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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
-
overall reaction
-
-
?
3 S-adenosyl-L-methionine + biotinylated [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + biotinylated [histone H3]-N6-methyl-L-lysine9
-
-
-
?
biotinyl-MARTKQTARKSTGGKAPRKQ + S-adenosyl-L-methionine
?
-
Dim-5 methylates the histone H3 tail at position Lys9
-
-
?
L-lysyl9-[histone H3] + 3 S-adenosyl-L-methionine
N6,N6,N6-trimethyl-L-lysyl9-[histone H3] + 3 S-adenosyl-L-homocysteine
-
-
-
?
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 + ACINUS
?
-
-
-
?
S-adenosyl-L-methionine + CDYL1
?
-
-
-
?
S-adenosyl-L-methionine + dimethylated histone H3(K9)
S-adenosyl-L-homocysteine + trimethylated histone H3(K9)
-
the activity on dimethylated histone H3(K9) peptides is several folds lower than when monomethylated histone H3(K9) peptides are used
-
-
?
S-adenosyl-L-methionine + DNA methyltransferase 1
?
-
-
-
-
?
S-adenosyl-L-methionine + H2B ubiquitinated nucleosome
?
-
-
-
?
S-adenosyl-L-methionine + histone H2A
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + histone H2B
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3
?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3 (1-13)
?
-
-
-
-
?
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-methionine + histone H3(K9)
S-adenosyl-L-homocysteine + ?
S-adenosyl-L-methionine + histone H4
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + histone K4-acetylK9
?
-
-
-
-
?
S-adenosyl-L-methionine + histone K4-trimethylK9
?
-
-
-
-
?
S-adenosyl-L-methionine + histone K4AK9
?
-
-
-
-
?
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)
-
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
-
-
?
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
-
-
?
S-adenosyl-L-methionine + WIZ
?
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine9
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine9
-
-
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
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
-
-
?
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
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]-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
-
-
-
?
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
-
-
-
?
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]-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,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
-
-
-
?
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
preferred substrate
-
-
?
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,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 + 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
-
-
-
?
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
-
-
-
?
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 + 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(K9)
?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
?
-
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
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
?
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
S-adenosyl-L-homocysteine + ?
-
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
-
-
?
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
-
-
-
-
?
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
-
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
-
-
?
additional information
?
-
-
no activity is observed on trimethylated histone H3(K9) peptides either with or without ubiquitin
-
-
?
additional information
?
-
SETDB1 specifically methylates H3K9, but not H3K4 or H3K27. SETDB1 methylates H3 to generate K9me1, K9me2, and K9me3 in a sequential manner
-
-
-
additional information
?
-
-
SETDB1 specifically methylates H3K9, but not H3K4 or H3K27. SETDB1 methylates H3 to generate K9me1, K9me2, and K9me3 in a sequential manner
-
-
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the NF-kappaB factor RelB and histone H3 lysine methyltransferase G9a directly interact to generate epigenetic silencing in endotoxin tolerance
-
-
?
additional information
?
-
the enzyme is able to add methyl groups to lysine 27 as well as 9 in histone H3
-
-
?
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
-
-
?
additional information
?
-
the enzyme is automethylated at K239
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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 + ACINUS
?
-
-
-
?
S-adenosyl-L-methionine + CDYL1
?
-
-
-
?
S-adenosyl-L-methionine + dimethylated histone H3(K9)
S-adenosyl-L-homocysteine + trimethylated histone H3(K9)
-
the activity on dimethylated histone H3(K9) peptides is several folds lower than when monomethylated histone H3(K9) peptides are used
-
-
?
S-adenosyl-L-methionine + H2B ubiquitinated nucleosome
?
-
-
-
?
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)
-
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
-
-
?
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
-
-
?
S-adenosyl-L-methionine + WIZ
?
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6-methyl-L-lysine9
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6,N6-dimethyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6,N6-trimethyl-L-lysine9
-
-
-
-
?
S-adenosyl-L-methionine + [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + [histone H3]-N6,N6-dimethyl-L-lysine9
-
-
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
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
-
-
?
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
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]-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
-
-
-
?
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
-
-
-
?
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]-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,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
-
-
-
?
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
preferred substrate
-
-
?
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,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 + 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
-
-
-
?
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
-
-
-
?
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 + 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
-
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
-
-
-
?
additional information
?
-
-
no activity is observed on trimethylated histone H3(K9) peptides either with or without ubiquitin
-
-
?
additional information
?
-
-
histone methylation has significant effects on heterochromatin formation and transcriptional regulation
-
-
?
additional information
?
-
the enzyme is automethylated at K239
-
-
?
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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
-
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
-
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
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
-
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 depletion results in embryonic lethality with severe differentiation defects in embryonic stem cells. Enzyme depletion inhibits cell proliferation in several cancer cell lines
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
enzyme knockdown stimulates myoblast differentiation
malfunction
enzyme loss blocks germ cell differentiation
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
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
-
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
-
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
-
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
-
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
-
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
-
SUVR4 is involved in the epigenetic defense mechanism by trimethylating histone H3(K9) to suppress potentially harmful transposon activity
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 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
-
the enzyme acts as a critical regulatory hub between the transcriptional and metabolic responses to oxidative stress
physiological function
-
the enzyme contributes to heterochromatin formation
physiological function
the enzyme contributes to the regulation of chromatin structure
physiological function
the enzyme is a key mediator of oncogenic processes in breast cancer cells
physiological function
the enzyme is essential for full virulence of Botrytis cinerea and plays an important role in growth and development
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 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 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 plays a role in the promotion of endothelial cell proliferation
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 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
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
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
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
knockdown of SETDB1 gene expression leads to gonocyte apoptosis and a decrease in H3K27me3, but no significant change in H3K9me3
physiological function
-
the enzyme is essential for full virulence of Botrytis cinerea and plays an important role in growth and development
-
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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
brenda
Yeates, T.O.
Structures of SET domain proteins: protein lysine methyltransferases make their mark
Cell
111
5-7
2002
Neurospora crassa
brenda
Nishio, H.; Walsh, M.J.
CCAAT displacement protein/cut homolog recruits G9a histone lysine methyltransferase to repress transcription
Proc. Natl. Acad. Sci. USA
101
11257-11262
2004
Homo sapiens
brenda
Gowher, H.; Zhang, X.; Cheng, X.; Jeltsch, A.
Avidin plate assay system for enzymatic characterization of a histone lysine methyltransferase
Anal. Biochem.
342
287-291
2005
Neurospora crassa
brenda
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
brenda
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
brenda
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
brenda
Duan, Z.; Zarebski, A.; Montoya-Durango, D.; Grimes, H.L.; Horwitz, M.
Gfi1 coordinates epigenetic repression of p21Cip/WAF1 by recruitment of histone lysine methyltransferase G9a and histone deacetylase 1
Mol. Cell. Biol.
25
10338-10351
2005
Homo sapiens
brenda
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
brenda
Rathert, P.; Zhang, X.; Freund, C.; Cheng, X.; Jeltsch, A.
Analysis of the substrate specificity of the Dim-5 histone lysine methyltransferase using peptide arrays
Chem. Biol.
15
5-11
2008
Neurospora crassa
brenda
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
brenda
Brower-Toland, B.; Riddle, N.C.; Jiang, H.; Huisinga, K.L.; Elgin, S.C.
Multiple SET methyltransferases are required to maintain normal heterochromatin domains in the genome of Drosophila melanogaster
Genetics
181
1303-1319
2009
Drosophila melanogaster
brenda
Chen, X.; El Gazzar, M.; Yoza, B.K.; McCall, C.E.
The NF-kappaB factor RelB and histone H3 lysine methyltransferase G9a directly interact to generate epigenetic silencing in endotoxin tolerance
J. Biol. Chem.
284
27857-27865
2009
Homo sapiens
brenda
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
brenda
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
brenda
Chang, Y.; Zhang, X.; Horton, J.R.; Upadhyay, A.K.; Spannhoff, A.; Liu, J.; Snyder, J.P.; Bedford, M.T.; Cheng, X.
Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
Nat. Struct. Mol. Biol.
16
312-317
2009
Homo sapiens
brenda
Ushijima, Y.; Inoue, Y.H.; Konishi, T.; Kitazawa, D.; Yoshida, H.; Shimaji, K.; Kimura, H.; Yamaguchi, M.
Roles of histone H3K9 methyltransferases during Drosophila spermatogenesis
Chromosome Res.
20
319-331
2012
Drosophila melanogaster
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Rattus norvegicus
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Arabidopsis thaliana
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Homo sapiens
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Imai, K.; Kamio, N.; Cueno, M.E.; Saito, Y.; Inoue, H.; Saito, I.; Ochiai, K.
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Homo sapiens (O43463)
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Histone lysine methyltransferase SUV39H1 is a potent target for epigenetic therapy of hepatocellular carcinoma
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Homo sapiens (O43463), Homo sapiens (Q15047), Homo sapiens
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Hsiao, S.M.; Chen, M.W.; Chen, C.A.; Chien, M.H.; Hua, K.T.; Hsiao, M.; Kuo, M.L.; Wei, L.H.
The H3K9 methyltransferase G9a represses E-cadherin and is associated with myometrial invasion in endometrial cancer
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Homo sapiens
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Histone methyltransferase G9a modulates hepatic insulin signaling via regulating HMGA1
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Homo sapiens (Q96KQ7)
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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.
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Mus musculus (Q9Z148), Mus musculus
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Au Yeung, W.K.; BrindAmour, J.; Hatano, Y.; Yamagata, K.; Feil, R.; Lorincz, M.C.; Tachibana, M.; Shinkai, Y.; Sasaki, H.
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Mus musculus (Q9Z148), Mus musculus
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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
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Mus musculus (Q9Z148), Mus musculus
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Gu, Q.; Ji, T.; Sun, X.; Huang, H.; Zhang, H.; Lu, X.; Wu, L.; Huo, R.; Wu, H.; Gao, X.
Histone H3 lysine 9 methyltransferase FvDim5 regulates fungal development, pathogenicity and osmotic stress responses in Fusarium verticillioides
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Fusarium verticillioides (W7MCU7), Fusarium verticillioides, Fusarium verticillioides 7600 (W7MCU7)
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Mus musculus (Q9Z148)
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Botrytis cinerea (A0A384JX50), Botrytis cinerea, Botrytis cinerea B05.10 (A0A384JX50)
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Homo sapiens (Q8TEK3)
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Mus musculus (O54864)
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Tachibana, M.; Sugimoto, K.; Fukushima, T.; Shinkai, Y.
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Homo sapiens (Q96KQ7)
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Xiong, Y.; Li, F.; Babault, N.; Dong, A.; Zeng, H.; Wu, H.; Chen, X.; Arrowsmith, C.H.; Brown, P.J.; Liu, J.; Vedadi, M.; Jin, J.
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Homo sapiens (Q96KQ7)
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Homo sapiens (O43463), Homo sapiens
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The H3K9 methyltransferase SETDB1 maintains female identity in Drosophila germ cells
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Drosophila melanogaster, Drosophila melanogaster (Q32KD2)
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Akoury, E.; Ma, G.; Demolin, S.; Broenner, C.; Zocco, M.; Cirilo, A.; Ivic, N.; Halic, M.
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Schizosaccharomyces pombe
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Pharmacological and transcriptional inhibition of the G9a histone methyltransferase suppresses proliferation and modulates redox homeostasis in human microvascular endothelial cells
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Homo sapiens (Q96KQ7), Homo sapiens
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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.
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Drosophila melanogaster
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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
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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
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Homo sapiens (Q96KQ7)
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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
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Mus musculus (Q96KQ7)
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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
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Mus musculus (O54864)
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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
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Homo sapiens (O43463)
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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
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Drosophila melanogaster (Q32KD2), Drosophila melanogaster
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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
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Sus scrofa (F1SS95), Sus scrofa
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