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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.11.73 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

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.63 Mus musculus P0C872 bifunctional peptidase and (3S)-lysyl hydroxylase
-
1.14.11.73 Mus musculus Q9CXT6 bifunctional peptidase and arginyl hydroxylase
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.14.11.63 JMJD7
-
 Mus musculus
1.14.11.73 JMJD5
-
 Mus musculus
1.14.11.73 KDM8
-
 Mus musculus

General Information

EC Number General Information Comment Organism
1.14.11.63 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
1.14.11.73 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