JMJD6 is a member of the Jumonji C (JmjC)-domain family. This family consists of α-ketoglutarate dependent enzymes which use a cupin fold to coordinate an iron atom. JMJD6 was initially proposed to function as a histone arginine demethylase. Further studies suggest that JMJD6 has hydroxylase activity towards histone tails, the splicing regulatory protein LUC7-Like2, or single-stranded RNA. Recent evidence suggests that JMJD6 gene expression may be a biomarker for aggressive breast cancers.
