Lysine demethylase 7A (KDM7A)

Lysine demethylase 7A (KDM7A) is a nuclear enzyme belonging to the Jumonji C (JmjC) domain-containing family of histone demethylases, specifically catalyzing the removal of mono- and di-methyl groups from lysine residues 9, 27, and 36 of histone H3 (notably H3K9me2, H3K27me2, and H3K36me2), as well as monomethylated lysine 20 of histone H4 (H4K20me1) [1][4]. By altering these chromatin marks, KDM7A plays a central role in chromatin remodeling, gene activation or repression, and cell lineage determination. Its activity is critical for normal embryonic, neural, and skeletal development; it also regulates adipogenic and osteogenic differentiation, bone homeostasis, and immune responses. Dysregulation of KDM7A has been linked to cancers, inflammatory diseases, osteoporosis, neurodevelopmental disorders, and infection processes such as hepatitis B virus (HBV) replication. While not yet the target of any approved drugs, KDM7A is considered a promising therapeutic target in oncology, metabolic bone disorders, immune modulation, and antiviral strategies.

Other names

Lysine-specific demethylase 7AJHDM1DKDM7KIAA1718JmjC domain-containing histone demethylation protein 1D

Inhibition of histone demethylase activity, particularly at H3K9me2 and H3K27me2 marks [1][3][4]; Modulation of gene expression through altered removal of methylation marks; Regulation of viral promoter function (HBV) via histone mark modification [7]