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Literature summary for 1.14.11.27 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
Homo sapiens P0C870 cf. EC 1.14.11.63
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Homo sapiens Q8N371 cf. EC 1.14.11.73
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Synonyms

Synonyms Comment Organism
JMJD5
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Homo sapiens
JMJD7
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Homo sapiens

General Information

General Information Comment Organism
physiological function JMJD5 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, JMJD5 acting as aminopeptidase, progressively digests the C-terminal products. JMJD5-deficient fibroblasts exhibit dramatically increased levels of methylated arginines and histones Homo sapiens
physiological function JMJD5 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, JMJD5 acting as aminopeptidase, progressively digests the C-terminal products. JMJD5-deficient fibroblasts exhibit dramatically increased levels of methylated arginines and histones. Depletion of JMJD7 in breast cancer cells greatly decreases cell proliferation Homo sapiens