Information on EC 2.1.1.43 - histone-lysine N-methyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9BYW2

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Homo sapiens
UNIPROT: Q9BYW2


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.43
-
RECOMMENDED NAME
GeneOntology No.
histone-lysine N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
carnitine metabolism
-
-
Lysine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:histone-L-lysine N6-methyltransferase
One of a group of enzymes methylating proteins; see also EC 2.1.1.59, [cytochrome-c]-lysine N-methyltransferase and EC 2.1.1.60, calmodulin-lysine N-methyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9055-08-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + chicken nucleosome
S-adenosyl-L-homocysteine + chicken nucleosome N6-methyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + histone H3(K36) N6-methyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + histone H3(peptide 21-44)
S-adenosyl-L-homocysteine + histone H3(peptide21-44) N6-methyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + histone H3(peptide31-50)
S-adenosyl-L-homocysteine + N6-methylated K36 in histone H3(peptide 31-50)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H4(peptide35-55)
S-adenosyl-L-homocysteine + N6-methylated K44 in histone H4(peptide 35-55)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + recombinant nucleosome
S-adenosyl-L-homocysteine + recombinant nucleosome N6-methyl-L-lysine
show the reaction diagram
-
-
-
?
ARTKQTARKSTGGKAPRK(biot)G + S-adenosyl-L-methionine
ART-methyl-KQTARKSTGGKAPRK(biot)G + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + biotin-aminohexanoyl-GSRAHSSHLKSKKGQSTSRH
?
show the reaction diagram
-
100% activity
-
-
?
S-adenosyl-L-methionine + biotin-ARTKQTARKST
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + CDYL1 protein
?
show the reaction diagram
-
target of histone lysine methyltransferase G9a (KMT1C)
-
-
?
S-adenosyl-L-methionine + chicken nucleosome
S-adenosyl-L-homocysteine + chicken nucleosome N6-methyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + CSB protein
?
show the reaction diagram
-
target of histone lysine methyltransferase G9a (KMT1C)
-
-
?
S-adenosyl-L-methionine + DNA methyltransferase 1
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + estrogen receptor alpha(K302)
?
show the reaction diagram
estrogen receptor alpha is directly methylated at lysine-302 by SET-7, a K303R mutation inhibits methylation at K302 in vivo
-
-
?
S-adenosyl-L-methionine + HDAC1 protein
?
show the reaction diagram
-
target of histone lysine methyltransferase G9a (KMT1C)
-
-
?
S-adenosyl-L-methionine + histone (K4)
S-adenosyl-L-homocysteine + methylated histone (K4)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H1
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H1.4(K121)
?
show the reaction diagram
-
less than 10% methylation at Lys-34
-
-
?
S-adenosyl-L-methionine + histone H1.4(K26)
?
show the reaction diagram
-
70% methylation at Lys-26, methylation of the K26A mutant of histone H1.4 is strongly reduced but not completely abolished
-
-
?
S-adenosyl-L-methionine + histone H1.4(K34)
?
show the reaction diagram
-
10-15% methylation at Lys-34
-
-
?
S-adenosyl-L-methionine + histone H1.4(K52)
?
show the reaction diagram
-
less than 1% methylation at Lys-34
-
-
?
S-adenosyl-L-methionine + histone H2A
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H2B
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H2B L-lysine
S-adenosyl-L-homocysteine + histone H2B N6-methyl-L-lysine
show the reaction diagram
-
about 150% activity compared to biotin-aminohexanoyl-GSRAHSSHLKSKKGQSTSRH, H2B is more efficient substrate with 3fold higher specific activity compared to H3
-
-
?
S-adenosyl-L-methionine + histone H3
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H3 L-lysine
S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine
show the reaction diagram
-
efficient substrate, about 40% activity compared to biotin-aminohexanoyl-GSRAHSSHLKSKKGQSTSRH
-
-
?
S-adenosyl-L-methionine + histone H3(K27)
?
show the reaction diagram
S-adenosyl-L-methionine + histone H3(K27)
S-adenosyl-L-homocysteine + N-methylated histone H3(K27)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K27)
S-adenosyl-L-homocysteine + N6-methylated histone H3(K27)
show the reaction diagram
-
-
isoforms NSD1, NSD2 and NSD3, mainly trimethylation
-
?
S-adenosyl-L-methionine + histone H3(K36)
?
show the reaction diagram
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + histone H3(K36) N6-methyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + N-methylated histone H3(K36)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K36)
S-adenosyl-L-homocysteine + N6-methylated histone H3(K36)
show the reaction diagram
-
-
preferable in vitro substrate for isoform NSD1
-
?
S-adenosyl-L-methionine + histone H3(K4)
?
show the reaction diagram
S-adenosyl-L-methionine + histone H3(K4)
S-adenosyl-L-homocysteine + N6-methylated histone H3(K4)
show the reaction diagram
-
-
isoforms NSD1 and NSD2, mainly trimethylation
-
?
S-adenosyl-L-methionine + histone H3(K79)
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K79)
S-adenosyl-L-homocysteine + N6-methylated histone H3(K79)
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
?
show the reaction diagram
S-adenosyl-L-methionine + histone H3(K9)
S-adenosyl-L-homocysteine + N6-methylated histone H3(K9)
show the reaction diagram
-
-
isoforms NSD1, NSD2 and NSD3, mainly dimethylation
-
?
S-adenosyl-L-methionine + histone H3(N)
?
show the reaction diagram
methylated by GST-HYPB protein
-
-
?
S-adenosyl-L-methionine + histone H3(N27)
?
show the reaction diagram
methylated by GST-HYPB protein
-
-
?
S-adenosyl-L-methionine + histone H3(N4)
?
show the reaction diagram
methylated by GST-HYPB protein
-
-
?
S-adenosyl-L-methionine + histone H3(N9)
?
show the reaction diagram
methylated by GST-HYPB protein
-
-
?
S-adenosyl-L-methionine + histone H3.2 L-lysine
S-adenosyl-L-homocysteine + histone H3.2 N6-methyl-L-lysine
show the reaction diagram
-
about 30% activity compared to biotin-aminohexanoyl-GSRAHSSHLKSKKGQSTSRH
-
-
?
S-adenosyl-L-methionine + histone H4
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + histone H4
S-adenosyl-L-homocysteine + N-methylated histone H4
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + histone H4 L-lysine
S-adenosyl-L-homocysteine + histone H4 N6-methyl-L-lysine
show the reaction diagram
-
best substrate, H4 is more efficient substrate with 5fold higher specific activity compared to H3, about 240% activity compared to biotin-aminohexanoyl-GSRAHSSHLKSKKGQSTSRH
-
-
?
S-adenosyl-L-methionine + histone H4(K20)
?
show the reaction diagram
S-adenosyl-L-methionine + histone H4(K20)
S-adenosyl-L-homocysteine + N6-methylated histone H4(K20)
show the reaction diagram
-
-
isoform NSD1, mainly mono- and trimethylation, isoforms NSD2 and NSD3, mainly di-and trimethylation
-
?
S-adenosyl-L-methionine + histone H4(K344)
?
show the reaction diagram
histone H4 lysine-44 is the primary target of NSD2 in the case of octamer substrates, irrespective of the histones being native or recombinant
-
-
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
show the reaction diagram
S-adenosyl-L-methionine + p300/CBP-associated factor
?
show the reaction diagram
-
K78 and K89 are preferentially methylated in full-length p300/CBP-associated factor in vitro
-
-
?
S-adenosyl-L-methionine + p53
?
show the reaction diagram
S-adenosyl-L-methionine + p53 (K382)
?
show the reaction diagram
-
SET8 activity is strongly reduced by the arginine methylation at position R379
-
-
?
S-adenosyl-L-methionine + p53 protein
S-adenosyl-L-homocysteine + N-methylated p53 protein
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + p53(K373)
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + recombinant nucleosome
S-adenosyl-L-homocysteine + recombinant nucleosome N6-methyl-L-lysine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + TAF10-K189 peptide
?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + transcriptional factor p53
?
show the reaction diagram
-
methylation of transcriptional factor p53 with the sequence LKSKKGQSTY occurs at Lys-4
-
-
?
S-adenosyl-L-methionine + WIZ protein
?
show the reaction diagram
-
target of histone lysine methyltransferase G9a (KMT1C)
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
the enzyme contains three tightly bound zinc ions that are important for maintaining the structural integrity and catalytic activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-chloro-6,7-dimethoxyquinazoline
-
less than 30% inhibition at 0.001 mM
5-(6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-4-(1-methylpiperidin-4-ylamino)quinazolin-7-yloxy)pentanamide
-
less than 30% inhibition at 0.001 mM
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-4-(1-methylpiperidin-4-yloxy)quinazoline
-
less than 30% inhibition at 0.001 mM
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpyrrolidin-3-yl)quinazolin-4-amine
-
-
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(piperidin-4-yl)quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(tetrahydro-2H-pyran-4-yl)quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
6,7-dimethoxy-2-(4-methylpiperazin-1-yl)-N-(1-methylpiperidin-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-morpholinoquinazolin-4-amine
-
-
6,7-dimethoxy-N-methyl-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
6,7-dimethoxy-N-methyl-2-(4-methyl-1,4-diazepan-1-yl)quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
6,7-dimethoxy-N2,N2-dimethyl-N4-(1-methylpiperidin-4-yl)-quinazoline-2,4-diamine
-
-
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-7-(3-(methylamino)-propoxy)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-7-(4-methylpentyloxy)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(2-(2-(pyrrolidin-1-yl)ethoxy)ethoxy)quinazolin-4-amine
-
-
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(3-(piperidin-1-yl)propoxy)quinazolin-4-amine
-
-
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(3-(pyrrolidin-1-yl)propoxy)quinazolin-4-amine
-
-
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(3-morpholinopropoxy)quinazolin-4-amine
-
-
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(piperidin-3-ylmethoxy)quinazolin-4-amine
-
-
6-methoxy-7-(3-(methyl(propyl)amino)propoxy)-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
6-methoxy-7-(4-methoxybutoxy)-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
7-(2-(2-(dimethylamino)ethoxy)ethoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
UNC0321, G9a inhibitor with picomolar potency and the most potent G9a inhibitor
7-(2-(dimethylamino)ethoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
7-(3-(diethylamino)propoxy)-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
-
UNC0224, potent G9a inhibitor
7-(4-(dimethylamino)butoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
7-(5-(dimethylamino)pentyloxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
7-(5-aminopentyloxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
7-(6-(dimethylamino)hexyloxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
-
aldosterone
-
-
BIX-01294
BIX-01338
chaetocin
cyclohexamide
-
decreases nuclear G9a protein but does not prevent its relative increase during hypoxic stress
eosin
-
AMI-5, numerous different substitutes of eosin synthesized and tested for inhibition
N-(1-benzylpiperidin-4-yl)-6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)quinazolin-4-amine
-
BIX01294, selective small molecule inhibitor of enzyme forms G9a and GLP
N-cyclohexyl-6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
N-cyclopropyl-6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
N-isopropyl-6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-quinazolin-4-amine
-
less than 30% inhibition at 0.001 mM
N1-(2-(6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-4-(1-methylpiperidin-4-ylamino)quinazolin-7-yloxy)ethyl)-N1,N2,N2-trimethylethane-1,2-diamine
-
-
N2,N2-diethyl-6,7-dimethoxy-N4-(1-methylpiperidin-4-yl)quinazoline-2,4-diamine
-
-
S-adenosyl-L-homocysteine
-
competitive inhibition
sinefungin
-
-
TCEP
-
suppresses activity in a dose-dependent manner
tert-butyl 4-(6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-4-(1-methylpiperidin-4-ylamino)quinazolin-7-yloxy)butylcarbamate
-
less than 30% inhibition at 0.001 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deferoxamine
-
increases G9a protein and activity in A549 cells, moreover, increases the methyltransferase activity of overexpressed GFP-hG9a fusion proteins
dimethyloxalylglycine
-
increases G9a protein and activity in A549 cells
heat shock protein 90alpha
-
the interaction of SMYD2 with heat shock protein 90alpha enhances SMYD2 histone methyltransferase activity and specificity for histone H3 at lysine 4 by 10fold, histone H3K36 methyltransferase activity is independent of ist interaction with heat shock protein 90alpha
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0089
chicken nucleosome
pH 9.0, 23C
-
0.0005
histone H3(peptide 21-44)
pH 9.0, 23C
-
0.0081
recombinant nucleosome
pH 9.0, 23C
-
0.0033 - 0.0055
S-adenosyl-L-methionine
0.00027
chicken nucleosome
pH 9.0, 23C
-
0.00003
recombinant nucleosome
pH 9.0, 23C
-
0.00012 - 0.0038
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0061
chicken nucleosome
pH 9.0, 23C
-
0.0031
histone H3(peptide 21-44)
pH 9.0, 23C
-
0.0013
recombinant nucleosome
pH 9.0, 23C
-
0.0031
chicken nucleosome
pH 9.0, 23C
-
0.0001
recombinant nucleosome
pH 9.0, 23C
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000063
7-(2-(2-(dimethylamino)ethoxy)ethoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00035
S-adenosyl-L-homocysteine
-
wild type enzyme, using p53 as cosubstrate, in 50 mM Tris pH 9.0, at 22C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00033
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00091
6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpyrrolidin-3-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00015
6,7-dimethoxy-2-(4-methylpiperazin-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00055
6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-(piperidin-1-yl)-quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.0016
6,7-dimethoxy-N-(1-methylpiperidin-4-yl)-2-morpholinoquinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.0011
6,7-dimethoxy-N2,N2-dimethyl-N4-(1-methylpiperidin-4-yl)-quinazoline-2,4-diamine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00012
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-7-(3-(methylamino)-propoxy)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.0034
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-7-(4-methylpentyloxy)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000057
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(2-(2-(pyrrolidin-1-yl)ethoxy)ethoxy)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000025
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(3-(piperidin-1-yl)propoxy)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000008
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(3-(pyrrolidin-1-yl)propoxy)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00088
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(3-morpholinopropoxy)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.0015
6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)-7-(piperidin-3-ylmethoxy)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00051
6-methoxy-7-(3-(methyl(propyl)amino)propoxy)-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000009
7-(2-(2-(dimethylamino)ethoxy)ethoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00011
7-(2-(dimethylamino)ethoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000052
7-(3-(diethylamino)propoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000043
7-(3-(dimethylamino)propoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00014
7-(4-(dimethylamino)butoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000095
7-(5-(dimethylamino)pentyloxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000235
7-(5-aminopentyloxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.0015
7-(6-(dimethylamino)hexyloxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.0007 - 0.0027
BIX-01294
0.005
BIX-01338
Homo sapiens;
-
histone lysine methyltransferase G9a
0.00018
N-(1-benzylpiperidin-4-yl)-6,7-dimethoxy-2-(4-methyl-1,4-diazepan-1-yl)quinazolin-4-amine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.000345
N1-(2-(6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-4-(1-methylpiperidin-4-ylamino)quinazolin-7-yloxy)ethyl)-N1,N2,N2-trimethylethane-1,2-diamine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.00091
N2,N2-diethyl-6,7-dimethoxy-N4-(1-methylpiperidin-4-yl)quinazoline-2,4-diamine
Homo sapiens;
-
enzyme form G9a, in PBS buffer, pH 7.4, at 22C
0.02
sinefungin
Homo sapiens;
-
pH 9.8, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.1
-
SMYD2 activity increases dramatically from pH 8.5 to pH 9.2, peaking at pH 9.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32
-
SMYD2 has maximal activity at about 32C, with activity rapidly dropping at temperatures above 37C
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 40
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
interaction between growth factor independent 1 and G9a in vivo
Manually annotated by BRENDA team
-
myeloma cell, derived from KMS-11 cell
Manually annotated by BRENDA team
-
myeloma cell, derived from KMS-11 cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
G9a protein not detected in the cytoplasm
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
SDS-PAGE
49700
-
calculated from amino acid sequence
52000
-
about 52000 Da, SDS-PAGE
53000
-
x * 53000, MALDI-TOF mass spectrometry
53100
-
x * 53100, calculated from amino acid sequence
60000
-
x * 60000, GST-tagged SET8 domain, SDS-PAGE
400000 - 800000
-
the activity peak migrates at high molecular mass (400000-800000 Da), gel filtration
450000
Western analysis of Set1/CXXC finger protein 1 complex
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 45000, SDS-PAGE
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
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)
-
molecular modelling and docking of 6-mer peptides H3K4 1-7, H3K9 5-11, H3K27 23-29, H3K36 32-38, H3K79 75-81, H4K20 16-22 with the catalytic domain of isoform NSD1, NSD2, NSD3
-
the ternary structures of SET7-estrogen receptor peptide-AdoMet analog are solved by molecular replacement
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SMYD2 shows minimal activity in HEPES buffer with pH values below 7.5 and moderate activity in Tris buffer from pH 7.5 to pH 8.5
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Tween-20
-
0.001% (w/v) Tween-20 enhances SMYD2 methyltransferase activity by more than 4fold. The enzyme remains stable in the presence of 0.01-0.05% (v/v) Tween-20
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA bead chromatography, glutathione bead chromatography, and Superdex 200 gel filtration
ammonium sulfateprecipitation, heparin-Sepharose column chromatography, DEAE 5PW column chromatography, Mono S column chromatography, and Superose 6 gel filtration
-
anti-FLAG antibody immunoprecipitation
-
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
-
nickel-chelating column chromatography, HiTrap-Q column chromatography, and Superdex-75 and -200 gel filtration
-
Sepharose bead chromatography
-
tandem affinity purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GST-SET domain fusion proteins are expressed in Escherichia coli, SET2-C is expressed in baculovirus insect cells
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 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in HEK-293 cells
-
expressed in LNCaP, MCF-7, and A-549 cells
-
expressed in Sf21 insect cells
-
expressed in U2OS cells
-
expression in Escherichia coli and HEK-293 cell
expression of wild-type SET9 and mutants in Escherichia coli, His-tagged
-
FLAG-tagged and untagged SMYD3 proteins are expressed in HEK-293T and MCF-7 cells
-
for HMTase activity assays and glutathione S-transferase pull-down assays subcloned into pGEX-5X1 vector, for transactivation assays subcloned into pBIND vector, for coimmunoprecipitation assays subcloned into pFLAG-CMV4 vector, expressed in Escherichia coli strain BL21
-
glutathione-S-transferase-fusion protein, SET gene
into the pEGFP-C2 vector
recombinant full-length G9a is obtained using a baculoviral expression system
-
TAP-tagged protein is expressed in L929 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RE-IIBP expression and histone methylation are increased in leukemia patients
-
the enzyme is overexpressed in human cancer cells
-
the expression of SET7/9 is not altered by tissue necrosis factor-alpha treatment
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R1952W
-
mutation identifiied in Sotos patient, complete loss of activity
R1984Q
-
mutation identifiied in Sotos patient, complete loss of activity
R2017W
-
mutation identifiied in Sotos patient, complete loss of activity
Y1997C
-
mutation identifiied in Sotos patient, complete loss of activity
C483A
-
no activity, the SET domain cysteine 483 is a critical residue for the histone methyltransferase activity of RE-IIBP
DELTAGEE
-
the deletion mutant shows no histone methyltransferase activity
DELTANHSC
-
the deletion mutant shows no histone methyltransferase activity
G18A/G20A
-
the mutations impaire S-adenosyl-L-methionine binding and significantly decrease enzymatic activity
H2113K
-
methyltransferase-deficient mutant
H297A
-
catalytically inactive mutant
R477A
-
no activity, the SET domain 477 is a critical residue for the histone methyltransferase activity of RE-IIBP
Y245A
-
the mutant acts as a trimethylase
Y245F
-
the mutation converts the enzyme from a mono- to a dimethyltransferase
additional information
-
arginine 1122-to-histidine mutant of HYPB, both the HMTase activity and auto-methylation activity is significantly impaired
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
Sotos mutations in R1952, R1984, R2017, and Y1997 in the SET domain inactivate the enzyme
analysis
medicine
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