Function | Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase. 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 a 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). |
Protein Name | Bifunctional Peptidase And3s-Lysyl Hydroxylase Jmjd7Jmjc Domain-Containing Protein 7Jumonji Domain-Containing Protein 7L-Lysine3s-Hydroxylase Jmjd7 |
Database Links | Reactome: R-HSA-9629569 |
Cellular Localisation | NucleusCytoplasm |
Alternative Antibody Names | Anti-Bifunctional Peptidase And antibodyAnti-3s-Lysyl Hydroxylase Jmjd7 antibodyAnti-Jmjc Domain-Containing Protein 7 antibodyAnti-Jumonji Domain-Containing Protein 7 antibodyAnti-L-Lysine antibodyAnti-3s-Hydroxylase Jmjd7 antibodyAnti-JMJD7 antibody |
Information sourced from Uniprot.org