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ENZYME entry: EC 2.1.1.372

Accepted Name
[Histone H4]-lysine(20) N-trimethyltransferase.
Reaction catalysed
3 S-adenosyl-L-methionine + a [histone H4]-L-lysine(20) <=> 3 S-adenosyl-L-homocysteine + a [histone H4]-N(6),N(6),N(6)-trimethyl-L-lysine(20)
Comment(s)
  • The enzyme, characterized from the fission yeast Schizosaccharomyces pombe, catalyzes three successive methylations of the L-lysine-20 residue of histone H4 (H4K20), forming the trimethylated form.
  • The methylation of this site is apparently not involved in the regulation of gene expression or heterochromatin function but participates in DNA damage response.
  • Cf. EC 2.1.1.361 and EC 2.1.1.362.
  • Formerly EC 2.1.1.43.
Cross-references
BRENDA2.1.1.372
EC2PDB2.1.1.372
ExplorEnz2.1.1.372
PRIAM enzyme-specific profiles2.1.1.372
KEGG Ligand Database for Enzyme Nomenclature2.1.1.372
IUBMB Enzyme Nomenclature2.1.1.372
IntEnz2.1.1.372
MEDLINEFind literature relating to 2.1.1.372
MetaCyc2.1.1.372
Rhea expert-curated reactions2.1.1.372
UniProtKB/Swiss-Prot
Q4X1W8, SET9_ASPFU;  Q2TZH4, SET9_ASPOR;  Q0C9E6, SET9_ASPTN;  
Q2H8D5, SET9_CHAGB;  Q1E9C0, SET9_COCIM;  Q5AZY3, SET9_EMENI;  
Q4I8C9, SET9_GIBZE;  Q7SBJ9, SET9_NEUCR;  Q0U3A4, SET9_PHANO;  
Q9USK2, SET9_SCHPO;  Q6C519, SET9_YARLI;  Q5ZIZ2, SMYD5_CHICK;  
F1RET2, SMYD5_DANRE;  Q6GMV2, SMYD5_HUMAN;  Q3TYX3, SMYD5_MOUSE;  
Q6GPQ4, SMYD5_XENLA;  

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