BRENDA - Enzyme Database show
show all sequences of 1.14.11.27

KDM4C (GASC1) lysine demethylase is associated with mitotic chromatin and regulates chromosome segregation during mitosis

Kupershmit, I.; Khoury-Haddad, H.; Awwad, S.W.; Guttmann-Raviv, N.; Ayoub, N.; Nucleic Acids Res. 42, 6168-6182 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene KDM4A, recombinant expression of EGFP-tagged full-length and truncated enzymes versions; gene KDM4B, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4B; gene KDM4C, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4C, recombinant expression of EGFP-tagged full-length and truncated, andmutant enzymes versions; gene KDM4D is Y chromosome encoded and a truncated enzyme variant compared to KDM4A-C
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization; enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences
Homo sapiens
R919D
site-directed mutagenesis, the mutant is not associated with mitotic chromatin in contrast to the wild-type enzyme
Homo sapiens
S198M
site-directed mutagenesis, a KDM4C demethylase dead mutant
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chromatin
isozyme KDM4C is associated with chromatin during mitosis, residue R919 on the proximal Tudor domains of KDM4C is critical for its association with chromatin during mitosis. KDM4C protein is localized to mitotic chromatin from prometaphase to telophase
Homo sapiens
785
-
additional information
the isozyme is not associated with chromatin during mitosis; the isozyme is not associated with chromatin during mitosis; the isozyme is not associated with chromatin during mitosis
Homo sapiens
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
histone H3 N6,N6,N6-trimethyl-L-lysine26 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
O75164
-
-
Homo sapiens
O94953
-
-
Homo sapiens
Q6B0I6
-
-
Homo sapiens
Q9H3R0
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
breast cancer cell
-
Homo sapiens
-
esophageal squamous cell carcinoma cell
-
Homo sapiens
-
gastric cancer cell line
-
Homo sapiens
-
medulloblastoma cell
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
histone H3 N6,N6,N6-trimethyl-L-lysine26 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
enzyme domain structure includign JmjN, JmjC, PHD and Tudor domains, overview; enzyme domain structure including JmjN and JmjC domains, isozyme KDM4D lacks the PHD and Tudor domains, overview; enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview; enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
gene KDM4A, recombinant expression of EGFP-tagged full-length and truncated enzymes versions
Homo sapiens
gene KDM4C, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4C, recombinant expression of EGFP-tagged full-length and truncated, andmutant enzymes versions
Homo sapiens
gene KDM4B, recombinant isozyme expression in U2OS-TetON stable cell line that conditionally expresses the fusion protein EGFP-KDM4B
Homo sapiens
gene KDM4D is Y chromosome encoded and a truncated enzyme variant compared to KDM4A-C
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization
Homo sapiens
additional information
enzyme engineering and swapping of the C-terminus region containing the distal Tudor domain between isozymes KDM4C and KDM4A. Chimera5, which encodes the first 934 amino acids of KDM4C fused with the last 129 amino acid containing the distal Tudor domain of KDM4A, is excluded from mitotic chromatin. On the other hand, chimera6 that encodes the first 954 amino acids of KDM4A fused to 101 amino acids of KDM4C, which includes its distal Tudor domain, remains excluded from chromatin. The C-terminus of KDM4C containing the distal Tudor domain is essential but not sufficient for its mitotic chromatin localization. EGFP-KDM4CRDTF/DNLY mutant is excluded from mitotic chromatin. For isozyme knockout, U2OS cells are transfected with KDM4B-C siRNA sequences
Homo sapiens
R919D
site-directed mutagenesis, the mutant is not associated with mitotic chromatin in contrast to the wild-type enzyme
Homo sapiens
S198M
site-directed mutagenesis, a KDM4C demethylase dead mutant
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chromatin
isozyme KDM4C is associated with chromatin during mitosis, residue R919 on the proximal Tudor domains of KDM4C is critical for its association with chromatin during mitosis. KDM4C protein is localized to mitotic chromatin from prometaphase to telophase
Homo sapiens
785
-
additional information
the isozyme is not associated with chromatin during mitosis
Homo sapiens
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
histone H3 N6,N6,N6-trimethyl-L-lysine26 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
breast cancer cell
-
Homo sapiens
-
esophageal squamous cell carcinoma cell
-
Homo sapiens
-
gastric cancer cell line
-
Homo sapiens
-
medulloblastoma cell
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
histone H3 N6,N6,N6-trimethyl-L-lysine26 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine26 + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine9 + 2-oxoglutarate + O2
-
745919
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine9 + succinate + formaldehyde + CO2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
enzyme domain structure including JmjN, JmjC, PHD and Tudor domains, overview
Homo sapiens
More
enzyme domain structure includign JmjN, JmjC, PHD and Tudor domains, overview
Homo sapiens
More
enzyme domain structure including JmjN and JmjC domains, isozyme KDM4D lacks the PHD and Tudor domains, overview
Homo sapiens
General Information
General Information
Commentary
Organism
evolution
two families of lysine demethylases (KDM) are identified. The KDM4 family consists of four members: KDM4A, KDM4B, KDM4C and KDM4D; two families of lysine demethylases (KDM) are identified. The KDM4 family consists of four members: KDM4A, KDM4B, KDM4C and KDM4D; two families of lysine demethylases (KDM) are identified. The KDM4 family consists of four members: KDM4A, KDM4B, KDM4C and KDM4D; two families of lysine demethylases (KDM) are identified. The KDM4 family consists of four members: KDM4A, KDM4B, KDM4C and KDM4D
Homo sapiens
malfunction
dysregulated expression of KDM4A-D family promotes chromosomal instabilities; dysregulated expression of KDM4A-D family promotes chromosomal instabilities; dysregulated expression of KDM4A-D family promotes chromosomal instabilities. Depletion or overexpression of KDM4B does not leads to an increase in the frequency of abnormal mitotic cells and has no detectable effect on mitotic chromosome segregation; dysregulated expression of KDM4A-D family promotes chromosomal instabilities. Depletion or overexpression of KDM4C, but not KDM4B, leads to over 3fold increase in the frequency of abnormal mitotic cells showing either misaligned chromosomes at metaphase, anaphase-telophase lagging chromosomes or anaphase-telophase bridges. Overexpression of a KDM4C demethylase dead mutant has no detectable effect on mitotic chromosome segregation
Homo sapiens
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4A is not associated with chromatin during mitosis, in contrast to isozyme KDM4C; the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4B is not associated with chromatin during mitosis, in contrast to isozyme KDM4C; the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4D is not associated with chromatin during mitosis, in contrast to isozyme KDM4C; the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Unlike KDM4A-B, isozyme KDM4C is associated with chromatin during mitosis. This association is accompanied by a decrease in the mitotic levels of H3K9me3. The C-terminal region, containing the Tudor domains of KDM4C, is essential for its association with mitotic chromatin, especially residue R919 on the proximal Tudor domain of KDM4C is critical for its association with chromatin during mitosis. The demethylase activity and the mitotic localization of KDM4C influence the integrity of mitotic chromosome segregation
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
evolution
two families of lysine demethylases (KDM) are identified. The KDM4 family consists of four members: KDM4A, KDM4B, KDM4C and KDM4D
Homo sapiens
malfunction
dysregulated expression of KDM4A-D family promotes chromosomal instabilities
Homo sapiens
malfunction
dysregulated expression of KDM4A-D family promotes chromosomal instabilities. Depletion or overexpression of KDM4C, but not KDM4B, leads to over 3fold increase in the frequency of abnormal mitotic cells showing either misaligned chromosomes at metaphase, anaphase-telophase lagging chromosomes or anaphase-telophase bridges. Overexpression of a KDM4C demethylase dead mutant has no detectable effect on mitotic chromosome segregation
Homo sapiens
malfunction
dysregulated expression of KDM4A-D family promotes chromosomal instabilities. Depletion or overexpression of KDM4B does not leads to an increase in the frequency of abnormal mitotic cells and has no detectable effect on mitotic chromosome segregation
Homo sapiens
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4A is not associated with chromatin during mitosis, in contrast to isozyme KDM4C
Homo sapiens
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Unlike KDM4A-B, isozyme KDM4C is associated with chromatin during mitosis. This association is accompanied by a decrease in the mitotic levels of H3K9me3. The C-terminal region, containing the Tudor domains of KDM4C, is essential for its association with mitotic chromatin, especially residue R919 on the proximal Tudor domain of KDM4C is critical for its association with chromatin during mitosis. The demethylase activity and the mitotic localization of KDM4C influence the integrity of mitotic chromosome segregation
Homo sapiens
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4B is not associated with chromatin during mitosis, in contrast to isozyme KDM4C
Homo sapiens
physiological function
the KDM4 isozymes are involved in histone methylation, a reversible and dynamically regulated process. Various types of human cancers exhibit amplification or deletion of KDM4A-D members, which selectively demethylate lysine residues on histone H3, i.e. H3K9 and H3K36, thus implicating their activity in promoting carcinogenesis. Isozyme KDM4D is not associated with chromatin during mitosis, in contrast to isozyme KDM4C
Homo sapiens
Other publictions for EC 1.14.11.27
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743916
Hancock
The activity of JmjC histone ...
Homo sapiens
ACS Chem. Biol.
12
1011-1019
2017
-
1
1
-
1
-
-
1
-
1
-
-
-
1
1
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1
-
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1
1
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1
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1
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1
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1
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-
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
745949
An
HistoneH3 demethylase JMJD2A ...
Homo sapiens
Oncotarget
8
49093-49109
2017
-
-
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
4
-
-
1
-
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-
-
-
-
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-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
744722
Morera
4-biphenylalanine- and 3-phen ...
Homo sapiens
ChemMedChem
11
2063-2083
2016
1
-
1
-
-
-
33
1
-
1
-
2
-
2
-
-
1
1
-
2
-
-
4
-
1
-
-
-
1
-
-
-
-
-
30
1
-
1
-
-
-
-
30
33
-
1
-
1
-
2
-
-
-
1
-
2
-
-
4
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
744785
Pedersen
Continual removal of H3K9 pro ...
Mus musculus, Mus musculus C57BL/6
EMBO J.
35
1550-1564
2016
-
-
1
-
-
-
-
-
2
1
-
8
-
5
-
-
-
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
2
-
8
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
-
-
3
6
-
-
-
745803
Gacek-Matthews
KdmA, a histone H3 demethylas ...
Aspergillus nidulans, Aspergillus nidulans WIM126
Mol. Microbiol.
96
839-860
2015
-
-
1
-
1
-
-
-
1
1
-
4
-
3
-
-
-
-
-
-
-
-
6
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
4
-
-
-
-
-
-
-
-
6
-
1
-
-
-
-
-
-
-
-
3
3
-
-
-
744589
Ryu
Yeast histone H3 lysine 4 dem ...
Saccharomyces cerevisiae
BMC Biol.
12
75
2014
-
-
1
-
1
-
-
-
-
1
-
7
-
3
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
3
-
7
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
3
9
-
-
-
745919
Kupershmit
KDM4C (GASC1) lysine demethyl ...
Homo sapiens
Nucleic Acids Res.
42
6168-6182
2014
-
-
1
-
3
-
-
-
2
-
-
4
-
5
-
-
-
-
-
4
-
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5
1
-
-
-
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-
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-
-
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-
4
-
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4
-
-
-
-
-
4
-
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4
-
-
-
-
-
16
-
-
5
4
-
-
-
-
-
-
-
-
-
3
12
-
-
-
724709
Black
KDM4A lysine demethylase induc ...
Homo sapiens
Cell
154
541-555
2013
-
-
1
-
2
-
-
-
1
-
-
1
-
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
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1
-
-
-
-
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3
-
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1
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-
-
-
-
-
2
2
-
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-
724813
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