Thymine-DNA Glycosylase (TDG) Human Recombinant Protein

The protein encoded by this gene belongs to the TDG/mug DNA glycosylase family. Thymine-DNA glycosylase (TDG) removes thymine moieties from G/T mismatches by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of DNA and the mispaired thymine. With lower activity, this enzyme also removes thymine from C/T and T/T mispairings. TDG can also remove uracil and 5-bromouracil from mispairings with guanine. This enzyme plays a central role in cellular defense against genetic mutation caused by the spontaneous deamination of 5-methylcytosine and cytosine. This gene may have a pseudogene in the p arm of chromosome 12. [provided by RefSeq, Jul 2008]

TDG: In the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. This enzyme corrects G/T mispairs to G/C pairs. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar- phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine. Belongs to the TDG/mug DNA glycosylase family.

Protein type: Nuclear receptor co-regulator; Hydrolase; DNA repair, damage; EC 3.2.2.29

Chromosomal Location of Human Ortholog: 12q24.1

Cellular Component: nucleoplasm; PML body; plasma membrane; nucleus

Molecular Function: protein domain specific binding; protein binding; structure-specific DNA binding; protein homodimerization activity; protein kinase C binding; SUMO binding; DNA N-glycosylase activity; double-stranded DNA binding; damaged DNA binding; transcription factor binding; pyrimidine-specific mismatch base pair DNA N-glycosylase activity; mismatched DNA binding

Biological Process: transcription from RNA polymerase II promoter; embryonic development; mismatch repair; base-excision repair, AP site formation; depyrimidination; base-excision repair; gene expression; negative regulation of transcription from RNA polymerase II promoter; chromatin modification; DNA repair; negative regulation of protein binding; regulation of gene expression, epigenetic