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ENZYME entry: EC 2.1.1.356

Accepted Name
[Histone H3]-lysine(27) N-trimethyltransferase.
Reaction catalysed
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine(27) <=> 3 S-adenosyl-L-homocysteine + a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(27)
Comment(s)
  • This entry describes enzymes that successively methylate the L-lysine(27) residue of histone H3 (H3K27), ultimately generating a trimethylated form.
  • These modifications influence the binding of chromatin-associated proteins.
  • The methylation of lysine(27) leads to transcriptional repression of the affected target genes.
  • The enzyme associates with other proteins to form a complex that is essential for activity.
  • The enzyme can also methylate some non-histone proteins.
  • Formerly EC 2.1.1.43.
Cross-references
BRENDA2.1.1.356
EC2PDB2.1.1.356
ExplorEnz2.1.1.356
PRIAM enzyme-specific profiles2.1.1.356
KEGG Ligand Database for Enzyme Nomenclature2.1.1.356
IUBMB Enzyme Nomenclature2.1.1.356
IntEnz2.1.1.356
MEDLINEFind literature relating to 2.1.1.356
MetaCyc2.1.1.356
UniProtKB/Swiss-Prot
Q5VN06, CLF_ORYSJ;  Q8S4P6, EZ1_MAIZE;  Q84UI6, EZ1_ORYSI;  
Q10MI4, EZ1_ORYSJ;  Q8S4P5, EZ2_MAIZE;  Q8S4P4, EZ3_MAIZE;  
Q9ZSM8, EZA1_ARATH;  A7E2Z2, EZH1_BOVIN;  Q92800, EZH1_HUMAN;  
P70351, EZH1_MOUSE;  Q5RDS6, EZH1_PONAB;  Q98SM3, EZH2A_XENLA;  
Q4V863, EZH2B_XENLA;  Q08BS4, EZH2_DANRE;  Q15910, EZH2_HUMAN;  
Q4R381, EZH2_MACFA;  Q61188, EZH2_MOUSE;  Q28D84, EZH2_XENTR;  
P42124, EZ_DROME;  O65312, MEDEA_ARATH;  O17514, MES2_CAEEL;  
O96028, NSD2_HUMAN;  Q8BVE8, NSD2_MOUSE;  

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