Literature summary for 1.14.11.73 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 1.14.11.73

Crystallization (Commentary)

Crystallization (Comment)	Organism
the complex structures of JMJD5 and arginine derivatives reveals a Tudor domain-like binding pocket to accommodate the methylated sidechain of arginine, but not lysine	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
Q275A	mutation nearly abolishes catalytic activity	Mus musculus
Q275E	mutation displays increased enzymatic activity	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9CXT6	bifunctional peptidase and arginyl hydroxylase	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	both isoforms JMJD5 and JMJD7 bind to H3R2(me2) and H4R3(me2) peptides with similar binding affinities	Mus musculus	?	-	-

Synonyms

Synonyms	Comment	Organism
JMJD5	-	Mus musculus
KDM8	-	Mus musculus

General Information

General Information	Comment	Organism
physiological function	JMJD5 and JMJD7, EC 1.14.11.73, 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

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Release 2023.1 (January 2023)