Literature summary for 1.14.11.63 extracted from

Liu, H.; Wang, C.; Lee, S.; Ning, F.; Wang, Y.; Zhang, Q.; Chen, Z.; Zang, J.; Nix, J.; Dai, S.; Marrack, P.; Hagman, J.; Kappler, J.; Zhang, G.
Specific recognition of arginine methylated histone tails by JMJD5 and JMJD7 (2018), Sci. Rep., 8, 3275 .

Search for more literature for 1.14.11.63

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P0C872	bifunctional peptidase and (3S)-lysyl hydroxylase	-

Synonyms

Synonyms	Comment	Organism
JMJD7	-	Mus musculus

General Information

General Information	Comment	Organism
physiological function	JMJD5, EC 1.14.11.73, and JMJD7 function as endopeptidases that cleave histone tails specifically adjacent to methylated arginine residues and continue to degrade N-terminal residues of histones via their aminopeptidase activity. Recognition between the enzymes and histone substrates is specific. JMJD5 and JMJD7 show high structural similarity, share common substrates and high binding affinity. JMJD5 does not bind to arginine methylated histone tails with additional lysine acetylation while JMJD7 does not bind to arginine methylated histone tails with additional lysine methylation	Mus musculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)