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Information on EC 2.1.1.355 - [histone H3]-lysine9 N-trimethyltransferase
for references in articles please use BRENDA:EC2.1.1.355
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.355 [histone H3]-lysine9 N-trimethyltransferase
IUBMB 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.
The enzyme appears in viruses and cellular organisms
- 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
Reaction Schemes
showSynonyms
histone methyltransferase, suv39h1, setdb1, ehmt2, su(var)3-9, ehmt1, prdm2, h3k9 methyltransferase, prdm8, histone methyltransferase g9a, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Clr4
Dim-5
Dim5
EC 2.1.1.43
-
-
formerly, part transferred
-
EHMT1
-
-
-
-
EHMT2
ESET
FmKmt1
G9a
G9a histone methyltransferase
GLP
H3K9 histone methyltransferase
H3K9 methyltransferase
H3K9-specific histone methyltransferase
histone H3 lysine 9 methyltransferase
histone H3K9 methyltransferase
histone lysine methyltransferase
histone methyltransferase
histone methyltransferase G9a
HKMT
HMTase
KHMTase
KMT1A
KMT1B
-
-
-
-
KMT1C
KMT1D
-
-
-
-
KMT1F
-
-
-
-
MT8
-
-
-
-
PRDM2
-
-
-
-
SETDB1
SU(VAR)3-9
SUV39H1
SUV39H1 histone methyltransferase
Suv39h2
Trire2_111216
G9a
-
-
-
-
KMT1A
-
-
-
-
KMT1C
-
-
-
-
SUV39H1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
(1a)
-
-
-
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
(1c)
-
-
-
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9 = S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
(1b)
-
-
-
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
enzyme is encoded on genes containing the SET-domain sequence, substrate specificity is connected to SET sequence
-
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
SET structure
-
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
-
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
-
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
-
-
-
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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.
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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
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + biotinylated [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + biotinylated [histone H3]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
?
biotinyl-MARTKQTARKSTGGKAPRKQ + S-adenosyl-L-methionine
?
-
Substrates: Dim-5 methylates the histone H3 tail at position Lys9
Products: -
Products: -
?
L-lysyl9-[histone H3] + 3 S-adenosyl-L-methionine
N6,N6,N6-trimethyl-L-lysyl9-[histone H3] + 3 S-adenosyl-L-homocysteine
Substrates: -
Products: -
Products: -
?
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 + dimethylated histone H3(K9)
S-adenosyl-L-homocysteine + trimethylated histone H3(K9)
-
Substrates: the activity on dimethylated histone H3(K9) peptides is several folds lower than when monomethylated histone H3(K9) peptides are used
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA methyltransferase 1
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + H2B ubiquitinated nucleosome
?
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H2A
S-adenosyl-L-homocysteine + ?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H2B
S-adenosyl-L-homocysteine + ?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3 (S10phos)
?
-
Substrates: phosphorylation of the proximal amino acids impairs Lys-9 methylation via impairing enzyme-substrate interaction
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3 (T11phos)
?
-
Substrates: phosphorylation of the proximal amino acids impairs Lys-9 methylation via impairing enzyme-substrate interaction
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3(K27A)
?
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3(K4A)
?
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H4
S-adenosyl-L-homocysteine + ?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone K4-trimethylK9
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
S-adenosyl-L-methionine + monomethylated histone H3(K9)
S-adenosyl-L-homocysteine + trimethylated histone H3(K9)
-
Substrates: the SUVR4 product specificity shifts from di- to trimethylation in the presence of free ubiquitin. SUVR4 in vivo specifically converts monomethylated histone H3(K9) to trimethylated histone H3(K9) at transposons and pseudogenes
Products: -
Products: -
?
S-adenosyl-L-methionine + p53
?
Substrates: the enzyme is responsible for p53 methylation at lysine 373
Products: -
Products: -
?
S-adenosyl-L-methionine + reptin
?
Substrates: the enzyme is responsible for reptin methylation at lysine 67
Products: -
Products: -
?
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,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-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: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: Su(var)3-9 is a di- and trimethyltransferase of H3K9
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: activity toward histones in chromatin. SUV39H1 trimethylates H3K9, thereby creating a binding site for HP1, which recruits SUV4-20H. This enzyme generates H4K20me3 using as a substrate the H4K20me1 generated by SET8. Consequently, SUV39H1 indirectly affects the methylation of H4K20 via two pathways: it modifies SET8, thereby enhancing its activity, and creates a site for the binding of SUV4-20H
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: activity toward histones in chromatin
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
r
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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]-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]-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]-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]-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]-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]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: preferred substrate
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: the enzyme introduce H3K9me3 at pericentric heterochromatin
Products: -
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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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
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
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: -
?
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: -
?
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: -
?
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: -
?
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: the enzyme introduce H3K9me3 at pericentric heterochromatin
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: -
?
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: -
?
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: -
r
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 + histone H3(K9)
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3(K9)
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3(K9)
?
-
Substrates: Dim-5 recognizes R8-G12 of the H3 tail with T11 and G12 being the most important specificity determinants, phosphorylation of H3 tail residues S10 and T11may regulate the activity of Dim-5
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3(K9)
S-adenosyl-L-homocysteine + ?
-
Substrates: SETDB1 is mainly responsible for mono- and trimethylation of histone H3 lysine 9 and SU (VAR)3-9 for monomethylation of histone H3 lysine 9 during spermatogenesis
Products: -
Products: -
?
S-adenosyl-L-methionine + histone H3(K9)
S-adenosyl-L-homocysteine + ?
-
Substrates: PRDM8 specifically methylates H3(K9) of histones
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Substrates: Lys9 of histone H3
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Substrates: Lys9 of histone 3
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity is observed on trimethylated histone H3(K9) peptides either with or without ubiquitin
Products: -
Products: -
?
additional information
?
-
Substrates: SETDB1 specifically methylates H3K9, but not H3K4 or H3K27. SETDB1 methylates H3 to generate K9me1, K9me2, and K9me3 in a sequential manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: SETDB1 specifically methylates H3K9, but not H3K4 or H3K27. SETDB1 methylates H3 to generate K9me1, K9me2, and K9me3 in a sequential manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: growth factor independent 1 and G9a complex methylates the wild-type H3 substrate as well as the mutants replaced at K4, K36, and K79, substitution at K27 slightly reduces methylation of the H3 substrate, whereas substitution at K9 blocks methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the NF-kappaB factor RelB and histone H3 lysine methyltransferase G9a directly interact to generate epigenetic silencing in endotoxin tolerance
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is able to add methyl groups to lysine 27 as well as 9 in histone H3
Products: -
Products: -
?
additional information
?
-
Substrates: SUV39H2 also trimethylates LSD1 at K322. SUV39H2 also methylates K134 of H2AX
Products: -
Products: -
-
additional information
?
-
Substrates: SUV39H2 also trimethylates LSD1 at K322. SUV39H2 also methylates K134 of H2AX
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme also methylates the non-histone substrates SET8 and DOT1L
Products: -
Products: -
-
additional information
?
-
Substrates: the enzyme also methylates the non-histone substrates SET8 and DOT1L
Products: -
Products: -
-
additional information
?
-
Substrates: other non-histone substrates of SUV39H1 also have chromatin associated roles: methylation of RAG2 by SUV39H1 occurs within its NLS and it alter its sub-nuclear localization. SUV39H1 can also methylate DOT1L.
Products: -
Products: -
-
additional information
?
-
Substrates: other non-histone substrates of SUV39H1 also have chromatin associated roles: methylation of RAG2 by SUV39H1 occurs within its NLS and it alter its sub-nuclear localization. SUV39H1 can also methylate DOT1L.
Products: -
Products: -
-
additional information
?
-
Substrates: SUV39H2 is capable of automethylation. The enzyme also methylates the non-histone substrates LSD1 and SUV39H2
Products: -
Products: -
-
additional information
?
-
Substrates: SUV39H2 is capable of automethylation. The enzyme also methylates the non-histone substrates LSD1 and SUV39H2
Products: -
Products: -
-
additional information
?
-
-
Substrates: histone methylation has significant effects on heterochromatin formation and transcriptional regulation
Products: -
Products: -
?
additional information
?
-
-
Substrates: minimal substrate methylated by G9a contains seven amino acids (TARKSTG) of the histone H3 tail
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is automethylated at K239
Products: -
Products: -
?
additional information
?
-
Substrates: Clr4 automethylates lysines K455 and K472
Products: -
Products: -
-
additional information
?
-
Substrates: Clr4 automethylates lysines K455 and K472
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
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 + dimethylated histone H3(K9)
S-adenosyl-L-homocysteine + trimethylated histone H3(K9)
-
Substrates: the activity on dimethylated histone H3(K9) peptides is several folds lower than when monomethylated histone H3(K9) peptides are used
Products: -
Products: -
?
S-adenosyl-L-methionine + H2B ubiquitinated nucleosome
?
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
S-adenosyl-L-methionine + monomethylated histone H3(K9)
S-adenosyl-L-homocysteine + trimethylated histone H3(K9)
-
Substrates: the SUVR4 product specificity shifts from di- to trimethylation in the presence of free ubiquitin. SUVR4 in vivo specifically converts monomethylated histone H3(K9) to trimethylated histone H3(K9) at transposons and pseudogenes
Products: -
Products: -
?
S-adenosyl-L-methionine + p53
?
Substrates: the enzyme is responsible for p53 methylation at lysine 373
Products: -
Products: -
?
S-adenosyl-L-methionine + reptin
?
Substrates: the enzyme is responsible for reptin methylation at lysine 67
Products: -
Products: -
?
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,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-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: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: activity toward histones in chromatin. SUV39H1 trimethylates H3K9, thereby creating a binding site for HP1, which recruits SUV4-20H. This enzyme generates H4K20me3 using as a substrate the H4K20me1 generated by SET8. Consequently, SUV39H1 indirectly affects the methylation of H4K20 via two pathways: it modifies SET8, thereby enhancing its activity, and creates a site for the binding of SUV4-20H
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: overall reaction
Products: -
Products: -
r
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
Substrates: -
Products: -
Products: -
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-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]-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]-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]-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]-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]-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]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
Substrates: -
Products: -
Products: -
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: preferred substrate
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
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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
Substrates: the enzyme introduce H3K9me3 at pericentric heterochromatin
Products: -
Products: -
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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
Substrates: -
Products: -
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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
Substrates: -
Products: -
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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
-
Substrates: -
Products: -
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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
Substrates: -
Products: -
Products: -
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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
Substrates: -
Products: -
Products: -
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
Substrates: -
Products: -
Products: -
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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: -
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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: -
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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: -
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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: -
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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: -
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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: -
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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: -
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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: -
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S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
Substrates: the enzyme introduce H3K9me3 at pericentric heterochromatin
Products: -
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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: -
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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: -
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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: -
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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: -
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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: -
r
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: -
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S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Substrates: Lys9 of histone 3
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S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
Substrates: -
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additional information
?
-
-
Substrates: no activity is observed on trimethylated histone H3(K9) peptides either with or without ubiquitin
Products: -
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additional information
?
-
-
Substrates: histone methylation has significant effects on heterochromatin formation and transcriptional regulation
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additional information
?
-
Substrates: the enzyme is automethylated at K239
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(4,4-difluoropiperidin-1-yl)-6,7-dimethoxy-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
2-(4,4-difluoropiperidin-1-yl)-6-methoxy-N-[1-(propan-2-yl)piperidin-4-yl]-7-[3-(pyrrolidin-1-yl)propoxy]quinazolin-4-amine
-
2-(azepan-1-yl)-6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-quinazolin-4-amine
-
2-cyclohexyl-6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-quinazolin-4-amine
-
2-cyclohexyl-6-methoxy-N-[1-(propan-2-yl)piperidin-4-yl]-7-[3-(pyrrolidin-1-yl)propoxy]quinazolin-4-amine
MS0124, selective inhibitor
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
6,7-dimethoxy-2-morpholino-N-(1-propylpiperidin-4-yl)-quinazolin-4-amine
-
6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-(piperidin-1-yl)-quinazolin-4-amine
-
6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-(pyrrolidin-1-yl)-quinazolin-4-amine
-
6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-(tetrahydro-2H-pyran-4-yl)quinazolin-4-amine
-
6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
6,7-dimethoxy-N2-methyl-N4-(1-methylpiperidin-4-yl)-N2-pentyl-quinazoline-2,4-diamine
-
6,7-dimethoxy-N4-(1-methylpiperidin-4-yl)-N2-pentylquinazoline-2,4-diamine
-
6-ethoxy-7-methoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
6-fluoro-7-methoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
6-isopropoxy-7-methoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
6-methoxy-7-methyl-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
7-ethoxy-6-methoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
7-fluoro-6-methoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
7-isopropoxy-6-methoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
7-methoxy-6-methyl-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
-
7-[(5-aminopentyl)oxy]-N4-[1-(5-aminopentyl)piperidin-4-yl]-N2-[3-(dimethylamino)propyl]-6-methoxyquinazoline-2,4-diamine
-
7-[2-[2-(dimethylamino)ethoxy]ethoxy]-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
7-[3-(dimethylamino)propoxy]-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
A-366
-
the inhibitor protects penumbra cells from apoptosis and reduces the volume of photothrombotic stroke-induced cerebral infarction
-
cyclohexamide
-
decreases nuclear G9a protein but does not prevent its relative increase during hypoxic stress
E72
i.e. 7-[(5-aminopentyl)oxy]-N4-[-1-(5-aminopentyl)piperidin-4-yl]-N2-[3-(dimethylamino)propyl]-6-methoxyquinazoline-2,4-diamine
N-(1-benzylpiperidin-4-yl)-6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)quinazolin-4-amine
-
N-(1-cyclopropylpiperidin-4-yl)-6,7-dimethoxy-2-morpholinoquinazolin-4-amine
-
N-(1-isopropylpiperidin-4-yl)-6,7-dimethoxy-2-morpholinoquinazolin-4-amine
-
N2-butyl-6,7-dimethoxy-N2-methyl-N4-(1-methylpiperidin-4-yl)-quinazoline-2,4-diamine
-
N2-heptyl-6,7-dimethoxy-N4-(1-methylpiperidin-4-yl)-quinazoline-2,4-diamine
-
N2-hexyl-6,7-dimethoxy-N2-methyl-N4-(1-methylpiperidin-4-yl)-quinazoline-2,4-diamine
-
N2-hexyl-6,7-dimethoxy-N4-(1-methylpiperidin-4-yl)quinazoline-2,4-diamine
MS012, selective inhibitor
RNA
-
the presence of RNA strongly inhibits enzyme activity in vitro
BIX-01294
-
specific inhibitor of isoform EHMT2, specifically decreases global H3K9Me2 level but not H3K27Me2. The inhibition of EHMT2 decreases proliferation of NB cells and induces apoptosis by increasing caspase 8/caspase 3 activity. BIX-01294 inhibits NB cell mobility and invasion accompanied with a decreased expression of the MYCN oncogene. Inhibition of EHMT2 enhances a doxorubicin induced inhibitory effect on cell proliferation and modulates global DNA methylation levels in NB cells
BIX-01294
diazepin-quinazolin-amine derivative, specific competitive inhibitor
BIX01294
-
the inhibitor protects penumbra cells from apoptosis and reduces the volume of photothrombotic stroke-induced cerebral infarction
additional information
-
SUVR4 enzyme activity is not affected by monomethylated histone H3(K4)
-
additional information
-
hypoxia does not cause any measurable changes of G9a mRNA at earlier time intervals (1 and 3 hours) but leads to a significant decrease at 6 hours after challenge
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deferoxamine
-
increases G9a protein and activity in A549 cells, moreover, increases the methyltransferase activity of overexpressed GFP-hG9a fusion proteins
additional information
-
hypoxia increases nuclear G9a protein by posttranslational mechanisms and its methyltransferase activity
-
additional information
the addition of an [histone H3]-N6,N6,N6-trimethyl-L-lysine9-containing peptide strongly enhances enzyme activity on unmodified chromatin
-
additional information
-
the addition of an [histone H3]-N6,N6,N6-trimethyl-L-lysine9-containing peptide strongly enhances enzyme activity on unmodified chromatin
-
additional information
the enzyme activity is stimulated by histone H2B Lys120 ubiquitination
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012 - 0.0013
S-adenosyl-L-methionine
-
in methylation buffer containing 50 mM glycine (pH 9.8), 2 mM dithiothreitol, 0.025 mg/ml bovine serum albumin, 10% (v/v) glycerol, at 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
BIX-01294
Homo sapiens
-
G9a-like protein lysine methyltransferase, in 20 mM Tris (pH 8.5), at 30°C
0.0019
BIX-01294
Homo sapiens
-
histone lysine methyltransferase G9a, in 20 mM Tris (pH 8.5), at 30°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
SUV39H1 expression is significantly up-regulated in human colorectal carcinoma as compared to normal colon
brenda
-
PRDM8 of 30 kDa is expressed most prominently in cardiomyocytes from the heart
brenda
-
interaction between growth factor independent 1 and G9a in vivo
brenda
additional information
SUV39H1 expression is significantly up-regulated in human colorectal carcinoma as compared to normal colon
brenda
SETDB1 expression gradually increases during testis development
brenda
-
PRDM8 is expressed most prominently in striated skeletal muscle from the tongue
brenda
additional information
-
PRDM8 is not expressed in intestinal smooth muscles
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme localizes at euchromatin and heterochromatin
brenda
-
the full-length of PRDM8 is localized exclusively in the nuclear region
brenda
SETDB1 localizes weakly in nuclei in GFRA1-positive spermatogonia
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
evolution
malfunction
metabolism
SUV39H1 trimethylates H3K9, thereby creating a binding site for HP1, which recruits SUV4-20H. This enzyme generates H4K20me3 using as a substrate the H4K20me1 generated by SET8. Consequently, SUV39H1 indirectly affects the methylation of H4K20 via two pathways: it modifies SET8, thereby enhancing its activity, and creates a site for the binding of SUV4-20H
physiological function
additional information
drug target
HF6 recruits methyltransferase SUV39H1 to the nucleolar region in leukemia and provids a potential therapeutic target for PHF6-mutant leukemia
drug target
pharmacological inhibition of SUV39H1 is an effective approach to suppress human colorectal carcinoma
evolution
protein BLAST analyses shows that Dim5 orthologues are widely distributed amongst filamentous Trichoderma, Penicillium, Fusarium, Neurospora and Aspergillus species, although they exhibit different amino acid lengths. To analyse the phylogenetic relationship between Dim5 homologues from filamentous fungi and SpClr4, a phylogenetic tree is built using Dim5 orthologues from this species as well as SpClr4. Filamentous fungi Dim5 orthologues form two distinct clusters from SpClr4. Amongst them, Trichoderma Dim5 shows a close evolutionary relationship with the orthologues from Fusarium and Neurospora species
evolution
-
protein BLAST analyses shows that Dim5 orthologues are widely distributed amongst filamentous Trichoderma, Penicillium, Fusarium, Neurospora and Aspergillus species, although they exhibit different amino acid lengths. To analyse the phylogenetic relationship between Dim5 homologues from filamentous fungi and SpClr4, a phylogenetic tree is built using Dim5 orthologues from this species as well as SpClr4. Filamentous fungi Dim5 orthologues form two distinct clusters from SpClr4. Amongst them, Trichoderma Dim5 shows a close evolutionary relationship with the orthologues from Fusarium and Neurospora species
-
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
-
knockdown of G9a or SETDB1 throughout development with an ACT5C-GAL4 driver produces organism- level defects only in the case of dSETDB1
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
-
G9a deficiency causes loss of imprinting in the placenta but not the embryo
malfunction
-
inhibition of G9a/GLP in the entorhinal cortex (EC), but not in the hippocampus, enhances contextual fear conditioning relative to control animals. Downregulation of G9a/GLP activity in the EC enhances histone H3(K9) dimethylation in hippocampus area CA1, resulting in transcriptional silencing of the non-memory permissive gene COMT in the hippocampus
malfunction
-
during oxidative stress exposure, enzyme mutants show overactivation of stress response genes, rapid depletion of glycogen, and inability to access lipid energy stores
malfunction
enzyme inhibition attenuates oncogenicity and activates the hypoxia signaling pathway
malfunction
enzyme inhibition attenuates the proliferation of HMEC-1 cells, nuclear localization of phosphorylated checkpoint kinase 1, and induces cell cycle arrest in G1 phase
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
malfunction
in cultured hepatic cells, enzyme knockdown results in downregulation of insulin receptor, p-AKT and p-GSK3beta
malfunction
inhibiting the methyltransferase activity of the enzyme aggravates lipopolysaccharide-induced liver damage
malfunction
an enzyme deletion mutant shows significant defects in conidiation, perithecium production and fungal virulence. Enzyme deletion results in increased tolerance to osmotic stresses and upregulated Hog1 phosphorylation
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
deletion of the clr4 gene eliminates H3K9me2/me3 but not H3K9me1, indicating the presence of another protein capable of monomethylating H3K9
malfunction
Suv39h1 and Suv39h2 knockdown in newborn cells of the adult mouse dentate gyrus by retrovirus-mediated RNA interference impairs neuronal differentiation of progenitor cells
malfunction
loss of FmKmt1 has a moderate though significant impact on fungal hyphal growth and asexual development. Removal of FmKMT1 results in an almost complete loss of fusapyrone and deoxyfusapyrone. Deletion of FmKMT1 increases beauvericin biosynthesis
malfunction
TrDIM5 deletion causes an impaired vegetative growth as well as conidiation, whereas the DELTATrdim5 strain displays a remarkable increase in sorbicillinoid production. Post TrDIM5 deletion, the transcription of sorbicillinoid biosynthesis-related genes is significantly upregulated with a more open chromatin structure
malfunction
SUV39H1 knockout causes a marked decrease in the level of H3K9me3 and results in altered expression of some of the examined differentiation-associated genes. The rise in expression following SUV39H1 knockout concerns mainly genes of the middle/late stage of differentiation and reinforces the differentiation process in comparison to wild-type HaCaT cells
malfunction
the siRNA-mediated knockdown of SUV39H1 increases Mkp-1 expression and suppresses p-CREB and Bdnf expression in HT22 cells and in the hippocampus of mice
malfunction
dysregulation of SUV39H1 is observed in different cancers
malfunction
inhibition of SUV39H1 alters the expression of genes with known functions in DNA replication and cell cycle in the metastatic colon carcinoma cells, which is associated with cell cycle arrest at S phase in the metastatic human colon carcinoma cells, resulting in tumor cell apoptosis and growth inhibition in a concentration-dependent manner in vitro
malfunction
-
an enzyme deletion mutant shows significant defects in conidiation, perithecium production and fungal virulence. Enzyme deletion results in increased tolerance to osmotic stresses and upregulated Hog1 phosphorylation
-
malfunction
-
TrDIM5 deletion causes an impaired vegetative growth as well as conidiation, whereas the DELTATrdim5 strain displays a remarkable increase in sorbicillinoid production. Post TrDIM5 deletion, the transcription of sorbicillinoid biosynthesis-related genes is significantly upregulated with a more open chromatin structure
-
malfunction
-
deletion of the clr4 gene eliminates H3K9me2/me3 but not H3K9me1, indicating the presence of another protein capable of monomethylating H3K9
-
malfunction
Fusarium mangiferae MRC7560
-
loss of FmKmt1 has a moderate though significant impact on fungal hyphal growth and asexual development. Removal of FmKMT1 results in an almost complete loss of fusapyrone and deoxyfusapyrone. Deletion of FmKMT1 increases beauvericin biosynthesis
-
physiological function
-
DNA methylation of retrotransposons in embryonic stem cells requires the lysine methyltransferase G9a but not its catalytic activity
physiological function
-
SETDB1 acts to maintain heterochromatin during metamorphosis, at a later stage in development than the reported action of SU(VAR)3-9, depletion of both of these enzymes has less deleterious effect than depletion of one, SETDB1 acts as a heterochromatin maintenance factor that may be required for the persistence of earlier developmental events normally governed by SU(VAR)3-9
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
-
G9a/GLP activity is critical for hippocampus-dependent long-term potentiation initiated in the entorhinal cortex via the perforant pathway, but not the temporoammonic pathway. G9a/GLP histone lysine dimethyltransferase complex activity in the hippocampus and the entorhinal cortex is required for gene activation and silencing during memory consolidation
physiological function
-
SUVR4 is involved in the epigenetic defense mechanism by trimethylating histone H3(K9) to suppress potentially harmful transposon activity
physiological function
-
SETDB1 is mainly responsible for mono- and trimethylation of histone H3 lysine 9 and SU (VAR)3-9 for monomethylation of histone H3 lysine 9 during spermatogenesis. Enzyme form dG9a plays no apparent role for histone H3 lysine 9 methylation during spermatogenesis and spermiogenesis
physiological function
the SET domain of isoformn Suv39 h1 is essential for repressing gene expression of BZLF1, which acts as a master regulator of the transition from latency to the lytic replication cycle in latently Epstein-Barr virus-infected cells. Depletion of Suv39 h1 protein by siRNA results in increased expression of BZLF1 mRNA in B958 cells, and Suv39 h1 inhibitor chaetocin activates BZLF1 transcription
physiological function
SUV39H1 knockdown reduces H3K9me3 levels and impairs HCC cell growth and sphere formation. The pharmacological inhibition of SUV39H1 by chaetocin results in cell growth inhibition and inducing cellular apoptosis in culture and xenograft subcutaneous tumors. 24 of 42 HCC surgical samples display high levels of SUV39H1 expression compared with corresponding nontumor tissues. Tumor tissues show high levels of H3K9me3 and H3K9-specific methyltransferase ESET proteins in 23 (54.8%) and 29 (69.0%) samples, respectively. Expression levels of SUV39H1 but not those of ESET are significantly correlated with H3K9me3 levels
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 contributes to heterochromatin formation
physiological function
-
the enzyme acts as a critical regulatory hub between the transcriptional and metabolic responses to oxidative stress
physiological function
the enzyme is a key mediator of oncogenic processes in breast cancer cells
physiological function
the enzyme plays a role in the promotion of endothelial cell proliferation
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
-
the enzyme represses E-cadherin and is associated with myometrial invasion in endometrial cancer
physiological function
the enzyme contributes to the regulation of chromatin structure
physiological function
the enzyme modulates hepatic insulin signaling via regulating HMGA1 (high mobility group AT-hook 1, a key regulator responsible for the transcription of insulin receptor gene). In cultured hepatic cells, enzyme upregulation prevents the palmitic acid- or glucosamine-induced insulin resistance by preserving the normal level of insulin receptor and integrity of insulin signaling.
physiological function
the enzyme regulates chromatin reorganization in mouse oocytes. Maternal enzyme is vital for proper chromosome segregation in preimplantation embryos
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 is essential for the repression of developmental genes and is required during development
physiological function
the enzyme is essential for full virulence of Botrytis cinerea and plays an important role in growth and development
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
physiological function
Drosophila melanogaster SETDB1 is an H3K9 methyltransferase and a pleiotropic regulator of the fly's development. Drosophila mutants hypomorphic or null in SETDB1 expression lose most of the H3K9 methylation as well as HP1-binding on the fourth chromosome. Binding of painting of fourth (POF), a fourth chromosome-specific protein, and the SETDB1-controlled H3K9 methylation of this chromosome are interdependent. POF and dSETDB1 interact with each other in vivo. The deregulation of H3K9 methylation, HP1-binding, and POF-binding result in a global reduction of gene expression from the fourth chromosome but not the other chromosomes. Deficiency of dSETDB1 also upregulates the expression of HP1
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
female identity is secured by an H3K9me3 epigenetic pathway in which Sxl is the upstream female-specific regulator, SETDB1 is the required chromatin writer, and phf7 is one of the critical SETDB1 target genes. Germ cell specific loss of the H3K9me3 pathway members, the H3K9 methyltransferase SETDB1, WDE, and HP1a, leads to ectopic expression of genes, many of which are normally expressed in testis. SETDB1 controls the accumulation of H3K9me3 over a subset of these genes without spreading into neighboring loci
physiological function
knockdown of SETDB1 gene expression leads to gonocyte apoptosis and a decrease in H3K27me3, but no significant change in H3K9me3
physiological function
during embryonic development, the repressive modification trimethylation of histone H3 on lysine 9 (H3K9me3) contributes to the cellular identity of different cell-types. H3K9me3 and H3K9 methyltransferases Suv39h1 and Suv39h2 are critically involved in the regulation of adult hippocampal neurogenesis by controlling the differentiation of neural progenitor cells
physiological function
biosynthesis of fusapyrone depends on the H3K9 methyltransferase FmKmt1. FmKmt1 slightly though significantly affects fungal growth and conidiation. FmKmt1 slightly but significantly contributes to the osmotic stress response in Fusarium mangiferae
physiological function
TrDim5 facilitates vegetative growth and conidiation of Trichoderma reesei
physiological function
PHF6 and SUV39H1 coordinately regulate cell proliferation in an interdependent manner.
physiological function
the enzyme has roles in the brain during early neurodevelopment. Important roles in the maintenance of heterochromatin and gene repression. The enzyme is connected to cancer, having oncogenic or tumor-suppressive roles depending on the tumor type
physiological function
important roles in the maintenance of heterochromatin and gene repression. The enzyme is connected to cancer, having oncogenic or tumor-suppressive roles depending on the tumor type. SUV39H1-mediated H3K9 trimethylation regulates the expression of several genes
physiological function
the enzyme controls the differentiation of neural progenitor cells during neurogenesis
physiological function
Suv39h1 regulates memory stability by inhibiting the expression of Shank1 in hippocampal newborn neurons
physiological function
-
TrDim5 facilitates vegetative growth and conidiation of Trichoderma reesei
-
physiological function
-
the enzyme is essential for full virulence of Botrytis cinerea and plays an important role in growth and development
-
physiological function
Fusarium mangiferae MRC7560
-
biosynthesis of fusapyrone depends on the H3K9 methyltransferase FmKmt1. FmKmt1 slightly though significantly affects fungal growth and conidiation. FmKmt1 slightly but significantly contributes to the osmotic stress response in Fusarium mangiferae
-
additional information
-
the histone H3K9 methyltransferase Clr4 is mainly sequestered at pericentric repeats. This selective sequestration of Clr4 depends not only on H3K9M but also on H3K14 ubiquitylation (H3K14ub), a modification deposited by a Clr4-associated E3 ubiquitin ligase complex. In vitro, H3K14ub synergizes with H3K9M to interact with Clr4 and potentiates the inhibitory effects of H3K9M on Clr4 enzymatic activity
additional information
-
helicase Chl1 coordinates with Clr4 to eliminate RNA/DNA hybrids, which contributes to the maintenance of genome integrity. Chl1 is required for genome stability in clr4DELTA cells
additional information
expression of Shank1 is transiently engaged to enhance synaptogenesis during learning and is strongly suppressed by Suv39h1 from 5 h after learning
Show AA Sequence and Transmembrane Helices (2425 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme interacts in vivo and in vitro with CCAAT displacement protein/cut homolog. Transcriptional repressor function of cut homolog is mediated through enzyme activity
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ubiquitination
ubiquitination
ubiquitination of lysine 867 of the human SETDB1 protein upregulates its histone H3 lysine 9 methyltransferase activity
ubiquitination
the Clr4 molecule contains many lysine residues that can be ubiquitinated. Without this modification at position K109, K110, K113, or K114, the enzyme can dimethylate but loses the ability to trimethylate H3K9
ubiquitination
-
the Clr4 molecule contains many lysine residues that can be ubiquitinated. Without this modification at position K109, K110, K113, or K114, the enzyme can dimethylate but loses the ability to trimethylate H3K9
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with BIX-01294, hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 18-20% (w/v) polyethylene glycol 4000 and 7-10% (v/v) isopropanol, in the absence or presence of DMSO (6-36% v/v)
-
in complex with S-adenosyl-L-methionine and either 6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine or N2-hexyl-6,7-dimethoxy-N4-(1-methylpiperidin-4-yl)quinazoline-2,4-diamine, hanging drop vapor diffusion method, using 20% (w/v) PEG 20,000, 2% (v/v) 1,4-dioxane, 0.1 M bicine (pH 9.0)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C1197A
mutation of conserved residue within the SET domain, loss of catalytic activity
F326A
I290A
the mutant shows significantly reduced activity compared to the wild type enzyme
L284A
the mutant shows significantly reduced activity compared to the wild type enzyme
L329A
the mutant shows significantly reduced activity compared to the wild type enzyme
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
D209A
-
in solution experiments with the wild type histone H3 sequence, the mutant shows a 100fold reduced activity as compared to wild-type Dim-5
D209S
-
in solution experiments with the wild type histone H3 sequence, the mutant shows a 100fold reduced activity as compared to wild-type Dim-5
E227A
-
in solution experiments with the wild type histone H3 sequence, the mutant shows a 10fold reduced activity as compared to wild-type Dim-5
E227S
-
in solution experiments with the wild type histone H3 sequence, the mutant shows a 10fold reduced activity as compared to wild-type Dim-5
Y178F
-
shows catalytic activity, although the methylation rates of this variant are low
F449Y
additional information
F326A
the mutant shows significantly reduced activity compared to the wild type enzyme
F449Y
mutation blocks the conversion of H3K9me2 into H3K9me3
F449Y
-
mutation blocks the conversion of H3K9me2 into H3K9me3
-
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SUV39H2 is degraded through the ubiquitin-proteasomal pathway and its half-life was reduced by interaction with the translationally controlled tumor protein
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutahione S-transferase affinity column chromatography, anion exchange column chromatography, and gel filtration
nickel-chelating column chromatography, HiTrap-Q column chromatography, and Superdex-75 and -200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cotransfection of growth factor independent 1 with both HA epitope-tagged G9a and Myc epitope-tagged Suv39H1 into HeLa cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Sf9 insect cells
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aged mice show decreased expression of SUV39H1 histone methyltransferase in the hippocampus
an increase in the level of SUV39H1 in the penumbra at 24 h after photothrombotic stroke
-
expression of SUV39H1 declines with age in hematopoietic stem cells
high levels of expression at early stages of neurogenesis and the expression decreased upon differentiation
SUV39H1 expression is significantly up-regulated in human colorectal carcinoma as compared to normal colon
SUV39H2 is overexpressed in many cancer tissues, such as leukemia, lymphomas, lung cancer, breast cancer, colorectal cancer, gastric cancer and hepatocellular cancer
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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
additional information
analysis
-
development of a microplate biotin/avidin peptide methylation assay, which is convenient, very accurate, reproducible, and inexpensive. Because it yields quantitative results, it can be employed for a characterization of the enzymatic properties of histone lysine methyltransferases and other protein methyltransferases and is also well suited for high-throughput applications
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
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
medicine
-
treatment with inhibitor BIX-01294 specifically decreases global H3K9Me2 level but not H3K27Me2. The inhibition of EHMT2 decreases proliferation of NB cells and induces apoptosis by increasing caspase 8/caspase 3 activity. BIX-01294 inhibits NB cell mobility and invasion accompanied with a decreased expression of the MYCN oncogene. Inhibition of EHMT2 enhances a doxorubicin induced inhibitory effect on cell proliferation and modulates global DNA methylation levels in NB cells
medicine
SUV39H1 knockdown reduces H3K9me3 levels and impairs HCC cell growth and sphere formation. The pharmacological inhibition of SUV39H1 by chaetocin results in cell growth inhibition and inducing cellular apoptosis in culture and xenograft subcutaneous tumors. 24 of 42 HCC surgical samples display high levels of SUV39H1 expression compared with corresponding nontumor tissues. Tumor tissues show high levels of H3K9me3 and H3K9-specific methyltransferase ESET proteins in 23 (54.8%) and 29 (69.0%) samples, respectively. Expression levels of SUV39H1 but not those of ESET are significantly correlated with H3K9me3 levels. The cumulative HCC recurrence rate is significantly higher for patients with elevated SUV39H1 expression and H3K9me3 levels
medicine
hepatocellular tumor tissues show high levels of H3K9me3 and H3K9-specific methyltransferase ESET proteins in 23 (54.8%) and 29 (69.0%) of 42 samples, respectively. Expression levels of isoform SUV39H1 but not those of ESET are significantly correlated with H3K9me3 levels. The cumulative HCC recurrence rate is significantly higher for patients with elevated SUV39H1 expression and H3K9me3 levels
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
additional information
-
growth factor independent 1 interacts with G9a and recruits G9a and histone deacetylase 1 to its target promoters, including the cell cycle regulator p21Cip/WAF1 and other cell cycle regulators, in order to repress transcription through histone H3(K9) dimethylation
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YEAR
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PUBMED ID
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Neurospora crassa
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388
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15
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Neurospora crassa
brenda
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27
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Genetics
181
1303-1319
2009
Drosophila melanogaster
brenda
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284
27857-27865
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Homo sapiens
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181
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Mus musculus
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Mol. Cell. Biol.
28
1104-1113
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Mus musculus
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16
312-317
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Homo sapiens
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20
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32
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Rattus norvegicus
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24
484-493
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Homo sapiens
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Homo sapiens (O43463)
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Homo sapiens (O43463), Homo sapiens (Q15047), Homo sapiens
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Homo sapiens
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47
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Schizosaccharomyces pombe
brenda
Wojtala, M.; Macierzynska-Piotrowska, E.; Rybaczek, D.; Pirola, L.; Balcerczyk, A.
Pharmacological and transcriptional inhibition of the G9a histone methyltransferase suppresses proliferation and modulates redox homeostasis in human microvascular endothelial cells
Pharmacol. Res.
128
252-263
2018
Homo sapiens (Q96KQ7), Homo sapiens
brenda
Riahi, H.; Brekelmans, C.; Foriel, S.; Merkling, S.H.; Lyons, T.A.; Itskov, P.M.; Kleefstra, T.; Ribeiro, C.; van Rij, R.P.; Kramer, J.M.; Schenck, A.
The histone methyltransferase G9a regulates tolerance to oxidative stress-induced energy consumption
PLoS Biol.
17
e2006146
2019
Drosophila melanogaster
brenda
Ishimoto, K.; Kawamata, N.; Uchihara, Y.; Okubo, M.; Fujimoto, R.; Gotoh, E.; Kakinouchi, K.; Mizohata, E.; Hino, N.; Okada, Y.; Mochizuki, Y.; Tanaka, T.; Hamakubo, T.; Sakai, J.; Kodama, T.; Inoue, T.; Tachibana, K.; Doi, T.
Ubiquitination of lysine 867 of the human SETDB1 protein upregulates its histone H3 lysine 9 (H3K9) methyltransferase activity
PLoS ONE
11
e0165766
2016
Homo sapiens (Q15047), Homo sapiens
brenda
Ho, J.C.; Abdullah, L.N.; Pang, Q.Y.; Jha, S.; Chow, E.K.; Yang, H.; Kato, H.; Poellinger, L.; Ueda, J.; Lee, K.L.
Inhibition of the H3K9 methyltransferase G9A attenuates oncogenicity and activates the hypoxia signaling pathway
PLoS ONE
12
e0188051
2017
Homo sapiens (Q96KQ7)
brenda
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)
brenda
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)
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 (O43463)
brenda
Tzeng, T.Y.; Lee, C.H.; Chan, L.W.; Shen, C.K.
Epigenetic regulation of the Drosophila chromosome 4 by the histone H3K9 methyltransferase dSETDB1
Proc. Natl. Acad. Sci. USA
104
12691-12696
2007
Drosophila melanogaster (Q32KD2), Drosophila melanogaster
brenda
Liu, T.; Zhang, P.; Li, T.; Chen, X.; Zhu, Z.; Lyu, Y.; Li, X.; Tian, X.; Zeng, W.
SETDB1 plays an essential role in maintenance of gonocyte survival in pigs
Reproduction
154
23-34
2017
Sus scrofa (F1SS95), Sus scrofa
brenda
Tsai, H.I.; Wu, Y.; Huang, R.; Su, D.; Wu, Y.; Liu, X.; Wang, L.; Xu, Z.; Pang, Y.; Sun, C.; He, C.; Shu, F.; Zhu, H.; Wang, D.; Cheng, F.; Huang, L.; Chen, H.
PHF6 functions as a tumor suppressor by recruiting methyltransferase SUV39H1 to nucleolar region and offers a novel therapeutic target for PHF6-muntant leukemia
Acta Pharm. Sin. B
12
1913-1927
2022
Homo sapiens (O43463)
brenda
Koryakov, D.E.
Diversity and functional specialization of H3K9-specific histone methyltransferases
Bioessays
46
e2300163
2024
Schizosaccharomyces pombe (O60016), Neurospora crassa (Q8X225), Homo sapiens (O43463), Homo sapiens (Q9H5I1), Mus musculus (O54864), Mus musculus (Q9EQQ0), Drosophila melanogaster (P45975), Schizosaccharomyces pombe ATCC 24843 (O60016), Neurospora crassa DSM 1257 (Q8X225)
brenda
Lu, C.; Klement, J.D.; Yang, D.; Albers, T.; Lebedyeva, I.O.; Waller, J.L.; Liu, K.
SUV39H1 regulates human colon carcinoma apoptosis and cell cycle to promote tumor growth
Cancer Lett.
476
87-96
2020
Homo sapiens (O43463)
brenda
Shan, C.M.; Kim, J.K.; Wang, J.; Bao, K.; Sun, Y.; Chen, H.; Yue, J.X.; Stirpe, A.; Zhang, Z.; Lu, C.; Schalch, T.; Liti, G.; Nagy, P.L.; Tong, L.; Qiao, F.; Jia, S.
The histone H3K9M mutation synergizes with H3K14 ubiquitylation to selectively sequester histone H3K9 methyltransferase Clr4 at heterochromatin
Cell Rep.
35
109137
2021
Schizosaccharomyces pombe
brenda
Sobiak, B.; Lesniak, W.
Effect of SUV39H1 histone methyltransferase knockout on expression of differentiation-associated genes in HaCaT keratinocytes
Cells
9
2628
2020
Homo sapiens (O43463)
brenda
Chen, Q.N.; Ding, X.L.; Guo, X.X.; Zhou, G.; Guan, J.S.
Suv39h1 regulates memory stability by inhibiting the expression of Shank1 in hippocampal newborn neurons
Eur. J. Neurosci.
55
1424-1441
2022
Mus musculus (O54864)
brenda
Guerra, M.V.; Caceres, M.I.; Herrera-Soto, A.; Arredondo, S.B.; Varas-Godoy, M.; van Zundert, B.; Varela-Nallar, L.
H3K9 Methyltransferases Suv39h1 and Suv39h2 control the differentiation of neural progenitor cells in the adult hippocampus
Front. Cell Dev. Biol.
9
778345
2021
Mus musculus (O54864), Mus musculus (Q9EQQ0)
brenda
Atanasoff-Kardjalieff, A.K.; Luenne, F.; Kalinina, S.; Strauss, J.; Humpf, H.U.; Studt, L.
Biosynthesis of fusapyrone depends on the H3K9 methyltransferase, FmKmt1, in Fusarium mangiferae
Front. Fungal Biol.
2
671796
2021
Fusarium mangiferae (A0A1L7TZE5), Fusarium mangiferae MRC7560 (A0A1L7TZE5)
brenda
Sharifulina, S.; Dzreyan, V.; Guzenko, V.; Demyanenko, S.
Histone methyltransferases SUV39H1 and G9a and DNA methyltransferase DNMT1 in penumbra neurons and astrocytes after photothrombotic stroke
Int. J. Mol. Sci.
22
12483
2021
Rattus norvegicus
brenda
He, D.; Guo, Y.; Cheng, J.; Wang, Y.
Chl1 coordinates with H3K9 methyltransferase Clr4 to reduce the accumulation of RNA-DNA hybrids and maintain genome stability
iScience
25
104313
2022
Schizosaccharomyces pombe
brenda
Weirich, S.; Khella, M.S.; Jeltsch, A.
Structure, activity and function of the Suv39h1 and Suv39h2 protein lysine methyltransferases
Life
11
703
2021
Homo sapiens (O43463), Homo sapiens (Q9H5I1)
brenda
Wang, L.; Liu, J.; Li, X.; Lyu, X.; Liu, Z.; Zhao, H.; Jiao, X.; Zhang, W.; Xie, J.; Liu, W.
A histone H3K9 methyltransferase Dim5 mediates repression of sorbicillinoid biosynthesis in Trichoderma reesei
Microb. Biotechnol.
15
2533-2546
2022
Trichoderma reesei (G0RU80), Trichoderma reesei QM6a (G0RU80)
brenda
Lee, J.E.; Park, S.Y.; Han, P.L.
Aging-dependent downregulation of SUV39H1 histone methyltransferase increases susceptibility to stress-induced depressive behavior
Mol. Neurobiol.
58
6427-6442
2021
Mus musculus (O54864)
brenda
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