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Information on EC 1.14.11.27 - [histone H3]-dimethyl-L-lysine36 demethylase
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1.14.11.27 [histone H3]-dimethyl-L-lysine36 demethylaseIUBMB Comments
Requires iron(II). Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys36 (K36me2), which is its natural substrate, to form the monomethylated and unmethylated forms of Lys36. It can also demethylate monomethylated (but not the trimethylated) Lys36. cf. EC 1.14.11.69, [histone H3]-trimethyl-L-lysine36 demethylase.
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Word Map
- 1.14.11.27
- demethylases
- chromatin
-
demethylation
-
h3k9me3
-
jumonji
-
trimethylation
- methyltransferases
-
lysine-specific
- heterochromatin
-
tri-methylated
-
tudor
- setdb1
-
chromatin-modifying
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
dKDM2, dKDM4A, dRAF, GASC1, H3-K36 demethylase, H3-K36-specific demethylase, H3K36 demethylase, H3K36me2 demethylase, H3K36me2 histone demethylase, H3K36me2-specific demethylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H3-K36 demethylase
H3K36 demethylase
H3K36me2-specific demethylase
histone H3 lysine 36 demethylase
JHDM1A
JmjC domain-containing histone demethylase 1
JMJD5
KDM4
additional information
additional information
-
the enzyme belongs to large family of Jumonji C (JmjC)-domain-containing histone lysine demethylases, JHDMs
additional information
-
JHDM1A is a member of the JHDM (JmjC-domain-containing histone demethylase) family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2 = a [histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
overall reaction
-
-
-
a [histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
(1a)
-
-
-
a [histone H3]-N6-methyl-L-lysine36 + 2-oxoglutarate + O2 = a [histone H3]-L-lysine36 + succinate + formaldehyde + CO2
(1b)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6-dimethyl-L-lysine36,2-oxoglutarate:oxygen oxidoreductase
Requires iron(II). Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys36 (K36me2), which is its natural substrate, to form the monomethylated and unmethylated forms of Lys36. It can also demethylate monomethylated (but not the trimethylated) Lys36. cf. EC 1.14.11.69, [histone H3]-trimethyl-L-lysine36 demethylase.
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CAS REGISTRY NUMBER
COMMENTARY
55071-98-2
-
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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
dimethyl-histone 3 L-lysine 36 + 2-oxoglutarate + O2
methyl-histone 3 L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine26 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine26 + 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,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + 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
protein 6-N,6-N-dimethyl-L-lysine + 2-oxoglutarate + O2
protein 6-N-methyl-L-lysine + succinate + formaldehyde + CO2
-
specifically demethylates Lys36 of histone H3
-
-
?
protein 6-N-methyl-L-lysine + 2-oxoglutarate + O2
protein L-lysine + succinate + formaldehyde + CO2
-
specifically demethylates Lys36 of histone H3
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
protein N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
specifically demethylates Lys36 of histone H3
-
-
?
protein N6-methyl-L-lysine + 2-oxoglutarate + O2
protein L-lysine + succinate + formaldehyde + CO2
-
specifically demethylates Lys36 of histone H3
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
predicted site-specificity from phylogenetic analysis
-
-
?
[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-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
predicted site-specificity from phylogenetic analysis
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
predicted site-specificity from phylogenetic analysis
-
-
?
[histone H3]-N6-methyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-L-lysine 36 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
predicted site-specificity from phylogenetic analysis
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-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,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
substrate is preferred compared to histone H3-N6,N6-dimethyl-L-lysine36
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
low activity
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
Jhdm1a is a histone demethylase that specifically demethylates dimethylated H3K36
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
KDM2b/JHDM1b is an H3K36me2-specific demethylase
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
Jhdm1a is a histone demethylase that specifically demethylates dimethylated H3K36
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
Jhdm1a is a histone demethylase that specifically demethylates dimethylated H3K36
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
-
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
Jhdm1a actively demethylates dimethylated H3K36 on the C/EBPalpha locus
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
-
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
-
H3K36 demethylation activity of the fly dKDM4A is dramatically stimulated upon HP1a association
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
removal of histone H3 Lys36 dimethylation is coupled to histone H2A monoubiquitinylation, overview
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
the effect of Jhdm1b on cell proliferation and cellular senescence is mediated through de-repression of p15Ink4b as loss of p15Ink4b function rescues cell proliferation defects in Jhdm1b knockdown cells
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
-
predicted site-specificity from phylogenetic analysis
-
-
?
additional information
?
-
-
dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information
-
-
?
additional information
?
-
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
-
-
?
additional information
?
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
-
-
?
additional information
?
-
KDM4D and -E only act on H3K9, with no evidence for demethylation of H3K36, while KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates. No activity by all isozymes with H3K4me3, H3K9me1, and H3K27me3
-
-
?
additional information
?
-
substrate specificity of Jhdm1b in vivo using HEK293 cells overexpressing the enzyme, overview
-
-
?
additional information
?
-
-
substrate specificity of Jhdm1b in vivo using HEK293 cells overexpressing the enzyme, overview
-
-
?
additional information
?
-
Jhdm1b, like its paralogue, JHDM1A, can specifically demethylate H3K36me2 and H3K36me1 histone substrates, but they are not active on methylated Lys4
-
-
?
additional information
?
-
-
Jhdm1b, like its paralogue, JHDM1A, can specifically demethylate H3K36me2 and H3K36me1 histone substrates, but they are not active on methylated Lys4
-
-
?
additional information
?
-
-
the enzyme is active on H3 trimethylated at K4 and dimethylated at K36, it might preferentially demethylate H3 trimethylated at K4 (EC 1.14.11.67)
-
-
?
additional information
?
-
-
histone methyl-lysine marks display dynamic changes during the parasite asexual erythrocytic cycle, suggesting that they constitute an important epigenetic mechanism of gene regulation in malaria parasites
-
-
?
additional information
?
-
-
the enzyme also demethylates [histone H3]-N6,N6-dimethyl-L-lysine36
-
-
?
additional information
?
-
-
the enzymealso demethylates [histone H3]-N6,N6-dimethyl-L-lysine9
-
-
?
additional information
?
-
-
Ndy1 is a physiological inhibitor of senescence in dividing cells and inhibition of senescence depends on histone H3 demethylation
-
-
?
additional information
?
-
no substrate: methyl-histone 3 L-lysine 4, histone 3 L-lysine 79
-
-
?
additional information
?
-
enzyme Jhd1 is also active on H3K9 methyl groups
-
-
?
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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
histone H3 N6,N6,N6-trimethyl-L-lysine26 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine26 + 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,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + 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
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + 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-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
predicted site-specificity from phylogenetic analysis
-
-
?
[histone H3]-N6-methyl-L-lysine 36 + 2-oxoglutarate + O2
[histone H3]-L-lysine 36 + 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,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,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
Jhdm1a is a histone demethylase that specifically demethylates dimethylated H3K36
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
KDM2b/JHDM1b is an H3K36me2-specific demethylase
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
Jhdm1a is a histone demethylase that specifically demethylates dimethylated H3K36
-
-
?
histone H3-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3-N6-methyl-L-lysine36 + succinate + formaldehyde + CO2
-
Jhdm1a is a histone demethylase that specifically demethylates dimethylated H3K36
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
Jhdm1a actively demethylates dimethylated H3K36 on the C/EBPalpha locus
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
-
-
-
?
protein C/EBPalpha-N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2
protein C/EBPalpha-N6-methyl-L-lysine + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
-
H3K36 demethylation activity of the fly dKDM4A is dramatically stimulated upon HP1a association
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
removal of histone H3 Lys36 dimethylation is coupled to histone H2A monoubiquitinylation, overview
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
the effect of Jhdm1b on cell proliferation and cellular senescence is mediated through de-repression of p15Ink4b as loss of p15Ink4b function rescues cell proliferation defects in Jhdm1b knockdown cells
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2-oxoglutarate + O2
[histone H3]-L-lysine36 + succinate + formaldehyde + CO2
-
predicted site-specificity from phylogenetic analysis
-
-
?
additional information
?
-
-
dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information
-
-
?
additional information
?
-
substrate specificity of Jhdm1b in vivo using HEK293 cells overexpressing the enzyme, overview
-
-
?
additional information
?
-
-
substrate specificity of Jhdm1b in vivo using HEK293 cells overexpressing the enzyme, overview
-
-
?
additional information
?
-
-
histone methyl-lysine marks display dynamic changes during the parasite asexual erythrocytic cycle, suggesting that they constitute an important epigenetic mechanism of gene regulation in malaria parasites
-
-
?
additional information
?
-
-
Ndy1 is a physiological inhibitor of senescence in dividing cells and inhibition of senescence depends on histone H3 demethylation
-
-
?
additional information
?
-
enzyme Jhd1 is also active on H3K9 methyl groups
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HP1a
-
H3K36 demethylation activity of the fly dKDM4A is dramatically stimulated upon HP1a association
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the mRNA expression of porcine JHDM1A is significantly higher in the middle at 65 days and later at 90 days period's embryo skeletal muscle than that of 33 days, and showed a ubiquitously expression but with the highest abundance in kidney, lung and liver of an adult pig
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isozyme KDM4C is associated with chromatin during mitosis, residue R919 on the proximal Tudor domains of KDM4C is critical for its association with chromatin during mitosis. KDM4C protein is localized to mitotic chromatin from prometaphase to telophase
brenda
additional information
additional information
the isozyme is not associated with chromatin during mitosis
-
brenda
additional information
the isozyme is not associated with chromatin during mitosis
-
brenda
additional information
the isozyme is not associated with chromatin during mitosis
-
brenda
additional information
the isozyme is not associated with chromatin during mitosis
-
brenda
additional information
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the isozyme is not associated with chromatin during mitosis
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
human JMJD2 (KDM4) H3K9 and H3K36 demethylases can be divided into members that act on both H3K9 and H3K36 and H3K9 alone, structural and phylogenetic analysis, overview. KDM4A/B/C act on both H3K9 and, less efficiently, on H3K36-methylated substrates, substrate selectivity of the human KDM4 histone demethylase subfamily, overview
evolution
two families of lysine demethylases (KDM) are identified. The KDM4 family consists of four members: KDM4A, KDM4B, KDM4C and KDM4D
malfunction
-
depletion of Kdm2b/Jhdm1b in hematopoietic progenitors significantly impairs Hoxa9/Meis1-induced leukemic transformation. In leukemic stem cells, knockdown of Kdm2b/Jhdm1b impairs their self-renewing capability in vitro and in vivo
malfunction
-
Jhdm1a knockdown mice are still able to maintain normal glycemia, but display higher glucose production upon injection of the gluconeogenic substrate pyruvate
malfunction
-
Jmjd5-/- embryos show severe growth retardation, resulting in embryonic lethality at the mid-gestation stage, Cdkn1a expression is upregulated in Jmjd5neo/neo MEFs and Jmjd5-/- embryos, which is responsible for the growth defects. phenotypes, overview. Jmjd5neo/neo hypomorphic mouse embryonic fibroblasts proliferate more slowly than wild-type
malfunction
-
silencing of Jhdm1a promotes liver glucose synthesis, while its exogenous expression reduces blood glucose level in vivo
malfunction
changes in RENT component recruitment at NTS regions due to loss of H3 methylases or demethylases
malfunction
dysregulated expression of KDM4A-D family promotes chromosomal instabilities
malfunction
dysregulated expression of KDM4A-D family promotes chromosomal instabilities. Depletion or overexpression of KDM4B does not leads to an increase in the frequency of abnormal mitotic cells and has no detectable effect on mitotic chromosome segregation
malfunction
dysregulated expression of KDM4A-D family promotes chromosomal instabilities. Depletion or overexpression of KDM4C, but not KDM4B, leads to over 3fold increase in the frequency of abnormal mitotic cells showing either misaligned chromosomes at metaphase, anaphase-telophase lagging chromosomes or anaphase-telophase bridges. Overexpression of a KDM4C demethylase dead mutant has no detectable effect on mitotic chromosome segregation
malfunction
-
Ndy1 knockdown by siRNA enhances sensitivity to oxidative stress, downregulation of Ndy1 activates the phosphorylation of AMPK, JNK, and p38MAPK and the cleavage of caspase-3 both before and after treatment with H2O2, Ndy1 overexpression protects cells against oxidative stress, overexpression of Ndy1 inhibits the phosphorylation of AMPK, JNK, and p38MAPK and the cleavage of caspase-3 both before and after treatment with H2O2. Knocking down Ndy1 sensitizes the cells to H2O2-induced oxidative stress. Genes Nqo1 and Prdx4 are direct Ndy1 targets. First, Ndy1 but not its DELTACXXC mutant binds specific regions in the promoters of both genes. Second, whereas Ndy1 upregulates their expression, the DELTACXXC mutant does not, suggesting that binding to the promoter region is necessary for their induction
malfunction
-
Jhdm1a knockdown mice are still able to maintain normal glycemia, but display higher glucose production upon injection of the gluconeogenic substrate pyruvate
-
metabolism
dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group gene silencing as a mode of histone crosstalk, the enzyme acts as part of the dRING-associated factor, dRAF, a Polycomb group silencing complex harboring also the histone H2A ubiquitin ligase dRING, Posterior sex combs and the F-box protein, overview. dRAF and PCR1 are separtate Polycomb group complexes, dKDM2 and PRC1 control overlapping transcriptomes, mechanisms, overview
metabolism
different roles of histone H3 methylases in regulating Net1/Sir2 recruitment to rDNA regions and the resultant rDNA silencing. In particular, both H3K4 and H3K79 methylation by Set1 and Dot1 positively regulate rDNA silencing, whereas H3K36 methylation by Set2 has the opposite effect
metabolism
-
Ndy1 epigenetically regulates several redox genes and the regulation of these genes by Ndy1 is responsible for the modulation of H2O2 levels and for the resistance of Ndy1-expressing cells to oxidative stress. Genes Nqo1 and Prdx4 are direct Ndy1 targets
physiological function
-
histone methyl-L-lysine marks display dynamic changes during the parasite asexual erythrocytic cycle, suggesting that they constitute an important epigenetic mechanism of gene regulation in malaria parasites
physiological function
-
histone methyl-lysine marks display dynamic changes during the parasite asexual erythrocytic cycle, suggesting that they constitute an important epigenetic mechanism of gene regulation in malaria parasites
physiological function
in vivo, the enzyme cooperates with Polycomb but antagonizes gene activation by particular trxG methyltransferases, gene dkdm2 is an enhancer of Polycomb but a suppressor of histone methyltransferases trx and ash1
physiological function
the H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b), Jhdm1b targets the p15Ink4b locus and regulates its expression in an enzymatic activity-dependent manner, overview
physiological function
-
JHDM1A plays an central role in gene silencing, cell cycle, cell growth and cancer development through histone H3K36 demethylation modification
physiological function
-
demethylation of H3K36 reduces DSB repair. Expression of JHDM1a decreases the association of early NHEJ repair components with an induced DSB and decreased DSB repair
physiological function
-
histone demethylase Jhdm1a regulates hepatic gluconeogenesis, regulation of gluconeogenesis by Jhdm1a requires its demethylation activity. Jhdm1a is a key negative regulator of gluconeogenic gene expression. Jhdm1a regulates the expression of a major gluconeogenic regulator, C/EBPalpha, by its USF1-dependent association with the C/EBPa promoter and its subsequent demethylation of dimethylated H3K36 on the C/EBPa lpha locus
physiological function
-
Jhdm1a has a physiological role in hepatic gluconeogenesis in vivo, and this role is mediated by its histone demethylation activity
physiological function
-
Jmjd5 is involved in the maintenance of H3K36me2 at the Cdkn1a locus
physiological function
-
Kdm2b/Jhdm1b functions as an oncogene and plays a critical role in leukemia development and maintenance, KDM2b/JHDM1b is required for initiation and maintenance of acute myeloid leukemia. Functions of Kdm2b/Jhdm1b are mediated by its silencing of p15Ink4b expression through active demethylation of histone H3-N6,N6-dimethyl-L-lysine. Kdm2b/Jhdm1b directly regulates p15Ink4b expression in leukemic cells
physiological function
changes in histone H3 lysine methylation levels distinctly regulate rDNA silencing by recruiting different silencing proteins to rDNA, thereby contributing to rDNA silencing and nucleolar organization in yeast. Jhd1 positively affects transcription
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4A is not associated with chromatin during mitosis, in contrast to isozyme KDM4C
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4B is not associated with chromatin during mitosis, in contrast to isozyme KDM4C
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4D is not associated with chromatin during mitosis, in contrast to isozyme KDM4C
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Unlike KDM4A-B, isozyme KDM4C is associated with chromatin during mitosis. This association is accompanied by a decrease in the mitotic levels of H3K9me3. The C-terminal region, containing the Tudor domains of KDM4C, is essential for its association with mitotic chromatin, especially residue R919 on the proximal Tudor domain of KDM4C is critical for its association with chromatin during mitosis. The demethylase activity and the mitotic localization of KDM4C influence the integrity of mitotic chromosome segregation
physiological function
-
the JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress. Ndy1 promotes the expression of genes encoding the antioxidant enzymes aminoadipic semialdehyde synthase (Aass), NAD(P)H quinone oxidoreductase-1 (Nqo1), peroxiredoxin-4 (Prdx4), and serine peptidase inhibitor b1b (Serpinb1b) and represses the expression of interleukin-19. At least two of these genes (Nqo1 and Prdx4) are regulated directly by Ndy1, which binds to specific sites within their promoters and demethylates promoter-associated histone H3 dimethylated at K36 and histone H3 trimethylated at K4. Simultaneous knockdown of Aass, Nqo1, Prdx4, and Serpinb1b in Ndy1-expressing cells to levels equivalent to those detected in control cells is sufficient to suppress the Ndy1 redox phenotype. The enzyme protects cells against oxidative stress by inhibiting reactive oxygen species-dependent signaling, overview. Ndy1 inhibits the oxidation of deoxyguanosine and DNA damage, and the accumulation of H2O2 in both H2O2-treated and untreated cells. Ndy1 enhances the antioxidant activity of cells. The gene Serpinb1b, upregulated by Ndy1, and gene IL-19, which is downregulated by Ndy1, play indirect roles in redox homeostasis, overview. Endogenous Ndy1 is a physiological redox regulator of the cellular response to oxidative stress. Ndy1 functions as an activator of transcription are in agreement with recently published data showing that Ndy1 promotes the transcriptional activation of the Hoxd1 gene. Ndy1 can also function as a repressor. Genes Nqo1 and Prdx4 are direct Ndy1 targets. First, Ndy1 but not its DELTACXXC mutant binds specific regions in the promoters of both genes. Second, whereas Ndy1 upregulates their expression, the DELTACXXC mutant does not, suggesting that binding to the promoter region is necessary for their induction
physiological function
JMJD5 has divalent cation-dependent protease activities that preferentially cleave the tails of histones 2, 3, or 4 containing methylated arginines. After the initial specific cleavage, JMJD5 acting as aminopeptidase, progressively digests the C-terminal products. JMJD5-deficient fibroblasts exhibit dramatically increased levels of methylated arginines and histones
physiological function
JMJD5 has divalent cation-dependent protease activities that preferentially cleave the tails of histones 2, 3, or 4 containing methylated arginines. After the initial specific cleavage, JMJD5 acting as aminopeptidase, progressively digests the C-terminal products. JMJD5-deficient fibroblasts exhibit dramatically increased levels of methylated arginines and histones. Depletion of JMJD7 in breast cancer cells greatly decreases cell proliferation
physiological function
-
Jhdm1a has a physiological role in hepatic gluconeogenesis in vivo, and this role is mediated by its histone demethylation activity
-
additional information
-
ectopic expression of Kdm2b/Jhdm1b is sufficient to transform hematopoietic progenitors
additional information
-
expression of the wild-type Jhdm1a, but not the H212A point mutant, decreased the expression of PEPCK and G6Pase in diabetic ob/ob mice
additional information
-
nuclear protein Jmjd5 or Kdm8 is a histone lysine demethylase that contains a JmjC domain in the C-terminal region
additional information
-
substrate selectivity is determined by multiple interactions within the catalytic domain but outside the active site, structural basis of sequence celectivity between KDM4 members, overview
additional information
substrate selectivity is determined by multiple interactions within the catalytic domain but outside the active site, structural basis of sequence celectivity between KDM4 members, overview
additional information
substrate selectivity is determined by multiple interactions within the catalytic domain but outside the active site, structural basis of sequence celectivity between KDM4 members, overview
additional information
-
expression of the wild-type Jhdm1a, but not the H212A point mutant, decreased the expression of PEPCK and G6Pase in diabetic ob/ob mice
-
Show AA Sequence and Transmembrane Helices (1618 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme domain structure includign JmjN, JmjC, PHD and Tudor domains, overview
additional information
enzyme domain structure includign JmjN, JmjC, PHD and Tudor domains, overview
additional information
enzyme domain structure includign JmjN, JmjC, PHD and Tudor domains, overview
additional information
enzyme domain structure includign JmjN, JmjC, PHD and Tudor domains, overview
additional information
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enzyme domain structure includign JmjN, JmjC, PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN and JmjC domains, isozyme KDM4D lacks the PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN and JmjC domains, isozyme KDM4D lacks the PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN and JmjC domains, isozyme KDM4D lacks the PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN and JmjC domains, isozyme KDM4D lacks the PHD and Tudor domains, overview
additional information
-
enzyme domain structure including JmjN and JmjC domains, isozyme KDM4D lacks the PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview
additional information
enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview
additional information
-
enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
H305A
additional information
additional information
-
Kdm2b/Jhmd1b is required for Hoxa9/Meis1-induced leukemic transformation in vitro
additional information
-
shRNA knockdown of Jhdm1a in Hep-G2 cells elevating gluconeogenic gene expression
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization
additional information
-
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences
additional information
-
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences
additional information
-
Jhdm1a knockdown or scramble adenoviruses are transduced into the liver of wild-type male C57BL/6J mice
additional information
-
Ndy1 knockdown by siRNA in fibroblasts. Significant reduction in K36-dimethylated histone H3 associated with the promoters of Nqo1 and Prdx4 genes in cells engineered to overexpress Ndy1 but not its CXXC deletion mutant. Trimethylation of histone H3 at K4 is also reduced in the promoter regions of both genes, though in a spatially restricted manner that spared the region near the transcription start site. But the effect of Ndy1 on histone H3K4 trimethylation is weak
additional information
-
Jhdm1a knockdown or scramble adenoviruses are transduced into the liver of wild-type male C57BL/6J mice
-
additional information
-
histone methyl-lysine marks display dynamic changes during the parasite asexual erythrocytic cycle, suggesting that they constitute an important epigenetic mechanism of gene regulation in malaria parasites
additional information
-
expression of histone demthylase Ndy1 in mouse embryo fibroblast results in immortalization in absence of replicative senescence via a JmjC domain-dependent process that targets the Rb and p53 pathways. Knockdown of endogenous Ndy1 or expression of JmjC domain mutants of Ndy1 promote senescence, suggesting that Ndy1 is a physiological inhibitor of senescence in dividing cells and that inhibition of senescence depends on histone H3 demethylation
additional information
overexpression results in moderate decrease in dimethyl-histone 3 L-lysine 36 and a slight decrease in trimethyl-histone 3 L-lysine 36 along with unaltered methyl-histone 3 L-lysine 36 levels. Deletion of the N-terminal PHD domain leads to about 50% decrease in activity. Deletion of C-terminal 125, 193, or 244 amino acids results in more than 90% loss of activity
additional information
generation of a jhd1DELTA deletion mutant, phenotype overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, chromosomal location and association analysis , the porcine JHDM1A gene encodes 1,162 amino acids and contains JmjC, F-box, and CXXC zinc-finger domains, which coding sequence and deduced protein shares 91 and 99% similarity with human JHDM1A, respectively
-
ectopic expression of either wild-type Jhdm1a or H212A point mutant in the liver of diabetic ob/ob mice
-
ectopic expression of Jhdm1a in HeLa and wild-type and enzyme-deficient Hep-G2 cells via lentivirus transfection
-
expression analysis by quantitative reverse transcriptase PCR, overexpression of wild-type Jhdm1b in HeLa and HEK293 cells
gene Jmjd5, FLAG-His6 tagged mutant H319A is cloned into the pDON-5 Neo plasmid to produce retroviruses, shRNA-expressing retroviruses are used for silencing of the enzyme, expression of C-terminally His-tagged JMJD5 in Escherichia coli, quantitative reverse transcription PCR expression analysis
-
gene KDM4A, recombinant expression of EGFP-tagged full-length and truncated enzymes versions
gene KDM4B, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4B
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, andmutant enzymes versions
gene KDM4D is Y chromosome encoded and a truncated enzyme variant compared to KDM4A-C
gene MAL8P1.111, located on chromosome 8, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis, overview
-
gene PFF1440w, located on chromosome 6, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis, overview
-
recombinant Ndy1 overexpression in mouse embryonic fibroblasts, quantitative real-time reverse transcriptase PCR expression analysis
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
knockdown of Jhdm1b in primary mouse embryonic fibroblasts inhibits cell proliferation and induces cellular senescence in a pRb and p53 pathway-dependent manner. The effect of Jhdm1b on cell proliferation and cellular senescence is mediated through de-repression of p15Ink4b as loss of p15Ink4b function rescues cell proliferation defects in Jhdm1b knockdown cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsukada, Y.; Fang, J.; Erdjument-Bromage, H.; Warren, M.E.; Borchers, C.H.; Tempst, P.; Zhang, Y.
Histone demethylation by a family of JmjC domain-containing proteins
Nature
439
811-816
2006
Saccharomyces cerevisiae, Homo sapiens
brenda
Fang, J.; Hogan, G.J.; Liang, G.; Lieb, J.D.; Zhang, Y.
The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2
Mol. Cell. Biol.
27
5055-5065
2007
Saccharomyces cerevisiae (P40034)
brenda
Pfau, R.; Tzatsos, A.; Kampranis, S.C.; Serebrennikova, O.B.; Bear, S.E.; Tsichlis, P.N.
Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process
Proc. Natl. Acad. Sci. USA
105
1907-1912
2008
Rattus norvegicus
brenda
Lagarou, A.; Mohd-Sarip, A.; Moshkin, Y.; Chalkley, G.; Bezstarosti, K.; Demmers, J.; Verrijzer, C.
dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing
Genes Dev.
22
2799-2810
2008
Drosophila melanogaster (Q9VHH9)
brenda
Cui, L.; Fan, Q.; Cui, L.; Miao, J.
Histone lysine methyltransferases and demethylases in Plasmodium falciparum
Int. J. Parasitol.
38
1083-1097
2008
Plasmodium falciparum
brenda
He, J.; Kallin, E.M.; Tsukada, Y.; Zhang, Y.
The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b)
Nat. Struct. Mol. Biol.
15
1169-1175
2008
Mus musculus (Q6P1G2), Mus musculus
brenda
Lan, F.; Shi, Y.
Epigenetic regulation: methylation of histone and non-histone proteins
Sci. China C Life Sci.
52
311-322
2009
Drosophila melanogaster
brenda
Peng, Y.B.; Fan, B.; Han, X.L.; Xu, X.W.; Rothschild, M.F.; Yerle, M.; Liu, B.
Molecular characterization of the porcine JHDM1A gene associated with average daily gain: evaluation its role in skeletal muscle development and growth
Mol. Biol. Rep.
38
4697-4704
2011
Sus scrofa
brenda
He, J.; Nguyen, A.T.; Zhang, Y.
KDM2b/JHDM1b, an H3K36me2-specific demethylase, is required for initiation and maintenance of acute myeloid leukemia
Blood
117
3869-3880
2011
Homo sapiens
brenda
Ishimura, A.; Minehata, K.; Terashima, M.; Kondoh, G.; Hara, T.; Suzuki, T.
Jmjd5, an H3K36me2 histone demethylase, modulates embryonic cell proliferation through the regulation of Cdkn1a expression
Development
139
749-759
2012
Mus musculus
brenda
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, Homo sapiens (O75164), Homo sapiens (Q9H3R0)
brenda
Pan, D.; Mao, C.; Zou, T.; Yao, A.Y.; Cooper, M.P.; Boyartchuk, V.; Wang, Y.X.
The histone demethylase Jhdm1a regulates hepatic gluconeogenesis
PLoS Genet.
8
e1002761
2012
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
brenda
Fnu, S.; Williamson, E.; De Haro, L.; Brenneman, M.; Wray, J.; Shaheen, M.; Radhakrishnan, K.; Lee, S.; Nickoloff, J.; Hromas, R.
Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining
Proc. Natl. Acad. Sci. USA
108
540-545
2011
Homo sapiens
brenda
Ryu, H.; Ahn, S.
Yeast histone H3 lysine 4 demethylase Jhd2 regulates mitotic ribosomal DNA condensation
BMC Biol.
12
75
2014
Saccharomyces cerevisiae (P40034)
brenda
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 (Q6B0I6), Homo sapiens (Q9H3R0), Homo sapiens
brenda
Liu, H.; Wang, C.; Lee, S.; Deng, Y.; Wither, M.; Oh, S.; Ning, F.; Dege, C.; Zhang, Q.; Liu, X.; Johnson, A.M.; Zang, J.; Chen, Z.; Janknecht, R.; Hansen, K.; Marrack, P.; Li, C.Y.; Kappler, J.W.; Hagman, J.; Zhang, G.
Clipping of arginine-methylated histone tails by JMJD5 and JMJD7
Proc. Natl. Acad. Sci. USA
114
E7717-E7726
2017
Homo sapiens (P0C870), Homo sapiens (Q8N371)
brenda
Polytarchou, C.; Pfau, R.; Hatziapostolou, M.; Tsichlis, P.
The JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress
Mol. Cell. Biol.
28
7451-7464
2008
Mus musculus
brenda
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