Information on EC 1.14.11.B1 - [histone-H3]-lysine-9-demethylase and Organism(s) Homo sapiens and UniProt Accession O75164

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UNIPROT: O75164
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The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.B1
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
[histone-H3]-lysine-9-demethylase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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. 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, substrate selectivity of the human KDM4 histone demethylase subfamily, overview
evolution
malfunction
metabolism
-
expression levels of JMJD2B and CDK6 were significantly correlated in various types of cell lines
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
dimethyl-histone 3 L-lysine 9 + alpha-ketoglutarate + O2
methyl-histone 3 L-lysine 9 + ?
show the reaction diagram
-
-
-
?
dimethylated histone 3-Lys4 peptide + H2O
?
show the reaction diagram
-
the enzyme specifically removes methyl groups from Lys4 of histone 3. The enzyme exhibits oxidase activity (with production of H2O2) but it can function also with a synthetic mono-electronic acceptor
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6-methyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
protein 6-N,6-N-dimethyl-L-lysine + 2-oxoglutarate + O2
?
show the reaction diagram
-
demethylation of lysine 4
-
-
?
trimethyl-histone 3 L-lysine 9 + alpha-ketoglutarate + O2
dimethyl-histone 3 L-lysine 9 + ?
show the reaction diagram
-
-
-
?
trimethyl-histone 3 L-lysine 9 mutant A7H + alpha-ketoglutarate + O2
dimethyl-histone 3 L-lysine 9 mutant A7H + ?
show the reaction diagram
-
-
-
?
trimethyl-histone 3 L-lysine 9 mutant A7R + alpha-ketoglutarate + O2
dimethyl-histone 3 L-lysine 9 mutant A7R + ?
show the reaction diagram
-
-
-
?
trimethyl-histone 3 L-lysine 9 mutant G12P + alpha-ketoglutarate + O2
dimethyl-histone 3 lysine 9 mutant G12P + ?
show the reaction diagram
-
-
-
?
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3 peptide]-L-lysine4 + succinate + H2O2
show the reaction diagram
-
the peptide substrate comprises the 21 N-terminal residues of histone H3, with a dimethylated lysyl residue at position 4. The reductive half-reaction is rate-limiting at physiological pH
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
-
-
-
?
histone H3 N6,N6-dimethyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
histone H3 N6-methyl-L-lysine9 + 2-oxoglutarate + O2
histone H3 L-lysine9 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-N6,N6-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
-
?
[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
show the reaction diagram
[protein p53]-N6,N6-dimethyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
O60341
LSD1 demethylates mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1
-
-
?
[protein p53]-N6-methyl-L-lysine370 + 2-oxoglutarate + O2
[protein p53]-L-lysine370 + succinate + formaldehyde + CO2
show the reaction diagram
O60341
LSD1 demethylates mono- and dimethylated Lys370 in the regulatory domain of the tumor suppressor p53, precluding the binding of the transcriptional coactivator 53BP1
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
the mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate
Zn2+
structure of Zn2+ binding sites of the isozymes, overview
Iron
-
Fe(II) center
Zn2+
structure of Zn2+ binding sites of the isozymes, overview
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(12E)-N,N'-diethyl-5,10,16,21-tetraazapentacos-12-ene-1,25-diamine
-
-
(13Z)-N,N'-diethyl-6,11,16,21-tetraazahexacos-13-ene-1,26-diamine
-
-
(19E)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
-
-
(19Z)-N,N'-diethyl-6,12,17,22,27,33-hexaazaoctatriacont-19-ene-1,38-diamine
-
-
(25E)-N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
-
-
(25Z)-N,N'-diethyl-6,12,18,23,28,33,39,45-octaazapentacont-25-ene-1,50-diamine
-
-
(2Z)-N-ethyl-N'-[4-[(4-[[(2Z)-4-(ethylamino)but-2-en-1-yl]amino]butyl)amino]butyl]but-2-ene-1,4-diamine
-
-
(2Z)-N-[4-(ethylamino)butyl]-N'-(4-[[4-(ethylamino)butyl]amino]butyl)but-2-ene-1,4-diamine
-
-
3,8,13,18,23-pentaazapentacosan-1-ol
-
-
biguanide
-
inhibits LSD1 and is capable of reactivating genes that are pathologically silenced in the development of colon cancer
bisguanidine
-
inhibits LSD1/KDM1
bisguanidine polyamine analogues
-
inhibit LSD1 and are capable of reactivating genes that are pathologically silenced in the development of colon cancer
-
H3 21mer peptide
-
the peptide is covalently attached to LSD1-flavin by suicide inactivation
-
HCF-1
-
is a component of the Set1 and MLL1 histone H3 Lys4 methyltransferase complexes, it thus coordinates modulation of repressive H3 Lys9 methylation levels with addition of activating H3 Lys4 trimethylation marks
-
N,N'-diethyl-5,11,17,22,27,33-hexaazaoctatriacontane-1,38-diamine
-
-
N,N'-diethyl-5,11,17,23,28,33,39,45-octaazapentacontane-1,50-diamine
-
-
N-ethyl-N'-[[2-([[4-([[2-([[4-(ethylamino)butyl]amino]methyl)cyclopropyl]methyl]amino)butyl]amino]methyl)cyclopropyl]methyl]butane-1,4-diamine
-
-
Peptide inhibitor
a suicide inhibitor consisting of a 21 residue histone H3 peptide in which K4 is modified by an Nmethylpropargyl group. Interactions with the inhibitor include hydrogen bonds to its R2 and Q5 side chains and a salt bridge interaction between the alpha-amine of A1 and Asp555 in LSD1, binding structure, overview
-
Tranylcypromine
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
required
CoREST
-
the co-repressor CoREST stabilizes LSD1 and increases in vitro LSD1 activity by approximately twofold and is essential for LSD1-mediated demethylation in intact nucleosomes in vivo and for the in vitro demethylation of nucleosomal particles, binding structure, overview
-
tetrahydrofolate
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.045
histone H3 N6,N6,N6-trimethyl-L-lysine9
KDM4A, pH and temperature not specified in the publication
-
0.073
histone H3 N6,N6-dimethyl-L-lysine9
KDM4A, pH and temperature not specified in the publication
-
0.23 - 0.41
dimethyl-histone 3 L-lysine 9
-
0.023 - 0.048
histone H3 N6,N6,N6-trimethyl-L-lysine9
-
0.025 - 0.074
histone H3 N6,N6-dimethyl-L-lysine9
-
0.195
O2
-
pH 7.5, 25°C, recombinant enzyme
0.063 - 0.071
trimethyl-histone 3 L-lysine 9
-
0.11
trimethyl-histone 3 L-lysine 9 mutant A7H
-
pH 7.3, 37°C
-
0.18
trimethyl-histone 3 L-lysine 9 mutant A7R
-
pH 7.3, 37°C
-
0.93
trimethyl-histone 3 L-lysine 9 mutant G12P
-
pH 7.3, 37°C
-
0.0026
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4
-
pH 7.5, 25°C, recombinant enzyme
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
histone H3 N6,N6,N6-trimethyl-L-lysine9
Homo sapiens
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
KDM4A, pH and temperature not specified in the publication
-
0.0029
histone H3 N6,N6-dimethyl-L-lysine9
Homo sapiens
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
KDM4A, pH and temperature not specified in the publication
-
0.00008 - 0.005
dimethyl-histone 3 L-lysine 9
-
0.015 - 0.076
histone H3 N6,N6,N6-trimethyl-L-lysine9
-
0.005 - 0.065
histone H3 N6,N6-dimethyl-L-lysine9
-
0.00025 - 0.0005
trimethyl-histone 3 L-lysine 9
-
0.00018
trimethyl-histone 3 L-lysine 9 mutant A7H, trimethyl-histone 3 L-lysine 9 mutant A7R
Homo sapiens
-
pH 7.3, 37°C
-
0.00012
trimethyl-histone 3 L-lysine 9 mutant G12P
Homo sapiens
-
pH 7.3, 37°C
-
0.199
[histone H3 peptide]-N6,N6-dimethyl-L-lysine4
Homo sapiens
-
pH 7.5, 25°C, recombinant enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22
histone H3 N6,N6,N6-trimethyl-L-lysine9
Homo sapiens
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
KDM4A, pH and temperature not specified in the publication
7053
4
histone H3 N6,N6-dimethyl-L-lysine9
Homo sapiens
B2RXH2, O75164, O94953, Q6B0I6, Q9H3R0
KDM4A, pH and temperature not specified in the publication
6384
41 - 330
histone H3 N6,N6,N6-trimethyl-L-lysine9
7053
10 - 260
histone H3 N6,N6-dimethyl-L-lysine9
6384
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.5
-
assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
kcat/KM-pH profiles for LSD1 with protiated and deuterated H3 K4 21-mer dimethylated peptide, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
levels of KDM4B histone demethylase are elevated in different types of cancer cells
Manually annotated by BRENDA team
-
expression pattern in early mammalian development: the maternally stored transcript is no longer detectable by the maternal-to-embryo transition, when the embryo becomes transcriptionally competent. LSD1/KDM1 expression then recovers to oocyte levels by the blastula stage
Manually annotated by BRENDA team
-
JMJD2C/KDM4C is preferentially expressed in undifferentiated embryonic stem cells, as compared with blastocysts and both hepatocyte and neural progenitor cells
Manually annotated by BRENDA team
-
JMJD1A is expressed in human cancers such as glioblastoma and breast cancer in vivo, and expression is associated with the hypoxic marker CA9
Manually annotated by BRENDA team
-
BALB c nu/nu athymic nude mice are implanted with the human colorectal cancer HCT-116 cells
Manually annotated by BRENDA team
-
up-regulation of mRNA and protein after exposure to hypoxia or iron scavengers in vitro. Blocking of hypoxia-inducible factor 1 signaling abrogates the up-regulation
Manually annotated by BRENDA team
-
elevated activity of JMJD2B expression
Manually annotated by BRENDA team
-
short isoform of JMJD2A is upregulated during muscle differentiation, expression analysis and pattern, overview
Manually annotated by BRENDA team
-
LSD1 expression correlates with adverse outcome and is inversely correlated with differentiation in neuroblastic tumors; LSD1 is strongly expressed in poorly differentiated neuroblastomas, real-time reverse transcription-PCR expression analysis
Manually annotated by BRENDA team
-
expression pattern in early mammalian development: the maternally stored transcript is no longer detectable by the maternal-to-embryo transition, when the embryo becomes transcriptionally competent. LSD1/KDM1 expression then recovers to oocyte levels by the blastula stage
Manually annotated by BRENDA team
-
elevated levels of JMJD2B expression
Manually annotated by BRENDA team
-
retinoblastoma cells
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
JMJD1A is localized in both cytoplasm and nucleus
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
-
-
-
-
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95059
-
1 * 95059, LSD1 without N-terminal methionine, mass spectrometry
100000
-
about, recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 95059, LSD1 without N-terminal methionine, mass spectrometry
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structures of JMJD2A-Ni(II)-Zn(II) inhibitor complexes bound to tri-, di- and monomethyl forms of histone 3 lysine 9 and the trimethyl form of histone 3 lysine 36. The structures reveal a lysyl-binding pocket in which substrates are bound in distinct bent conformations involving the Zn-binding site. The mechansim for achieving methylation state selectivity involves the orientation of the substrate methyl groups towards a ferryl intermediate
-
crystal structures of LSD1/Co-REST complexes bound to histone H3 peptides. LSD1/Co-REST-C complex co-crystallized with a 20-residue histone H3 peptide inhibitor in which Lys4 is mutated to a methionine. Cocrystallization of the enzyme with a suicide inhibitor consisting of a 21-residue histone H3 peptide in which K4 is modified by an N-methylpropargylgroup. Complex structure analysis, overview
enzyme complex LSD1-CoREST crystal structure in complex with a histone H3 peptide, overview
-
in complex with trimethyl-histone 3 L-lysine 9, dimethyl-histone 3 L-lysine 36, and trimethyl-histone 3 L-lysine 36, and N-oxalylglycine, alpha-ketoglutarate, and succinate, respectively. Histone substrates are recognized through a network of backbone hydrogen bonds and hydrophobic interactions that deposit the trimethyllysine into the active site. The trimethylated epsilon-ammonium cation is coordinated within a methylammonium-binding pocket through carbonoxygen hydrogen bonds that position one of the methyl groups adjacent to the Fe(II) center for hydroxylation and demethylation
-
JMJD2A-tudor in complex with H4K20me3, X-ray diffraction structure determination and analysis at 2.8 A resolution
-
LSD1 with bound inhibitor histone H3 21mer peptide, protein to peptide ratio of 1:5, with or without inhibitor tranylcypromine, from 20 mM MES-Na buffer, pH 6.0, containing 1 mM DTT, with 100 mM HEPES-Na buffer, pH 7.5, containing 5% 2-methyl-2,4-pentanediol and 3.5-4.0% w/v PEG monomethyl ether 2000, with or without 5 mM tranylcypromine, the cryoprotectant contains 25% w/v 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 2.25-2.7 A resolution
-
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
recombinant enzyme, hanging-drop vapor diffusion method, 2.8 A-resolution crystal structure
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5
-
purified recombinant enzyme, 60 min, inactivation
696340
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the molecular chaperon Hsp90 interacts with and stabilizes KDM4B protein
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged KDM4A from Escherichia coli by nickel affinity chromatography
recombinant
-
recombinant GST-tagged LSD1 from Escherichia coli by glutathione affinity chromatography, cleavageof the tag, and cation exchange chromatography
-
recombinant His-tagged truncated LSD1 mutant from Escherichia coli strain Rosetta 2 by nickel affinity chromatography, gel filtration, and anion exchange chromatography
-
recombinant N-terminally His-tagged enzyme by nickel affinity chromatography from Escherichia coli BL21(DE3), or by ammonium sulfate fractionation and anionexchange chrmatography, recombinant N-terminally truncated GST-tagged LSD1 by glutathione affinity chromatography
-
recombinant N-terminally His-tagged KDM4B from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His-tagged KDM4C from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His-tagged KDM4D from Escherichia coli by nickel affinity chromatography
recombinant N-terminally His-tagged KDM4E from Escherichia coli by nickel affinity chromatography
two LSD1 truncated forms, lacking the first 157 and 184 amino acids, respectively
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His-tagged KDM4A in Escherichia coli
expression in Escherichia coli, His-tagged
-
expression of functional doxycycline-inducible EGFP-KDM4B in U2-OSTetON cell line
-
expression of N-terminally His-tagged KDM4B in Escherichia coli
expression of N-terminally His-tagged KDM4C in Escherichia coli
expression of N-terminally His-tagged KDM4D in Escherichia coli
expression of N-terminally His-tagged KDM4E in Escherichia coli
expression of the His-tagged truncated LSD1 mutant in Escherichia coli strain Rosetta 2
-
gene Jmjd2b, real-time quantitative PCR expression analysis
-
JMJD2B quantitative real-time PCR expression analysis
-
JMJD2B quantitative RT-PCR expression analysis, overview
-
LSD1 expression analysis; real-time reverse transcription-PCR expression analysis
-
LSD1 expression in Escherichia coli as GST-tagged protein
-
LSD1 overexpression in HCT cells
-
mouse Jmjd2b is transfected into JMJD2B-depleted MCF-7 cells, with stable transfection of JMJD2B-specific siRNA molecules
-
RBP2, gene expression profiling and computational analyses of gene targeting
-
short isoform of JMJD2A expression analysis, overview
-
two LSD1 truncated forms, lacking the first 157 and 184 amino acids, respectively, expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
differentiation of neuroblastoma cells result in downregulation of LSD1; differentiation of neuroblastoma cells results in down-regulation of LSD1
-
estrogen receptor alpha is important for JMJD2B expression in hypoxia, JMJD2B can be upregulated in hypoxia in an HIF-1alpha-dependent manner
-
JMJD2B, JMJD2C, JMJD1A, and JMJD1B are induced by hypoxia. HIFalpha-dependent induction of JMJD1A
-
short isoform of JMJD2A is upregulated during muscle differentiation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
I71L
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
I87K
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
N86H
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
N940R
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the mutation does not perturb JMJD2A binding to H4K20me3 but decreases its affinity for H3K4me3 by about 46fold
Q88K
KDM4E mutant, the mutant shows demethylation of H3K9me2, and the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
R309G
KDM4E mutant, poor demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
S288A
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demethylation of trimethyl-histone 3 L-lysine 9 and dimethyl-histone 3 L-lysine 9 with 2-fold and 12-fold greater efficiency, respectively
T968A
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the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
T968R
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the mutation does not appreciably alter the interaction of JMJD2A with either H3K4me3 or H4K20me3
Y942A
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the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
Y942R
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the mutation has no marked effect on the Kd of JMJD2A for H3K4me3 or H4K20me3
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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dimethylation of histone H3 at lysine 4 in combination with trimethylation of histone H3 at lysine 4 is associated with an activated transcriptional state. An increase of H3K4diMe in neoplastic tissues is predictive of clinical outcome. In particular, tumor recurrence occurs earlier in low-grade prostate carcinoma patients with low H3K4diMe, independently of other clinical and pathologic parameters. Similarly, in large cell and squamous cell carcinomas, low H3K4diMe expression correlates with short survival
drug development
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potential pharmacological value of LSD1 as a drug target originating from it being a flavin-dependent demethylase, rather than an iron-dependent enzyme of the Jumonji class
medicine