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Information on EC 2.1.1.355 - [histone H3]-lysine9 N-trimethyltransferase and Organism(s) Homo sapiens and UniProt Accession O43463

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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.
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This record set is specific for:
Homo sapiens
UNIPROT: O43463
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
histone methyltransferase, suv39h1, setdb1, ehmt2, su(var)3-9, ehmt1, prdm2, h3k9 methyltransferase, prdm8, histone methyltransferase g9a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EHMT1
-
-
-
-
EHMT2
G9a histone methyltransferase
-
G9a-like protein lysine methyltransferase
-
-
H3K9 methyltransferase
histone H3 Lys79 methyltransferase
-
histone H3 lysine methyltransferase G9a
-
-
histone lysine methyltransferase G9a
-
-
histone methyltransferase
-
histone methyltransferase G9a
-
-
HKMT
-
-
KMT1A
-
-
-
-
KMT1B
-
-
-
-
KMT1C
KMT1D
-
-
-
-
KMT1F
-
-
-
-
lysine-preferring HMTase
-
MT8
-
-
-
-
PRDM2
-
-
-
-
SETDB1
SUV39H1
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[histone H3]-L-lysine9 N6-methyltransferase
This entry describes several enzymes that successively methylate the L-lysine9 residue of histone H3 (H3K9), ultimately generating a trimethylated form. These modifications influence the binding of chromatin-associated proteins. In general, the methylation of H3K9 leads to transcriptional repression of the affected target genes. cf. EC 2.1.1.367, [histone H3]-lysine9 N-methyltransferase, EC 2.1.1.368, [histone H3]-lysine9 N-dimethyltransferase, and EC 2.1.1.366, [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
show the reaction diagram
-
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
show the reaction diagram
3 S-adenosyl-L-methionine + biotinylated [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + biotinylated [histone H3]-N6-methyl-L-lysine9
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
show the reaction diagram
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
show the reaction diagram
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
show the reaction diagram
S-adenosyl-L-methionine + DNA methyltransferase 1
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + H2B ubiquitinated nucleosome
?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + histone H3(K9)
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
overall reaction
-
-
?
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
show the reaction diagram
-
-
-
?
3 S-adenosyl-L-methionine + a [histone H3]-L-lysine9
3 S-adenosyl-L-homocysteine + a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
show the reaction diagram
S-adenosyl-L-methionine + a [histone H3]-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6-methyl-L-lysine9
show the reaction diagram
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
show the reaction diagram
S-adenosyl-L-methionine + a [histone H3]-N6-methyl-L-lysine9
S-adenosyl-L-homocysteine + a [histone H3]-N6,N6-dimethyl-L-lysine9
show the reaction diagram
S-adenosyl-L-methionine + H2B ubiquitinated nucleosome
?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
5 mM used in assay conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
chaetocin
specific isoform Suv39 h1 inhibitor
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
-
BIX-01294
chaetocin
-
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-ethylpiperidin-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
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
-
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
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007 - 0.0019
BIX-01294
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
G9a protein not detected in the cytoplasm
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUV91_HUMAN
412
0
47907
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ubiquitination
ubiquitination of lysine 867 of the human SETDB1 protein upregulates its histone H3 lysine 9 methyltransferase 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)
-
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)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
R282A
the mutation dramatically decreases the enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-FLAG M2 affinity column chromatography
glutahione S-transferase affinity column chromatography, anion exchange column chromatography, and gel filtration
glutathione Sepharose 4B column chromatography
HiTrap chelating column chromatography and Superdex S200 gel filtration
nickel-chelating column chromatography, HiTrap-Q column chromatography, and Superdex-75 and -200 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 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 codon-plus RIL cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Mus musculus
expressed in Sf9 insect cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased enzyme expression is identified in endometrial cancer tissues
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Lu, Z.; Tian, Y.; Salwen, H.R.; Chlenski, A.; Godley, L.A.; Raj, J.U.; Yang, Q.
Histone-lysine methyltransferase EHMT2 is involved in proliferation, apoptosis, cell invasion, and DNA methylation of human neuroblastoma cells
Anticancer Drugs
24
484-493
2013
Homo sapiens
Manually annotated by BRENDA team
Imai, K.; Kamio, N.; Cueno, M.E.; Saito, Y.; Inoue, H.; Saito, I.; Ochiai, K.
Role of the histone H3 lysine 9 methyltransferase Suv39 h1 in maintaining Epstein-Barr virus latency in B95-8 cells
FEBS J.
281
2148-2158
2014
Homo sapiens (O43463)
Manually annotated by BRENDA team
Chiba, T.; Saito, T.; Yuki, K.; Zen, Y.; Koide, S.; Kanogawa, N.; Motoyama, T.; Ogasawara, S.; Suzuki, E.; Ooka, Y.; Tawada, A.; Otsuka, M.; Miyazaki, M.; Iwama, A.; Yokosuka, O.
Histone lysine methyltransferase SUV39H1 is a potent target for epigenetic therapy of hepatocellular carcinoma
Int. J. Cancer
136
289-298
2015
Homo sapiens (O43463), Homo sapiens (Q15047), Homo sapiens
Manually annotated by BRENDA team
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
Ann. Surg. Oncol.
22
S1556-S1565
2015
Homo sapiens
Manually annotated by BRENDA team
Xue, W.; Huang, J.; Chen, H.; Zhang, Y.; Zhu, X.; Li, J.; Zhang, W.; Yuan, Y.; Wang, Y.; Zheng, L.; Huang, K.
Histone methyltransferase G9a modulates hepatic insulin signaling via regulating HMGA1
Biochim. Biophys. Acta
1864
338-346
2018
Homo sapiens (Q96KQ7)
Manually annotated by BRENDA team
Jang, S.; Kang, C.; Yang, H.S.; Jung, T.; Hebert, H.; Chung, K.Y.; Kim, S.J.; Hohng, S.; Song, J.J.
Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase
Genes Dev.
33
620-625
2019
Homo sapiens (Q8TEK3)
Manually annotated by BRENDA team
Tachibana, M.; Sugimoto, K.; Fukushima, T.; Shinkai, Y.
Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3
J. Biol. Chem.
276
25309-25317
2001
Homo sapiens (Q96KQ7)
Manually annotated by BRENDA team
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.
Discovery of potent and selective inhibitors for G9a-like protein (GLP) lysine methyltransferase
J. Med. Chem.
60
1876-1891
2017
Homo sapiens (Q96KQ7)
Manually annotated by BRENDA team
Mueller, M.M.; Fierz, B.; Bittova, L.; Liszczak, G.; Muir, T.W.
A two-state activation mechanism controls the histone methyltransferase Suv39h1
Nat. Chem. Biol.
12
188-193
2016
Homo sapiens (O43463), Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team