Function and Biology

LINKED KDM5A JMJ DOMAIN BOUND TO THE INHIBITOR N67 i.e. 2-(5-phenyl-4-(phenyl(2-(piperidin-1-yl)ethoxy)methyl)-1H-pyrazol-1-yl)isonicotinic acid

Source organism: Homo sapiens
Biochemical function: not assigned
Biological process: not assigned
Cellular component: not assigned

EC 1.14.11.67: [Histone H3]-trimethyl-L-lysine(4) demethylase

Reaction catalysed:
(1a) a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(4) + 2-oxoglutarate + O(2) = a [histone H3]-N(6),N(6)-dimethyl-L-lysine(4) + succinate + formaldehyde + CO(2)
Systematic name:
[Histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(4),2-oxoglutarate:oxygen oxidoreductase

GO terms

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Sequence families

Pfam Protein families (Pfam)
PF02373
Domain description: JmjC domain, hydroxylase
Occurring in:
  1. Lysine-specific demethylase 5A
The deposited structure of PDB entry 6dqe contains 1 copy of Pfam domain PF02373 (JmjC domain, hydroxylase) in Lysine-specific demethylase 5A. Showing 1 copy in chain A.

PF02375
Domain description: jmjN domain
Occurring in:
  1. Lysine-specific demethylase 5A
The deposited structure of PDB entry 6dqe contains 1 copy of Pfam domain PF02375 (jmjN domain) in Lysine-specific demethylase 5A. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR003349
Domain description: JmjN domain
Occurring in:
  1. Lysine-specific demethylase 5A
IPR003347
Domain description: JmjC domain
Occurring in:
  1. Lysine-specific demethylase 5A