Jumonji domain-containing protein 7 (JMJD7)

Jumonji domain-containing protein 7 (JMJD7) is a **bifunctional enzyme** in humans, part of the JmjC domain-containing protein family, acting both as a Fe(II)- and 2-oxoglutarate-dependent oxygenase as well as a histone endopeptidase. JMJD7 **catalyzes stereospecific (3S)-lysyl hydroxylation** of highly conserved lysine residues on the translation GTPase proteins DRG1 and DRG2, which promotes their interaction with RNA and is implicated in the regulation of cell growth and translational machinery[1][2][3][4][5]. JMJD7 also *cleaves histone tails* (methylated arginine or lysine residues), facilitating transcriptional elongation[4][5][6]. Mutations in JMJD7 have been correlated with neurological conditions such as autism and intellectual disability, as well as some cancers[1][2][4]. Structural studies show it shares similarities with JmjC hydroxylases but not demethylases and has a unique dimerization interface[1][2]. The precise physiological and pathological roles of JMJD7, including its value as a drug target, remain under investigation.

Other names

Jumonji domain-containing 7JmjC domain-containing protein 7Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7L-lysine (3S)-hydroxylase JMJD7

Inhibition of lysyl hydroxylase activity (anticipated for experimental inhibitors, not yet linked to approved drugs)[3][7].