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Literature summary for 1.14.11.63 extracted from

  • Liu, H.; Wang, C.; Lee, S.; Deng, Y.; Wither, M.; Oh, S.; Ning, F.; Dege, C.; Zhang, Q.; Liu, X.; Johnson, A.M.; Zang, J.; Chen, Z.; Janknecht, R.; Hansen, K.; Marrack, P.; Li, C.Y.; Kappler, J.W.; Hagman, J.; Zhang, G.
    Clipping of arginine-methylated histone tails by JMJD5 and JMJD7 (2017), Proc. Natl. Acad. Sci. USA, 114, E7717-E7726 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Mus musculus P0C872 bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information JMJD7 has divalent cation-dependent protease activities that preferentially cleave the tails of histones 2, 3, or 4 containing methylated arginines. After the initial specific cleavage, JMJD7, acting as aminopeptidase, progressively digests the C-terminal products Mus musculus ?
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General Information

General Information Comment Organism
physiological function the content of arginine methylation of both histones H3R2/H4R3 and overall H3/H4 is increased with the knockout of JMJD7, and the colony-forming abilities of JMJD7-deficient MDA-MB-231 cells are greatly decreased Mus musculus