Target Background
cofactor:Binds 1 Fe(2+) ion per subunit.,domain:The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails.,function:Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate.,similarity:Belongs to the JHDM3 histone demethylase family.,similarity:Contains 1 JmjC domain.,similarity:Contains 1 JmjN domain.,similarity:Contains 2 PHD-type zinc fingers.,similarity:Contains 2 Tudor domains.,cofactor:Binds 1 Fe(2+) ion per subunit.,domain:The 2 Tudor domains recognize and bind methylated histones. Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails.,function:Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate.,similarity:Belongs to the JHDM3 histone demethylase family.,similarity:Contains 1 JmjC domain.,similarity:Contains 1 JmjN domain.,similarity:Contains 2 PHD-type zinc fingers.,similarity:Contains 2 Tudor domains.,
