| Description | Uracil-DNA glycosylase (UNG) [ ] is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. The sequence of uracil-DNA glycosylase is extremely well conserved [] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses []. In eukaryotic cells, UNG activity is found in both the nucleus and the mitochondria. Human UNG1 protein is transported to both the mitochondria and the nucleus []. The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localisation [], but the presence of a mitochondrial transit peptide has not been directly demonstrated. The most N-terminal conserved region contains an aspartic acid residue which has been proposed, based on X-ray structures [, ] to act as a general base in the catalytic mechanism.This signature pattern covers the most N-terminal conserved region, which contains an aspartic acid residue that has been proposed, based on X-ray structures [ , ] to act as a general base in the catalytic mechanism. | Name | Uracil-DNA glycosylase, active site |
| Short Name | Ura-DNA_Glyclase_AS | Type | Active_site |
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