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ENZYME entry: EC 2.1.1.362

Accepted Name
[Histone H4]-N-methyl-L-lysine(20) N-methyltransferase.
Reaction catalysed
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)
Comment(s)
  • This entry describes a group of enzymes that catalyze a single methylation of monomethylated lysine(20) of histone H4 (H4K20m1, generated by EC 2.1.1.361), 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 2.1.1.34.
Cross-references
BRENDA2.1.1.362
EC2PDB2.1.1.362
ExplorEnz2.1.1.362
PRIAM enzyme-specific profiles2.1.1.362
KEGG Ligand Database for Enzyme Nomenclature2.1.1.362
IUBMB Enzyme Nomenclature2.1.1.362
IntEnz2.1.1.362
MEDLINEFind literature relating to 2.1.1.362
MetaCyc2.1.1.362
UniProtKB/Swiss-Prot
Q29RP8, KMT5B_BOVIN;  Q5U3H2, KMT5B_DANRE;  Q4FZB7, KMT5B_HUMAN;  
Q3U8K7, KMT5B_MOUSE;  P0C2N5, KMT5B_RAT;  Q86Y97, KMT5C_HUMAN;  
Q6Q783, KMT5C_MOUSE;  P0C2N6, KMT5C_RAT;  A0JMZ4, KMT5C_XENLA;  
Q6GP17, KT5BA_XENLA;  Q5RJX8, KT5BB_XENLA;  Q6P2A1, PRDM9_DANRE;  
Q9NQV7, PRDM9_HUMAN;  Q96EQ9, PRDM9_MOUSE;  P0C6Y7, PRDM9_RAT;  
A8WTV9, SUV42_CAEBR;  Q09265, SUV42_CAEEL;  Q9W5E0, SUV42_DROME;  

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