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Information on EC 2.1.1.367 - [histone H3]-lysine9 N-methyltransferase
for references in articles please use BRENDA:EC2.1.1.367
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.367 [histone H3]-lysine9 N-methyltransferase
IUBMB Comments
This entry describes several enzymes that methylate the L-lysine-9 residue of histone H3 (H3K9) only once, generating a monomethylated form. These modifications influence the binding of chromatin-associated proteins. cf. EC 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, EC 2.1.1.355, [histone H3]-lysine9 N-trimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.
The enzyme appears in viruses and cellular organisms
- 2.1.1.367
- adipose
- adipocytes
- obesity
-
thermogenesis
-
thermogenic
-
beige
-
adipogenesis
- myeloid
-
cidea
-
depot
-
high-fat
-
diet-induced
-
adipogenic
- preadipocytes
-
brown-like
-
adiposity
-
tmem26
-
inguinal
-
hfd-induced
-
ppargc1a
-
anti-obesity
-
fat-specific
- tfam
-
fat-like
-
cited1
-
adipocyte-specific
-
non-shivering
-
multilocular
-
interscapular
-
irisin
-
adipose-specific
Reaction Schemes
showSynonyms
prdm16, mecom, prdm3, suvh3, positive regulatory domain containing 16, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EHMT2
EHMT2 histone methyltransferases
G9a
GLP
histone methyltransferase G9a
KMT1C
PRDM16
PRDM3
PRDM16
-
-
-
-
PRDM3
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a [histone H3]-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
-
-
-
-
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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-methyltransferase
This entry describes several enzymes that methylate the L-lysine-9 residue of histone H3 (H3K9) only once, generating a monomethylated form. These modifications influence the binding of chromatin-associated proteins. cf. EC 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, EC 2.1.1.355, [histone H3]-lysine9 N-trimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.
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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
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-methionine + histone H3 peptide
S-adenosyl-L-homocysteine + [histone H3 peptide]-N6-methyl-L-lysine9
Substrates: amino acids 6-11 of histone H3
Products: -
Products: -
?
S-adenosyl-L-methionine + [histone H3 peptide 6-11]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3 peptide 6-11]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: PRDM16 is able to mono- and dimethylate H3K4 in nucleosomes, i.e. reaction of EC 2.1.1.370. No trimethylation of H3K4 or methylation of other lysine residues of H3 is detected
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: -
?
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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
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 + histone H3 peptide
S-adenosyl-L-homocysteine + [histone H3 peptide]-N6-methyl-L-lysine9
Substrates: amino acids 6-11 of histone H3
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
the cysteine-rich region adopts an unusual compact fold with four bound zinc atoms. The structure consists of a RING domain preceded by a smaller zinc-binding motif and an N-terminal segment. The smaller zinc-binding motif straddles the N-terminal end of the RING domain, and the N-terminal segment runs in an extended conformation along one side of the structure and interacts with both the smaller zinc-binding motif and the RING domain. The interface between the N-terminal segment and the RING domain includes one of the zinc atoms
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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
-
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-(1-methylpiperidin-4-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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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000213
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
0.0000152
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
0.000145
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
0.0000105
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
0.0000282
N2-[3-(azepan-4-yl)-4-methoxyphenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.00000325
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
0.00000632
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
0.000225
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
0.0000929
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
0.000451
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
0.0000151
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
0.001494
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
0.000588
N2-[4-methoxy-3-(1-methylpiperidin-4-yl)phenyl]-N4,6-dimethylpyrimidine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000833
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
0.0000431
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
0.0000169
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
0.000853
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
PRDM16 is specifically expressed in ventricular but not atrial cardiomyocytes, and its expression declines postnatall
brenda
additional information
additional information
broadly expressed during plant development with the highest levels found in proliferating cells
brenda
additional information
-
broadly expressed during plant development with the highest levels found in proliferating cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
localizes in subnuclear foci and remains associated with condensed chromosomes throughout mitosis
brenda
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
Prdm16 localizes at the nuclear lamina where it cooperates with the H3K9 methyltransferases G9a/GLP to mediate tethering and silencing of myogenic genes, thus repressing an alternative myogenic fate in fibro-adipogenic progenitors. Genetic and pharmacological disruption of this repressive pathway confers to fibro-adipogenic progenitor myogenic competence, preventing fibro-adipogenic degeneration of dystrophic muscles
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
drug target
EHMT2 (G9a) inhibition mitigates tumorigenicity in Myc-driven liver cancer. Targeting G9a could prove to be a potential therapeutic avenue for Myc-driven liver cancer
malfunction
pathogenic mutations in humans lead to cardiomyopathy, conduction abnormalities, and heart failure. Cardiomyocyte-specific deletion of Prdm16 during cardiac development results in contractile dysfunction and abnormal electrophysiology of the postnatal heart, resulting in premature death. Myocardial loss of PRDM16 during development resulted in hyperplasia of the (distal) ventricular conduction system
malfunction
embryos from oocytes in which Ehmt2 is ablated at the same time of oocyte growth are less affected, and some develop normally into healthy pups
malfunction
EHMT2 depletion elevates the expression of zygotic genome activation-associated transcripts in 2-cell-like cells and synergizes with spliceosome inhibition and retinoic acid signaling in facilitating the mouse embryonic stem cell-to-2CLC transition
malfunction
the maternal allele of noncanonical imprinted genes is derepressed from its endogenous retrovirus-K promoter in the Ehmt2-/- ectoplacental cone. In Ehmt2-/- embryos, loss of DNA methylation accompanied biallelic derepression of the ERVK promoters. Canonical imprinting and imprinted X chromosome inactivation are generally undisturbed
malfunction
loss of maternal EHMT1 results in prenatal developmental arrest
physiological function
Prdm3 and Prdm16 are redundant histone H3K9me1-specific methyltransferases that direct cytoplasmic H3K9me1 methylation. The H3K9me1 is converted in the nucleus to H3K9me3 by the Suv39h enzymes to reinforce heterochromatin. Simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription. Combined impairment of Prdm3 and Prdm16 results in disintegration of heterochromatic foci and disruption of the nuclear lamina
physiological function
SUVH3 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
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
overexpression of the PR domain of PRDM16 represses the differentiation of porcine preadipocytes. Overexpression of the PR domain significantly increases the level of lipolysis and mitochondrial oxidative capacity during differentiation. The protein coded by the PR domain has H3K9me1 methyltransferase activity
physiological function
PRDM16 is a histone H3 K9 methyltransferase on chromatin. Mutation in the N-terminal PR-domain of PRDM16 completely abolishes the intrinsic enzymatic activity of PRDM16. The methyltransferase activity of PRDM16 is required for specific suppression of mixed lineage leukemia leukemogenesis both in vitro and in vivo. PRDM16 directly activates the SNAG family transcription factor GFI1b, which in turn down regulates the HOXA gene cluster. Knockdown GFI1b represses PRDM16-mediated tumor suppression while GFI1b overexpression mimics PRDM16 overexpression. Silencing PRDM16 by DNA methylation is concomitant with mixed lineage leukemia MLL-AF9 induced leukemic transformation
physiological function
A5XCD6
loss of Prdm3 or Prdm16 in zebrafish causes craniofacial defects including hypoplasia of the craniofacial cartilage elements, undefined posterior ceratobranchials, and decreased mineralization of the parasphenoid. Prdm3 and Prdm16 compensate for each other as well as a Prdm1a. Combinatorial loss of Prdm1a, Prdm3, and Prdm16 alleles results in severe hypoplasia of the anterior cartilage elements, abnormal formation of the jaw joint, complete loss of the posterior ceratobranchials, and clefting of the ethmoid plate. Loss of Prdm3 and Prdm16 reduces methylation of histone 3 lysine 9 (repression) and histone 3 lysine 4 (activation) in zebrafish
physiological function
loss of Prdm16 causes craniofacial defects including anterior mandibular hypoplasia, clefting in the secondary palate and severe middle ear defects. Loss of Prdm16 significantly decreases histone 3 lysine 9 methylation in the palatal shelves but does not change histone 3 lysine 4 methylation
physiological function
simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription. Combined impairment of Prdm3 and Prdm16 results in disintegration of heterochromatic foci and disruption of the nuclear lamina
physiological function
PRDM16 determines specification of ventricular cardiomyocytes by suppressing alternative cell fates. PRDM16 plays an indispensable role during cardiac development by driving ventricular working cardiomyocyte identity
physiological function
Prdm16 as a nuclear envelope protein that anchors H3K9-methylated chromatin in a cell-specific manner. Prdm16 mediates fibro-adipogenic progenitor developmental capacities by orchestrating lamina-associated domain organization and heterochromatin sequestration at the nuclear periphery
physiological function
EZH2/EHMT2 catalyzes H3K27me3/H3K9me2 to inhibit the transcription of DLX5, thus promoting the transformation from myelodysplastic syndrome to acute myeloid leukemia
physiological function
EZH2/EHMT2 catalyzes H3K27me3/H3K9me2 to inhibit the transcription of DLX5, thus promoting the transformation from myelodysplastic syndrome to acute myeloid leukemia
physiological function
overexpression of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase effectively prevents development of cholangiocarcinoma. NAD+-dependent 15-hydroxyprostaglandin dehydrogenase is epigenetically silenced by histone methyltransferase G9a. The G9a-15PGDH signaling axis is importantly implicated in cholangiocarcinoma development and progression
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
physiological function
EHMT2 is predominantly required for H3K9me2 in oogenesis. EHMT2 can be partially compensated by EHMT1
physiological function
EHMT2 attenuates the bidirectional differentiation potential of mouse pluripotent stem cells and defines molecular modes for locus-specific transcriptional repression by this essential histone methyltransferase
physiological function
EHMT2 is essential for repressing the maternal allele in noncanonical imprinting
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
the enzyme regulates gene expression and is essential for development and the ability of organisms to change and adapt
physiological function
overexpression of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase effectively prevents development of cholangiocarcinoma. NAD+-dependent 15-hydroxyprostaglandin dehydrogenase is epigenetically silenced by histone methyltransferase G9a. The G9a-15PGDH signaling axis is importantly implicated in cholangiocarcinoma development and progression
Show AA Sequence and Transmembrane Helices (2249 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop method. The structure of the cysteine-rich region from human EHMT2 is determined by X-ray crystallography. The cysteine-rich region adopts an unusual compact fold with four bound zinc atoms. The structure consists of a RING domain preceded by a smaller zinc-binding motif and an N-terminal segment. The smaller zinc-binding motif straddles the N-terminal end of the RING domain, and the N-terminal segment runs in an extended conformation along one side of the structure and interacts with both the smaller zinc-binding motif and the RING domain. The interface between the N-terminal segment and the RING domain includes one of the zinc atoms
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an intron located in the 5'-UTR is a key regulator of strong and constitutive SUVH3 expression
EHMT2 (G9a) is frequently overexpressed in many cancer types, including hepatocellular carcinoma. Hepatocellular carcinoma patients with higher c-Myc and G9a expression levels portend a poorer survival with lower median survival months
EHMT2 is promoted in both myelodysplastic syndrome patients and melodysplastic syndrome/acute myeloid leukemia patients
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pinheiro, I.; Margueron, R.; Shukeir, N.; Eisold, M.; Fritzsch, C.; Richter, F.M.; Mittler, G.; Genoud, C.; Goyama, S.; Kurokawa, M.; Son, J.; Reinberg, D.; Lachner, M.; Jenuwein, T.
Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian heterochromatin integrity
Cell
150
948-960
2012
Mus musculus (P14404), Mus musculus (A2A935), Mus musculus
brenda
Gu, T.; Xu, G.; Jiang, C.; Hou, L.; Wu, Z.; Wang, C.
PRDM16 represses the pig white lipogenesis through promoting lipolysis activity
BioMed Res. Int.
2019
1969413
2019
Sus scrofa (I3L9C5), Sus scrofa
brenda
Shull, L.C.; Sen, R.; Menzel, J.; Goyama, S.; Kurokawa, M.; Artinger, K.B.
The conserved and divergent roles of Prdm3 and Prdm16 in zebrafish and mouse craniofacial development
Dev. Biol.
461
132-144
2020
Danio rerio (A5XCD6), Danio rerio, Mus musculus (A2A935), Mus musculus
brenda
Casas-Mollano, J.A.; Lao, N.T.; Kavanagh, T.A.
Intron-regulated expression of SUVH3, an Arabidopsis Su(var)3-9 homologue
J. Exp. Bot.
57
3301-3311
2006
Arabidopsis thaliana (Q9C5P4), Arabidopsis thaliana
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
Zhou, B.; Wang, J.; Lee, S.Y.; Xiong, J.; Bhanu, N.; Guo, Q.; Ma, P.; Sun, Y.; Rao, R.C.; Garcia, B.A.; Hess, J.L.; Dou, Y.
PRDM16 suppresses MLL1r leukemia via intrinsic histone methyltransferase activity
Mol. Cell
62
222-236
2016
Homo sapiens (Q9HAZ2)
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 (Q9C5P4), 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 (Q96KQ7)
brenda
Chatterjee, K.; Uyehara, C.M.; Kasliwal, K.; Madhuranath, S.; Scourzic, L.; Polyzos, A.; Apostolou, E.; Stadtfeld, M.
Coordinated repression of totipotency-associated gene loci by histone methyltransferase EHMT2 through binding to LINE-1 regulatory elements
bioRxiv
FEHLT
0000
2024
Mus musculus (Q9Z148)
brenda
Zeng, T.B.; Pierce, N.; Liao, J.; Szabo, P.E.
H3K9 methyltransferase EHMT2/G9a controls ERVK-driven noncanonical imprinted genes
Epigenomics
13
1299-1314
2021
Mus musculus (Q9Z148)
brenda
Zheng, Z.; Li, L.; Li, G.; Zhang, Y.; Dong, C.; Ren, F.; Chen, W.; Ma, Y.
EZH2/EHMT2 histone methyltransferases inhibit the transcription of DLX5 and promote the transformation of myelodysplastic syndrome to acute myeloid leukemia
Front. Cell Dev. Biol.
9
619795
2021
Homo sapiens (Q96KQ7), 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 (Q9Z148), 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
Kerchner, K.M.; Mou, T.C.; Sun, Y.; Rusnac, D.V.; Sprang, S.R.; Briknarova, K.
The structure of the cysteine-rich region from human histone-lysine N-methyltransferase EHMT2 (G9a)
J. Struct. Biol. X
5
100050
2021
Homo sapiens (Q96KQ7)
brenda
Van Wauwe, J.; Mahy, A.; Craps, S.; Ekhteraei-Tousi, S.; Vrancaert, P.; Kemps, H.; Dheedene, W.; Donate Puertas, R.; Trenson, S.; Roderick, H.L.; Beerens, M.; Luttun, A.
PRDM16 determines specification of ventricular cardiomyocytes by suppressing alternative cell fates
Life Sci. Alliance
7
e202402719
2024
Homo sapiens (Q9HAZ2)
brenda
Zhang, J.; Chen, W.; Ma, W.; Song, K.; Lee, S.; Han, C.; Wu, T.
Epigenetic silencing of 15-hydroxyprostaglandin dehydrogenase by histone methyltransferase EHMT2/G9a in cholangiocarcinoma
Mol. Cancer Res.
20
350-360
2022
Mus musculus (Q9Z148), Homo sapiens (Q96KQ7)
brenda
Thng, D.K.H.; Hooi, L.; Toh, C.C.M.; Lim, J.J.; Rajagopalan, D.; Syariff, I.Q.C.; Tan, Z.M.; Rashid, M.B.M.A.; Zhou, L.; Kow, A.W.C.; Bonney, G.K.; Goh, B.K.P.; Kam, J.H.; Jha, S.; Dan, Y.Y.; Chow, P.K.H.; Toh, T.B.; Chow, E.K.
Histone-lysine N-methyltransferase EHMT2 (G9a) inhibition mitigates tumorigenicity in Myc-driven liver cancer
Mol. Oncol.
17
2275-2294
2023
Homo sapiens (Q96KQ7)
brenda
Biferali, B.; Bianconi, V.; Perez, D.F.; Kronawitter, S.P.; Marullo, F.; Maggio, R.; Santini, T.; Polverino, F.; Biagioni, S.; Summa, V.; Toniatti, C.; Pasini, D.; Stricker, S.; Di Fabio, R.; Chiacchiera, F.; Peruzzi, G.; Mozzetta, C.
Prdm16-mediated H3K9 methylation controls fibro-adipogenic progenitors identity during skeletal muscle repair
Sci. Adv.
7
eabd9371
2021
Mus musculus (A2A935)
brenda
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