis.
VHR, a Vaccinia virus VH1 (show DUSP12 Proteins)-related dual-specific protein phosphatase, is phosphorylated at Y138 by ZAP-70 (show ZAP70 Proteins).
VHR is required for cell-cycle progression as it modulates MAP kinase (show MAPK1 Proteins) activation in a cell-cycle phase-dependent manner.
Data suggest levels of gene expression of both Dusp3 (dual specificity phosphatase 3) and Psme3 (proteasome activator subunit 3 (show PSME3 Proteins)) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model.
Platelets from DUSP3-deficient mice displayed a selective impairment of aggregation and granule secretion.
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 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.
dual specificity phosphatase 3 (vaccinia virus phosphatase VH1-related)
, dual specificity phosphatase 3
, dual specificity protein phosphatase 3
, dual specificity protein phosphatase VHR
, serine/threonine specific protein phosphatase
, vaccinia H1-related phosphatase
, vaccinia virus phosphatase VH1-related