Recombinant Human JmjC domain-containing protein 7 (JMJD7)

Uniprot Id

P0C870

Target Species

Human

Target Name

JMJD7

Target Full Name

Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7

Target Function

Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monoxygenase. 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. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Additionally, may play a role in protein biosynthesis by modifying the translation machinery. Acts as Fe(2+) and 2-oxoglutarate-dependent monoxygenase, 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).

Target Subcellular Location

Nucleus. Cytoplasm.

Target Research Area

Cell Biology

Target Synonyms

JMJD7; Bifunctional peptidase and; 3S)-lysyl hydroxylase JMJD7; EC 1.14.11.63; EC 3.4.-.-; JmjC domain-containing protein 7; Jumonji domain-containing protein 7; L-lysine; 3S)-hydroxylase JMJD7

Target Background

This gene 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. Most tissues also express read-through transcripts from this gene into the downstream phospholipase A2, group IVB (cytosolic) gene, some of which may encode fusion proteins combining the N-terminus of this protein with the phospholipase A2, group IVB protein.