JMJD7

JMJD7 (Jumonji Domain Containing 7) encodes a highly conserved protein with a JmjC domain, which are part of the cupin metalloenzyme superfamily. JmjC proteins may function as 2-oxoglutarate-Fe(II)-dependent dioxygenases.

Full Name

jumonji domain containing 7

Function

Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (PubMed:28847961, PubMed:29915238).
Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961).
Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4 (PubMed:28847961).
After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961).
Additionally, may play a role in protein biosynthesis by modifying the translation machinery (PubMed:29915238).
Acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (PubMed:29915238).

Biological Process

Protein hydroxylationManual Assertion Based On ExperimentIDA:UniProtKB

Cellular Location

Nucleus; Cytoplasm