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Literature summary for 1.14.11.65 extracted from

  • Lan, F.; Shi, Y.
    Epigenetic regulation: methylation of histone and non-histone proteins (2009), Sci. China C Life Sci., 52, 311-322.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
HP1a Suv(Var)3-9/KMT1 interacts with HP1 that binds [histone H3]-N6,N6-trimethyl-L-lysine9 Drosophila melanogaster

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Drosophila melanogaster dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information ?
-
?
additional information Schizosaccharomyces pombe dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information ?
-
?
additional information Drosophila melanogaster dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information. Upon stimulation, the bivalent domains segregate into either H3K4me3- or H3K27me3 marked genes for activation and repression, respectively ?
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2 Drosophila melanogaster
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[histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 Drosophila melanogaster LSD1 is associated with protein BHC80. Upon demethylation of H3K4me2 to H3K4me0 by LSD1/KDM1, BHC80 binds the demethylation product H3K4me0 to maintain LSD1/KDM1 at target loci and to prevent re-methylation of H3K4 [histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2 Schizosaccharomyces pombe propagation of the silencing mark, H3K9me3, at the centromeric and Mating type regions requires the RNAi machinery and DNA recognition factors [histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
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?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2 Drosophila melanogaster the lysine methylase complexes recognize its own reaction products. The H3K9me2 methylases G9A/KMT1C and GLP/KMT1D, can also bind to their reaction product H3K9me2 via their ankyrin repeat domains [histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-
Schizosaccharomyces pombe
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information Drosophila melanogaster ?
-
?
additional information dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information Schizosaccharomyces pombe ?
-
?
additional information dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information. Upon stimulation, the bivalent domains segregate into either H3K4me3- or H3K27me3 marked genes for activation and repression, respectively Drosophila melanogaster ?
-
?
[histone H3]-N6,N6,N6-trimethyl-L-lysine4 + 3 2-oxoglutarate + 3 O2
-
Drosophila melanogaster [histone H3]-L-lysine4 + 3 succinate + 3 formaldehyde + 3 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
-
Drosophila melanogaster [histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 LSD1 is associated with protein BHC80. Upon demethylation of H3K4me2 to H3K4me0 by LSD1/KDM1, BHC80 binds the demethylation product H3K4me0 to maintain LSD1/KDM1 at target loci and to prevent re-methylation of H3K4 Drosophila melanogaster [histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
-
Drosophila melanogaster [histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2
-
Schizosaccharomyces pombe [histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2 propagation of the silencing mark, H3K9me3, at the centromeric and Mating type regions requires the RNAi machinery and DNA recognition factors Schizosaccharomyces pombe [histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
?
[histone H3]-N6,N6-dimethyl-L-lysine9 + 2 2-oxoglutarate + 2 O2 the lysine methylase complexes recognize its own reaction products. The H3K9me2 methylases G9A/KMT1C and GLP/KMT1D, can also bind to their reaction product H3K9me2 via their ankyrin repeat domains Drosophila melanogaster [histone H3]-L-lysine9 + 2 succinate + 2 formaldehyde + 2 CO2
-
?

Synonyms

Synonyms Comment Organism
G9A/KMT1C
-
Drosophila melanogaster
GLP/KMT1D
-
Drosophila melanogaster
H3K4me2 demethylase
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Drosophila melanogaster
H3K9me2 methylase
-
Drosophila melanogaster
H3K9me3 methylase
-
Drosophila melanogaster
KDM1
-
Drosophila melanogaster
LSD1
-
Drosophila melanogaster
LSD1/KDM1
-
Drosophila melanogaster
Suv(Var)3-9/KMT1
-
Drosophila melanogaster

General Information

General Information Comment Organism
physiological function histone methylation at H3K9 and demethylation at H3K4 play a role in the recruitment of DNA methylases. Co-existence of H3K4me3, an active methyl mark, and H3K27me3, a repressive mark, on developmentally important genes in stem cells Drosophila melanogaster