EC Number   |
Natural Substrates |
|---|
   2.1.1.359 | 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 |
overall reaction |
| 2.1.1.359 | 3 S-adenosyl-L-methionine + a [histone H3]-L-lysine36 |
overall reaction. Trimethylation of [histone H3]-L-lysine36 by the enzyme is directed through its association with the phosphorylated repeats of the RNA polymerase C-terminal domain |
| 2.1.1.359 | 3 S-adenosyl-L-methionine + [histone H3]-L-lysine36 |
overall reaction |
| 2.1.1.359 | more |
SDG724 prefers oligonucleosomes rather than core histones as a substrate |
| 2.1.1.359 | more |
Asf1 stimulates the enzyme occupancy of the coding region of a highly transcribed gene by a mechanism that depends on Asf1 binding to histone H3/H4. This function of Asf1 promotes the switch from di- to trimethylation of histone H3 lysine 36 at that gene |
| 2.1.1.359 | more |
no activity with unmethylated/methylated [histone H3]-L-lysine27 and [histone H3]-L-lysine20 as well as trimethylated [histone H3]-L-lysine4 and [histone H3]-L-lysine36 peptides |
| 2.1.1.359 | more |
no activity with [histone H3]-L-lysine9 and [histone H3]-L-lysine4 |
| 2.1.1.359 | more |
the enzyme also efficiently trimethylates [histone H3]-L-lysine4 |
| 2.1.1.359 | S-adenosyl-L-methionine + a [histone H3]-L-lysine36 |
- |
| 2.1.1.359 | S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine36 |
- |
