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Literature summary for 1.14.11.69 extracted from

  • Lloret-Llinares, M.; Carre, C.; Vaquero, A.; de Olano, N.; Azorin, F.
    Characterization of Drosophila melanogaster JmjC+N histone demethylases (2008), Nucleic Acids Res., 36, 2852-2863 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene CG15835 or Kdm4A, sequence comparisons, recombinant overexpression of FLAG-tagged wild-type and mutant enzymes in S2 cells Drosophila melanogaster
gene CG33182, sequence comparisons, recombinant overexpression of FLAG-tagged enzyme in S2 cells Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
H195A site-directed mutagenesis, mutation of an Fe2+ binding residue, abolishes demethylase activity of dJMJD2(1)/CG15835 Drosophila melanogaster
additional information construction of transgenic lines carrying a UASGAL4-CG15835-Flag construct, where expression of dJMJD2(1)/CG15835 is under the control of the yeast activator GAL4, allowing its overexpression upon crossing with lines expressing GAL4. Overexpression of CG15835 results in spreading of HP1 into euchromatin and a strong decrease on the levels of H3K9me3 and H3K36me3 Drosophila melanogaster

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required for catalytic activity Drosophila melanogaster
Fe2+ required for catalytic activity. The coordination of Fe(II) involves residues H195, E197 and H223 Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2 Drosophila melanogaster
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[histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2 Drosophila melanogaster
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[histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q9V333
-
-
Drosophila melanogaster Q9V6L0
-
-

Source Tissue

Source Tissue Comment Organism Textmining
larva
-
Drosophila melanogaster
-
salivary gland
-
Drosophila melanogaster
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information dJMJD2(1)/CG15835 is capable of demethylating H3K9me3 and H3K36me3 Drosophila melanogaster ?
-
?
additional information dJMJD2(2)/CG33182 is capable of demethylating H3K9me3 and H3K36me3 Drosophila melanogaster ?
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine 36 + 2-oxoglutarate + O2
-
Drosophila melanogaster [histone H3]-N6,N6-dimethyl-L-lysine 36 + succinate + formaldehyde + CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine 36 + 2-oxoglutarate + O2
-
Drosophila melanogaster [histone H3]-N6-methyl-L-lysine 36 + succinate + formaldehyde + CO2
-
?

Synonyms

Synonyms Comment Organism
CG15835
-
Drosophila melanogaster
CG33182
-
Drosophila melanogaster
KDM4A
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Drosophila melanogaster
KDM4B
-
Drosophila melanogaster
LD33386
-
Drosophila melanogaster
More see also EC 1.14.11.66 Drosophila melanogaster

General Information

General Information Comment Organism
evolution enzyme CG15835 shows higher identity to mammalian JMJD2D (40%) than to any of the other mammalian JMJD2 isoforms (22%) Drosophila melanogaster
evolution enzyme CG33182 shows higher identity to mammalian JMJD2D (40%) than to any of the other mammalian JMJD2 isoforms (22%) Drosophila melanogaster
malfunction overexpression of CG15835 results in spreading of HP1 into euchromatin and a strong decrease on the levels of H3K9me3 and H3K36me3, while the levels of H3K4me3 and H3K27me3 are not significantly altered. Demethylase activity of dJMJD2(1)/CG15835 depends on the JmjC domain, as it is abolished by mutations that affect its catalytic activity. The single-point mutation H195A, mutating one of the Fe2+ binding residues, abolishes demethylase activity of dJMJD2(1)/CG15835 Drosophila melanogaster
physiological function H3K36me3 acts as a barrier that prevents spreading of HP1 into euchromatin. Both H3K36 and H3K4 methylation associate to actively transcribed genes, suggesting that gene activity is a main determinant to delimit hetero- and euchromatic territories Drosophila melanogaster
physiological function H3K36me3 acts as a barrier that prevents spreading of HP1 into euchromatin. Both H3K36 and H3K4 methylation associate to actively transcribed genes, suggesting that gene activity is a main determinant to delimit hetero- and euchromatic territories. dJMJD2(1)/CG15835 influences heterochromatin organization, but is excluded from heterochromatin. Overexpression of dJMJD2(1)/CG15835 does not affect the pattern of H3K9me2,3 at heterochromatin. dJMJD2(1)/CG15835 localizes to multiple euchromatic sites, where it mostly regulates H3K36me3, as its overexpression results in a strong decrease in the levels of H3K36me3. dJMJD2(1)/CG15835 regulates spreading of HP1 Drosophila melanogaster