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' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. 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.,tissue specificity:Overexpressed in several esophageal squamous cell carcinomas (ESCs).,
Nucleus .
Overexpressed in several esophageal squamous cell carcinomas (ESCs).