Literature summary for 1.14.11.69 extracted from

Lin, C.H.; Li, B.; Swanson, S.; Zhang, Y.; Florens, L.; Washburn, M.P.; Abmayr, S.M.; Workman, J.L.
Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase (2008), Mol. Cell, 32, 696-706.

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Activating Compound

Activating Compound	Comment	Organism	Structure
ascorbate	required	Drosophila melanogaster
HP1 a protein	HP1a, encoded by the Su(var)2-5 gene and involved in the establishment and maintenance of higher-order structure of heterochromatin, stimulates the histone H3K36 demethylation activity of dKDM4A, and this stimulation depends on the H3K9me-binding motif of HP1a. HP1a and dKDM4A interact with each other, and loss of HP1a leads to an increased level of histone H3K36me3. The CSD of HP1a and a consensus HP1-interacting PxVxL motif in dKDM4A are responsible for the HP1a-dKDM4A interaction	Drosophila melanogaster

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant dKDM4A in Spodoptera frugiperda Sf21 cells using baculovirus transfection	Drosophila melanogaster

Protein Variants

Protein Variants	Comment	Organism
H195A	construction of a mutant dKDM4A in which a conserved amino acid in the iron-binding site is mutated to alanine, the mutant dKDM4A has no demethylation activity on histones H3K36me3 and H3K36me2	Drosophila melanogaster
additional information	construction of a P-element insertion mutant of dKDMA4, the mutant is homozygous viable, the P element insertion elevates the bulk level of histone H3K36me3 in mutant embryos. Overexpression of dKDM4A seems to only lead to demethylation of histone H3K36, since the level of histone H3K9me3 and H3K4me2 remains unchanged	Drosophila melanogaster

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	required for the catalytic activity	Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Drosophila melanogaster	HP1a and dKDM4A interact with each other and loss of HP1a leads to an increased level of histone H3K36me3	?	-	?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2	Drosophila melanogaster	histone H3K36 methylation is enriched in coding regions of actively transcribed genes. dKDM4A is a JmjC domain-containing protein specifically demethylates H3K36me2 and H3K36me3 both in vitro and in vivo. H3K36 methylation is also subject to dynamic regulation. HP1a regulates histone H3K36 methylation in Drosophila larvae	[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	Q9V333	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	HP1a and dKDM4A interact with each other and loss of HP1a leads to an increased level of histone H3K36me3	Drosophila melanogaster	?	-	?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2	histone H3K36 methylation is enriched in coding regions of actively transcribed genes. dKDM4A is a JmjC domain-containing protein specifically demethylates H3K36me2 and H3K36me3 both in vitro and in vivo. H3K36 methylation is also subject to dynamic regulation. HP1a regulates histone H3K36 methylation in Drosophila larvae	Drosophila melanogaster	[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2	-	?
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2	with HeLa cell core histone 3. dKDM4A is a JmjC domain-containing protein specifically demethylates H3K36me2 and H3K36me3 both in vitro and in vivo. The demethylation reaction mediated by dKDM4A requires Fe2+, 2-oxoglutarate, and ascorbate as cofactors	Drosophila melanogaster	[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2	-	?

Synonyms

Synonyms	Comment	Organism
KDM4A demethylase	-	Drosophila melanogaster

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Release 2023.1 (January 2023)