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Information on EC 2.1.1.355 - [histone H3]-lysine9 N-trimethyltransferase and Organism(s) Mus musculus and UniProt Accession Q9Z148
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2.1.1.355 [histone H3]-lysine9 N-trimethyltransferaseIUBMB Comments
This entry describes several enzymes that successively methylate the L-lysine9 residue of histone H3 (H3K9), ultimately generating a trimethylated 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 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.
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Word Map
- 2.1.1.355
- chromatin
-
trimethylation
- heterochromatin
-
zeste
-
h3k9me3
- leukemia
-
polycomb
- drosophila
- metastasis
-
euchromatic
- deacetylase
- hp1
- tumorigenesis
- demethylase
- nucleosomes
-
mixed-lineage
-
trithorax
-
self-renewal
- hdacs
-
variegation
-
pericentric
-
monomethylation
-
epigenome
-
chromodomain
-
chromatin-modifying
-
suvar3-9
-
histone-modifying
-
hypermethylation
-
corepressors
- medicine
- analysis
-
polytene
-
centromeres
- lys4
-
writer
-
telomeres
-
pericentromeric
- prdm16
-
di-methylation
-
chromatin-associated
-
leukemogenesis
-
subtelomeric
-
bromodomains
-
chip-seq
-
non-histone
-
menin
-
homeotic
-
weaver
- dnmt3a
-
h3k9ac
- prc1
-
chromatin-remodeling
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
histone methyltransferase, suv39h1, setdb1, ehmt2, su(var)3-9, ehmt1, prdm2, h3k9 methyltransferase, prdm8, histone methyltransferase g9a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EHMT1
-
-
-
-
G9a
KMT1A
-
-
-
-
KMT1B
-
-
-
-
KMT1C
-
-
-
-
KMT1D
-
-
-
-
KMT1F
-
-
-
-
MT8
-
-
-
-
PRDM2
-
-
-
-
SUV39H1
G9a
-
-
-
-
SUV39H1
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
H3-Lys9 methylation is catalyzed by the Suv39h family proteins
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-methyltransferase
This entry describes several enzymes that successively methylate the L-lysine9 residue of histone H3 (H3K9), ultimately generating a trimethylated 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 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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 + p53
?
the enzyme is responsible for p53 methylation at lysine 373
-
-
?
S-adenosyl-L-methionine + reptin
?
the enzyme is responsible for reptin methylation at lysine 67
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
?
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,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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 (S10phos)
?
-
phosphorylation of the proximal amino acids impairs Lys-9 methylation via impairing enzyme-substrate interaction
-
-
?
S-adenosyl-L-methionine + histone H3 (T11phos)
?
-
phosphorylation of the proximal amino acids impairs Lys-9 methylation via impairing enzyme-substrate interaction
-
-
?
S-adenosyl-L-methionine + histone H3(K27A)
?
-
mutation in the unstructured amino-terminal tail of histone H3 does not affect the central globular domain, but reduces the turnover numbers of the substrates
-
-
?
S-adenosyl-L-methionine + histone H3(K4A)
?
-
mutation in the unstructured amino-terminal tail of histone H3 does not affect the central globular domain, but reduces the turnover numbers of the substrates
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
S-adenosyl-L-homocysteine + ?
-
PRDM8 specifically methylates H3(K9) of histones
-
-
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
r
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]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-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]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
-
-
-
r
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
r
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 + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-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 + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
-
-
-
r
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
-
-
-
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Lys9 of histone H3
-
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Lys9 of histone 3
-
?
additional information
?
-
-
histone methylation has significant effects on heterochromatin formation and transcriptional regulation
-
-
?
additional information
?
-
-
minimal substrate methylated by G9a contains seven amino acids (TARKSTG) of the histone H3 tail
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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 + p53
?
the enzyme is responsible for p53 methylation at lysine 373
-
-
?
S-adenosyl-L-methionine + reptin
?
the enzyme is responsible for reptin methylation at lysine 67
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
?
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,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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 L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Lys9 of histone 3
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
overall reaction
-
-
r
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]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-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]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
-
-
-
r
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
r
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 + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-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 + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
-
-
-
r
additional information
?
-
-
histone methylation has significant effects on heterochromatin formation and transcriptional regulation
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
BIX-01294
diazepin-quinazolin-amine derivative, specific competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
PRDM8 of 30 kDa is expressed most prominently in cardiomyocytes from the heart
-
PRDM8 is expressed most prominently in striated skeletal muscle from the tongue
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the full-length of PRDM8 is localized exclusively in the nuclear region
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
physiological function
malfunction
enzyme depletion results in embryonic lethality with severe differentiation defects in embryonic stem cells. Enzyme depletion inhibits cell proliferation in several cancer cell lines
malfunction
inhibiting the methyltransferase activity of the enzyme aggravates lipopolysaccharide-induced liver damage
physiological function
the enzyme is essential for the repression of developmental genes and is required during development
physiological function
the enzyme is required for cardiomyocyte homeostasis in the adult heart by mediating the repression of key genes regulating cardiomyocyte function via dimethylation of H3 lysine 9 and interaction with enhancer of zeste homolog 2, the catalytic subunit of polycomb repressive complex 2, and MEF2C-dependent gene expression by forming a complex with this transcription factor. The enzyme-MEF2C complex is required for the maintenance of heterochromatin needed for the silencing of developmental genes in the adult heart. The enzyme promotes cardiac hypertrophy by repressing antihypertrophic genes
physiological function
the enzyme regulates chromatin reorganization in mouse oocytes. Maternal enzyme is vital for proper chromosome segregation in preimplantation embryos
malfunction
-
embryonic stem cells lacking the H3K9 HMTase G9a show a significant reduction in DNA methylation of retrotransposons, major satellite repeats and densely methylated CpG-rich promoters
malfunction
-
G9a deficiency causes loss of imprinting in the placenta but not the embryo
malfunction
-
lymphocyte development is unperturbed in G9a-deficient mice, G9a deficiency results in reduced usage of Iglambda L chains and a corresponding inhibition of Iglambda gene assembly in bone marrow precursors
malfunction
macrophage-specific enzyme-knockout mice exhibit higher serum interleukin-6 concentrations in response to lipopolysaccharide challenge and are more susceptible to endotoxin shock than wild type mice. Enzyme deficiency increases nuclear factor-kappaB p65 recruitment to the interleukin 6 promoter
physiological function
-
DNA methylation of retrotransposons in embryonic stem cells requires the lysine methyltransferase G9a but not its catalytic activity
physiological function
-
PRDM8 repressed the expression of steroidogenic markers, p450c17c and luteinizing hormone receptor, which indicates its regulatory role in mouse testis development and steroidogenesis
physiological function
the enzyme modulates myogenic gene expression and activation during skeletal muscle differentiation. The enzyme inhibits myoblast differentiation. The enzyme interacts with myocyte enhancer factor 2C directly and inhibits myocyte enhancer factor 2 transcription activity in a dose-dependent manner
physiological function
the enzyme regulates toll-like receptor 4-mediated inflammatory responses in macrophages. The enzyme is an epigenetic regulator of proinflammatory cytokine expression in macrophages. The enzyme suppresses transcriptional activity of interleukin 6 promoter
physiological function
Prdm3 and Prdm16 are redundant histone H3K9me1-specific methyltransferases that direct cytoplasmic H3K9me1 methylation. H3K9me1 is converted in the nucleus to H3K9me3 by the Suv39h enzyme to reinforce heterochromatin. Suv39h double null immortalized mouse embryonic fibroblasts are depleted for nuclear H3K9me3. Simultaneous depletion of Prdm3 and Prdm16 abrogates H3K9me1 methylation, prevents Suv39h-dependent H3K9me3 trimethylation, and derepresses major satellite transcription
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
-
the 30 kDa PRDM8 is most abundant in testis, heart, liver, and kidney, SDS-PAGE
70000
-
the 70 kDa full-length PRDM8 is most abundant in brain and testis, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
deltaSET
-
lacks the enzymatic activity in vitro, synergistic coactivator function observed with glucocorticoid receptor interacting protein 1, coactivator-associated arginine methyltransferase 1 is reduced but not eliminated
H1166K
-
lacks the enzymatic activity in vitro, synergistic coactivator function observed with glucocorticoid receptor interacting protein 1, coactivator-associated arginine methyltransferase 1 is reduced but not eliminated
additional information
additional information
-
G9a deficient embryos, drastically decreased activity in vivo
additional information
-
in G9a-/- embryonic stem cells, the increase in dimethylated histone H3 lysine 9 is significantly mitigated following hypoxia challenge
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PCR-amplified EcoRI-XhoI insert encoding the murine long form of G9a cloned into the EcoRI-XhoI sites of pSG5.HA and pSG5.FLAG, PCR-amplified EcoRI-SalI inserts of G9a residues 1-333, 72-333, 330-690, 685-1018, 936-1263 (deltaANK), 1-1088 (deltaSET), 730-1263, and 464-1263 cloned into the EcoRI-SalI sites of the vector pM for Gal4 DNA binding domain fusions and into the EcoRI-XhoI sites of pSG5.HA or pSG5.FLAG, expression in CV-1 and Cos-7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is overexpressed in a number of cancers, including esophageal squamous cell carcinoma, hepato-cellular carcinoma, aggressive lung cancer, brain cancer, multiple myeloma, and aggressive ovarian carcinoma
the expression of 70 kDa PRDM8 in brain and testis abruptly increases 3 weeks after birth
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
sequence context of modified residue affects G9a activity and modification in the proximal amino acids influences methylation
medicine
-
G9a plays an important role in the hypoxia-induced dimethylated histone H3 lysine 9, which inhibits the expression of several genes that likely leads to solid tumor progression
additional information
-
functions as a coactivator for nuclear receptors, cooperating synergistically with nuclear receptor coactivators glucocorticoid receptor interacting protein 1, coactivator-associated arginine methyltransferase 1, and p300 in transient transfection assays, synergy depends strongly on the arginine-specific protein methyltransferase activity of CARM1 but does not absolutely require the enzymatic activity of G9a and is specific to CARM1 and G9a among various protein methyltransferases, link between histone arginine and lysine methylation and a mechanism for controlling whether G9a functions as a corepressor or coactivator
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tachibana, M.; Sugimoto, K.; Nozaki, M.; Ueda, J.; Ohta, T.; Ohki, M.; Fukuda, M.; Takeda, N.; Niida, H.; Kato, H.; Shinkai, Y.
G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
Genes Dev.
16
1779-1791
2002
Mus musculus
Chin, H.G.; Pradhan, M.; Esteve, P.O.; Patnaik, D.; Evans, T.C.; Pradhan, S.
Sequence specificity and role of proximal amino acids of the histone H3 tail on catalysis of murine G9A lysine 9 histone H3 methyltransferase
Biochemistry
44
12998-13006
2005
Mus musculus
Chen, H.; Yan, Y.; Davidson, T.L.; Shinkai, Y.; Costa, M.
Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells
Cancer Res.
66
9009-9016
2006
Homo sapiens, Mus musculus
Lee, D.Y.; Northrop, J.P.; Kuo, M.H.; Stallcup, M.R.
Histone H3 lysine 9 methyltransferase G9a is a transcriptional coactivator for nuclear receptors
J. Biol. Chem.
281
8476-8485
2006
Mus musculus
Eom, G.H.; Kim, K.; Kim, S.M.; Kee, H.J.; Kim, J.Y.; Jin, H.M.; Kim, J.R.; Kim, J.H.; Choe, N.; Kim, K.B.; Lee, J.; Kook, H.; Kim, N.; Seo, S.B.
Histone methyltransferase PRDM8 regulates mouse testis steroidogenesis
Biochem. Biophys. Res. Commun.
388
131-136
2009
Mus musculus
Dong, K.B.; Maksakova, I.A.; Mohn, F.; Leung, D.; Appanah, R.; Lee, S.; Yang, H.W.; Lam, L.L.; Mager, D.L.; Schuebeler, D.; Tachibana, M.; Shinkai, Y.; Lorincz, M.C.
DNA methylation in ES cells requires the lysine methyltransferase G9a but not its catalytic activity
EMBO J.
27
2691-2701
2008
Mus musculus
Thomas, L.R.; Miyashita, H.; Cobb, R.M.; Pierce, S.; Tachibana, M.; Hobeika, E.; Reth, M.; Shinkai, Y.; Oltz, E.M.
Functional analysis of histone methyltransferase G9a in B and T lymphocytes
J. Immunol.
181
485-493
2008
Mus musculus
Wagschal, A.; Sutherland, H.; Woodfine, K.; Henckel, A.; Chebli, K.; Schulz, R.; Oakey, R.; Bickmore, W.; Feil, R.
G9a histone methyltransferase contributes to imprinting in the mouse placenta
Mol. Cell. Biol.
28
1104-1113
2008
Mus musculus
Zhang, Y.; Xue, W.; Zhang, W.; Yuan, Y.; Zhu, X.; Wang, Q.; Wei, Y.; Yang, D.; Yang, C.; Chen, Y.; Sun, Y.; Wang, S.; Huang, K.; Zheng, L.
Histone methyltransferase G9a protects against acute liver injury through GSTP1
Cell Death Differ.
27
1243-1258
2019
Mus musculus (Q9Z148), Mus musculus
Au Yeung, W.K.; BrindAmour, J.; Hatano, Y.; Yamagata, K.; Feil, R.; Lorincz, M.C.; Tachibana, M.; Shinkai, Y.; Sasaki, H.
Histone H3K9 methyltransferase G9a in oocytes is essential for preimplantation development but dispensable for CG methylation protection
Cell Rep.
27
282-293.e4
2019
Mus musculus (Q9Z148), Mus musculus
Papait, R.; Serio, S.; Pagiatakis, C.; Rusconi, F.; Carullo, P.; Mazzola, M.; Salvarani, N.; Miragoli, M.; Condorelli, G.
Histone methyltransferase G9a is required for cardiomyocyte homeostasis and hypertrophy
Circulation
136
1233-1246
2017
Mus musculus (Q9Z148), Mus musculus
Casciello, F.; Windloch, K.; Gannon, F.; Lee, J.S.
Functional role of G9a histone methyltransferase in cancer
Front. Immunol.
6
487
2015
Mus musculus (Q9Z148)
Jin, W.; Shang, Y.; Peng, J.; Jiang, S.
Histone H3 methyltransferase Suv39h1 prevents myogenic terminal differentiation by repressing MEF2 activity in muscle cells
Int. J. Mol. Sci.
17
1908
2016
Mus musculus (O54864)
Hachiya, R.; Shiihashi, T.; Shirakawa, I.; Iwasaki, Y.; Matsumura, Y.; Oishi, Y.; Nakayama, Y.; Miyamoto, Y.; Manabe, I.; Ochi, K.; Tanaka, M.; Goda, N.; Sakai, J.; Suganami, T.; Ogawa, Y.
The H3K9 methyltransferase Setdb1 regulates TLR4-mediated inflammatory responses in macrophages
Sci. Rep.
6
28845
2016
Mus musculus (Q96KQ7)
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 (O54864)
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