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Information on EC 1.14.11.66 - [histone H3]-trimethyl-L-lysine9 demethylase and Organism(s) Homo sapiens and UniProt Accession B2RXH2

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IUBMB Comments
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated Lys-9 residues in the tail of the histone protein H3 (H3K9). 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. cf. EC 1.14.11.65, [histone H3]-dimethyl-L-lysine9 demethylase.
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This record set is specific for:
Homo sapiens
UNIPROT: B2RXH2
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
histone demethylase, kdm3a, jmjd1a, lysine-specific demethylase 1, jmjd2b, jmjd2c, histone lysine demethylase, jmjd2d, kdm3b, jhdm2a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H3K9 demethylase
-
GASC1
H3K9 demethylase
-
H3K9 trimethyl demethylase
-
-
H3K9/36me3 lysine demethylase
-
H3K9me3 histone demethylase
-
H3K9me3-specific demethylase
-
-
histone demethylase
histone demethylase JmjD2A
-
histone demethylase JMJD2A/KDM4A
-
histone demethylase JMJD2B
-
-
histone H3 demethylase
-
histone H3K9 demethylase
-
histone H3K9/H3K36 trimethyldemethylase
-
histone lysine demethylase
-
JDHM3A
-
-
JmjC histone lysine demethylase
-
JmjC-domain-containing histone demethylase 3A
-
-
JMJD2A
JMJD2A demethylase
-
JMJD2A/KDM4A
-
-
JMJD2B
JMJD2C
JMJD2D
-
-
jumonji C-domaincontaining histone demethylase 3A
-
-
jumonji domain containing 2A
-
Jumonji domaincontaining demethylase
-
-
JumonjiC-domain-containing histone demethylase
-
KDM4A
KDM4A lysine demethylase
-
KDM4A/JMJD2A
-
KDM4B
KDM4B/JMJD2B histone demethylase
-
-
Kdm4c
KDM4D
LSD1 demethylase
-
-
LSD1 H3 demethylase
-
-
lysine-specific demethylase 1
-
-
lysine-specific demethylase 4C
-
-
lysine-specific demethylase 4D
-
trimethylated histone H3-lysine 9-specific demethylase
-
-
trimethyllysine-specific histone demethylase
-
trimethyllysine-specific JmjC HDM
-
[histone H3]-lysine-9 demethylase
-
additional information
SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6,N6-trimethyl-L-lysine9,2-oxoglutarate:oxygen oxidoreductase
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated Lys-9 residues in the tail of the histone protein H3 (H3K9). 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. cf. EC 1.14.11.65, [histone H3]-dimethyl-L-lysine9 demethylase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
overall reaction
-
-
?
a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
a [histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
a [histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
a [histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
ATKAARK(me3)-SAPATGGVKKPHRYRPG-GK(biotin) + 2-oxoglutarate + O2
ATKAARKSAPATGGVKKPHRYRPG-GK(biotin) + succinate + formaldehyde + CO2
show the reaction diagram
usage of immunodetection for assay quantification
-
-
?
CDYL1-K135me3 + 2-oxoglutarate + O2
CDYL1-K135me2 + succinate + formaldehyde + CO2
show the reaction diagram
from chromodomain Y-like protein
-
-
?
CSB-K1054me3 + 2-oxoglutarate + O2
CSB-K1054me2 + succinate + formaldehyde + CO2
show the reaction diagram
CBS is the Cockayne syndrome group B protein
-
-
?
CSB-K170me3 + 2-oxoglutarate + O2
CSB-K170me2 + succinate + formaldehyde + CO2
show the reaction diagram
CBS is the Cockayne syndrome group B protein
-
-
?
CSB-K297me3 + 2-oxoglutarate + O2
CSB-K297me2 + succinate + formaldehyde + CO2
show the reaction diagram
CBS is the Cockayne syndrome group B protein
-
-
?
CSB-K448me3 + 2-oxoglutarate + O2
CSB-K448me2 + succinate + formaldehyde + CO2
show the reaction diagram
CBS is the Cockayne syndrome group B protein
-
-
?
G9a-K185me3 + 2-oxoglutarate + O2
G9a-K185me2 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
H31-15K9me3 + 2-oxoglutarate + O2
H31-15K9me2 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
WIZ-K305me3 + 2-oxoglutarate + O2
WIZ-K305me2 + succinate + formaldehyde + CO2
show the reaction diagram
from widely interspaced zinc finger motifs protein
-
-
?
[chromodomain Y-like protein]-N6,N6,N6-trimethyl-L-lysine135 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine1054 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine170 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine297 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[Cockayne syndrome group B protein]-N6,N6,N6-trimethyl-L-lysine448 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
[G9a protein]-N6,N6,N6-trimethyl-L-lysine185 + 2-oxoglutarate + O2
?
show the reaction diagram
-
a customer synthesized protein
-
-
?
[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
show the reaction diagram
-
-
-
?
[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
show the reaction diagram
-
-
-
?
[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
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 26 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 26 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
[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
show the reaction diagram
-
overall reaction
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
[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
show the reaction diagram
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine9 + 3 succinate + 3 formaldehyde + 3 CO2
show the reaction diagram
-
overall reaction
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6-methyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[polycomb 2 protein]-N6,N6-dimethyl-L-lysine191 + 2-oxoglutarate + O2
[polycomb 2 protein]-N6-methyl-L-lysine191 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
[widely interspaced zinc finger motifs protein]-N6,N6,N6-trimethyl-L-lysine305 + 2-oxoglutarate + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
overall reaction
-
-
?
a [histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
a [histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
a [histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
a [histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6,N6-trimethyl-L-lysine 26 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 26 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
[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
show the reaction diagram
-
overall reaction
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
[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
show the reaction diagram
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine9 + 3 succinate + 3 formaldehyde + 3 CO2
show the reaction diagram
-
overall reaction
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
[histone H3]-N6-methyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[polycomb 2 protein]-N6,N6-dimethyl-L-lysine191 + 2-oxoglutarate + O2
[polycomb 2 protein]-N6-methyl-L-lysine191 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
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
show the reaction diagram
LSD1 demethylates mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
alteration of multiple H3 methylation marks by KDM4A at different oxygen concentrations, overview
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-2-(1-(1-benzoylpiperidin-3-yl)-1H-1,2,3-triazol-4-yl)isonicotinic acid
-
(R)-2-hydroxyglutarate
-
-
(S)-2-hydroxyglutarate
-
-
1-(3-(ethylsulfonyl)phenyl)-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
1-(3-(methylsulfonyl)phenyl)-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
1-(4-(methylsulfonyl)phenyl)-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
1-phenyl-2-(4-(pyridin-2-yl)thiazol-2-yl)ethan-1-one
-
2-(1-hydroxyvinyl)isonicotinic acid
-
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
-
2-(2-aminothiazol-4-yl)isonicotinamide
2-(2-aminothiazol-4-yl)isonicotinic acid
2-(2-benzamidothiazol-4-yl)isonicotinic acid
-
2-(2-methylthiazol-4-yl)isonicotinic acid
-
2-(thiazol-4-yl)isonicotinic acid
-
3-((2-(pyridin-2-yl)-6-(1,2,4,5-tetrahydro-3H-benzo[d]azepin-3-yl)pyrimidin-4-yl)amino)propanoic acid
-
3-(2-((2-aminoethyl)carbamoyl)pyridin-4-yl)benzoic acid
-
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
-
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
-
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
4-((methyl((1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)methyl)amino)methyl)benzonitrile
-
4-((methyl(2-(1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)ethyl)amino)methyl)benzonitrile
-
4-(1-(2-(1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)ethyl)piperidin-4-yl)benzonitrile
-
4-(pyridin-2-yl)thiazol-2-amine
low inhibition activity
4-(pyridin-3-yl)thiazol-2-amine
low inhibition activity
5-(anilinomethyl)quinolin-8-ol
-
-
5-tetrazolyl acetohydrazide
-
8-(((furan-2-ylmethyl)amino)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-((4-(pyridin-2-yl)piperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-((4-methylpiperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-((4-phenylpiperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-((benzylamino)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-((dimethylamino)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(1-methyl-1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(2-aminothiazol-4-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(((3,4-dichlorobenzyl)(methyl)amino)methyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-((dimethylamino)methyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-((methyl(4-(methylsulfonyl)benzyl)amino)methyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-((4-fluorobenzyl) (methyl)amino)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-((5-cyclopropyl-1,2,4-oxadiazol-3-yl)methyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(2,4-difluorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(2-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(3,4-dichlorobenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(3,5-dichlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(3,5-difluorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(3-(trifluoromethyl)phenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(3-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(3-methoxybenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(4-(methylsulfonyl)phenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(4-(trifluoromethyl)benzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(4-chlorobenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(4-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-(4-(2-(4-(4-fluorobenzyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(4-fluorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(4-methoxyphenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(benzo[d][1,3]dioxol-5-ylmethyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(pyridin-3-ylmethyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(pyridin-4-yl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-(thiophen-2-yl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-benzylpiperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(2-(4-phenylpiperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(hydroxymethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(piperidin-1-ylmethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(4-(pyrrolidin-1-ylmethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
-
8-(piperidin-1-ylmethyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
8-(thiazol-4-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
8-chloropyrido[3,4-d]pyrimidin-4(3H)-one
-
caffeic acid
Co2+
has an activating on multiple histone modifications at the global level. Cobalt ions significantly increase global histone H3K4me3, H3K9me2, H3K9me3, H3K27me3 and H3K36me3, as well as uH2A and uH2B and decreases acetylation at histone H4 (AcH4) in vivo. Cobalt ions increase H3K9me3 and H3K36me3 by inhibiting histone demethylation process in vivo. And cobalt ions directly inhibit demethylase activity of JMJD2A in vitro. Cobalt ions do not increase the level of uH2A in the in vitro histone ubiquitinating assay and inhibit histone-deubiquitinating enzyme activity in vitro
dimethyl 4-hydroxy-1H-pyrazole-3,5-dicarboxylate
-
-
H2O2
loss of KDM4A activity in hypoxia resulting in changes to global histone lysine methylation
lithium 2-(((furan-2-ylmethyl)amino)methyl)isonicotinate
-
lithium 2-((benzylamino)methyl)isonicotinate
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
-
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
methyl (S)-3-(2'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
-
methylstat
-
-
N-oxalylglycine
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
-
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
-
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
NCDM-32
-
-
Peptide inhibitor
a suicide inhibitor consisting of a 21 residue histone H3 peptide in which K4 is modified by an Nmethylpropargyl group. Interactions with the inhibitor include hydrogen bonds to its R2 and Q5 side chains and a salt bridge interaction between the alpha-amine of A1 and Asp555 in LSD1, binding structure, overview
-
pyrido[3,4-d]pyrimidin-4(3H)-one
-
SW55
a hydroxamate-based histone deacetylase (HDAC) inhibitor, slight inhibition
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
-
tert-butyl benzo[b]tellurophen-2-ylmethylcarbamate
shows KDM4 specific inhibitory activity in cervical cancer HeLa cells. The compound also induces cell death in cervical and colon cancer but not in normal cells
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
fisetin
fisetin induces DNA damage via critical transcription factor RFXAP/KDM4A-dependent histone H3K36 demethylation, thus causing inhibition of proliferation in pancreatic adenocarcinoma (PDAC). Fisetin inhibits cell proliferation and induces DNA damage and S-phase arrest in PDAC. Expression of RFXAP and other DNA-damage response genes is upregulated by fisetin. RFXAP targets KDM4A. Overexpression of RFXAP upregulates KDM4A and attenuates methylation of H3K36, impairing DNA repair and enhancing the DNA damage induced by fisetin
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
histone H3 N6,N6,N6-trimethyl-L-lysine9
KDM4E, pH and temperature not specified in the publication
0.025
histone H3 N6,N6-dimethyl-L-lysine9
KDM4E, pH and temperature not specified in the publication
0.023
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9
pH and temperature not specified in the publication, recombinant isozyme KDM4E
0.025
[histone H3]-N6,N6-dimethyl-L-lysine 9
pH and temperature not specified in the publication, recombinant isozyme KDM4E
0.0247
2-oxoglutarate
0.0232
H31-15K9me3
-
0.031 - 0.048
histone H3 N6,N6,N6-trimethyl-L-lysine9
0.05 - 0.074
histone H3 N6,N6-dimethyl-L-lysine9
0.173
O2
0.11
[histone H3, A7H]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.18
[histone H3, A7R]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.93
[histone H3, G12P]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.031 - 0.071
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9
0.05 - 0.074
[histone H3]-N6,N6-dimethyl-L-lysine 9
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.076
histone H3 N6,N6,N6-trimethyl-L-lysine9
KDM4E, pH and temperature not specified in the publication
0.065
histone H3 N6,N6-dimethyl-L-lysine9
KDM4E, pH and temperature not specified in the publication
0.076
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9
pH and temperature not specified in the publication, recombinant isozyme KDM4E
0.065
[histone H3]-N6,N6-dimethyl-L-lysine 9
pH and temperature not specified in the publication, recombinant isozyme KDM4E
0.01 - 0.029
histone H3 N6,N6,N6-trimethyl-L-lysine9
0.0029 - 0.012
histone H3 N6,N6-dimethyl-L-lysine9
0.000183
[histone H3, A7H]-N6,N6,N6-trimethyl-L-lysine 9, [histone H3, A7R]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.00012
[histone H3, G12P]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.00025 - 0.029
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9
0.0029 - 0.072
[histone H3]-N6,N6-dimethyl-L-lysine 9
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
330
histone H3 N6,N6,N6-trimethyl-L-lysine9
KDM4E, pH and temperature not specified in the publication
260
histone H3 N6,N6-dimethyl-L-lysine9
KDM4E, pH and temperature not specified in the publication
3.304
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9
pH and temperature not specified in the publication, recombinant isozyme KDM4E
2.6
[histone H3]-N6,N6-dimethyl-L-lysine 9
pH and temperature not specified in the publication, recombinant isozyme KDM4E
22 - 90
histone H3 N6,N6,N6-trimethyl-L-lysine9
4 - 16
histone H3 N6,N6-dimethyl-L-lysine9
0.00166
[histone H3, A7H]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.00102
[histone H3, A7R]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.00013
[histone H3, G12P]-N6,N6,N6-trimethyl-L-lysine 9
pH 7.3, 37°C, recombinant enzyme
-
0.0035 - 0.903
[histone H3]-N6,N6,N6-trimethyl-L-lysine 9
0.0397 - 1.09
[histone H3]-N6,N6-dimethyl-L-lysine 9
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.079
(R)-2-hydroxyglutarate
Homo sapiens
-
pH and temperature not specified in the publication
0.097
(S)-2-hydroxyglutarate
Homo sapiens
-
pH and temperature not specified in the publication
0.037
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.003
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.2
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0703
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0606
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0068
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0136
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0371
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0021
5-(anilinomethyl)quinolin-8-ol
Homo sapiens
-
pH and temperature not specified in the publication
0.0466
5-tetrazolyl acetohydrazide
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0085
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0137
caffeic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.147
dimethyl 4-hydroxy-1H-pyrazole-3,5-dicarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0258
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0706
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.056
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0171
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0563
methyl (S)-3-(2'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0476
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.029
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0483
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0548
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0522
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0939
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0254
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0276
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0068
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0034
methylstat
Homo sapiens
-
pH and temperature not specified in the publication
0.5
N-oxalylglycine
Homo sapiens
-
pH and temperature not specified in the publication
0.2
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0145
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0188
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0166
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.001
NCDM-32
Homo sapiens
-
pH and temperature not specified in the publication
0.0254
SW55
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0143
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.201
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
Homo sapiens
pH 7.5, 37°C, recombinant enzyme
0.0302
tert-butyl benzo[b]tellurophen-2-ylmethylcarbamate
Homo sapiens
37°C, pH not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00029
0.0004
recombinant isozyme JMJD2B, pH 7.5, 22°C, substrate CSB-K297me3
0.0005
0.0006
recombinant isozyme JMJD2A, pH 7.5, 22°C, substrate CSB-K448me3
0.00064
recombinant isozyme JMJD2A, pH 7.5, 22°C, substrate CSB-K297me3
0.00095
recombinant isozyme JMJD2B, pH 7.5, 22°C, substrate CDYL1-K135me3
0.001
0.0011
recombinant isozyme JMJD2A, pH 7.5, 22°C, substrate CSB-K170me3
0.00143
recombinant isozyme JMJD2B, pH 7.5, 22°C, substrate CSB-K1054me3
0.0015
recombinant isozyme JMJD2C, pH 7.5, 22°C, substrate CSB-K297me3
0.00163
recombinant isozyme JMJD2C, pH 7.5, 22°C, substrate CSB-K1054me3
0.00188
recombinant isozyme JMJD2A, pH 7.5, 22°C, substrate WIZ-K305me3
0.0019
0.002
recombinant isozyme JMJD2B, pH 7.5, 22°C, substrate CSB-K170me3
0.00212
recombinant isozyme JMJD2C, pH 7.5, 22°C, substrate G9a-K185me3
0.00232
recombinant isozyme JMJD2C, pH 7.5, 22°C, substrate CSB-K448me3
0.0024
recombinant isozyme JMJD2B, pH 7.5, 22°C, substrate G9a-K185me3
0.0025
recombinant isozyme JMJD2B, pH 7.5, 22°C, substrate CSB-K448me3
0.0026
recombinant isozyme JMJD2A, pH 7.5, 22°C, substrate G9a-K185me3
0.0031
recombinant isozyme JMJD2C, pH 7.5, 22°C, substrate WIZ-K305me3
0.0034
recombinant isozyme JMJD2C, pH 7.5, 22°C, substrate CDYL1-K135me3
0.0035
recombinant isozyme JMJD2B, pH 7.5, 22°C, substrate WIZ-K305me3
additional information
-
specific isozyme activities with non-histone substrates, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
JMJD2B expression profile in gastric cancer, overview
Manually annotated by BRENDA team
-
short isoform of JMJD2A is upregulated during muscle differentiation, expression analysis and pattern, overview
Manually annotated by BRENDA team
the short isoform of JMJD2A is upregulated during muscle differentiation, expression analysis and pattern, overview
Manually annotated by BRENDA team
elevated levels of JMJD2B expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KDM4E_HUMAN
506
0
56804
Swiss-Prot
other Location (Reliability: 3)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complex with inhibitor, sitting drop vapor diffusion method, mixing of 10 mg/ml protein and 2.5 mM 2,4-pyridinedicarboxylic acid with well solution, containing 20% v/v PEG 3350, 0.1 M sodium citrate, pH 5.5, and 2 mM NiCl2, in a 2:1 ratio, 4°C, X-ray diffraction structure determination and analysis at 2.1 A resolution. The zinc-binding site in KDM4E is disordered possibly due to loss of zinc in the crystallization process
crystal structure determinations of JMJD2A in complex with histone H3 peptides bearing different methylated forms of K9 and K36
crystal structures of LSD1/Co-REST complexes bound to histone H3 peptides. LSD1/Co-REST-C complex co-crystallized with a 20-residue histone H3 peptide inhibitor in which Lys4 is mutated to a methionine. Cocrystallization of the enzyme with a suicide inhibitor consisting of a 21-residue histone H3 peptide in which K4 is modified by an N-methylpropargylgroup. Complex structure analysis, overview
purified JMJD2A catalytic domain in complex with H3K9me3, H3K36me2 and H3K36me3 peptides, vapor diffusion method, from 0.2 M sodium/potassium phosphate, pH 6.5, and 20% w/v PEG 3350, at 4°C, and by microseeding from 12% w/v PEG monomethyl ether 5000 and 0.1 M HEPES, pH 7.0, X-ray diffraction structure determination and analysis at 2.05-2.30 A resolution
purified recombinant detagged enzyme in apo form and in complex with several inhibitors, hanging drop vapor diffusion method, mixing of 0.0015 ml of 7 mg/ml protein solution with 0.0015 ml of reservoir solution containing 2-16% w/v PEG 4000 and 0.1 M BTP, pH 7.5, and equilibration against 0.8 ml, 18°C, 1 week, the crystals are then soaked by addition of 750 nL of ligand solution at 10-200 mM in DMSO directly to the crystallizatin drops, followed by 4-48 h incubation at 18°C, X-ray diffraction structure determination and analysis
purified recombinant enzyme in complex with inhibitor, sitting drop vapor diffusion method, mixing of 7 mg/ml protein and 2 mM N-oxalylglycine with well solution, containing 25% v/v PEG 3350, 0.2 M sodium nitrate, 0.1 M bis-tris propane, pH 6.5, 5% v/v ethylene glycol, 0.01 M NiCl2, in a 2:1 ratio, 4°C, X-ray diffraction structure determination and analysis at 2.55 A resolution
purified recombinant enzyme in complex with substrate peptides, by vapour diffusion at 4°C from 0.1 M citrate, pH 5.5, 20% PEG 3350 and 4 mM NiCl2, X-ray diffraction structure determination and analysis
purified recombinant KDM4C, sitting drop vapor diffusion method, mixing of 7 mg/ml protein with 2 mM N-oxalylglycine with well solution, containing 25% v/v PEG 3350, 0.2 M sodium nitrate, 0.1 M Bis tris propane, pH 6.5, 5% v/v ethylene glycol, 0.01 M NiCl2, in a 2:1 ratio, 4°C, X-ray diffraction structure determination and analysis at 2.55 A resolution
structures of JMJD2A-Ni(II)-Zn(II) inhibitor complexes bound to tri-, di- and monomethyl forms of histone 3 lysine 9 and the trimethyl form of histone 3 lysine 36. The structures reveal a lysyl-binding pocket in which substrates are bound in distinct bent conformations involving the Zn-binding site. The mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I71L
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
I87K
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
N86H
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
Q88K
KDM4E mutant, the mutant shows demethylation of H3K9me2, and the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
R309G
KDM4E mutant, poor demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
D191A
site-directed mutagenesis, the mutant shows about 95%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
H188A
-
inactive
H188A/E190A
site-directed mutagenesis, inactive mutant
N202M
site-directed mutagenesis, a KDM4D demethylase-dead mutant, that binds RNA like the wild-type enzyme
N290A
site-directed mutagenesis, the mutant shows no activity with H3K36me3 and almost no activity with H3K9me3
N290D
site-directed mutagenesis, the mutant shows about 98%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
R919D
site-directed mutagenesis, the mutant is not associated with mitotic chromatin in contrast to the wild-type enzyme
S198M
site-directed mutagenesis, a KDM4C demethylase dead mutant
S288A
Y175F
site-directed mutagenesis, the mutant shows about 90%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
Y177F
site-directed mutagenesis, the mutant shows about 90%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the molecular chaperon Hsp90 interacts with and stabilizes KDM4B protein
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged KDM4E from Escherichia coli by nickel affinity chromatography
Ni-NTA resin column chromatography
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography and dialysis
recombinant GST-tagged isozymes JMJD2A, JMJD2B, and JMJD2C from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography and gel filtration
recombinant His-tagged KDM4A residues 1-359 from Escherichia coli strain BL21 Codon-Plus-Ril by nickel affinity chromatography to over 90% purity
recombinant N-terminally GST-tagged enzyme from Spodoptera frugiperda Sf9 cells by glutathione affinity chromatography and gel filtration, recombinant N-terminally His-tagged KDM4A 1-359 from Escherichia coli by nickel affinity chromatography, followed by tag removal with TEV protease, another step of nickel affinity chromatography using the eluate, and gel filtration
recombinant N-terminally His-tagged enzyme from Escherichia coli by nickel affinity chromatography, gel filtration, and anion exchange chromatography
recombinant N-terminally His-tagged KDM4A catalytic domain from Escherichia coli
recombinant N-terminally His-tagged KDM4A from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His-tagged KDM4B from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His-tagged KDM4C from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His-tagged KDM4D from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His6-tagged truncated KDM4A1-359 from Escherichia coli BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant N-terminally His6-tagged truncated KDM4A1-359 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant wild-type and mutant benzonae-treated His6-tagged full-length enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His-tagged KDM4E in Escherichia coli
gene KDM4E, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4E catalytic domain in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in NIH-3T3 cells and early mouse embryos
-
expressed in Sf9 insect cells
-
expression of functional doxycycline-inducible EGFP-KDM4B in U2-OSTetON cell line
-
expression of N-terminally His-tagged KDM4A in Escherichia coli
expression of N-terminally His-tagged KDM4B in Escherichia coli
expression of N-terminally His-tagged KDM4C in Escherichia coli
expression of N-terminally His-tagged KDM4D in Escherichia coli
gene KDM4A, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4A catalytic domain in Escherichia coli
gene KDM4A, real-time RT-PCR enzyme expression analysis
gene KDM4A, recombinant expression of EGFP-tagged full-length and truncated enzymes versions in U2-O2 cells
gene KDM4A, recombinant expression of FLAG-tagged JMJD2A in Spodoptera frugiperda Sf9 cells
gene KDM4A, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
gene KDM4A, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
gene KDM4A, recombinant expression of His-tagged KDM4A residues 1-359 in Escherichia coli strain BL21 Codon-Plus-Ril from plasmid pNIC28-Bsa4
gene KDM4A, recombinant expression of N-terminally FLAG-tagged wild-type KDM4A or KDM4A H188A variant in U2OS cells and in HeLa cells, quantitative RT-PCR enzyme expression analysis, recombinant expression of N-terminally His6-tagged truncated KDM4A1-359 in Escherichia coli BL21(DE3)
gene KDM4A, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli
gene KDM4A, recombinant overexpression in U2O2 cells, recombinant expression of N-terminally FLAG-tagged KDM4A or KDM4A mutant H188A in HeLa cells, recombinant expression of N-terminally His6-tagged truncated KDM4A1-359 in Escherichia coli strain BL21(DE3)
gene KDM4A, short isoform of JMJD2A, DELTAN-JMJD2A, expression analysis, expression profiling of C2C12 cells, overview. DELTAN1-JMJD2A and DELTAN2-JMJD2A mRNAs are expressed at about 20% of the amount of the full-length mRNAs
gene KDM4A, transient recombinant overexpression in RPE cells
gene KDM4B or Jmjd2b, real-time quantitative PCR expression analysis
gene KDM4B, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4B catalytic domain in Escherichia coli
gene KDM4B, quantitative real-time PCR enzyme expression analysis
gene KDM4B, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
gene KDM4B, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4B
gene KDM4C, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4C catalytic domain in Escherichia coli
gene KDM4C, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
gene KDM4C, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4C, recombinant expression of EGFP-tagged full-length and truncated, and mutant enzymes versions
gene KDM4D, functional recombinant expression of wild-type and mutant His6-tagged full-length enzyme in Escherichia coli strain BL21(DE3). To establish the U2OS-TetON stable cell line that conditionally expresses myc-KDM4D or EGFP-KDM4D-1H4R-HRK-FL, fragments including the myc-KDM4D or EGFP-KDM4D-1H4R-HRK-FL are subcloned into pTRE2-puro plasmid. The resulting pTRE2-puro-myc-KDM4D and pTRE2-puro-EGFP-KDM4D-1H4R-HRK-FL vectors are transfected into U2OS-Tet-ON cells. REcombinant expression of the His-tagged N-terminus, residues 1.350, of the enzyme, expressing the His-tagged C-terminus of KDM4D proves unsuccessful
gene KDM4D, phylogenetic analysis, recombinant expression of N-terminally His-tagged KDM4D catalytic domain in Escherichia coli
gene KMD4A, recombinant expression of N-terminally His-tagged KDM4A construct (residues 1-359) in Escherichia coli, recombinant expression of N-terminally GST-tagged enzyme in Spodoptera frugiperda Sf9 cells via baculovirus transfection method
JMJD2A-C genes, DNA and amino acid sequence determination and analysis, expression of the GST-tagged isozymes JMJD2A, JMJD2B, and JMJD2C in Escherichia coli strain BL21(DE3)
-
JMJD2B quantitative real-time PCR expression analysis
JMJD2B quantitative RT-PCR expression analysis, overview
-
mouse Jmjd2b is transfected into JMJD2B-depleted MCF-7 cells, with stable transfection of JMJD2B-specific siRNA molecules
-
short isoform of JMJD2A expression analysis, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a significant upregulation of KDM4D is observed in gastrointestinal stromal tumour tissue compared with matched normal tissue
enzyme expression is markedly increased in Hep-G2 cells treated with palmitate and oleate or liver X receptor agonist T09013178
-
estrogen receptor alpha is important for JMJD2B expression in hypoxia, JMJD2B can be upregulated in hypoxia in an HIF-1alpha-dependent manner
-
short isoform of JMJD2A is upregulated during muscle differentiation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
KDM4A possesses the potential to act as an oxygen sensor in the context of chromatin modifications, with possible implications for epigenetic regulation in hypoxic disease states
medicine
pharmacology
KDM4A possesses the potential to act as an oxygen sensor in the context of chromatin modifications, with possible implications for epigenetic regulation in hypoxic disease states
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ng, S.S.; Kavanagh, K.L.; McDonough, M.A.; Butler, D.; Pilka, E.S.; Lienard, B.M.; Bray, J.E.; Savitsky, P.; Gileadi, O.; von Delft, F.; Rose, N.R.; Offer, J.; Scheinost, J.C.; Borowski, T.; Sundstrom, M.; Schofield, C.J.; Oppermann, U.
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity
Nature
448
87-91
2007
Homo sapiens (O75164), Homo sapiens
Manually annotated by BRENDA team
Ponnaluri, V.; Vavilala, D.; Putty, S.; Gutheil, W.; Mukherji, M.
Identification of non-histone substrates for JMJD2A-C histone demethylases
Biochem. Biophys. Res. Commun.
390
280-284
2009
Homo sapiens
Manually annotated by BRENDA team
Marmorstein, R.; Trievel, R.C.
Histone modifying enzymes: structures, mechanisms, and specificities
Biochim. Biophys. Acta
1789
58-68
2009
Homo sapiens (O60341)
Manually annotated by BRENDA team
Brasacchio, D.; Okabe, J.; Tikellis, C.; Balcerczyk, A.; George, P.; Baker, E.K.; Calkin, A.C.; Brownlee, M.; Cooper, M.E.; El-Osta, A.
Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with gene-activating epigenetic marks that coexist on the lysine tail
Diabetes
58
1229-1236
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Yang, J.; Jubb, A.M.; Pike, L.; Buffa, F.M.; Turley, H.; Baban, D.; Leek, R.; Gatter, K.C.; Ragoussis, J.; Harris, A.L.
The histone demethylase JMJD2B is regulated by estrogen receptor alpha and hypoxia, and is a key mediator of estrogen induced growth
Cancer Res.
70
6456-6466
2010
Homo sapiens
Manually annotated by BRENDA team
Toyokawa, G.; Cho, H.; Iwai, Y.; Yoshimatsu, M.; Takawa, M.; Hayami, S.; Maejima, K.; Shimizu, N.; Tanaka, H.; Tsunoda, T.; Field, H.; Kelly, J.; Neal, D.; Ponder, B.; Maehara, Y.; Nakamura, Y.; Hamamoto, R.
The histone demethylase JMJD2B plays an essential role in human carcinogenesis through positive regulation of cyclin-dependent kinase 6
Cancer Prev. Res. (Phila)
4
2051-2061
2011
Homo sapiens (O94953), Homo sapiens
Manually annotated by BRENDA team
Hillringhaus, L.; Yue, W.W.; Rose, N.R.; Ng, S.S.; Gileadi, C.; Loenarz, C.; Bello, S.H.; Bray, J.E.; Schofield, C.J.; Oppermann, U.
Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family
J. Biol. Chem.
286
41616-41625
2011
Homo sapiens (B2RXH2), Homo sapiens (O75164), Homo sapiens (O94953), Homo sapiens (Q6B0I6), Homo sapiens (Q9H3R0), Homo sapiens
Manually annotated by BRENDA team
Ipenberg, I.; Guttmann-Raviv, N.; Khoury, H.P.; Kupershmit, I.; Ayoub, N.
Heat shock protein 90 (Hsp90) selectively regulates the stability of KDM4B/JMJD2B histone demethylase
J. Biol. Chem.
288
14681-14687
2013
Homo sapiens
Manually annotated by BRENDA team
Verrier, L.; Escaffit, F.; Chailleux, C.; Trouche, D.; Vandromme, M.
A new isoform of the histone demethylase JMJD2A/KDM4A is required for skeletal muscle differentiation
PLoS Genet.
7
e1001390
2011
Homo sapiens
Manually annotated by BRENDA team
Shi, L.; Sun, L.; Li, Q.; Liang, J.; Yu, W.; Yi, X.; Yang, X.; Li, Y.; Han, X.; Zhang, Y.; Xuan, C.; Yao, Z.; Shang, Y.
Histone demethylase JMJD2B coordinates H3K4/H3K9 methylation and promotes hormonally responsive breast carcinogenesis
Proc. Natl. Acad. Sci. USA
108
7541-7546
2011
Homo sapiens
Manually annotated by BRENDA team
Hancock, R.L.; Masson, N.; Dunne, K.; Flashman, E.; Kawamura, A.
The activity of JmjC histone lysine demethylase KDM4A is highly sensitive to oxygen concentrations
ACS Chem. Biol.
12
1011-1019
2017
Homo sapiens (O75164)
Manually annotated by BRENDA team
Morera, L.; Roatsch, M.; Fuerst, M.C.; Hoffmann, I.; Senger, J.; Hau, M.; Franz, H.; Schuele, R.; Heinrich, M.R.; Jung, M.
4-biphenylalanine- and 3-phenyltyrosine-derived hydroxamic acids as inhibitors of the JumonjiC-domain-containing histone demethylase KDM4A
ChemMedChem
11
2063-2083
2016
Homo sapiens (O75164), Homo sapiens
Manually annotated by BRENDA team
Bavetsias, V.; Lanigan, R.M.; Ruda, G.F.; Atrash, B.; McLaughlin, M.G.; Tumber, A.; Mok, N.Y.; Le Bihan, Y.V.; Dempster, S.; Boxall, K.J.; Jeganathan, F.; Hatch, S.B.; Savitsky, P.; Velupillai, S.; Krojer, T.; England, K.S.; Sejberg, J.; Thai, C.; Donovan, A.; Pal, A.; Scozzafava, G.; Bennett, J.M.; Kawamu, A.
8-Substituted pyrido[3,4-d]pyrimidin-4(3H)-one derivatives as potent, cell permeable, KDM4 (JMJD2) and KDM5 (JARID1) histone lysine demethylase inhibitors
J. Med. Chem.
59
1388-1409
2016
Homo sapiens (O75164), Homo sapiens (O94953)
Manually annotated by BRENDA team
Yuan, X.; Kong, J.; Ma, Z.; Li, N.; Jia, R.; Liu, Y.; Zhou, F.; Zhan, Q.; Liu, G.; Gao, S.
KDM4C, a H3K9me3 histone demethylase, is involved in the maintenance of human ESCC-initiating cells by epigenetically enhancing SOX2 expression
Neoplasia
18
594-609
2016
Homo sapiens (Q9H3R0), Homo sapiens
Manually annotated by BRENDA team
Zoabi, M.; Nadar-Ponniah, P.T.; Khoury-Haddad, H.; Usaj, M.; Budowski-Tal, I.; Haran, T.; Henn, A.; Mandel-Gutfreund, Y.; Ayoub, N.
RNA-dependent chromatin localization of KDM4D lysine demethylase promotes H3K9me3 demethylation
Nucleic Acids Res.
42
13026-13038
2014
Homo sapiens, Homo sapiens (Q6B0I6)
Manually annotated by BRENDA team
Kupershmit, I.; Khoury-Haddad, H.; Awwad, S.W.; Guttmann-Raviv, N.; Ayoub, N.
KDM4C (GASC1) lysine demethylase is associated with mitotic chromatin and regulates chromosome segregation during mitosis
Nucleic Acids Res.
42
6168-6182
2014
Homo sapiens (O75164), Homo sapiens (O94953), Homo sapiens (Q9H3R0)
Manually annotated by BRENDA team
An, J.; Xu, J.; Li, J.; Jia, S.; Li, X.; Lu, Y.; Yang, Y.; Lin, Z.; Xin, X.; Wu, M.; Zheng, Q.; Pu, H.; Gui, X.; Li, T.; Lu, D.
HistoneH3 demethylase JMJD2A promotes growth of liver cancer cells through up-regulating miR372
Oncotarget
8
49093-49109
2017
Homo sapiens (O75164)
Manually annotated by BRENDA team
Jang, M.K.; Kim, J.H.; Jung, M.H.
Histone H3K9 demethylase JMJD2B activates adipogenesis by regulating H3K9 methylation on PPARgamma and C/EBPalpha during adipogenesis
PLoS ONE
12
e0168185
2017
Homo sapiens (O94953)
Manually annotated by BRENDA team
Ponnaluri, V.; Vavilala, D.; Putty, S.; Gutheil, W.; Mukherji, M.
Identification of non-histone substrates for JMJD2A-C histone demethylases
Biochem. Biophys. Res. Commun.
390
280-284
2009
Homo sapiens (O75164), Homo sapiens (O94953), Homo sapiens (Q9H3R0)
Manually annotated by BRENDA team
Li, W.; Zhao, L.; Zang, W.; Liu, Z.; Chen, L.; Liu, T.; Xu, D.; Jia, J.
Histone demethylase JMJD2B is required for tumor cell proliferation and survival and is overexpressed in gastric cancer
Biochem. Biophys. Res. Commun.
416
372-378
2011
Homo sapiens (O94953)
-
Manually annotated by BRENDA team
Marmorstein, R.; Trievel, R.C.
Histone modifying enzymes structures, mechanisms, and specificities
Biochim. Biophys. Acta
1789
58-68
2009
Homo sapiens (O75164)
Manually annotated by BRENDA team
Li, Q.; Ke, Q.; Costa, M.
Alterations of histone modifications by cobalt compounds
Carcinogenesis
30
1243-1251
2009
Homo sapiens (O75164), Homo sapiens
Manually annotated by BRENDA team
Black, J.C.; Manning, A.L.; Van Rechem, C.; Kim, J.; Ladd, B.; Cho, J.; Pineda, C.M.; Murphy, N.; Daniels, D.L.; Montagna, C.; Lewis, P.W.; Glass, K.; Allis, C.D.; Dyson, N.J.; Getz, G.; Whetstine, J.R.
KDM4A lysine demethylase induces site-specific copy gain and rereplication of regions amplified in tumors
Cell
154
541-555
2013
Homo sapiens (O75164)
Manually annotated by BRENDA team
Hillringhaus, L.; Yue, W.W.; Rose, N.R.; Ng, S.S.; Gileadi, C.; Loenarz, C.; Bello, S.H.; Bray, J.E.; Schofield, C.J.; Oppermann, U.
Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family
J. Biol. Chem.
286
41616-41625
2011
Homo sapiens (B2RXH2), Homo sapiens (O75164), Homo sapiens (O94953), Homo sapiens (Q6B0I6), Homo sapiens (Q9H3R0), Homo sapiens
Manually annotated by BRENDA team
Tan, M.K.; Lim, H.J.; Harper, J.W.
SCF(FBXO22) regulates histone H3 lysine 9 and 36 methylation levels by targeting histone demethylase KDM4A for ubiquitin-mediated proteasomal degradation
Mol. Cell. Biol.
31
3687-3699
2011
Homo sapiens
Manually annotated by BRENDA team
Couture, J.; Collazo, E.; Ortiz-Tello, P.A.; Brunzelle, J.S.; Trievel, R.C.
Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase
Nat. Struct. Mol. Biol.
14
689-695
2007
Homo sapiens (O75164)
Manually annotated by BRENDA team
Klose, R.J.; Yamane, K.; Bae, Y.; Zhang, D.; Erdjument-Bromage, H.; Tempst, P.; Wong, J.; Zhang, Y.
The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
Nature
442
312-316
2006
Homo sapiens
Manually annotated by BRENDA team
Ng, S.S.; Kavanagh, K.L.; McDonough, M.A.; Butler, D.; Pilka, E.S.; Lienard, B.M.; Bray, J.E.; Savitsky, P.; Gileadi, O.; von Delft, F.; Rose, N.R.; Offer, J.; Scheinost, J.C.; Borowski, T.; Sundstrom, M.; Schofield, C.J.; Oppermann, U.
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity
Nature
448
87-91
2007
Homo sapiens (O75164), Homo sapiens
Manually annotated by BRENDA team
Verrier, L.; Escaffit, F.; Chailleux, C.; Trouche, D.; Vandromme, M.
A new isoform of the histone demethylase JMJD2A/KDM4A is required for skeletal muscle differentiation
PLoS Genet.
7
e1001390
2011
Homo sapiens (O75164)
Manually annotated by BRENDA team
Chen, Z.; Zang, J.; Kappler, J.; Hong, X.; Crawford, F.; Wang, Q.; Lan, F.; Jiang, C.; Whetstine, J.; Dai, S.; Hansen, K.; Shi, Y.; Zhang, G.
Structural basis of the recognition of a methylated histone tail by JMJD2A
Proc. Natl. Acad. Sci. USA
104
10818-10823
2007
Homo sapiens (O75164)
Manually annotated by BRENDA team
Holowatyj, A.; Yang, Z.
The role of histone demethylase GASC1 in cancer and its therapeutic potential
Curr. Cancer. Ther. Rev.
9
78-85
2013
Homo sapiens
-
Manually annotated by BRENDA team
Jeong, Y.S.; Park, J.S.; Ko, Y.; Kang, Y.K.
JHDM3A module as an effector molecule in guide-directed modification of target chromatin
J. Biol. Chem.
286
4461-4470
2011
Homo sapiens
Manually annotated by BRENDA team
Kim, T.D.; Oh, S.; Shin, S.; Janknecht, R.
Regulation of tumor suppressor p53 and HCT116 cell physiology by histone demethylase JMJD2D/KDM4D
PLoS ONE
7
e34618
2012
Homo sapiens
Manually annotated by BRENDA team
Kim, J.H.; Jung, D.Y.; Nagappan, A.; Jung, M.H.
Histone H3K9 demethylase JMJD2B induces hepatic steatosis through upregulation of PPARgamma2
Sci. Rep.
8
13734
2018
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Li, M.; Cheng, J.; Ma, Y.; Guo, H.; Shu, H.; Huang, H.; Kuang, Y.; Yang, T.
The histone demethylase JMJD2A promotes glioma cell growth via targeting Akt-mTOR signaling
Cancer Cell Int.
20
101
2020
Homo sapiens (O75164), Homo sapiens
Manually annotated by BRENDA team
Xiang, Y.; Yan, K.; Zheng, Q.; Ke, H.; Cheng, J.; Xiong, W.; Shi, X.; Wei, L.; Zhao, M.; Yang, F.; Wang, P.; Lu, X.; Fu, L.; Lu, X.; Li, F.
Histone demethylase KDM4B promotes DNA damage by activating long interspersed nuclear element-1
Cancer Res.
79
86-98
2019
Homo sapiens (O94953)
Manually annotated by BRENDA team
Jones, D.; Wilson, L.; Thomas, H.; Gaughan, L.; Wade, M.A.
The histone demethylase enzymes KDM3A and KDM4B co-operatively regulate chromatin transactions of the estrogen receptor in breast cancer
Cancers (Basel)
11
1122
2019
Homo sapiens (O94953)
Manually annotated by BRENDA team
Ding, G.; Xu, X.; Li, D.; Chen, Y.; Wang, W.; Ping, D.; Jia, S.; Cao, L.
Fisetin inhibits proliferation of pancreatic adenocarcinoma by inducing DNA damage via RFXAP/KDM4A-dependent histone H3K36 demethylation
Cell Death Dis.
11
893
2020
Homo sapiens (O75164)
Manually annotated by BRENDA team
Kim, Y.; Lee, D.; Choi, Y.; Jeong, J.; Kwon, S.
Benzo[b]tellurophenes as a potential histone H3 lysine 9 demethylase (KDM4) inhibitor
Int. J. Mol. Sci.
20
5098
2019
Homo sapiens (O75164)
Manually annotated by BRENDA team
Hu, F.; Li, H.; Liu, L.; Xu, F.; Lai, S.; Luo, X.; Hu, J.; Yang, X.
Histone demethylase KDM4D promotes gastrointestinal stromal tumor progression through HIF1beta/VEGFA signalling
Mol. Cancer
17
107
2018
Homo sapiens (Q6B0I6), Homo sapiens
Manually annotated by BRENDA team