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Information on EC 1.14.11.69 - [histone H3]-trimethyl-L-lysine36 demethylase
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1.14.11.69 [histone H3]-trimethyl-L-lysine36 demethylaseIUBMB Comments
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated Lys36 residues in the tail of the histone protein H3 (H3K36). This lysine residue can exist in three methylation states (mono-, di- and trimethylated), but this group of enzymes only act on the the tri- and di-methylated forms. The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. Since trimethylation of H3K36 enhances transcription, this enzyme acts as a transcription repressor. The enzymes that possess this activity often also catalyse the activity of EC 1.14.11.66, [histone H3]-trimethyl-L-lysine9 demethylase. cf. EC 1.14.11.27, [histone H3]-dimethyl-L-lysine36 demethylase.
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Word Map
- 1.14.11.69
-
demethylation
- demethylases
- chromatin
-
jumonji
-
trimethylation
- fbxl10
-
polycomb
-
heterochromatic
- hp1a
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
jmjc protein, jmjc demethylase, histone h3k36 demethylase, jmjd-2, h3k36 histone demethylase, rph1/kdm4, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
histone H3K36 demethylase
JHDM3A
JMJD2A
JMJD2B
JMJD2C
KDM4
KDM4A
KDM4A demethylase
KDM4B
Kdm4c
lysine-specific demethylase 4A
Rph1
Rph1/KDM4
additional information
JHDM3A
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-
-
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JMJD2A
-
-
-
-
JMJD2A
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JMJD2B
-
-
-
-
KDM4A
-
-
-
-
KDM4A
-
KDM4B
-
-
-
-
Rph1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2 = a [histone H3]-N6-methyl-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
overall reaction
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a [histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
(1a)
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a [histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
(1b)
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-
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SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6,N6-trimethyl-L-lysine36,2-oxoglutarate:oxygen oxidoreductase
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated Lys36 residues in the tail of the histone protein H3 (H3K36). This lysine residue can exist in three methylation states (mono-, di- and trimethylated), but this group of enzymes only act on the the tri- and di-methylated forms. The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. Since trimethylation of H3K36 enhances transcription, this enzyme acts as a transcription repressor. The enzymes that possess this activity often also catalyse the activity of EC 1.14.11.66, [histone H3]-trimethyl-L-lysine9 demethylase. cf. EC 1.14.11.27, [histone H3]-dimethyl-L-lysine36 demethylase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
a [histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
ATKAARK(me3)-SAPATGGVKKPHRYRPG-GK(biotin) + 2-oxoglutarate + O2
ATKAARKSAPATGGVKKPHRYRPG-GK(biotin) + succinate + formaldehyde + CO2
usage of immunodetection for assay quantification
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-
?
dimethyl-histone 3 L-lysine 36 + 2-oxoglutarate + O2
methyl-histone 3 L-lysine 36 + succinate + formaldehyde + CO2
-
enzyme Rph1 is specific for di- and trimethyl-histone 3 L-lysine36
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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
histone H3 N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
histone H3 N6-methyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 L-lysine36 + succinate + formaldehyde + 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-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
trimethyl-histone 3 L-lysine 36 + 2-oxoglutarate + O2
dimethyl-histone 3 L-lysine 36 + succinate + formaldehyde + CO2
-
enzyme Rph1 is specific for di- and trimethyl-histone 3 L-lysine36
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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
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 26 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyllysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyllysine36 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6,N6-trimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyllysine36 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
[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-dimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-lysine36 + succinate + formaldehyde + CO2
-
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?
[histone H3]-N6,N6-dimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyllysine36 + succinate + formaldehyde + CO2
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
calf thymus type II-A histones
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?
histone H3 N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
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?
histone H3 N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
calf thymus type II-A histones
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-
?
histone H3 N6-methyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 L-lysine36 + succinate + formaldehyde + CO2
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-
?
histone H3 N6-methyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 L-lysine36 + succinate + formaldehyde + CO2
calf thymus type II-A histones
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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
-
KDM4A demethylates H3K36me3, a modification enriched in the 3' end of active genes
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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-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
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?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
Aspergillus nidulans CBS 112.46
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
Aspergillus nidulans M139
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
Aspergillus nidulans NRRL 194
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-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
substrate binding structure, overview
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-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
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?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyllysine36 + 2 succinate + 2 formaldehyde + 2 CO2
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?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyllysine36 + 2 succinate + 2 formaldehyde + 2 CO2
-
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?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyllysine36 + 2 succinate + 2 formaldehyde + 2 CO2
-
-
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?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyllysine36 + succinate + formaldehyde + CO2
-
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?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyllysine36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyllysine36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6,N6-trimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyllysine36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
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?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
substrate binding structure, overview
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + 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-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
histone H3K36 methylation is enriched in coding regions of actively transcribed genes. dKDM4A is a JmjC domain-containing protein specifically demethylates H3K36me2 and H3K36me3 both in vitro and in vivo. H3K36 methylation is also subject to dynamic regulation. HP1a regulates histone H3K36 methylation in Drosophila larvae
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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
-
JmjC domain-containing protein dKDM4A is a histone H3K36 demethylase. Histone H3 methylation is one of the consistent marks distinguishing alternative chromatin packaging states
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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
with HeLa cell core histone 3. dKDM4A is a JmjC domain-containing protein specifically demethylates H3K36me2 and H3K36me3 both in vitro and in vivo. The demethylation reaction mediated by dKDM4A requires Fe2+, 2-oxoglutarate, and ascorbate as cofactors
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?
[histone H3]-N6,N6-dimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyllysine36 + succinate + formaldehyde + CO2
-
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-
?
[histone H3]-N6,N6-dimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyllysine36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyllysine36 + succinate + formaldehyde + CO2
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-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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?
additional information
?
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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-
?
additional information
?
-
Aspergillus nidulans CBS 112.46
the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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-
?
additional information
?
-
the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
-
-
?
additional information
?
-
Aspergillus nidulans M139
the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
-
-
?
additional information
?
-
Aspergillus nidulans NRRL 194
the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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-
?
additional information
?
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HP1a and dKDM4A interact with each other and loss of HP1a leads to an increased level of histone H3K36me3
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?
additional information
?
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HP1a and dKDM4A interact with each other and loss of HP1a leads to an increased level of histone H3K36me3
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?
additional information
?
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dJMJD2(1)/CG15835 is capable of demethylating H3K9me3 and H3K36me3
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?
additional information
?
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dJMJD2(1)/CG15835 is capable of demethylating H3K9me3 and H3K36me3
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?
additional information
?
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dJMJD2(2)/CG33182 is capable of demethylating H3K9me3 and H3K36me3
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?
additional information
?
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dJMJD2(2)/CG33182 is capable of demethylating H3K9me3 and H3K36me3
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?
additional information
?
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the bifunctional enzyme specifically demethylates Lys9 (EC 1.14.11.66) and Lys36 residues of histone H3
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?
additional information
?
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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
?
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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
?
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bifunctional H3K9/36me3 lysine demethylase KDM4A/JMJD2A acting on Lys 9 and Lys36 of histone 3
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?
additional information
?
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JMJD2A demethylates trimethylated histone K9/K36 to di- but not mono- or unmethylated products, i.e. JMJD2A also catalyzes the reactions of EC 1.14.11.66, H3K9 trimethyl demethylase
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?
additional information
?
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bifunctional enzyme active on H3K9me3/me2 (EC 1.14.11.66) and on H3K36me3/me2
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?
additional information
?
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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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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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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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enzyme additionally demethylates H3K9me3, reaction of EC 1.14.11.66
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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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additional information
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human JMJD2A exhibits dual specificity for the trimethylated and, to a lesser extent, the dimethylated forms of H3K9 and H3K36, 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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additional information
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JHDM3A removes the me3 group from modified H3 lysine 9 (H3K9) and H3 lysine 36 (H3K36)
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additional information
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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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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 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 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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additional information
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the bifunctional enzyme specifically demethylates Lys9 and Lys36 residues of histone H3 (EC 1.14.11.66)
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
?
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
?
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
?
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
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the bifunctional enzyme is active on H3K9me3/me2 (EC 1.14.11.66) and H3K36me3/me2 substrates
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additional information
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general function of histone demethylase for histone 3 L-lysine 36 is to promote transcription elongation by antagonizing repressive L-lysine 36 methylation by Set2 methyltransferase
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additional information
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Rph1 is a histone demethylase that can specifically demethylate tri- and dimethylated Lys36 of histone H3. 2-Oxoglutarate forms hydrogen-bonding interactions with the side chains of conserved residues. The substrate-binding cleft of Rph1 is formed with several structural elements of the JmjC domain, the long beta-hairpin and the mixed structural motif, and the methylated Lys36 of H3 is recognized by several conserved residues of the JmjC domain. Molecular basis for the substrate specificity of Rph1, overview
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additional information
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Rph1 is a histone demethylase specific to tri-methylated-H3K36. Rph1 binds to the URS of PHR1 through ZF domains and modulates chromatin modifications in specific regions of the PHR1 promoter
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additional information
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Rph1 is a histone demethylase specific to tri-methylated-H3K36. Rph1 binds to the URS of PHR1 through ZF domains and modulates chromatin modifications in specific regions of the PHR1 promoter
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a [histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
a [histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
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?
dimethyl-histone 3 L-lysine 36 + 2-oxoglutarate + O2
methyl-histone 3 L-lysine 36 + succinate + formaldehyde + CO2
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enzyme Rph1 is specific for di- and trimethyl-histone 3 L-lysine36
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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-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
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?
histone H3 N6-methyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 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
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
trimethyl-histone 3 L-lysine 36 + 2-oxoglutarate + O2
dimethyl-histone 3 L-lysine 36 + succinate + formaldehyde + CO2
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enzyme Rph1 is specific for di- and trimethyl-histone 3 L-lysine36
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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 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyllysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyllysine36 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6,N6-trimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyllysine36 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
[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-dimethyllysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyllysine36 + succinate + formaldehyde + CO2
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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KDM4A demethylates H3K36me3, a modification enriched in the 3' end of active genes
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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-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
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?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
Aspergillus nidulans CBS 112.46
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?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
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?