EC Number |
Natural Substrates |
---|
1.14.11.66 | a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2 |
overall reaction |
1.14.11.66 | a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2 |
- |
1.14.11.66 | a [histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2 |
- |
1.14.11.66 | histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2 |
- |
1.14.11.66 | histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2 |
- |
1.14.11.66 | histone H3 N6-methyl-L-lysine9 + 2-oxoglutarate + O2 |
- |
1.14.11.66 | more |
LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active nethylation mark |
1.14.11.66 | more |
LSD1 is also involved in androgen receptor-dependent demethylation of H3K9me1/2, a methylation site enriched in silent chromatin. The complexes in which LSD1 resides tightly coordinate its gene regulatory functions and also influence its specificity for histone and non-histone substrates |
1.14.11.66 | more |
JmjD2A is specific for H3K9me3 and H3K36me3 substrates in fibroblasts, and does not affect H3K27me3 methylation marks |
1.14.11.66 | more |
low level of JMJD2b in nucleoli is not associated with the high level of H3K9 methylation in this nuclear region |