Due to maintenance work, this service and ftp://ftp.expasy.org will be unavailable from Tuesday August 23rd 18:00 until Wednesday August 24th 08:00
CEST. Apologies for the inconvenience.
ENZYME entry: EC 2.1.1.368
Accepted Name |
[histone H3]-lysine(9) N-dimethyltransferase.
|
Reaction catalysed |
L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-methionine <=> 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 S-adenosyl-L-homocysteine |
Comment(s) |
- This entry describes several enzymes, characterized from plants, that
successively methylate the L-lysine-9 residue of histone H3 (H3K9)
twice, ultimately generating a dimethylated form.
- These modifications influence the binding of chromatin-associated
proteins.
- In general, the methylation of H3K9 leads to transcriptional
repression of the affected target genes.
- Cf. EC 2.1.1.367, EC 2.1.1.366, and EC 2.1.1.355.
|
Cross-references |
BRENDA | 2.1.1.368 |
EC2PDB | 2.1.1.368 |
ExplorEnz | 2.1.1.368 |
PRIAM enzyme-specific profiles | 2.1.1.368 |
KEGG Ligand Database for Enzyme Nomenclature | 2.1.1.368 |
IUBMB Enzyme Nomenclature | 2.1.1.368 |
IntEnz | 2.1.1.368 |
MEDLINE | Find literature relating to 2.1.1.368 |
MetaCyc | 2.1.1.368 |
Rhea expert-curated reactions | 2.1.1.368 |
UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-