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a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
a [histone H3]-N6-methyl-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
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overall reaction
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?
a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
a [histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
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?
a [histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
a [histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
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?
ATKAARK(me3)-SAPATGGVKKPHRYRPG-GK(biotin) + 2-oxoglutarate + O2
ATKAARKSAPATGGVKKPHRYRPG-GK(biotin) + succinate + formaldehyde + CO2
usage of immunodetection for assay quantification
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?
CDYL1-K135me3 + 2-oxoglutarate + O2
CDYL1-K135me2 + succinate + formaldehyde + CO2
from chromodomain Y-like protein
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?
CSB-K1054me3 + 2-oxoglutarate + O2
CSB-K1054me2 + succinate + formaldehyde + CO2
CBS is the Cockayne syndrome group B protein
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?
CSB-K170me3 + 2-oxoglutarate + O2
CSB-K170me2 + succinate + formaldehyde + CO2
CBS is the Cockayne syndrome group B protein
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?
CSB-K297me3 + 2-oxoglutarate + O2
CSB-K297me2 + succinate + formaldehyde + CO2
CBS is the Cockayne syndrome group B protein
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?
CSB-K448me3 + 2-oxoglutarate + O2
CSB-K448me2 + succinate + formaldehyde + CO2
CBS is the Cockayne syndrome group B protein
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?
G9a-K185me3 + 2-oxoglutarate + O2
G9a-K185me2 + succinate + formaldehyde + CO2
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?
H31-15K9me3 + 2-oxoglutarate + O2
H31-15K9me2 + succinate + formaldehyde + CO2
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
histone H3 N6-methyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 L-lysine9 + succinate + formaldehyde + CO2
WIZ-K305me3 + 2-oxoglutarate + O2
WIZ-K305me2 + succinate + formaldehyde + CO2
from widely interspaced zinc finger motifs protein
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?
[chromodomain Y-like protein]-N6,N6,N6-trimethyl-L-lysine135 + 2-oxoglutarate + O2
?
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?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine1054 + 2-oxoglutarate + O2
?
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?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine170 + 2-oxoglutarate + O2
?
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?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine297 + 2-oxoglutarate + O2
?
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?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine448 + 2-oxoglutarate + O2
?
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?
[G9a protein]-N6,N6,N6-trimethyl-L-lysine185 + 2-oxoglutarate + O2
?
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a customer synthesized protein
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?
[histone H3, A7H]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3, A7H]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3, A7R]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3, A7R]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3, G12P]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3, G12P]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 26 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 26 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyl-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,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine9 + 3 succinate + 3 formaldehyde + 3 CO2
-
overall reaction
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-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + 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-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
[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-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
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-
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?
[polycomb 2 protein]-N6,N6-dimethyl-L-lysine191 + 2-oxoglutarate + O2
[polycomb 2 protein]-N6-methyl-L-lysine191 + succinate + formaldehyde + CO2
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-
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-
?
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
[widely interspaced zinc finger motifs protein]-N6,N6,N6-trimethyl-L-lysine305 + 2-oxoglutarate + O2
?
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?
additional information
?
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H31-15K9me3 + 2-oxoglutarate + O2
H31-15K9me2 + succinate + formaldehyde + CO2
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?
H31-15K9me3 + 2-oxoglutarate + O2
H31-15K9me2 + succinate + formaldehyde + CO2
a 15mer histone peptide substrate H31-15K9me3
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?
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,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,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,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,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,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-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
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-
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-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
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-
-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
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-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
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-
?
histone H3 N6-methyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 L-lysine9 + succinate + formaldehyde + CO2
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-
?
histone H3 N6-methyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 L-lysine9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
substrate binding structure, overview
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
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overall reaction
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
-
overall reaction
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
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35% demethylation activity
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
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overall reaction
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
overall reaction
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
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overall reaction
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
overall reaction
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?
[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,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,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,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
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80% demethylation activity
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-
?
[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,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
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preferred target for all KDM4 proteins, in general exhibiting 4fold preference for [histone H3]-N6,N6,N6-trimethyl-L-lysine9 over [histone H3]-N6,N6,N6-trimethyl-L-lysine36. The preference for [histone H3]-N6,N6,N6-trimethyl-L-lysine9 over [histone H3]-N6,N6-dimethyl-L-lysine9 is more modest form KDM4A (less than 3fold), KDM4B (less than 1.5fold), and KDM4D (less than 2.5fold), while the preference for KDM4C is nearly equivalent
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?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
substrate binding structure, overview
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
25% demethylation activity
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + 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 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 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
LSD1 represses gene expression through the demethylation of H3K4me1/2, a methylation site frequently associated with transcriptionally poised or active genes, but LSD1 is also linked to gene activation. LSD1 associates with the androgen receptor to enhance the expression of adrogen receptor target genes
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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
-
-
-
-
?
[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-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
isozyme JMJD2A substrate binding structure, overview
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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
-
-
-
-
?
[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-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
-
30% demethylation activity
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
-
?
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
-
-
-
?
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
LSD1 demethylates mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1
-
-
?
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
-
-
-
?
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
LSD1 demethylates mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1
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-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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-
?
additional information
?
-
-
the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
-
-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
-
-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
-
-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
-
-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
-
-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
-
-
?
additional information
?
-
dJMJD2(1)/CG15835 is capable of demethylating H3K9me3 and H3K36me3
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-
?
additional information
?
-
dJMJD2(1)/CG15835 is capable of demethylating H3K9me3 and H3K36me3
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-
?
additional information
?
-
-
dJMJD2(1)/CG15835 is capable of demethylating H3K9me3 and H3K36me3
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-
?
additional information
?
-
dJMJD2(2)/CG33182 is capable of demethylating H3K9me3 and H3K36me3
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-
?
additional information
?
-
dJMJD2(2)/CG33182 is capable of demethylating H3K9me3 and H3K36me3
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-
?
additional information
?
-
-
dJMJD2(2)/CG33182 is capable of demethylating H3K9me3 and H3K36me3
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-
?
additional information
?
-
the bifunctional enzyme specifically demethylates Lys9 and Lys36 (1.14.11.69) residues of histone H3
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?
additional information
?
-
-
JmjD2A is specific for H3K9me3 and H3K36me3 substrates in fibroblasts, and does not affect H3K27me3 methylation marks
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?
additional information
?
-
JmjD2A is specific for H3K9me3 and H3K36me3 substrates. JmjD2A directly binds to regulatory regions of neural crest specifier genes in vivo
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?
additional information
?
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JmjD2A is specific for H3K9me3 and H3K36me3 substrates
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-
?
additional information
?
-
-
LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active nethylation mark
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?
additional information
?
-
LSD1 is also involved in androgen receptor-dependent demethylation of H3K9me1/2, a methylation site enriched in silent chromatin. The complexes in which LSD1 resides tightly coordinate its gene regulatory functions and also influence its specificity for histone and non-histone substrates
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?
additional information
?
-
aspects of mechanism and specificity of LSD1, overview. To catalyze efficient demethylation, the enzyme requires H3 peptides at least 16 residues in length, consistent with the well-defined electron density corresponding to the first 16 residues of the H3K4M inhibitor. LSD1 exhibits a strong preference toward H3K4me2 substrates lacking other covalent modifications, including R2me, R8me, S10ph, K9ac, and K14ac. The side chains of K9 and K14 are solvent-exposed and do not participate in direct contacts with LSD1
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?
additional information
?
-
JMJD2A also catalyzes the reaction of the [histone H3]-lysine-9 demethylase. JMJD2A exclusively catalyzes the demethylation of H3K9me3 and H3K36me3, converting H3K9/36me3 to H3K9/36me2 but it cannot convert H3K9/36me1 or unmethylated H3K9/K36, overview
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?
additional information
?
-
-
JMJD2A also catalyzes the reaction of the [histone H3]-lysine-9 demethylase. JMJD2A exclusively catalyzes the demethylation of H3K9me3 and H3K36me3, converting H3K9/36me3 to H3K9/36me2 but it cannot convert H3K9/36me1 or unmethylated H3K9/K36, overview
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?
additional information
?
-
-
substrate specificity of recombinant isozymes, overview
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-
?
additional information
?
-
bifunctional H3K9/36me3 lysine demethylase KDM4A/JMJD2A acting on Lys 9 and Lys36 of histone 3
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-
?
additional information
?
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
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-
?
additional information
?
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
-
-
?
additional information
?
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
-
-
?
additional information
?
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
-
-
?
additional information
?
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
-
-
?
additional information
?
-
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
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-
?
additional information
?
-
the enzyme is also active on histone H3 N6,N6,N6-trimethyl-L-lysine36, cf. EC 1.14.11.27
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-
?
additional information
?
-
the enzyme is also active on histone H3 N6,N6,N6-trimethyl-L-lysine36, cf. EC 1.14.11.27
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-
?
additional information
?
-
the enzyme KDM4A also seems to be active with histone H3 N6,N6,N6-trimethyl-L-lysine27 and histone H3 N6,N6,N6-trimethyl-L-lysine36 (EC 1.14.11.27), overview
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-
?
additional information
?
-
H3K9 demethylation by DELTAN-JMJD2A, e.g. on the Myog promoter, allows the removal of repressive chromatin marks, genome-wide analysis of JMJD2A targets, transcriptional profiling studies, overview
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-
?
additional information
?
-
the enzyme acts on H3K9me3/me2, but not on H3K36 substrates
-
-
?
additional information
?
-
the enzyme acts on H3K9me3/me2, but not on H3K36 substrates
-
-
?
additional information
?
-
the enzyme acts on H3K9me3/me2, but not on H3K36 substrates
-
-
?
additional information
?
-
the enzyme acts on H3K9me3/me2, but not on H3K36 substrates
-
-
?
additional information
?
-
the enzyme acts on H3K9me3/me2, but not on H3K36 substrates
-
-
?
additional information
?
-
-
the enzyme acts on H3K9me3/me2, but not on H3K36 substrates
-
-
?
additional information
?
-
bifunctional enzyme active on H3K9me3/me2 and on H3K36me3/me2 (EC 1.14.11.69)
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4A preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4A preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4A preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4A preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4A preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4A preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4B preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4B preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4B preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4B preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4B preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4B preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4C preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4C preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4C preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4C preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4C preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
?
additional information
?
-
-
bifunctional KDM4A catalyzes demethylation of tri- and di-methylated forms of both histone H3 lysine 9 (H3K9me3/me2) and lysine 36 (H3K36me3/me2). Enzyme KDM4C preferentially catalyzes demethylation at Lys9 rather than Lys36 under identical conditions. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
-
-
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additional information
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human enzyme JMJD2A (jumonji domain containing 2A) is selective towards tri- and dimethylated histone H3 lysyl residues 9 and 36 (H3K9me3/me2 and H3K36me3/me2), it discriminates between methylation states and achieves sequence selectivity for H3K9. Structures reveal a lysyl-binding pocket in which substrates are bound in distinct bent conformations involving the Zn2+-binding site
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human enzyme JMJD2A (jumonji domain containing 2A) is selective towards tri- and dimethylated histone H3 lysyl residues 9 and 36 (H3K9me3/me2 and H3K36me3/me2), it discriminates between methylation states and achieves sequence selectivity for H3K9. Structures reveal a lysyl-binding pocket in which substrates are bound in distinct bent conformations involving the Zn2+-binding site
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human JMJD2A exhibits dual specificity for the trimethylated and, to a lesser extent, the dimethylated forms of H3K9 and H3K36, while other JMJD2 paralogues, such as JMJD2B and JMJD2D, are specific for H3K9me3/me2, with an approximately fivefold preference in specificity for the H3K9me3 substrate due to a higher KM value for the H3K36me3 peptide, suggesting that JMJD2A preferentially recognizes the H3K9me3 site
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JMJD2A is a JmjC histone demethylase (HDM) that catalyzes the demethylation of di- and trimethylated Lys9 and Lys36 in histone H3 (H3K9me2/3 and H3K36me2/3). Trimethylated Lys9 is the best substrate. JMJD2A preferentially demethylates trimethylated substrates. Histone substrates are recognized through a network of backbone hydrogen bonds and hydrophobic interactions that deposit the trimethyllysine into the active site. The trimethylated epsilon-ammonium cation is coordinated within a methylammonium-binding pocket through carbon-oxygen hydrogen bonds that position one of the zeta-methyl groups adjacent to the Fe(II) center for hydroxylation and demethylation. Analysis of the H3K9me3 or H3K36me3 peptide binding structure to the enzyme, overview
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates, and also on non-histone substrates, substrate specificities of isozymes JMJD2A-C, overview
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates, and also on non-histone substrates, substrate specificities of isozymes JMJD2A-C, overview
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates, and also on non-histone substrates, substrate specificities of isozymes JMJD2A-C, overview
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates. Usage of a formaldehyde dehydrogenase (FDH) enzyme-coupled demethylase activity assay
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates. Usage of a formaldehyde dehydrogenase (FDH) enzyme-coupled demethylase activity assay
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 substrates. The cellular activity of recombinant KDM4A against its primary substrate, H3K9me3, displays a graded response to depleting oxygen concentrations in line with the data obtained using isolated protein
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the bifunctional enzyme specifically demethylates Lys9 (H3K9me3/me2) and Lys36 (H3K36me3/me2, EC 1.14.11.69) residues of histone H3
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the bifunctional enzyme specifically demethylates Lys9 (H3K9me3/me2) and Lys36 (H3K36me3/me2, EC 1.14.11.69) residues of histone H3
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the bifunctional enzyme specifically demethylates Lys9 and Lys36 (EC 1.14.11.69) residues of histone H3
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the enzyme acts on tri- and di-methylated forms of H3K9, but not on H3K36 substrates. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
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additional information
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the enzyme acts on tri- and di-methylated forms of H3K9, but not on H3K36 substrates. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
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additional information
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the enzyme acts on tri- and di-methylated forms of H3K9, but not on H3K36 substrates. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
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additional information
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the enzyme acts on tri- and di-methylated forms of H3K9, but not on H3K36 substrates. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
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additional information
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the enzyme acts on tri- and di-methylated forms of H3K9, but not on H3K36 substrates. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
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additional information
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the enzyme acts on tri- and di-methylated forms of H3K9, but not on H3K36 substrates. Demethylation of H3K9me3 to H3K9me0 is observed on prolonged incubation of 15-residue H3K9me3 peptides
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the lysine demethylase KDM4D specifically catalyzes the demethylation of H3K9me2/me3. KDM4D lysine demethylase is an RNA-binding protein, KDM4D-RNA interaction analysis, detailed overview. KDM4D has two non-canonical RNA binding domains. The N-terminal region of KDM4D (His-KDM4D1-350) binds RNA (isolated from HEK-293 cells) in vitro
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the lysine demethylase KDM4D specifically catalyzes the demethylation of H3K9me2/me3. KDM4D lysine demethylase is an RNA-binding protein, KDM4D-RNA interaction analysis, detailed overview. KDM4D has two non-canonical RNA binding domains. The N-terminal region of KDM4D (His-KDM4D1-350) binds RNA (isolated from HEK-293 cells) in vitro
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the enzyme also demethylates lysine 26 at histone H1.4
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no activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine36
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SCFFBXO22 regulates enzyme abundance and ubiquitylation in cells and promotes enzyme ubiquitylation in vitro
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the enzyme binds RNA independently of its demethylase activity. RNA interactions with the enzyme's N-terminal region are critical for its association with chromatin and subsequently for demethylating [histone H3]-N6,N6,N6-trimethyl-L-lysine9 cells
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the enzyme binds RNA independently of its demethylase activity. RNA interactions with the enzyme's N-terminal region are critical for its association with chromatin and subsequently for demethylating [histone H3]-N6,N6,N6-trimethyl-L-lysine9 cells
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LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active nethylation mark
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low level of JMJD2b in nucleoli is not associated with the high level of H3K9 methylation in this nuclear region
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KDM4D can demethylate H3K9me2 and H3K9me3 into H3K9me1 without significant effects on most of the other histone H3 methylation patterns
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KDM4D can demethylate H3K9me2 and H3K9me3 into H3K9me1 without significant effects on most of the other histone H3 methylation patterns
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mouse Jmjd2b is a histone demethylase that specifically demethylates H3K9
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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isoform KDM4D does not use [histone H3]-N6,N6,N6-trimethyl-L-lysine36 as substrate. All KDM4 proteins show no activity with [histone H3]-N6,N6-dimethyl-L-lysine36
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 and H3K36me3/me2 (EC 1.14.11.69) substrates
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additional information
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the enzyme from rice is specific for Lys9 of histone H3
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additional information
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the enzyme from rice is specific for Lys9 of histone H3
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