| Primary Identifier | IPR030488 | Type | Domain |
| Short Name | DNMT3B_ADD |
| description | This entry represents the ADD domain of DNMT3B. The ADD domain is composed of three clearly distinguishable modules that packtogether through extensive hydrophobic interactions to form a single globulardomain. Packed against this GATA-like finger is a second subdomain,which binds two zinc ions and closely resembles the structure reported forseveral PHD fingers. Finally, there is a long C-terminal α-helix that runsout from the PHD finger and makes extensive hydrophobic contacts with the N-terminal GATA finger, bringing the N- and C-termini of the ADD domain closetogether. This combination of fused GATA-like and PHD fingers within a singledomain is thus far unique [, ].In mammals, DNA methylation patterns are thought to be established during embryonic development by de novo DNA methyltransferases 3A and 3B (DNMT3A/3B) []. DNMT3A/3B work synergistically to propagate methylation patterns with DNMT3B stimulating DNMT3A activity by promoting its association with nucleosomes []. Many DNMT3B isoforms from alternative splicing have been described, among which DNMT3B3 stimulates the basal activity of DNMT3 enzymes, but partially inhibits the stimulatory effect of DNMT3L, whereas DNMT3B4 significantly impairs de novo methylation [, ]. DNMT3B is involved in development and is associated with several diseases, including cancers []. |
