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Literature summary for 1.14.11.68 extracted from

  • Hong, S.; Cho, Y.W.; Yu, L.R.; Yu, H.; Veenstra, T.D.; Ge, K.
    Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases (2007), Proc. Natl. Acad. Sci. USA, 104, 18439-18444 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.68

Organism

Organism UniProt Comment Textmining
Homo sapiens O15550
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information UTX prefers H3K27me2 and H3K27me3 over H3K27me1 as substrates. No substrates: methylated histone residues H3K4, H3K9, and H3K36 Homo sapiens ?
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 ?
[histone H3]-N6,N6,N6-trimethyllysine27 + 2 2-oxoglutarate + 2 O2
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 Homo sapiens [histone H3]-N6-methyllysine27 + 2 succinate + 2 formaldehyde + 2 CO2
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 ?
[histone H3]-N6,N6,N6-trimethyllysine27 + 2-oxoglutarate + O2
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 Homo sapiens [histone H3]-N6,N6-dimethyllysine27 + succinate + formaldehyde + CO2
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 ?
[histone H3]-N6,N6-dimethyllysine27 + 2-oxoglutarate + O2
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 Homo sapiens [histone H3]-N6-methyllysine27 + succinate + formaldehyde + CO2
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 ?
[histone H3]-N6-methyllysine27 + 2-oxoglutarate + O2
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 Homo sapiens [histone H3]-lysine27 + succinate + formaldehyde + CO2
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 ?

General Information

General Information Comment Organism
physiological function UTX specifically removes methyl marks on H3K27 in vitro. The demethylase activity of UTX requires a catalytically active JmjC domain. Overexpression of UTX leads to reduced di- and trimethylation on H3K27 in cells Homo sapiens