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Information on EC 2.1.1.368 - [histone H3]-lysine9 N-dimethyltransferase
for references in articles please use BRENDA:EC2.1.1.368
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.368 [histone H3]-lysine9 N-dimethyltransferase
IUBMB Comments
This entry describes several enzymes, characterized from plants, that successively methylate the L-lysine-9 residue of histone H3 (H3K9) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.367, [histone H3]-lysine9 N-methyltransferase, EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase, and EC 2.1.1.355, [histone H3]-lysine9 N-trimethyltransferase.
The enzyme appears in viruses and cellular organisms
- 2.1.1.368
-
suvar3-9
- chromatin
-
rna-directed
-
heterochromatinization
- methyltransferases
-
monomethylated
-
heterochromatic
-
chromatin-remodeling
-
redundantly
-
trimethylation
-
transposable
-
hmtases
-
heterochromatin-specific
-
dosage-dependent
-
chromocenter
-
microrchidia
- dnaj
Reaction Schemes
showSynonyms
suvh2, suvh1, suvr1, set13, set32, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EHMT2
G9a
GLP
KMT1C
SDG32
-
-
-
-
SET13
-
-
-
-
SET32
-
-
-
-
SUVH1
SUVR1
-
-
-
-
SUVH1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = 2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
overall reaction
-
-
-
S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
(1a)
-
-
-
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
(1b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-dimethyltransferase
This entry describes several enzymes, characterized from plants, that successively methylate the L-lysine-9 residue of histone H3 (H3K9) twice, ultimately generating a dimethylated form. These modifications influence the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.367, [histone H3]-lysine9 N-methyltransferase, EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase, and EC 2.1.1.355, [histone H3]-lysine9 N-trimethyltransferase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-methionine + [histone H3 peptide 1-15]-L-lysine9
S-adenosyl-L-homocysteine + [histone H3 peptide 1-15]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + [histone H3 peptide 1-15]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3 peptide 1-15]-N6,N6,N6-trimethyl-L-lysine9
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + [histone H3 peptide 1-15]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3 peptide 1-15]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: H3K9 methylation by SETDB1 occurs in a distributive manner
Products: -
Products: -
?
additional information
?
-
Substrates: SET1 methylates both K9 and less efficiently K27 of histone H3 in vitro, reactions of EC 2.1.1.368 and 2.1.1.371, respectively
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-methionine + [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
2 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
2 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[5-(2-methoxy-5-[[4-methyl-6-(methylamino)pyrimidin-2-yl]amino]phenyl)-2,3,4,7-tetrahydro-1H-azepin-1-yl]ethan-1-ol
-
4-[[4-methyl-6-(methylamino)pyrimidin-2-yl]amino]-2-(2,5,6,7-tetrahydro-1H-azepin-4-yl)benzonitrile
-
ATF7IP
SETDB1 partner protein. SETDB1 and the SETDB1:ATF7IP complex efficiently catalyze both monomethylation and dimethylation of H3K9 peptide substrates. The activity of the binary complex is 4fold lower than SETDB1 alone
-
N2-[3-(1-cyclobutyl-2,5,6,7-tetrahydro-1H-azepin-4-yl)-4-methoxyphenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[3-(1-ethyl-2,5,6,7-tetrahydro-1H-azepin-4-yl)-4-methoxyphenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[3-(azepan-4-yl)-4-methoxyphenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-(difluoromethoxy)-3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-chloro-3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-(1,2,3,6-tetrahydropyridin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-(1-methyl-1,2,3,6-tetrahydropyridin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-(1-methyl-1,2,5,6-tetrahydropyridin-3-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-(1-methyl-2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-(1-methyl-2,5-dihydro-1H-pyrrol-3-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-(2,3,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N2-[4-methoxy-3-[3-(pyrrolidin-1-yl)propoxy]phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
-
N4,6-dimethyl-N2-[3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)-4-(trifluoromethoxy)phenyl]pyrimidine-2,4-diamine
-
N4,6-dimethyl-N2-[4-methyl-3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]pyrimidine-2,4-diamine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.53
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C
0.54
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-N6-methyl-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C
0.56
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-N6-methyl-L-lysine9, pH 7.6, 23°C
0.68
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-L-lysine9, pH 7.6, 23°C
0.28
[histone H3 peptide 1-15]-L-lysine9
SETDB1:ATF7IP complex, pH 7.6, 23°C
-
0.41
[histone H3 peptide 1-15]-N6-methyl-L-lysine9
SETDB1:ATF7IP complex, pH 7.6, 23°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.072
S-adenosyl-L-methionine
substrate [histone H3 peptide 1-15]-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C
0.09
S-adenosyl-L-methionine
substrate [histone H3 peptide 1-15]-N6-methyl-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C
0.337
S-adenosyl-L-methionine
substrate [histone H3 peptide 1-15]-L-lysine9, pH 7.6, 23°C
0.352
S-adenosyl-L-methionine
substrate [histone H3 peptide 1-15]-N6-methyl-L-lysine9, pH 7.6, 23°C
0.027
[histone H3 peptide 1-15]-L-lysine9
SETDB1:ATF7IP complex, pH 7.6, 23°C
-
0.045
[histone H3 peptide 1-15]-N6-methyl-L-lysine9
SETDB1:ATF7IP complex, pH 7.6, 23°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.135
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C
0.167
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-N6-methyl-L-lysine9, SETDB1:ATF7IP complex, pH 7.6, 23°C
0.495
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-L-lysine9, pH 7.6, 23°C
0.628
S-adenosyl-L-methionine
substrate [histoneH3 peptide 1-15]-N6-methyl-L-lysine9, pH 7.6, 23°C
0.095
[histone H3 peptide 1-15]-L-lysine9
SETDB1:ATF7IP complex, pH 7.6, 23°C
-
0.11
[histone H3 peptide 1-15]-N6-methyl-L-lysine9
SETDB1:ATF7IP complex, pH 7.6, 23°C
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001586
2-[5-(2-methoxy-5-[[4-methyl-6-(methylamino)pyrimidin-2-yl]amino]phenyl)-2,3,4,7-tetrahydro-1H-azepin-1-yl]ethan-1-ol
Homo sapiens
pH and temperature not specified in the publication
0.0000432
4-[[4-methyl-6-(methylamino)pyrimidin-2-yl]amino]-2-(2,5,6,7-tetrahydro-1H-azepin-4-yl)benzonitrile
Homo sapiens
pH and temperature not specified in the publication
0.001066
N2-[3-(1-cyclobutyl-2,5,6,7-tetrahydro-1H-azepin-4-yl)-4-methoxyphenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000441
N2-[3-(1-ethyl-2,5,6,7-tetrahydro-1H-azepin-4-yl)-4-methoxyphenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.000342
N2-[3-(azepan-4-yl)-4-methoxyphenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000147
N2-[4-(difluoromethoxy)-3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000271
N2-[4-chloro-3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.001156
N2-[4-methoxy-3-(1,2,3,6-tetrahydropyridin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.000277
N2-[4-methoxy-3-(1-methyl-1,2,3,6-tetrahydropyridin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.000864
N2-[4-methoxy-3-(1-methyl-1,2,5,6-tetrahydropyridin-3-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0741
N2-[4-methoxy-3-(1-methyl-2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.002772
N2-[4-methoxy-3-(1-methyl-2,5-dihydro-1H-pyrrol-3-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.000479
N2-[4-methoxy-3-(2,3,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000323
N2-[4-methoxy-3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.000185
N2-[4-methoxy-3-[3-(pyrrolidin-1-yl)propoxy]phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.003801
N4,6-dimethyl-N2-[3-(2,5,6,7-tetrahydro-1H-azepin-4-yl)-4-(trifluoromethoxy)phenyl]pyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
SDG712 is highly expressed in leaves during reproductive growth stage with obvious circadian rhythmic pattern
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
physiological function
additional information
drug target
dimethylation of K9 at H3 is an important epigenetic modification that should be considered as a potential therapeutic target to treat nicotine reward and perhaps other drug addictions
drug target
the G9a-Sirt1 axis might be a therapeutic target for treatment of renal ischemia reperfusion injury
drug target
inhibition of H3K9 methyltransferase G9a could be a significant target for a brain tumor. A potent inhibitor of G9a could be a valuable target for hepatocellular carcinoma treatment. Inhibition/knockdown of G9a could be a significant target for ovarian cancers and cervical cancer
malfunction
loss of maternal EHMT1 results in prenatal developmental arrest
malfunction
-
mutation of SDG712 promotes rice flowering, while overexpression of SDG712 delays rice flowering
malfunction
silencing or suppression of G9a activity erases H3K9me2 from Sirt1 promoter and normalizes Sirt1 expression
physiological function
SET1 methylates both K9 and K27 of histone H3 in vitro. Ectopic expression of SET1 increases the amount of dimethylated H3K9 and induces chromosome-segregation defects in tobacco BY2 cells. The histone methyltransferase activity, the association with specific chromatin regions and with condensed chromosomes, and the cellular effects largely depend on the C-terminal region including the SET domain of the protein. The N-terminal part of SET1 is capable of targeting the green fluorescent protein to interphase chromatin. SET1 binds LHP1, the Arabidopsis homolog of animal heterochromatin protein 1, and LHP1 colocalizes with heterochromatin containing high amounts of dimethylated H3K9
physiological function
ectopic expression of SET1 causes an increase in methylated histone H3 lysine 9 and abnormal chromosome segregation in tobacco suspension cells, and inhibits tobacco plant growth. The inhibition of plant growth is caused by reduced cell expansion as well as by abnormal cell division and differentiation. Deletion of the C-terminally located catalytic domain of the protein abolishes the ectopic effects of SET1 on plant growth
physiological function
in SUVH2 null plants, mono- and dimethyl H3K9, mono- and dimethyl H3K27, and monomethyl H4K20 are significantly reduced. Loss of function suppresses, whereas overexpression enhances, gene silencing, causes ectopic heterochromatization and significant growth defects. Modification of transgene silencing by SUVH2 is partially transmitted to the offspring plants. This epigenetic stability correlates with heritable changes in DNA methylation. Mutational dissection of SUVH2 indicates an implication of its N-terminus and YDG domain in directing DNA methylation to target sequences. Gene silencing by SUVH2 depends on MET1 and DDM1, but not CMT3
physiological function
histone H3K9 methyltransferases G9a/KMT1C, GLP/KMT1D, SETDB1/KMT1E, and Suv39h1/KMT1A, coexist in the same megacomplex. In Suv39h or G9a null cells, the remaining histone H3K9 methyltransferases are destabilized at the protein level, indicating. The four enzymes are recruited to major satellite repeats, a known Suv39h1 genomic target, but also to multiple G9a target genes. The four H3K9 histone H3K9 methyltransferases display a functional cooperation in the regulation of known G9a target genes
physiological function
deletion of the catalytic domain of either histone methyltransferases EHMT2 or SETDB1 in growing oocytes leads to significant reduction of global H3K9me2 or H3K9me3 levels, respectively, in the maternal pronucleus. The asymmetry of global 5?methylcytosine (5mC) oxidation is significantly reduced in the zygotes that carry maternal mutation of either the Ehmt2 or Setdb1 genes. The levels of 5-hydroxymethylcytosine, 5-formylcytosine, and 5-carboxylcytosine increase, and 5mC levels decrease in the mutant maternal pronuclei. H3K9me3-rich rings around the nucleolar-like bodies retain 5mC in the maternal mutant zygotes. The maternal pronuclei expand in size in the mutant zygotes and contain a significantly increased number of nucleolar-like bodies compared with normal zygotes
physiological function
ectopic expression of SET1 increases the amount of dimethylated H3K9 and induces chromosome-segregation defects in tobacco BY2 cells. The histone methyltransferase activity, the association with specific chromatin regions and with condensed chromosomes, and the cellular effects largely depend on the C-terminal region including the SET domain of the protein. The N-terminal part of SET1 is capable of targeting the green fluorescent protein to interphase chromatin. SET1 binds LHP1, the Arabidopsis homolog of animal heterochromatin protein 1, and LHP1 colocalizes with heterochromatin containing high amounts of dimethylated H3K9
physiological function
SUVH1 acts as an anti-silencing factor and promotes the expression of several endogenous genes with promoter DNA methylation. SUVH1 mutation does not alter DNA methylation levels, thus, SUVH1 functions downstream of DNA methylation. Histone H3 lysine 4 trimethylation is reduced in a SUVH1 mutant, in contrast, H3K9 methylation levels remain unchanged
physiological function
SUVH1 binds methylated DNA in vitro, is associated with euchromatic methylation in vivo, and forms a complex with two DNAJ domain-containing homologs, DNAJ1 and DNAJ2. Ectopic recruitment of DNAJ1 enhances gene transcription
physiological function
EHMT1 is required for oocyte maturation and developmental competence. EHMT1 is a multifunctional repressive protein required for the appropriate establishment of the oocyte transcriptome, epigenome, and proteome. EHMT1 is critical for the developmental capacity of the oocyte, independent of EHMT2
physiological function
H3 methylation catalyzed by G9a/GLP is involved in nicotine-conditioned place preference induction. Dimethylation of K9 at H3 is an important epigenetic modification
physiological function
-
SDG712 is a negative flowering regulatory gene in rice, and it delays flowering through repressing key flowering regulator gene Ehd1 and the florigen genes Hd3a and RFT1. H3K9me2 levels at Hd3a and RFT1 loci are increased in SDG712 overexpression transgenic plants, indicating that SDG712 may mediate the H3K9 dimethylation on these loci to repress rice flowering
physiological function
G9a interacts with chromobox homolog 1 (CBX1) to catalyze H3K9 demethylation and forms a transcription repressor complex on the Sirt1 promoter, ultimately repressing Sirt1 transcription
physiological function
H3K9 methyltransferase G9a has a pivotal role in the development of embryos, cell growth, autophagy, adipogenesis, and other biological processes. Overexpression of G9a causes cell proliferation and metastasis in several human cancers, such as breast, ovarian, head and neck, gastric, colon, lung, bladder, liver, cervical, prostate, neuroendocrine tumors, and hematological malignancies. G9a-mediated H3K9 di-methylation silences the antioncogene genes, resulting in a potential increase in cancer cell proliferation
additional information
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SDG712 acts downstream of Hd1, while acts upstream of Ehd1, Hd3a and RFT1
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
renal ischemia reperfusion injury results in a rapid elevation of H3K9 histone methyltransferase G9a
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Naumann, K.; Fischer, A.; Hofmann, I.; Krauss, V.; Phalke, S.; Irmler, K.; Hause, G.; Aurich, A.C.; Dorn, R.; Jenuwein, T.; Reuter, G.
Pivotal role of AtSUVH2 in heterochromatic histone methylation and gene silencing in Arabidopsis
EMBO J.
24
1418-1429
2005
Arabidopsis thaliana (O22781)
brenda
Shen, W.H.; Meyer, D.
Ectopic expression of the NtSET1 histone methyltransferase inhibits cell expansion, and affects cell division and differentiation in tobacco plants
Plant Cell Physiol.
45
1715-1719
2004
Nicotiana tabacum (Q93YF5)
brenda
Yu, Y.; Dong, A.; Shen, W.H
Molecular characterization of the tobacco SET domain protein NtSET1 unravels its role in histone methylation, chromatin binding, and segregation
Plant J.
40
699-711
2004
Nicotiana tabacum (Q93YF5)
brenda
Basavapathruni, A.; Gureasko, J.; Porter Scott, M.; Hermans, W.; Godbole, A.; Leland, P.A.; Boriack-Sjodin, P.A.; Wigle, T.J.; Copeland, R.A.; Riera, T.V.
Characterization of the enzymatic activity of SETDB1 and its 1 1 complex with ATF7IP
Biochemistry
55
1645-1651
2016
Homo sapiens (Q15047)
brenda
Fritsch, L.; Robin, P.; Mathieu, J.R.; Souidi, M.; Hinaux, H.; Rougeulle, C.; Harel-Bellan, A.; Ameyar-Zazoua, M.; Ait-Si-Ali, S.
A subset of the histone H3 lysine 9 methyltransferases Suv39h1, G9a, GLP, and SETDB1 participate in a multimeric complex
Mol. Cell
37
46-56
2010
Homo sapiens (Q96KQ7), Homo sapiens (Q9H9B1)
brenda
Li, S.; Liu, L.; Li, S.; Gao, L.; Zhao, Y.; Kim, Y.J.; Chen, X.
SUVH1, a Su(var)3-9 family member, promotes the expression of genes targeted by DNA methylation
Nucleic Acids Res.
44
608-620
2016
Arabidopsis thaliana (Q9FF80)
brenda
Zeng, T.; Han, L.; Pierce, N.; Pfeifer, G.; Szabo, P.
EHMT2 and SETDB1 protect the maternal pronucleus from 5mC oxidation
Proc. Natl. Acad. Sci. USA
166
10834-10841
2019
Mus musculus (Q9Z148)
brenda
Harris, C.J.; Scheibe, M.; Wongpalee, S.P.; Liu, W.; Cornett, E.M.; Vaughan, R.M.; Li, X.; Chen, W.; Xue, Y.; Zhong, Z.; Yen, L.; Barshop, W.D.; Rayatpisheh, S.; Gallego-Bartolome, J.; Groth, M.; Wang, Z.; Wohlschlegel, J.A.; Du, J.; Rothbart, S.B.; Butter, F.; Jacobsen, S.E.
A DNA methylation reader complex that enhances gene transcription
Science
362
1182-1186
2018
Arabidopsis thaliana (Q9FF80), Arabidopsis thaliana
brenda
Katayama, K.; Ishii, K.; Tsuda, E.; Yotsumoto, K.; Hiramoto, K.; Suzuki, M.; Yasumatsu, I.; Igarashi, W.; Torihata, M.; Ishiyama, T.; Katagiri, T.
Discovery of novel histone lysine methyltransferase G9a/GLP (EHMT2/1) inhibitors Design, synthesis, and structure-activity relationships of 2,4-diamino-6-methylpyrimidines
Bioorg. Med. Chem. Lett.
30
127475
2020
Homo sapiens (Q9H9B1)
brenda
Liu, H.; Wang, W.; Weng, X.; Chen, H.; Chen, Z.; Du, Y.; Liu, X.; Wang, L.
The H3K9 histone methyltransferase G9a modulates renal ischemia reperfusion injury by targeting Sirt1
Free Radic. Biol. Med.
172
123-135
2021
Mus musculus (Q9Z148)
brenda
Demond, H.; Hanna, C.W.; Castillo-Fernandez, J.; Santos, F.; Papachristou, E.K.; Segonds-Pichon, A.; Kishore, K.; Andrews, S.; DSantos, C.S.; Kelsey, G.
Multi-omics analyses demonstrate a critical role for EHMT1 methyltransferase in transcriptional repression during oogenesis
Genome Res.
33
18-31
2023
Mus musculus (Q5DW34)
brenda
Rahman, Z.; Bazaz, M.R.; Devabattula, G.; Khan, M.A.; Godugu, C.
Targeting H3K9 methyltransferase G9a and its related molecule GLP as a potential therapeutic strategy for cancer
J. Biochem. Mol. Toxicol.
35
e22674
2021
Homo sapiens (Q9H9B1)
brenda
Faillace, M.; Ortiz, J.; Rocco, L.; Bernabeu, R.
Histone methyltransferase G9a plays an essential role on nicotine preference in zebrafish
Mol. Neurobiol.
61
6245-6263
2024
Danio rerio (A8TT22)
brenda
Zhang, S.; Hao, H.; Liu, X.; Li, Y.; Ma, X.; Liu, W.; Zheng, R.; Liang, S.; Luan, W.
SDG712, a putative H3K9-specific methyltransferase encoding gene, delays flowering through repressing the expression of florigen genes in rice
Rice (N.Y.)
14
73
2021
Oryza sativa
brenda
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