ENZYME entry: EC 188.8.131.522
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|[Histone H4]-N-methyl-L-lysine(20) N-methyltransferase.
|S-adenosyl-L-methionine + a [histone H4]-N(6)-methyl-L-lysine(20) <=> S-adenosyl-L-homocysteine + a [histone H4]-N(6),N(6)-dimethyl-L-lysine(20)|
- This entry describes a group of enzymes that catalyze a single
methylation of monomethylated lysine(20) of histone H4 (H4K20m1,
generated by EC 184.108.40.2061), forming the dimethylated form.
- This modification is broadly distributed across the genome and is
likely important for general chromatin-mediated processes.
- The double-methylated form of lysine(20) in histone H4 is the most
abundant methylation state of this residue and is found on ~80% of
all histone H4 molecules.
- Full activity of the enzyme requires that the lysine at position 9 of
histone H3 is trimethylated.
- Formerly EC 220.127.116.11.
|PRIAM enzyme-specific profiles||18.104.22.1682|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.1242|
|IUBMB Enzyme Nomenclature||126.96.36.1992|
|MEDLINE||Find literature relating to 188.8.131.522|
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