MBD4 is a protein belonging to the family of Methyl-CpG Binding Domains (MBD). It has a Cter domain with glycosylase activity, that excises mismatched T bases in CpG sites and functions in the context of transcriptional repression, and a MBD domain that recognizes methylated CpG dinucleotides (5mCG/5mCG). In addition, MBD4 also recognizes mismatched sites generated by spontaneous deamination of 5-methylcytosines (5mC --> spontaneous deamination--> T), or 5mCG/TG. Therefore, the combine activity of the glycosylase and Methyl-CpG Binding domains in MBD4 generates active DNA demethylation initiated by the deaminase-catalyzed conversion of 5-methylcytosine to thymine.