Protein Variants | Comment | Organism |
---|---|---|
additional information | depletion of UNG2 in macrophages by siRNA, HIV-1 virus fails to replicate in UNG2-depleted macrophages, UNG1 cannot compensate. Depletion of UNG2 in producer MAGI-CCR5 cells generates noninfectious virus, overview. Restoration of viral infectivity of UNG2-deficient virus by transfection of dUTPase-expressing vector in UNG2-depleted producer cells | Homo sapiens |
Q152L/D154E | a siRNA-insensitive, inactive UNG2 mutant, overexpression in UNG2-depleted MAGI-CCR5 producer cells fails to restore viral infectivity | Homo sapiens |
W231A/F234G | site-directed mutagenesis, the mutation impairs the association of UNG2 with viral protein Vpr UNG2-depleted MAGI-CCR5 producer cells and viral infectivity | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ugi peptide | - |
Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | uracil DNA glycosylase acts in removing uracil from the sugar backbone of DNA, leaving abasic sites and initiating the uracil base-excision-repair pathway, BER. The human UNG2 enzyme, but not UNG1, is packaged and incorporated into HIV-1 virions via specific interaction with the integrase domain of the Gag-Pol precursor, the virally Vpr protein might also able to mediate the incorporation of UNG2, packaged UNG2 can process uracil from DNA, indicating that HIV-1 has the ability to control dUTP misincorporation in viral DNA, the enzyme is essential to the HIV-1 life cycle. HIV-1 RT and UNG2 recombinant proteins can process uracil from primer-template substrate, molecular mechanism | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P22674 | UNG2 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HeLa-MAGI-CCR5 cell | - |
Homo sapiens | - |
macrophage | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | uracil DNA glycosylase acts in removing uracil from the sugar backbone of DNA, leaving abasic sites and initiating the uracil base-excision-repair pathway, BER. The human UNG2 enzyme, but not UNG1, is packaged and incorporated into HIV-1 virions via specific interaction with the integrase domain of the Gag-Pol precursor, the virally Vpr protein might also able to mediate the incorporation of UNG2, packaged UNG2 can process uracil from DNA, indicating that HIV-1 has the ability to control dUTP misincorporation in viral DNA, the enzyme is essential to the HIV-1 life cycle. HIV-1 RT and UNG2 recombinant proteins can process uracil from primer-template substrate, molecular mechanism | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
UNG2 | - |
Homo sapiens |
uracil DNA glycosylase | - |
Homo sapiens |