JMJD2A Protein, Human

JMJD2A Protein, a histone demethylase central to the intricate histone code, specifically targets 'Lys-9' and 'Lys-36' residues of histone H3. Notably, it does not demethylate histone H3 'Lys-4,' H3 'Lys-27,' nor H4 'Lys-20.' Its demethylase activity is confined to trimethylated H3 'Lys-9' and H3 'Lys-36' residues, with no discernible effect on mono- and dimethylated residues. This demethylation process generates formaldehyde and succinate as byproducts. JMJD2A participates in the transcriptional repression of ASCL2 and E2F-responsive promoters by recruiting histone deacetylases and NCOR1, respectively. With a critical role in muscle differentiation, JMJD2A promotes the transcriptional activation of the Myog gene by orchestrating the removal of repressive chromatin marks at its promoter. Noteworthy is the absence of the N-terminal demethylase domain in JMJD2A, highlighting its unique structural features and functional significance in chromatin dynamics and gene regulation.