Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
malfunction
lack of dUTPase leads to uracil-substituted DNA that perturbs base excision repair, resulting in DNA fragmentation and thymine-less cell death
malfunction
dUTPase knock-out results in lethality
malfunction
dUTPase down-regulation increases decitabine-induced toxicity in HeLa and MRC-5 cells at a wide range of doses
malfunction
enzyme null mutants are not viable
malfunction
-
enzyme null mutants are not viable
-
malfunction
-
dUTPase knock-out results in lethality
-
metabolism
the enzyme contributes to the cellular response to the anti-cancer nucleoside decitabine. Exposure of HeLa cells to decitabine upregulates the expression of several pyrimidine metabolic enzymes including DCTPP1, dUTPase, dCMP deaminase and thymidylate synthase. dUTPase down-regulation enhances the cytotoxic effect of decitabine producing an accumulation of nucleoside triphosphates containing uracil as well as uracil misincorporation and double-strand breaks in genomic DNA
metabolism
the enzyme is involved de novo biosynthesis of dTTP and sanitizing the deoxynucleotide pool by the specific removal of dUTP
physiological function
dUTPase is responsible for prevention of uracil incorporation into DNA
physiological function
the enzyme is involved in nucleotide metabolism that acts as first line of defence against uracil incorporation into DNA
physiological function
the enzyme plays a key role in preventing uracil incorporation into DNA
physiological function
-
enzyme activates nuclear factor NF-kappaB through ligation of TLR2/TLR1 heterodimers. Activation of NF-kappaB is inhibited by anti-TLR2 blocking antibodies and the overexpression of dominant-negative constructs of TLR2, lacking the TIR domain, and MyD88 in human embryonic kidney 293 cells expressing TLR2/TLR1. Treatment of human dendritic cells and peripheral blood mononuclear cells with the dUTPases results in the secretion of the inflammatory cytokines IL-1beta, IL-6, IL-8, IL-12, TNF-alpha, IL-10, and IFN-gamma
physiological function
-
enzyme activates nuclear factor NF-kappaB through ligation of TLR2/TLR1 heterodimers. Activation of NF-kappaB is inhibited by anti-TLR2 blocking antibodies and the overexpression of dominant-negative constructs of TLR2, lacking the TIR domain, and MyD88 in human embryonic kidney 293 cells expressing TLR2/TLR1. Treatment of human dendritic cells and peripheral blood mononuclear cells with the dUTPases results in the secretion of the inflammatory cytokines IL-1beta, IL-6, IL-8, IL-12, TNF-alpha, IL-10, and IFN-gamma
physiological function
enzyme activates nuclear factor NF-kappaB through ligation of TLR2/TLR1 heterodimers. Activation of NF-kappaB is inhibited by anti-TLR2 blocking antibodies and the overexpression of dominant-negative constructs of TLR2, lacking the TIR domain, and MyD88 in human embryonic kidney 293 cells expressing TLR2/TLR1. Treatment of human dendritic cells and peripheral blood mononuclear cells with the dUTPases results in the secretion of the inflammatory cytokines IL-1beta, IL-6, IL-8, IL-12, TNF-alpha, IL-10, and IFN-gamma
physiological function
enzyme activates nuclear factor NF-kappaB through ligation of TLR2/TLR1 heterodimers. Activation of NF-kappaB is inhibited by anti-TLR2 blocking antibodies and the overexpression of dominant-negative constructs of TLR2, lacking the TIR domain, and MyD88 in human embryonic kidney 293 cells expressing TLR2/TLR1. Treatment of human dendritic cells and peripheral blood mononuclear cells with the dUTPases results in the secretion of the inflammatory cytokines IL-1beta, IL-6, IL-8, IL-12, TNF-alpha, IL-10, and IFN-gamma
physiological function
Dubowvirus dv80alpha
enzyme induces the transfer of staphylococcal pathogenicity island-encoded virulence factors by switching between active (dUTP-bound) and inactive (apo state) conformations, a conversion catalyzed by their intrinsic dUTPase activity. Binding to dUTP reorders the C-terminal motif V of the enzyme, rendering the protein into the active conformation required for staphylococcal pathogenicity island derepression. The conversion to the apo state conformation by hydrolysis of the bound dUTP generates a protein that is unable to induce the staphylococcal pathogenicity island cycle
physiological function
the expression of phage-related pathogenicity islands transfer initiating proteins is repressed by proteins called Stl. Phage phi11 helper phage dUTPase eliminates Stl binding to its cognate DNA by binding tightly to Stl protein. dUTPase enzymatic activity is strongly inhibited in the dUTPase:Stl complex and the dUTPase:dUTP complex is inaccessible to the Stl repressor
physiological function
the enzyme is required for productive replication of African swine fever virus in swine macrophages
physiological function
-
the enzyme plays a role in modulating the host immune response. The enzyme contributes to the upregulation of type I interferons and is not required for virus replication in vitro
physiological function
-
the enzyme upregulates the expression of type I interferons, but is not required for viral DNA or virus replication in CH-SAH cells
physiological function
-
enzyme activates nuclear factor NF-kappaB through ligation of TLR2/TLR1 heterodimers. Activation of NF-kappaB is inhibited by anti-TLR2 blocking antibodies and the overexpression of dominant-negative constructs of TLR2, lacking the TIR domain, and MyD88 in human embryonic kidney 293 cells expressing TLR2/TLR1. Treatment of human dendritic cells and peripheral blood mononuclear cells with the dUTPases results in the secretion of the inflammatory cytokines IL-1beta, IL-6, IL-8, IL-12, TNF-alpha, IL-10, and IFN-gamma
-
physiological function
-
enzyme activates nuclear factor NF-kappaB through ligation of TLR2/TLR1 heterodimers. Activation of NF-kappaB is inhibited by anti-TLR2 blocking antibodies and the overexpression of dominant-negative constructs of TLR2, lacking the TIR domain, and MyD88 in human embryonic kidney 293 cells expressing TLR2/TLR1. Treatment of human dendritic cells and peripheral blood mononuclear cells with the dUTPases results in the secretion of the inflammatory cytokines IL-1beta, IL-6, IL-8, IL-12, TNF-alpha, IL-10, and IFN-gamma
-