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Information on EC 1.14.11.67 - [histone H3]-trimethyl-L-lysine4 demethylase and Organism(s) Homo sapiens and UniProt Accession O75164
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1.14.11.67 [histone H3]-trimethyl-L-lysine4 demethylaseIUBMB Comments
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 4 of histone H3 (H3K4). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri-, di-, and mono-methylated forms.
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Word Map
- 1.14.11.67
- chromatin
- demethylases
-
trimethylation
-
polycomb
-
x-linked
-
pluripotency
-
ccrcc
- methyltransferases
-
intellectual
-
self-renewal
-
corepressors
-
h3k4me2
-
chip-seq
-
x-inactivation
-
histone-modifying
- corest
- prc1
-
chromatin-modifying
- lys4
-
nanog
-
k-specific
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
kdm5b, jarid2, kdm5c, jarid1b, kdm5a, fbxl10, lysine-specific demethylase, jarid1c, jarid1a, kdm5d, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H3K4 demethylase
H3K4me3 demethylase
histone H3 lysine 4 demethylase
histone H3K4 demethylase
JARID1B
JARID1C
KDM5A
KDM5B
KDM5C
PLU-1
PLU1
RBP2
SMCX
SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6,N6-trimethyl-L-lysine4,2-oxoglutarate:oxygen oxidoreductase
Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 4 of histone H3 (H3K4). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri-, di-, and mono-methylated forms.
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
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[acetylated histone H3 21mer]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3 N-terminal 13mer] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 13mer] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 18mer mutant K14A/R17A/K18A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 18mer mutant K14A/R17A/K18A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 18mer mutant K14ac/K18ac] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 18mer mutant K14ac/K18ac] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 18mer] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 18mer] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant K9A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant K9A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant Q5A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant Q5A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant R2A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant R2A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant R8A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant R8A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant T3A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T3A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant T6A] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T6A] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant T6S] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T6S] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer mutant T6V] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer mutant T6V] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3 N-terminal 21mer] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 N-terminal 21mer] N-terminal N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3] N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3] N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
H3 residue Q5 is critical for substrate recognition by KDM5A
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
overall reaction
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-drimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone-H3]-dimethyllysine4 + 2-oxoglutarate + O2
?
-
recombinant PLU-1 can only demethylate H3K4me3 and H3K4me2 when analyzed in vitro
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
JMJD2A has the unique property of binding trimethylated peptides from histone sequences, H3K4me3 through itstandem hybrid tudor domains. JMJD2A Asp945 and Asp940 interact with Arg2 of the H3K4me3 peptide, but not with H4K20me3. Asn940 forms hydrogen bonds with the backbone amide and hydroxyl groups of H3K4me3 Thr3
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
overall reaction
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
recruitment of RBP2 to the promoter region of a key mitochondrial component results in demethylation of H3K4 at this promoter and its transcriptional repression
-
-
?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
RNA-interference-mediated depletion of SMCX increases H3K4 trimethylation at the sodium channel type 2A (SCN2A) and synapsin I (SYN1) promoters. SMCX activity impairs REST-mediated neuronal gene regulation, thereby contributing to SMCX-associated X-linked mental retardation
-
-
?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
-
recombinant PLU-1 can only demethylate H3K4me3 and H3K4me2 when analyzed in vitro
-
-
?
additional information
?
-
JMJD2A also demethylates histone H3 dimethylated or trimethylated at lysine 9 and lysine 36, by means of an N-terminal catalytic domain, as well as peptides from H4K20me3, recognized through its tudor domains. The hybrid tudor domains at the C terminus of JMJD2A are necessary for the demethylation activity of JMJD2A in vivo. H3K4me3 and H4K20me3 are recognized with similar affinities by JMJD2A, binding structures, overview. Two other amino acids of JMJD2A, Tyr942 and Thr968, involved in weaker intermolecular hydrogen bonds, selectively contact one peptide and not the other. The hydroxyl group of Thr968 in the wild-type structure forms a hydrogen bond with the guanido group of H4K20me3 Arg23 but does not contact H3K4me3. Tyr942 and Thr968 are not essential for the tight binding of JMJD2A to H3K4me3 and H4K20me3
-
-
?
additional information
?
-
-
RB-binding protein 2, RBP2, is a key effector for retinoblastoma protein mediating cell-cycle withdrawal and differentiation by interacting with a variety of proteins. During differentiation, RBP2 exerts inhibitory effects on multiple genes through direct interaction with their promoters. RBP2 shows high correlation with the presence of H3K4me3, and its target genes are separated into two functionally distinct classes: differentiation-independent and differentiation-dependent genes. Molecular mechanisms of RBP2 regulation of differentiation, overview. Functional analysis of RBP2 target genes and differentially expressed genes, overview
-
-
?
additional information
?
-
-
the enzyme interacts with the C-terminus of hPc2, a Polycomb group PcG protein, via its N-terminus in vitro and in vivo, role for hPc2 acting as a transcriptional co-repressor, interaction analysis, overview
-
-
?
additional information
?
-
KDM5A, a histone H3K4 demethylase, physically interacts with the nucleosome remodeling and deacetylase (NuRD) complex
-
-
?
additional information
?
-
KDM5B associates with the deacetylase NuRD complex
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
-
the enzyme is physically associated with the MLL2 complex in vivo
-
-
-
additional information
?
-
-
the enzyme does not demethylate [histone H3]-N6-methyl-L-lysine4
-
-
-
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-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-N6-methyl-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
overall reaction
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
[histone H3]-N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
[histone H3]-N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone H3]-N6,N6-drimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
[histone-H3]-trimethyllysine4 + 2-oxoglutarate + O2
?
RNA-interference-mediated depletion of SMCX increases H3K4 trimethylation at the sodium channel type 2A (SCN2A) and synapsin I (SYN1) promoters. SMCX activity impairs REST-mediated neuronal gene regulation, thereby contributing to SMCX-associated X-linked mental retardation
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
overall reaction
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
recruitment of RBP2 to the promoter region of a key mitochondrial component results in demethylation of H3K4 at this promoter and its transcriptional repression
-
-
?
additional information
?
-
-
RB-binding protein 2, RBP2, is a key effector for retinoblastoma protein mediating cell-cycle withdrawal and differentiation by interacting with a variety of proteins. During differentiation, RBP2 exerts inhibitory effects on multiple genes through direct interaction with their promoters. RBP2 shows high correlation with the presence of H3K4me3, and its target genes are separated into two functionally distinct classes: differentiation-independent and differentiation-dependent genes. Molecular mechanisms of RBP2 regulation of differentiation, overview. Functional analysis of RBP2 target genes and differentially expressed genes, overview
-
-
?
additional information
?
-
-
the enzyme interacts with the C-terminus of hPc2, a Polycomb group PcG protein, via its N-terminus in vitro and in vivo, role for hPc2 acting as a transcriptional co-repressor, interaction analysis, overview
-
-
?
additional information
?
-
KDM5A, a histone H3K4 demethylase, physically interacts with the nucleosome remodeling and deacetylase (NuRD) complex
-
-
?
additional information
?
-
KDM5B associates with the deacetylase NuRD complex
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
no activity with histone H3 N6-dimethyl-L-lysine4
-
-
?
additional information
?
-
-
the enzyme is physically associated with the MLL2 complex in vivo
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3-phenyl-1-(p-tolyl)-1H-pyrazol-4-yl)(4-(2-(pyrrolidin-1-yl) ethyl)piperazin-1-yl) methanone
-
-
(E)-2-((3-(4-(dimethylamino)but-2-enamido)-phenyl)(2-(piperidin-1-yl)ethoxy)methyl)thieno[3,2-b]pyridine-7-carboxylic acid
-
-
(R)-2-(1-(1-benzoylpiperidin-3-yl)-1H-1,2,3-triazol-4-yl)isonicotinic acid
-
1-(2-methoxyphenyl)-N-(2-methyl-2-morpholinopropyl)-3-phenyl-1H-pyrazole-4-carboxamide
-
-
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-(4-methoxyphenyl)-N-(2-methyl-2-morpholinopropyl)-3-phenyl-1H-pyrazole-4-carboxamide
compound is a cellular active KDM5B inhibitor that can inhibit MKN45 cell proliferation, wound healing and migration. The compound can bind and stabilize KDM5B and induce the accumulation of H3K4me2/3
-
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)-N-ethylisonicotinamide
-
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)-N-methylisonicotinamide
-
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinic acid
-
2-((2-chlorophenyl)(2-(1-methylpyrrolidin-2-yl)-ethoxy)methyl)thieno[3,2-b]pyridine-7-carboxylic acid
-
-
2-((3-aminophenyl)(2-(piperidin-1-yl)ethoxy)methyl)thieno[3,2-b]-pyridine-7-carboxylic acid
-
2-oxoglutarate-competitive inhibition
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-(pyridin-2-yl)-6-(4-(vinylsulfonyl)-1,4-diazepan-1-yl)pyrimidin-4-yl)amino)propanoic acid
-
-
3-((6-(4-acryloyl-1,4-diazepan-1-yl)-2-(pyridin-2-yl)-pyrimidin-4-yl)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
-
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-(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
-
ethyl 1-[3-[(4-methoxybenzene-1-sulfonyl)amino]benzoyl]prolinate
upon treatment with 30 microM, a strong increase of cells in G2/M and of the subG1 fraction is noted
-
ethyl 2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinate
-
ethyl 2-([(2-([2-(dimethylamino)ethyl](ethyl)amino)-2-oxoethyl)amino]methyl)pyridine-4-carboxylate
-
KDM5-C70
ethyl 2-[3-[(4-methoxybenzene-1-sulfonyl)amino]benzoyl]benzoate
compound can selectively inhibit KDM5 enzymes and is capable of increasing sensitivity of breast cancer cells to ionizing radiation and radiation-induced damage. The compound does not show any significant effect on cell cycle
-
JIB 04
inhibitor is active against native and temozolomide-resistant glioblastoma cells. GSK J4, inhibitor of lysine demethylase KDM6B, EC 1.14.11.68, and JIB 04 strongly synergize and are a potent combination against temozolomide-resistant glioblastoma cells
-
N-[2-(pyridin-2-yl)-6-(1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl)pyrimidin-4-yl]-beta-alanine
-
GSK-J1
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide
-
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide
the potent and selective KDM5A-D inhibitor stops cellular demethylation of H3K4me3 at transcription start sites and proliferation of MM1S myeloma cells
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide
the potent and selective KDM5A-D inhibitor stops cellular demethylation of H3K4me3 at transcription start sites and proliferation of MM1S myeloma cells. Analysis of enzyme-inhibitor binding structure from crystal structure analysis, overview
2-(piperazin-1-ylmethyl)isonicotinic acid
the potent and selective KDM5A-D inhibitor stops cellular demethylation of H3K4me3 at transcription start sites and proliferation of MM1S myeloma cells
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-dichlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
substitution from C4 of the pyrazole moiety allows access to the histone peptide substrate binding site, incorporation of a conformationally constrained 4-phenylpiperidine linker gives derivatives such as 8-(4-(2-(4-(3-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one which demonstrates equipotent activity versus the KDM4 (JMJD2) and KDM5 (JARID1) subfamily demethylases, selectivity over representative exemplars of the KDM2, KDM3, and KDM6 subfamilies, and cellular permeability in the Caco-2 assay
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-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
substitution from C4 of the pyrazole moiety allows access to the histone peptide substrate binding site, incorporation of a conformationally constrained 4-phenylpiperidine linker gives derivatives such as 8-(4-(2-(4-(3-chlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one which demonstrates equipotent activity versus the KDM4 (JMJD2) and KDM5 (JARID1) subfamily demethylases, selectivity over representative exemplars of the KDM2, KDM3, and KDM6 subfamilies, cellular permeability in the Caco-2 assay, and inhibition of H3K9Me3 and H3K4Me3 demethylation in a cell-based assay
Cd2+
at 0.001-0.005 mM, cadmium increases global histone H3 methylation, H3K4me3 and H3K9me2, by inhibiting the activities of histone demethylases, and aberrant histone methylation that occurs early (48 h) and at 4 weeks is associated with cadmium-induced transformation of BEAS-2B cells at the early stage
Cd2+
at 0.001-0.005 mM, cadmium induces histone H3 lysine methylation by inhibiting histone demethylase activity on H3K4 and H3K9. Cadmium increases global histone H3 methylation, H3K4me3 and H3K9me2, by inhibiting the activities of histone demethylases, and aberrant histone methylation that occurs early (48 h) and at 4 weeks is associated with cadmium-induced transformation of BEAS-2B cells at the early stage
GSK-J1
a selective inhibitor of the KDM6/KDM5 subfamilies. Docking study and identification of critical residues for binding of the inhibitor to the reconstituted KDM5 Jumonji domain
GSK-J1
a selective inhibitor of the KDM6/KDM5 subfamilies. Docking study and identification of critical residues for binding of the inhibitor to the reconstituted KDM5 Jumonji domain. GSK-J1 inhibits the demethylase activity of KDM5C with 8.5fold increased potency compared with that of KDM5B at 1 mM 2-oxoglutarate. Also inhibits the enzyme mutant KDM5BDELTAAP
GSK-J1
a selective inhibitor of the KDM6/KDM5 subfamilies. Docking study and identification of critical residues for binding of the inhibitor to the reconstituted KDM5 Jumonji domain. GSK-J1 inhibits the demethylase activity of KDM5C with 8.5fold increased potency compared with that of KDM5B at 1 mM 2-oxoglutarate. Also inhibits the enzyme mutant KDM5CDELTAAP
JIB-04
a pan-inhibitor of the Jumonji demethylase superfamily
JIB-04
a pan-inhibitor of the Jumonji demethylase superfamily, that is about 8fold more potent against KDM5B than against KDM5C. Also inhibits the enzyme mutant KDM5BDELTAAP
JIB-04
a pan-inhibitor of the Jumonji demethylase superfamily, that is about 8fold more potent against KDM5B than against KDM5C. Also inhibits the enzyme mutant KDM5CDELTAAP
KDOAM-25
inhibits KDM5 enzymes in vitro with IC50 below 100 nM. In MCF-7 cells, it induces an increase of H3K4me3 levels at 0.03-1 microM. The compound does not show any significant effect on cell cycle
additional information
discovery and synthesis of N-substituted 4-(pyridin-2-yl)thiazole-2-amine derivatives and their subsequent optimization, guided by structure-based design, to give 8-(1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-ones, a series of potent JmjC histone N-methyl lysine demethylase (KDM) inhibitors which bind to Fe(II) in the active site. No inhibition by 4-(pyridin-2-yl)thiazol-2-amine
-
additional information
discovery and synthesis of N-substituted 4-(pyridin-2-yl)thiazole-2-amine derivatives and their subsequent optimization, guided by structure-based design, to give 8-(1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-ones, a series of potent JmjC histone N-methyl lysine demethylase (KDM) inhibitors which bind to Fe(II) in the active site. No inhibition by 4-(pyridin-2-yl)thiazol-2-amine
-
additional information
discovery and synthesis of N-substituted 4-(pyridin-2-yl)thiazole-2-amine derivatives and their subsequent optimization, guided by structure-based design, to give 8-(1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-ones, a series of potent JmjC histone N-methyl lysine demethylase (KDM) inhibitors which bind to Fe(II) in the active site. No inhibition by 4-(pyridin-2-yl)thiazol-2-amine, 4-((methyl((1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)methyl)amino)methyl)benzonitrile, and 4-((methyl(2-(1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)ethyl)amino)methyl)benzonitrile, poor inhibition by 8-((4-phenylpiperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
additional information
discovery and synthesis of N-substituted 4-(pyridin-2-yl)thiazole-2-amine derivatives and their subsequent optimization, guided by structure-based design, to give 8-(1H-pyrazol-3-yl)pyrido[3,4-d]pyrimidin-4(3H)-ones, a series of potent JmjC histone N-methyl lysine demethylase (KDM) inhibitors which bind to Fe(II) in the active site. No inhibition by 4-(pyridin-2-yl)thiazol-2-amine, 4-((methyl((1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)methyl)amino)methyl)benzonitrile, and 4-((methyl(2-(1-(4-oxo-3,4-dihydropyrido[3,4-d]pyrimidin-8-yl)-1H-pyrazol-4-yl)ethyl)amino)methyl)benzonitrile, poor inhibition by 8-((4-phenylpiperazin-1-yl)methyl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
additional information
structural characterization of the linked JmjN-JmjC domain for the KDM5 family for the design of KDM5 demethylase inhibitors with improved potency and selectivity
-
additional information
structural characterization of the linked JmjN-JmjC domain for the KDM5 family for the design of KDM5 demethylase inhibitors with improved potency and selectivity
-
additional information
structural characterization of the linked JmjN-JmjC domain for the KDM5 family for the design of KDM5 demethylase inhibitors with improved potency and selectivity
-
additional information
structural characterization of the linked JmjN-JmjC domain for the KDM5 family for the design of KDM5 demethylase inhibitors with improved potency and selectivity, hypothetical modeling of the N-terminal half of KDM5, overview
-
additional information
structural characterization of the linked JmjN-JmjC domain for the KDM5 family for the design of KDM5 demethylase inhibitors with improved potency and selectivity, hypothetical modeling of the N-terminal half of KDM5, overview
-
additional information
structural characterization of the linked JmjN-JmjC domain for the KDM5 family for the design of KDM5 demethylase inhibitors with improved potency and selectivity, hypothetical modeling of the N-terminal half of KDM5, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
histone H3
-
the in vitro demethylase activity of the enzyme is allosterically enhanced by binding of its product, unmodified histone H3 peptides, to its PHD1 reader domain
-
additional information
interleukin-1beta enhances recruitment of LSD1 to mPGES-1 promoter
-
additional information
-
interleukin-1beta enhances recruitment of LSD1 to mPGES-1 promoter
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.489
[histone H3 N-terminal 13mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.514
[histone H3 N-terminal 18mer mutant K14A/R17A/K18A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.249
[histone H3 N-terminal 18mer mutant K14ac/K18ac] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0623
[histone H3 N-terminal 18mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0219
[histone H3 N-terminal 21mer mutant K9A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.4152
[histone H3 N-terminal 21mer mutant Q5A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.1536
[histone H3 N-terminal 21mer mutant R2A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0551
[histone H3 N-terminal 21mer mutant R8A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.009
[histone H3 N-terminal 21mer mutant T3A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0965
[histone H3 N-terminal 21mer mutant T6A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0147
[histone H3 N-terminal 21mer mutant T6S] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0394
[histone H3 N-terminal 21mer mutant T6V] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0125
[histone H3 N-terminal 21mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.0168
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
in the presence of 0.038 mM unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.0955
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
in the absence of unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.0547
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4
-
in the presence of 0.038 mM unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.229
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4
-
in the absence of unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
additional information
additional information
Kd values for H3K4me3 peptide with wild-type and mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics of wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.111
[histone H3 N-terminal 13mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.108
[histone H3 N-terminal 18mer mutant K14A/R17A/K18A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.101
[histone H3 N-terminal 18mer mutant K14ac/K18ac] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.078
[histone H3 N-terminal 18mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.061
[histone H3 N-terminal 21mer mutant K9A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.056
[histone H3 N-terminal 21mer mutant Q5A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.069
[histone H3 N-terminal 21mer mutant R2A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.054
[histone H3 N-terminal 21mer mutant R8A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.056
[histone H3 N-terminal 21mer mutant T3A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.075
[histone H3 N-terminal 21mer mutant T6A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.07
[histone H3 N-terminal 21mer mutant T6S] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.05
[histone H3 N-terminal 21mer mutant T6V] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.052
[histone H3 N-terminal 21mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.041
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
in the presence of 0.038 mM unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.047
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
in the absence of unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.023
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4
-
in the absence of unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.023
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4
-
in the presence of 0.038 mM unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.228
[histone H3 N-terminal 13mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.211
[histone H3 N-terminal 18mer mutant K14A/R17A/K18A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.405
[histone H3 N-terminal 18mer mutant K14ac/K18ac] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
1.249
[histone H3 N-terminal 18mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
2.791
[histone H3 N-terminal 21mer mutant K9A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.134
[histone H3 N-terminal 21mer mutant Q5A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.452
[histone H3 N-terminal 21mer mutant R2A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.981
[histone H3 N-terminal 21mer mutant R8A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
6.232
[histone H3 N-terminal 21mer mutant T3A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.773
[histone H3 N-terminal 21mer mutant T6A] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
4.756
[histone H3 N-terminal 21mer mutant T6S] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
1.259
[histone H3 N-terminal 21mer mutant T6V] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
4.126
[histone H3 N-terminal 21mer] N6,N6,N6-trimethyl-L-lysine4
pH not specified in the publication, temperature not specified in the publication
-
0.49
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
in the absence of unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
2.43
[acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4
-
in the presence of 0.038 mM unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.098
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4
-
in the absence of unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
0.43
[acetylated histone H3 21mer]-N6,N6-dimethyl-L-lysine4
-
in the presence of 0.038 mM unmodified histone H3 10mer peptide, at pH 7.5 and 25°C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000073
(3-phenyl-1-(p-tolyl)-1H-pyrazol-4-yl)(4-(2-(pyrrolidin-1-yl) ethyl)piperazin-1-yl) methanone
Homo sapiens
pH 7.5, temperature not specified in the publication
-
0.00022
(E)-2-((3-(4-(dimethylamino)but-2-enamido)-phenyl)(2-(piperidin-1-yl)ethoxy)methyl)thieno[3,2-b]pyridine-7-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000093
1-(2-methoxyphenyl)-N-(2-methyl-2-morpholinopropyl)-3-phenyl-1H-pyrazole-4-carboxamide
Homo sapiens
pH 7.5, temperature not specified in the publication
-
0.000024
1-(4-methoxyphenyl)-N-(2-methyl-2-morpholinopropyl)-3-phenyl-1H-pyrazole-4-carboxamide
Homo sapiens
pH 7.5, temperature not specified in the publication
-
0.000098
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)-N-ethylisonicotinamide
Homo sapiens
pH and temperature not specified in the publication
0.00027
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)-N-methylisonicotinamide
Homo sapiens
pH and temperature not specified in the publication
0.000019 - 0.000071
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide
0.000007
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinic acid
Homo sapiens
pH and temperature not specified in the publication
0.00032
2-((2-chlorophenyl)(2-(1-methylpyrrolidin-2-yl)-ethoxy)methyl)thieno[3,2-b]pyridine-7-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00049
2-((3-aminophenyl)(2-(piperidin-1-yl)ethoxy)methyl)thieno[3,2-b]-pyridine-7-carboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00098
2-(piperazin-1-ylmethyl)isonicotinic acid
Homo sapiens
pH and temperature not specified in the publication
0.083
3-((2-(pyridin-2-yl)-6-(4-(vinylsulfonyl)-1,4-diazepan-1-yl)pyrimidin-4-yl)amino)propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.071
3-((6-(4-acryloyl-1,4-diazepan-1-yl)-2-(pyridin-2-yl)-pyrimidin-4-yl)amino)propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000048
ethyl 2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinate
Homo sapiens
pH and temperature not specified in the publication
0.11
N-[2-(pyridin-2-yl)-6-(1,2,4,5-tetrahydro-3H-3-benzazepin-3-yl)pyrimidin-4-yl]-beta-alanine
Homo sapiens
-
pH and temperature not specified in the publication
0.000019
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide
Homo sapiens
pH and temperature not specified in the publication
0.000069
2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide
Homo sapiens
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
histone H3 lysine 4 demethylase JARID1B is up-regulated in prostate cancer. JARID1B associates with androgen receptor and regulates its transcriptional activity
additional information
the expression level of KDM5B is significantly lower in breast cancer estrogen receptor lacking ER- cells compared to ER+ cells, e.g. lower expression levels of KDM5B in the triple-negative breast cancer patients compared with patients with the ER+/PR+ subtype
-
PLU-1-mediated H3K4 demethylase activity plays an important role in the proliferative capacity of breast cancer cells through repression of tumor suppressor genes, including BRCA1
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
KDM5B colocalizes with HDAC1 and CHD4 at chromatin in K-562 cells
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
KDM5C is a member of the evolutionarily conserved KDM5 family of four proteins, KDM5A/B/C and D. KDM5A/C/D demethylate tri- and di-methylated forms of H3K4, whereas KDM5B is capable of demethylating all three forms (tri-, di-, and mono) of H3K4 methylation
evolution
the enzyme belongs to the superfamily of flavin adenine dinucleotide (FAD)-dependent amine oxidases
evolution
the enzyme blongs to the KDM5/JARID1 subfamily of histone H3 lysine 4 demethylases of the Fe(II)- and 2-oxoglutarate-dependent demethylases family. The KDM5 family is unique among the Jumonji domain-containing histone demethylases in that there is an atypical insertion of a DNA-binding ARID domain and a histone-binding PHD domain into the Jumonji domain, which separates the catalytic domain into two fragments (JmjN and JmjC)
malfunction
-
mutations in the X-linked KDM5C gene, encoding a histone H3 lysine 4 demethylase, lading to significant loss of DNA methylation in blood of males with intellectual disability, especially loss of DNA methylation at the promoters of the three top candidate genes FBXL5, SCMH1, CACYBP. Mutant clinical features most consistently reported in males with mutations include mild to severe intellectual disability, epilepsy, short stature, hyperreflexia, aggressive behavior and microcephaly, phenotypes, overview. Significant loss of DNA methylation at specific genomic loci in blood samples of male patients carrying KDM5C mutations, suggesting these genes are epigenetic targets of KDM5C
malfunction
423 genes are upregulated and 333 genes are downregulated in KDM5B knockdown MDA-MB 231 cells, downregulated genes in KDM5B knockdown cells do not cluster. The expression of the KDM5B-dependent genes is validated by quantitative real-time PCR. The PHD1 finger mutants may act as dominant-negative mutants, altering the dynamics and interactions of endogenous KDM5B. In contrast, the W1502A mutant of PHD3 that is defective in H3K4me3 binding shows an inhibitory effect oncell migration similar to the effect of the wild-type protein
malfunction
both pharmacological inhibition of LSD1 and small interfering RNA (siRNA) knockdown prevents interleukin 1beta-induced H3K9 demethylation at the mPGES-1 promoter as well as concomitant mPGES-1 protein expression. The level of LSD1 expression is elevated in osteoarthritis cartilage
malfunction
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes
malfunction
multiple myeloma MM1S cells treated with inhibitor 2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide show increased global H3K4 methylation at transcriptional start sites and impaired proliferation. Inhibitor 2-(((2-((2-(dimethylamino)ethyl)(ethyl)amino)-2-oxoethyl)amino)methyl)isonicotinamide increases H3K4me3 levels in HeLa cells
malfunction
multiple myeloma MM1S cells treated with inhibitor KDOAM-25 show increased global H3K4 methylation at transcriptional start sites and impaired proliferation. Inhibitor KDOAM-25 increases H3K4me3 levels in HeLa cells
malfunction
multiple myeloma MM1S cells treated with inhibitor KDOAM-25 show increased global H3K4 methylation at transcriptional start sites and impaired proliferation. Inhibitor KDOAM-25 increases H3K4me3 levels in HeLa cells. Increased KDM5B expression is associated with shorter survival in myeloma patients and ex vivo inhibition with KDOAM-25 results in cell-cycle arrest
malfunction
-
enzyme depletion impairs the estrogen-induced G1/S transition of the cell cycle in vitro and inhibits breast tumorigenesis in vivo
metabolism
KDM5B associates with the deacetylase NuRD complex, i.e. with two catalytic subunits of the NuRD complex. One subunit is a chromodomain helicase DNA binding protein 4 (CHD4) ATPase, which hydrolyses ATP necessary for DNA sliding and repositioning of nucleosomes. The second catalytic subunit is histone deacetylase 1 (HDAC1), which deacetylates acetylated lysine residues of histones. KDM5B is recruited to about 140000 genomic regions, and 76268 of these regions overlap with the regions occupied by HDAC1. About 50% of the KDM5B-HDAC1 binding sites overlap with tri-, di-, or monomethylated H3K4 (H3K4me3/2/1), which are substrates for the KDM5B enzymatic activity
metabolism
the protein-protein interactions between KDM5A and the histone H3 tail extend beyond the amino acids proximal to the substrate mark. Deletion or mutation of residues at positions 14-18 on the H3 tail results in an 8fold increase in the KMapp value, compared to wild-type 18mer peptide. Post-translational modifications on this distal epitope can modulate KDM5A-dependent demethylation
physiological function
-
role of RBP2 in mitochondrial biogenesis, which involves regulation of H3K4me3-modified nucleosomes
physiological function
-
JARID1B act as transcriptional repressor, with hPc2 acting as a transcriptional co-repressor, overview
physiological function
-
The KDM5C protein is likely to play a role not only in intellectual disability but also in sex-specific differences in brain function, parallel sex-specific DNA methylation profiles in brain samples from control males and females were observed at FBXL5 and CACYBP
physiological function
histone H3K4 methylation is linked to transcriptional activation. KDM5A, a histone H3K4 demethylase, physically interacts with the nucleosome remodeling and deacetylase (NuRD) complex, KDM5A and the NuRD complex cooperatively function to control developmentally regulated genes, and KDM5A and the NuRD complex cooperatively regulate H3K4me2/3 levels. CHD4 modulates H3K4 methylation levels at the promoter and coding regions of target genes
physiological function
histone lysine demethylase KDM5B regulates gene transcription and cell differentiation and is implicated in carcinogenesis
physiological function
LSD1 modulates gene expression through demethylation of either H3K4 or H3K9. H3K9 methylation usually suppresses transcription, whereas H3K4 methylation generally activates transcription. H3K4 methylation is a critical epigenetic marker of transcriptional activation. Lysine-specific demethylase 1-mediated demethylation of histone H3 lysine 9, but not lysine 4, contributes to interleukin 1beta-induced microsomal prostaglandin E synthase 1 (mPGES-1) expression in human osteoarthritic chondrocytes. Levels of di- and trimethylated H3K4 are significantly enhanced after 4 h of interleukin-1beta stimulation, reach a maximum at 12 h, persist through 24 h and decrease at 48 h. In contrast, the level of monomethylated H3K4 remain almost unchanged following interleukin-1beta stimulation. The increase in H3K4 di- and trimethylation by interleukin-1beta at the mPGES-1 promoter paralleles the increased transcription of mPGES-1, suggesting that, in addition to H3K9 demethylation, H3K4 methylation also contributes to interleukin-1beta-induced mPGES-1 expression, the induction of mPGES-1 by interleukin-1beta is associated with H3K4 methylation
physiological function
role for KDM5A (JARID1A/RBP2) as oncogenic driver
physiological function
role for KDM5B (JARID1B/PLU1) as oncogenic driver
physiological function
-
enzyme overexpression promotes the epithelial-mesenchymal transition process of cancer cells. The enzyme increases the expression of transcription factors, ZEB1 and ZEB2, followed by downregulation of E-cadherin and upregulation of mesenchymal marker genes. The enzyme represses the expression of the miR-200 family by changing histone H3 methylation status of their regulatory regions
physiological function
-
the enzyme is a corepressor of transforming growth factor-beta inducible early gene-1/Krueppel-like transcription factor 10 (TIEG1/KLF10)
physiological function
-
the enzyme plays a role in neuronal survival and dendritic development
physiological function
-
the enzyme plays an essential role in hypoxia signaling. The enzyme regulates the expression of hypoxia-induced neuroendocrine differentiation genes. The enzyme is essential for maintaining [histone H3]-N6,N6,N6-trimethyl-L-lysine4 levels on hypoxia-inducible genes. In the context of prostate cancer, the enzyme appears to execute its regulatory function during hypoxia signaling in androgen receptor-positive prostate cancer cells
physiological function
-
the enzyme promotes cell proliferation of breast cancer in vitro and tumorigenesis in vivo. The enzyme functions as a demethylase in estrogen signaling. The enzyme is transcriptionally regulated by estrogen receptor alpha. Through the up-regulation of the enzyme, estrogen receptor alpha and the enzyme form a feedforward regulatory loop to enhance and amplify the hormone response under physiological as well as pathological conditions
physiological function
-
the transcription factor TFAP2C-oncoprotein Myc-enzyme complex promotes cell cycle progression via direct cell cycle inhibitor p21cip repression, thereby contributing to tumorigenesis and therapy failure
physiological function
in dental pulp cells, KDM5A depletion results in greater alkaline phosphatase activity and more mineral deposition formation. The expression levels of the odontogenic markers DMP1, DSPP, OSX, and OCN are increased by KDM5A knockdown. KDM5A deficiency leads to a significant increment in total H3K4me3 levels, whereas no significant difference is found for H3K4 me2. H3K4me3 levels on the promoters of the odontogenic markers increase after KDM5A knockdown in dental pulp cells
physiological function
KDM5B is not a strong transcriptional repressor but rather a fine-tuning regulator of cell type-specific H3K4 methylation and transcript levels. The top up-regulated genes CYP1A1, CYP1B2, ALDH1A3 and AHRR are involved in the aryl hydrocarbon receptor (AhR) response
physiological function
the expression of STING, i.e. cyclic GMP-AMP synthase stimulator of interferon genes, is epigenetically suppressed by the histone H3K4 lysine demethylases KDM5B and KDM5C. The induction of STING expression by KDM5 blockade triggers a robust interferon response in a cytosolic DNA-dependent manner in breast cancer cells, resulting in resistance to infection by DNA and RNA viruses
additional information
enzyme KDM5A uses distinct domains to associate with the SIN3B and NuRD complexes
additional information
enzyme KDM5B contains multiple conserved chromatin-associated domains, including three PHD fingers. The first and third, but not the second, PHD finger of KDM5B possess histone binding activities. The PHD1 finger is highly specific for unmodified histone H3 (H3K4me0), whereas the PHD3 finger shows preference for the trimethylated histone mark H3K4me3, but also binds H3K4me0. Mechanism of H3K4me0 recognition by PHD1, the H3K4me0 binding mode is conserved overview. KDM5B inhibits the migration and invasion abilities of MDA-MB 231 breast cancer cells, and binding of the PHD1 finger to H3K4me0 is required to suppress cell migration
additional information
minimal requirements for enzymatic activity of the KDM5 family is the linked JmjNJmjC domain coupled with the immediate C-terminal helical zinc-binding domain
additional information
minimal requirements for enzymatic activity of the KDM5 family is the linked JmjNJmjC domain coupled with the immediate C-terminal helical zinc-binding domain
additional information
minimal requirements for enzymatic activity of the KDM5 family is the linked JmjNJmjC domain coupled with the immediate C-terminal helical zinc-binding domain
additional information
minimal requirements for enzymatic activity of the KDM5 family is the linked JmjNJmjC domain coupled with the immediate C-terminal helical zinc-binding domain, hypothetical modeling of the N-terminal half of KDM5, overview
additional information
minimal requirements for enzymatic activity of the KDM5 family is the linked JmjNJmjC domain coupled with the immediate C-terminal helical zinc-binding domain, hypothetical modeling of the N-terminal half of KDM5, overview
additional information
minimal requirements for enzymatic activity of the KDM5 family is the linked JmjNJmjC domain coupled with the immediate C-terminal helical zinc-binding domain, hypothetical modeling of the N-terminal half of KDM5, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the hybrid tudor domains at the C terminus of JMJD2A are necessary for the demethylation activity of JMJD2A in vivo
additional information
-
the enzyme consists of DNA binding domain, catalytic domain, and plant homeodomain
additional information
KDM5 domain structure and functional analysis, overview
additional information
KDM5 domain structure and functional analysis, overview
additional information
KDM5 domain structure and functional analysis, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
JMJD2A-tudor in complex with H4K20me3, X-ray diffraction structure determination and analysis at 2.8 A resolution
N-terminal fragments of the enzyme in complex with inhibitors, sitting drop vapor diffusion method, using 1.2-1.35 M (NH4)2SO4, 0.1 M Tris-HCl (pH 8.6-9.2), 0-20% (v/v) glycerol and 25 mM (Na/K) dibasic/monobasic phosphate
-
purified recombinant enzyme in complex with inhibitor KDOAM-25, sitting drop vapor diffusion method, mixing of 50 nl of 8.1 mg/ml protein in solution with 1 mM KDOAM-25 and 4 mM MnCl2, is mixed with ,precipitant solution consisting of 1.6 M Na/K phosphate, and 0.1 M HEPES, pH 7.5, and 20 nL of KDM5B seeds of crystals obtained from the same condition, 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, modeling
solution strucuture of apo and H3-bound domain PHD1. The H3 peptide adopts a helical conformation that allows for extended interactions between the H3 ligand and PHD1 reader domain. H3 residues A1, R2, and K4 are the major determinants of H3 peptide binding, with smaller contributions from H3T3
structure of intact multi-domain KDM5B. The PLU region, in the central region of KDM5B, has a curved alpha-helical three-dimensional structure that acts as a rigid linker between the catalytic core and a region comprising four alpha-helices, a loop comprising the PHD2 domain, two large intrinsically disordered loops and the PHD3 domain in close proximity. The dumbbell shaped and curved KDM5B architecture is complementary to the nucleosome surface and has a striking overall similarity to that of the functionally related KDM1A/CoREST complex
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D939R
the mutation increases the Kd of JMJD2A for H4K20me3 by about 200fold but does not markedly change the affinity for H3K4me3
D945R
the mutation increases the Kd of JMJD2A for H3K4me3 by about 200fold, but does not affect the interaction with H4K20me3
H18G
the mutation increases the Kd for H3K4me3 by fivefold compared to the wild-type enzyme
N940R
the mutation does not perturb JMJD2A binding to H4K20me3 but decreases its affinity for H3K4me3 by about 46fold
T968A
the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
T968R
the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
Y942A
the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
Y942R
the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
A388P
-
the mutant shows 14.4% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 45.1% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
D328A
site-directed mutagenesis, a loss-of-function mutations in the PHD1 finger domain
F642L
-
the mutant shows 40.1% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 71.6% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
H499A
-
the mutant shows significantly reduced activity compared to the wild type enzyme
H514A
-
the mutant shows no activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 2.0% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
L326W
site-directed mutagenesis, a loss-of-function mutations in the PHD1 finger domain
L731F
-
the mutant shows 37.2% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 48.1% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
W1502A
site-directed mutagenesis, a loss-of-function mutations in the PHD3 finger domain
Y751C
-
the mutant shows 51.4% of wild type activity with [histone H3]-N6,N6-dimethyl-L-lysine4 and 56.6% of wild type activity with [histone H3]-N6,N6,N6-trimethyl-L-lysine4
additional information
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5B(1-755)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain. Deletion of DELTAAP has no effect on kinetics of KDM5C
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5B(1-755)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain. Deletion of DELTAAP has no effect on kinetics of KDM5C
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5B(1-755)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain. Deletion of DELTAAP has no effect on kinetics of KDM5C
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5C(1-789)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5C(1-789)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain
additional information
internal deletion of the ARID and PHD1 domains has a negligible effect on in vitro enzymatic kinetics of the KDM5 family of enzymes. Generation of a KDM5C(1-789)DELTAAP mutant by deleting ARID and PHD1 (AP) domains by connecting residues 100 and 363. The DELTAAP constructs represent the domain arrangement of the conventional Jumonji domain followed by a C-terminal helical zinc binding domain
additional information
siRNA-mediated knockdown of KDM5A, and CHD4 or SIN3B in HeLa cells, and analysis of the changes in gene expression by microarray analysis. At least 435 genes (corresponding to 468 probes) are dysregulated in the KDM5A-knockdown cells. 66 and 63% of the KDM5A-regulated genes are also dysregulated in CHD4-and SIN3B-knockdown cells, respectively, and 47% of the KDM5A-regulated genes are affected by either CHD4 or SIN3B knockdown. Among the 435 KDM5A-regulated genes, 40% are upregulated, although more than half are downregulated. A similar proportion of genes is downregulated in response to SIN3B knockdown
additional information
the enzyme is knocked out by expression of specific siRNA for LSD1 in chondrocytes
additional information
-
the enzyme is knocked out by expression of specific siRNA for LSD1 in chondrocytes
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity column chromatography, anion exchange column chromatography, and gel filtration
-
recombinant His-SUMO-tagged enzyme from Escherichia coli strain BL21(DE3)C+ by nickel affinity chromatography, tag cleavage overnight by Ulp-1 protease, followed by anion exchange chromatography, gel filtration, and ultrafiltration
recombinant His-SUMO-tagged enzyme from Escherichia coli strain BL21(DE3)C+ by nickel affinity chromatography, tag cleavage overnight by Ulp-1 protease, followed by anion exchange chromatography, gel filtration, and ultrafiltration. Deletion of DELTAAP has no effect on kinetics of KDM5C
recombinant His-tagged N-terminal fragment of JARID1B from Sf9 insect cells by nickel affinity chromatography
-
recombinant N-terminally FLAG-tagged KDM5A from HeLa cell nuclear extract by gel filtration and immunoaffinity chromatography, the enzyme copurifies with the SIN3B-HDAC complex, and with additional proteins including CHD4, MTA2, GATAD2A, ZMYND8A, ZNF592, and ZNF687. CHD4, MTA2, and GATAD2A are known components of the NuRD (nucleosome remodeling and deacetylase) complex
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding for Myc-tagged JARID1B is transfected into HeLa cells, and the effect on histone lysine methylation is examined
-
co-expression of FLAG-CMV-tagged hPc2 and the HA-tagged N-terminal fragment of JARDI1B in HEK-293T cells. Expression the His-tagged N-terminal fragment of JARID1B in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
full-length Flag-tagged human PLU-1 is expressed in SF9 cells. PLU-1 is overexpressed in U2OS cells
-
gene KDM5A, cloned from a HeLa gene library, recombinant expression of N-terminally FLAG-tagged KDM5A in HeLa cells and HEK-293T cells, quantitative RT-PCR expression analysis
gene KDM5A, recombinant expression of soluble His-SUMO-tagged enzyme in Escherichia coli strain BL21(DE3)C+
gene KDM5B, recombinant expression of soluble His-SUMO-tagged enzyme in Escherichia coli strain BL21(DE3)C+
gene Kdm5c, encoded on the X-chromosome, genotyping, quantitative real-time RT-PCR expression analysis
-
gene KDM5C, recombinant expression ofsoluble His-SUMO-tagged enzyme in Escherichia coli strain BL21(DE3)C+
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
KDM5A demonstrates significantly enhanced expression during cytodifferentiation of dental pulp cells. KDM5A expression increases during early passages and in a time-dependent manner during odontogenic induction
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
in human tumors, KDM5B expression is inversely associated with STING expression in multiple cancer types, with the level of intratumoral CD8+ T cells, and with patient survival in cancers with a high level of cytosolic DNA, such as human papilloma virus-positive head and neck cancer
medicine
paclitaxel-resistant lung adenocarcinoma PTX-Calu-3 cells show significantly higher IC50 value (7 microM) upon paclitaxel treatxadment than lung adenocarcinoma SK-LI-1 (3.6 nM), Calu-3 (4.3 nM), and A549 (4.5 nM) cells. Expression of KDM5A and P-glycoprotein are significantly higher in PTX-Calu-3 cells compared to SK-LI-1, Calu-3, and A549 cells. A significantly higher number of PTX-Calu-3 cells are inxadvasive and motile compared to SK-LI-1, Calu-3, and A549 cells. A significantly higher expression of KDM5A is observed in lung adenocarcixadnoma patients' samples compared with adjacent normal tissues as well as in PTX-Calu-3 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamane, K.; Tateishi, K.; Klose, R.J.; Fang, J.; Fabrizio, L.A.; Erdjument-Bromage, H.; Taylor-Papadimitriou, J.; Tempst, P.; Zhang, Y.
PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation
Mol. Cell
25
801-812
2007
Homo sapiens
Tahiliani, M.; Mei, P.; Fang, R.; Leonor, T.; Rutenberg, M.; Shimizu, F.; Li, J.; Rao, A.; Shi, Y.
The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation
Nature
447
601-605
2007
Homo sapiens (P41229)
Xiang, Y.; Zhu, Z.; Han, G.; Ye, X.; Xu, B.; Peng, Z.; Ma, Y.; Yu, Y.; Lin, H.; Chen, A.P.; Chen, C.D.
JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer
Proc. Natl. Acad. Sci. USA
104
19226-19231
2007
Homo sapiens
Lopez-Bigas, N.; Kisiel, T.; DeWaal, D.; Holmes, K.; Volkert, T.; Gupta, S.; Love, J.; Murray, H.; Young, R.; Benevolenskaya, E.
Genome-wide analysis of the H3K4 histone demethylase RBP2 reveals a transcriptional program controlling differentiation
Mol. Cell
31
520-530
2008
Homo sapiens
Lee, J.; Thompson, J.; Botuyan, M.; Mer, G.
Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
Nat. Struct. Mol. Biol.
15
109-111
2008
Homo sapiens (O75164)
Zhou, W.; Chen, H.; Zhang, L.
The PcG protein hPc2 interacts with the N-terminus of histone demethylase JARID1B and acts as a transcriptional co-repressor
BMB Rep.
42
154-159
2009
Homo sapiens
Grafodatskaya, D.; Chung, B.H.; Butcher, D.T.; Turinsky, A.L.; Goodman, S.J.; Choufani, S.; Chen, Y.A.; Lou, Y.; Zhao, C.; Rajendram, R.; Abidi, F.E.; Skinner, C.; Stavropoulos, J.; Bondy, C.A.; Hamilton, J.; Wodak, S.; Scherer, S.W.; Schwartz, C.E.; Weksberg, R.
Multilocus loss of DNA methylation in individuals with mutations in the histone H3 lysine 4 demethylase KDM5C
BMC Med. Genomics
6
0000
2013
Homo sapiens
El Mansouri, F.; Nebbaki, S.; Kapoor, M.; Afif, H.; Martel-Pelletier, J.; Pelletier, J.; Benderdour, M.; Fahmi, H.
Lysine-specific demethylase 1-mediated demethylation of histone H3 lysine 9 contributes to interleukin 1beta-induced microsomal prostaglandin E synthase 1 expression in human osteoarthritic chondrocytes
Arthritis Res. Ther.
16
R113
2014
Homo sapiens (O60341), Homo sapiens
Maina, P.K.; Shao, P.; Jia, X.; Liu, Q.; Umesalma, S.; Marin, M.; Long, D.; Concepcion-Roman, S.; Qi, H.H.
Histone demethylase PHF8 regulates hypoxia signaling through HIF1alpha and H3K4me3
Biochim. Biophys. Acta
1860
1002-1012
2017
Homo sapiens
Tumber, A.; Nuzzi, A.; Hookway, E.S.; Hatch, S.B.; Velupillai, S.; Johansson, C.; Kawamura, A.; Savitsky, P.; Yapp, C.; Szykowska, A.; Wu, N.; Bountra, C.; Strain-Damerell, C.; Burgess-Brown, N.A.; Ruda, G.F.; Fedorov, O.; Munro, S.; England, K.S.; Nowak, R.P.; Schofield, C.J.; La Thangue, N.B.; Pawlyn, C.
Potent and selective KDM5 inhibitor stops cellular demethylation of H3K4me3 at transcription start sites and proliferation of MM1S myeloma cells
Cell Chem. Biol.
24
371-380
2017
Homo sapiens (P29375), Homo sapiens (P41229), Homo sapiens (Q9BY66), Homo sapiens (Q9UGL1)
Klein, B.J.; Piao, L.; Xi, Y.; Rincon-Arano, H.; Rothbart, S.B.; Peng, D.; Wen, H.; Larson, C.; Zhang, X.; Zheng, X.; Cortazar, M.A.; Pena, P.V.; Mangan, A.; Bentley, D.L.; Strahl, B.D.; Groudine, M.; Li, W.; Shi, X.; Kutateladze, T.G.
The histone-H3K4-specific demethylase KDM5B binds to its substrate and product through distinct PHD fingers
Cell Rep.
6
325-335
2014
Homo sapiens (Q9UGL1)
Nishibuchi, G.; Shibata, Y.; Hayakawa, T.; Hayakawa, N.; Ohtani, Y.; Sinmyozu, K.; Tagami, H.; Nakayama, J.
Physical and functional interactions between the histone H3K4 demethylase KDM5A and the nucleosome remodeling and deacetylase (NuRD) complex
J. Biol. Chem.
289
28956-28970
2014
Homo sapiens (P29375), Caenorhabditis elegans (Q23541), Caenorhabditis elegans
Horton, J.R.; Engstrom, A.; Zoeller, E.L.; Liu, X.; Shanks, J.R.; Zhang, X.; Johns, M.A.; Vertino, P.M.; Fu, H.; Cheng, X.
Characterization of a linked Jumonji domain of the KDM5/JARID1 family of histone H3 lysine 4 demethylases
J. Biol. Chem.
291
2631-2646
2016
Homo sapiens (P29375), Homo sapiens (P41229), Homo sapiens (Q9UGL1)
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 (P41229), Homo sapiens (Q9UGL1)
Xiao, C.; Liu, Y.; Xie, C.; Tu, W.; Xia, Y.; Costa, M.; Zhou, X.
Cadmium induces histone H3 lysine methylation by inhibiting histone demethylase activity
Toxicol. Sci.
145
80-89
2015
Homo sapiens (P29375), Homo sapiens
Kim, J.; Shin, S.; Subramaniam, M.; Bruinsma, E.; Kim, T.D.; Hawse, J.R.; Spelsberg, T.C.; Janknecht, R.
Histone demethylase JARID1B/KDM5B is a corepressor of TIEG1/KLF10
Biochem. Biophys. Res. Commun.
401
412-416
2010
Homo sapiens
Iwase, S.; Lan, F.; Bayliss, P.; de la Torre-Ubieta, L.; Huarte, M.; Qi, H.H.; Whetstine, J.R.; Bonni, A.; Roberts, T.M.; Shi, Y.
The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases
Cell
128
1077-1088
2007
Homo sapiens
Enkhbaatar, Z.; Terashima, M.; Oktyabri, D.; Tange, S.; Ishimura, A.; Yano, S.; Suzuki, T.
KDM5B histone demethylase controls epithelial-mesenchymal transition of cancer cells by regulating the expression of the microRNA-200 family
Cell Cycle
12
2100-2112
2013
Homo sapiens
Horton, J.R.; Woodcock, C.B.; Chen, Q.; Liu, X.; Zhang, X.; Shanks, J.; Rai, G.; Mott, B.T.; Jansen, D.J.; Kales, S.C.; Henderson, M.J.; Cyr, M.; Pohida, K.; Hu, X.; Shah, P.; Xu, X.; Jadhav, A.; Maloney, D.J.; Hall, M.D.; Simeonov, A.; Fu, H.; Vertino, P.M.; Cheng, X.
Structure-based engineering of irreversible inhibitors against histone lysine demethylase KDM5A
J. Med. Chem.
61
10588-10601
2018
Homo sapiens
Wong, P.P.; Miranda, F.; Chan, K.V.; Berlato, C.; Hurst, H.C.; Scibetta, A.G.
Histone demethylase KDM5B collaborates with TFAP2C and Myc to repress the cell cycle inhibitor p21cip (CDKN1A)
Mol. Cell. Biol.
32
1633-1644
2012
Homo sapiens
Longbotham, J.; Chio, C.; Dharmarajan, V.; Trnka, M.; Torres, I.; Goswami, D.; Ruiz, K.; Burlingame, A.; Griffin, P.; Fujimori, D.
Histone H3 binding to the PHD1 domain of histone demethylase KDM5A enables active site remodeling
Nat. Commun.
10
94
2019
Homo sapiens
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
Longbotham, J.E.; Kelly, M.J.S.; Fujimori, D.G.
Recognition of histone H3 methylation states by the PHD1 domain of histone demethylase KDM5A
ACS Chem. Biol.
FEHLT
0000
2021
Homo sapiens (P29375)
Xu, L.; Wu, H.; Hu, X.
Histone demethylase KDM5A enhances cell proliferation, induces EMT in lung adenocarcinoma cells, and have a strong causal association with paclitaxel resistance
Acta Biochim. Pol.
68
593-602
2021
Homo sapiens (P29375), Homo sapiens
Petronikolou, N.; Longbotham, J.E.; Fujimori, D.G.
Extended recognition of the histone H3 tail by histone demethylase KDM5A
Biochemistry
59
647-651
2020
Homo sapiens (P29375), Homo sapiens
Li, Q.M.; Li, J.L.; Feng, Z.H.; Lin, H.C.; Xu, Q.
Effect of histone demethylase KDM5A on the odontogenic differentiation of human dental pulp cells
Bioengineered
11
449-462
2020
Homo sapiens (P29375), Homo sapiens
Romani, M.; Daga, A.; Forlani, A.; Pistillo, M.P.; Banelli, B.
Targeting of histone demethylases KDM5A and KDM6B inhibits the proliferation of temozolomide-resistant glioblastoma cells
Cancers (Basel)
11
878
2019
Homo sapiens (P29375)
Zhao, B.; Liang, Q.; Ren, H.; Zhang, X.; Wu, Y.; Zhang, K.; Ma, L.; Zheng, Y.; Liu, H.
Discovery of pyrazole derivatives as cellular active inhibitors of histone lysine specific demethylase 5B (KDM5B/JARID1B)
Eur. J. Med. Chem.
192
112161
2020
Homo sapiens (Q9UGL1)
Pippa, S.; Mannironi, C.; Licursi, V.; Bombardi, L.; Colotti, G.; Cundari, E.; Mollica, A.; Coluccia, A.; Naccarato, V.; La Regina, G.; Silvestri, R.; Negri, R.
Small molecule inhibitors of KDM5 histone demethylases increase the radiosensitivity of breast cancer cells overexpressing JARID1B
Molecules
24
1739
2019
Homo sapiens (Q9UGL1)
Wu, L.; Cao, J.; Cai, W.; Lang, S.; Horton, J.; Jansen, D.; Liu, Z.; Chen, J.; Zhang, M.; Mott, B.; Pohida, K.; Rai, G.; Kales, S.; Henderson, M.; Hu, X.; Jadhav, A.; Maloney, D.; Simeonov, A.; Zhu, S.; Iwasaki, A.; Hall, M.; Cheng, X.; Shadel, G.; Yan, Q
KDM5 histone demethylases repress immune response via suppression of STING
PLoS Biol.
16
e2006134
2018
Homo sapiens (P41229), Homo sapiens (Q9UGL1), Homo sapiens
Dorosz, J.; Kristensen, L.H.; Aduri, N.G.; Mirza, O.; Lousen, R.; Bucciarelli, S.; Mehta, V.; Selles-Baiget, S.; Solbak, S.M.O.; Bach, A.; Mesa, P.; Hernandez, P.A.; Montoya, G.; Nguyen, T.T.T.N.; Rand, K.D.; Boesen, T.; Gajhede, M.
Molecular architecture of the Jumonji C family histone demethylase KDM5B
Sci. Rep.
9
4019
2019
Homo sapiens (Q9UGL1), Homo sapiens
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