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ARTK(me3)QTARKS + 2-oxoglutarate + O2
ARTK(me2)QTARKS + succinate + formaldehyde + CO2
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histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
trimethyl-histone 3 L-lysine 36 + alpha-ketoglutarate + O2
dimethyl-histone 3 L-lysine 36 + ?
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?
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[acetylated histone H3 21mer]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3 N-terminal 13mer] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 13mer] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3 N-terminal 18mer mutant K14A/R17A/K18A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 18mer mutant K14A/R17A/K18A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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-
?
[histone H3 N-terminal 18mer mutant K14ac/K18ac] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 18mer mutant K14ac/K18ac] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3 N-terminal 18mer] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 18mer] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3 N-terminal 21mer mutant K9A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant K9A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3 N-terminal 21mer mutant Q5A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant Q5A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3 N-terminal 21mer mutant R2A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant R2A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3 N-terminal 21mer mutant R8A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant R8A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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-
?
[histone H3 N-terminal 21mer mutant T3A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T3A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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-
?
[histone H3 N-terminal 21mer mutant T6A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T6A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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-
?
[histone H3 N-terminal 21mer mutant T6S] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T6S] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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-
?
[histone H3 N-terminal 21mer mutant T6V] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T6V] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3 N-terminal 21mer] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer] N-terminal N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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overall reaction
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-drimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
[histone-H3]-tridimethyllysine4 + 2-oxoglutarate + O2
?
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RBP2 is a demethylase that specifically catalyzes demethylation. RBP2 displayes robust H3K4 demethylase activity against H3K4me3 and me2, resulting in 80%-90% demethylation of the modified substrate, but fails to catalyze removal of the me1 modification state. The enzyme is capable of processively demethylating the H3K4me3 and me2 modifications to the unmodified state
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[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
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additional information
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histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
specific for
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
specific for
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
SE14 catalyzes H3K4me3 demethylation in the promoter region of RFT1
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
yeast Jhd2 demethylates histone H3 Lys4 near the rDNA locus, Jhd2 demethylates H3K4 within the rDNA regions in vivo
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histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
yeast Jhd2 demethylates histone H3 Lys4 near the rDNA locus
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
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dKDM2 is a histone lysine demethylase with specificity for H3K4me3, not H3K36me2, and regulates nucleolar organization. H3K4me3 modification is the site of active transcription
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[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
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overall reaction
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
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recruitment of RBP2 to the promoter region of a key mitochondrial component results in demethylation of H3K4 at this promoter and its transcriptional repression
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[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
JMJD2A has the unique property of binding trimethylated peptides from histone sequences, H3K4me3 through itstandem hybrid tudor domains. JMJD2A Asp945 and Asp940 interact with Arg2 of the H3K4me3 peptide, but not with H4K20me3. Asn940 forms hydrogen bonds with the backbone amide and hydroxyl groups of H3K4me3 Thr3
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[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
dJMJD2(1)/CG15835 and dJMJD2(2)/CG33182 demethylate both H3K9me3 and H3K36me3
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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overall reaction
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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KDM5b specifically demethylates lysine 4 of histone H3, thereby repressing gene transcription
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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very weak activity
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
dJMJD2(1)/CG15835 and dJMJD2(2)/CG33182 demethylate both H3K9me3 and H3K36me3
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?
[histone H3]-N6,N6-drimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6-drimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6-drimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-drimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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-
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?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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-
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?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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-
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-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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-
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?
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
Drosophila sp. (in: flies)
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the JARID1 family of demethylases specifically remove both the di- and trimethylated H3K4 epigenetic mark
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?
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
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recombinant PLU-1 can only demethylate H3K4me3 and H3K4me2 when analyzed in vitro
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?
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
-
RBP2 is a demethylase that specifically catalyzes demethylation. RBP2 displayes robust H3K4 demethylase activity against H3K4me3 and me2, resulting in 80%-90% demethylation of the modified substrate, but fails to catalyze removal of the me1 modification state. The enzyme is capable of processively demethylating the H3K4me3 and me2 modifications to the unmodified state
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?
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
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RBP2 is a demethylase that specifically catalyzes demethylation. The enzyme is capable of erasing trimethylated H3K4. The enzyme is capable of processively demethylating the H3K4me3 and me2 modifications to the unmodified state
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?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
Lid knockdown using RNA interference results in a specific genome-wide increase in H3K4me3 levels without affecting other patterns of H3 methylation
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?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
Drosophila sp. (in: flies)
-
the JARID1 family of demethylases specifically remove both the di- and trimethylated H3K4 epigenetic mark
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-
?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
RNA-interference-mediated depletion of SMCX increases H3K4 trimethylation at the sodium channel type 2A (SCN2A) and synapsin I (SYN1) promoters. SMCX activity impairs REST-mediated neuronal gene regulation, thereby contributing to SMCX-associated X-linked mental retardation
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?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
-
recombinant PLU-1 can only demethylate H3K4me3 and H3K4me2 when analyzed in vitro
-
-
?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
-
RBP2 is a demethylase that specifically catalyzes demethylation. RBP2 displayes robust H3K4 demethylase activity against H3K4me3 and me2, resulting in 80%-90% demethylation of the modified substrate, but fails to catalyze removal of the me1 modification state. The enzyme is capable of processively demethylating the H3K4me3 and me2 modifications to the unmodified state
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?
additional information
?
-
the enzyme shows no activity with histone H3 N6,N6-dimethyl-L-lysine4 and histone H3 N6-methyl-L-lysine4
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?
additional information
?
-
no activity with [histone H3]-N6,N6-dimethyl-L-lysine4, [histone H3]-N6-methyl-L-lysine4, [histone H3]-N6,N6,N6-trimethyl-L-lysine9, [histone H3]-N6,N6-dimethyl-L-lysine9, [histone H3]-N6,N6,N6-trimethyl-L-lysine27, [histone H3]-N6,N6-dimethyl-L-lysine27, [histone H3]-N6,N6,N6-trimethyl-L-lysine36 and [histone H3]-N6,N6-dimethyl-L-lysine36
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-
additional information
?
-
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no activity with [histone H3]-N6,N6-dimethyl-L-lysine9, [histone H3]-N6,N6-dimethyl-L-lysine27, spermine, spermidine, and putrescine
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-
-
additional information
?
-
the enzyme shows no activity with histone H3 N6,N6-dimethyl-L-lysine4 and histone H3 N6-methyl-L-lysine4
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?
additional information
?
-
KDM5A, a histone H3K4 demethylase, physically interacts with the nucleosome remodeling and deacetylase (NuRD) complex
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?
additional information
?
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-
KDM5A, a histone H3K4 demethylase, physically interacts with the nucleosome remodeling and deacetylase (NuRD) complex
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?
additional information
?
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no activity with monomethylated H3K4
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?
additional information
?
-
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no activity with monomethylated H3K4
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?
additional information
?
-
no activity with H3K4me1
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?
additional information
?
-
histone H3K4 demethylases are essential in development and differentiation
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?
additional information
?
-
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isoform dJMJD2(1)/CG15835 regulates heterochromatin organization. It is excluded from heterochromatin and localizes to multiple euchromatic sites, where it regulates trimethylated histone 3 lysine 36 methylation
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?
additional information
?
-
isoform dJMJD2(1)/CG15835 regulates heterochromatin organization. It is excluded from heterochromatin and localizes to multiple euchromatic sites, where it regulates trimethylated histone 3 lysine 36 methylation
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-
?
additional information
?
-
isoform dJMJD2(1)/CG15835 regulates heterochromatin organization. It is excluded from heterochromatin and localizes to multiple euchromatic sites, where it regulates trimethylated histone 3 lysine 36 methylation
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-
?
additional information
?
-
-
the demethylase activity of Lid is not affected by its association with other proteins, but Lid antagonizes Rpd3 function acting as a positive trancription regulator. Lid inhibits the activity of Rpd3 at an Rpd3 target gene
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?
additional information
?
-
-
demethylase activity of dJMJD2(1)/CG15835 depends on the JmjC domain. No activity with H3K4me3 and H3K27me3 by dJMJD2(1)/CG15835 and dJMJD2(2)/CG33182
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-
?
additional information
?
-
demethylase activity of dJMJD2(1)/CG15835 depends on the JmjC domain. No activity with H3K4me3 and H3K27me3 by dJMJD2(1)/CG15835 and dJMJD2(2)/CG33182
-
-
?
additional information
?
-
demethylase activity of dJMJD2(1)/CG15835 depends on the JmjC domain. No activity with H3K4me3 and H3K27me3 by dJMJD2(1)/CG15835 and dJMJD2(2)/CG33182
-
-
?
additional information
?
-
no activity with H3K4me1
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-
?
additional information
?
-
Drosophila sp. (in: flies)
-
histone H3K4 demethylases are essential in development and differentiation
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
Lid is required for Myc-induced cell growth
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-
?
additional information
?
-
-
RB-binding protein 2, RBP2, is a key effector for retinoblastoma protein mediating cell-cycle withdrawal and differentiation by interacting with a variety of proteins. During differentiation, RBP2 exerts inhibitory effects on multiple genes through direct interaction with their promoters. RBP2 shows high correlation with the presence of H3K4me3, and its target genes are separated into two functionally distinct classes: differentiation-independent and differentiation-dependent genes. Molecular mechanisms of RBP2 regulation of differentiation, overview. Functional analysis of RBP2 target genes and differentially expressed genes, overview
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?
additional information
?
-
JMJD2A also demethylates histone H3 dimethylated or trimethylated at lysine 9 and lysine 36, by means of an N-terminal catalytic domain, as well as peptides from H4K20me3, recognized through its tudor domains. The hybrid tudor domains at the C terminus of JMJD2A are necessary for the demethylation activity of JMJD2A in vivo. H3K4me3 and H4K20me3 are recognized with similar affinities by JMJD2A, binding structures, overview. Two other amino acids of JMJD2A, Tyr942 and Thr968, involved in weaker intermolecular hydrogen bonds, selectively contact one peptide and not the other. The hydroxyl group of Thr968 in the wild-type structure forms a hydrogen bond with the guanido group of H4K20me3 Arg23 but does not contact H3K4me3. Tyr942 and Thr968 are not essential for the tight binding of JMJD2A to H3K4me3 and H4K20me3
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?
additional information
?
-
-
the enzyme interacts with the C-terminus of hPc2, a Polycomb group PcG protein, via its N-terminus in vitro and in vivo, role for hPc2 acting as a transcriptional co-repressor, interaction analysis, overview
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-
?
additional information
?
-
KDM5A, a histone H3K4 demethylase, physically interacts with the nucleosome remodeling and deacetylase (NuRD) complex
-
-
?
additional information
?
-
KDM5B associates with the deacetylase NuRD complex
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-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with monomethylated H3K4
-
-
?
additional information
?
-
no activity with monomethylated H3K4
-
-
?
additional information
?
-
no activity with monomethylated H3K4
-
-
?
additional information
?
-
no activity with monomethylated H3K4
-
-
?
additional information
?
-
-
the enzyme is physically associated with the MLL2 complex in vivo
-
-
-
additional information
?
-
-
the enzyme does not demethylate [histone H3]-N6-methyl-L-lysine4
-
-
-
additional information
?
-
histone H3K4 demethylases are essential in development and differentiation
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-
?
additional information
?
-
-
the PRC2 enzyme complex recruits H3K4me3 demethylase Rbp2 to its target genes, where its acts as mediator for the repressive activity of the PRC2 complex during embryonic stem cell differentiation, Rbp2 binds directly to the PRC2 complex, overview
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-
?
additional information
?
-
-
H3K4me3 marks are found at regulatory elements as well as transcriptional start sites. In the Deltex-1 promoter region two major peaks are observed: one at the transcriptional start site, and one at the RBP-J-binding site, 1.2 kb upstream of the transcriptional start site, mechanism by which RBP-J bound to promoters of Notch target genes recruits KDM5A to facilitate histone demethylation, overview
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-
?
additional information
?
-
protein-protein interaction anaysis of wild-type and mutants and interactional domains between Rbp2 and Piasy, overview
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-
?
additional information
?
-
-
protein-protein interaction anaysis of wild-type and mutants and interactional domains between Rbp2 and Piasy, overview
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-
?
additional information
?
-
-
the enzyme is active on H3 trimethylated at K4 and dimethylated at K36 (EC 1.14.11.27), it might preferentially demethylate H3 trimethylated at K4
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-
?
additional information
?
-
-
no activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4, [histone H3]-N6,N6-dimethyl-L-lysine9, [histone H3]-N6,N6-dimethyl-L-lysine27 and [histone H3]-N6,N6-dimethyl-L-lysine36
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-
-
additional information
?
-
JMJ703 specifically reverses all three forms of H3K4me, mono-, di-, or trimethylated state histone 3, in rice
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-
?
additional information
?
-
-
JMJ703 specifically reverses all three forms of H3K4me, mono-, di-, or trimethylated state histone 3, in rice
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-
?
additional information
?
-
the recombinant enzyme is specific for H3K4me1/2/3 in vitro, no activity of FLAG:HA-tagged JmjN-JmjC-zinc finger region to demethylate H3K9me1/2/3, or H3K36me1/2/3. Binding affinities of c-JMJ703 to H3K4 peptides with mono-, di-, or trimethylation, overview
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-
?
additional information
?
-
-
the recombinant enzyme is specific for H3K4me1/2/3 in vitro, no activity of FLAG:HA-tagged JmjN-JmjC-zinc finger region to demethylate H3K9me1/2/3, or H3K36me1/2/3. Binding affinities of c-JMJ703 to H3K4 peptides with mono-, di-, or trimethylation, overview
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-
?
additional information
?
-
two LINE elements, Karma and its N-terminal truncation, are identified as direct targets of JMJ703 in epigenetic regulation by demethylation. Karma is directly associated with JMJ703
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-
?
additional information
?
-
the enzyme JMJ703 is specific for H3K4me3/me2/me1 residues, no activity on H3K9me3/2/1, H3K27me3/2/1 and H3K36me3/2/1
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-
?