Proteins > N-lysine methyltransferase SMYD2
Page last updated: 2024-08-08 00:18:17
N-lysine methyltransferase SMYD2
An N-lysine methyltransferase SMYD2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NRG4]
Synonyms
EC 2.1.1.-;
HSKM-B;
Histone methyltransferase SMYD2;
2.1.1.354;
Lysine N-methyltransferase 3C;
SET and MYND domain-containing protein 2
Research
Bioassay Publications (11)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 7 (63.64) | 24.3611 |
2020's | 4 (36.36) | 2.80 |
Compounds (4)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
az 505 | Homo sapiens (human) | Kd | 167.0000 | 3 | 3 |
Positioning of an unprecedented 1,5-oxaza spiroquinone scaffold into SMYD2 inhibitors in epigenetic space.European journal of medicinal chemistry, , Jan-05, Volume: 227, 2022
Protein Lysine Methyltransferase SMYD2: A Promising Small Molecule Target for Cancer Therapy.Journal of medicinal chemistry, , 08-11, Volume: 65, Issue:15, 2022
HIV latency reversal agents: A potential path for functional cure?European journal of medicinal chemistry, , Mar-05, Volume: 213, 2021
Discovery and Characterization of a Highly Potent and Selective Aminopyrazoline-Based in Vivo Probe (BAY-598) for the Protein Lysine Methyltransferase SMYD2.Journal of medicinal chemistry, , 05-26, Volume: 59, Issue:10, 2016
Selective inhibitors of protein methyltransferases.Journal of medicinal chemistry, , Feb-26, Volume: 58, Issue:4, 2015
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.ACS medicinal chemistry letters, , Jun-11, Volume: 6, Issue:6, 2015
Oncoepigenomics: making histone lysine methylation count.European journal of medicinal chemistry, , Volume: 56, 2012
Positioning of an unprecedented 1,5-oxaza spiroquinone scaffold into SMYD2 inhibitors in epigenetic space.European journal of medicinal chemistry, , Jan-05, Volume: 227, 2022
Protein Lysine Methyltransferase SMYD2: A Promising Small Molecule Target for Cancer Therapy.Journal of medicinal chemistry, , 08-11, Volume: 65, Issue:15, 2022
Synthesis and structure-activity relationship studies of LLY-507 analogues as SMYD2 inhibitors.Bioorganic & medicinal chemistry letters, , 11-15, Volume: 30, Issue:22, 2020
Histone methyl transferases: A class of epigenetic opportunities to counter uncontrolled cell proliferation.European journal of medicinal chemistry, , Mar-15, Volume: 166, 2019
Discovery and Characterization of a Highly Potent and Selective Aminopyrazoline-Based in Vivo Probe (BAY-598) for the Protein Lysine Methyltransferase SMYD2.Journal of medicinal chemistry, , 05-26, Volume: 59, Issue:10, 2016
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.ACS medicinal chemistry letters, , Jun-11, Volume: 6, Issue:6, 2015
Selective inhibitors of protein methyltransferases.Journal of medicinal chemistry, , Feb-26, Volume: 58, Issue:4, 2015
Enables
This protein enables 9 target(s):
Target | Category | Definition |
RNA polymerase II complex binding | molecular function | Binding to an RNA polymerase II core enzyme, a multisubunit eukaryotic nuclear RNA polymerase typically composed of twelve subunits. [GOC:txnOH] |
p53 binding | molecular function | Binding to one of the p53 family of proteins. [GOC:hjd] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
lysine N-methyltransferase activity | molecular function | Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the epsilon-amino group of a lysine residue. [GOC:mah] |
protein-lysine N-methyltransferase activity | molecular function | Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the epsilon-amino group of a lysine residue in a protein substrate. [PMID:12054878] |
metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
histone H3K36 methyltransferase activity | molecular function | Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 36) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 36). This reaction is the addition of a methyl group to the lysine residue at position 36 of the histone H3 protein. [GOC:ai] |
histone H3 methyltransferase activity | molecular function | Catalysis of the reaction: S-adenosyl-L-methionine + a histone H3 = S-adenosyl-L-homocysteine + a methylated histone H3. Histone methylation generally occurs on either an arginine or a lysine residue. [PMID:28450737] |
histone H3K4 trimethyltransferase activity | molecular function | Catalysis of the reaction: L-lysyl4-[histone H3] + 3 S-adenosyl-L-methionine = 2 H+ + N6,N6-trimethyl-L-lysyl4-[histone H3] + 3 S-adenosyl-L-homocysteine. This reaction is the successive addition of three methyl groups to the unmethylated lysine residue at position 4 of histone H3, producing histone H3K4me3. [PMID:18375658, RHEA:60260] |
Located In
This protein is located in 4 target(s):
Target | Category | Definition |
nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
Active In
This protein is active in 1 target(s):
Target | Category | Definition |
nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
Involved In
This protein is involved in 8 target(s):
Target | Category | Definition |
negative regulation of transcription by RNA polymerase II | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II. [GOC:go_curators, GOC:txnOH] |
chromatin remodeling | biological process | A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication. [GOC:jid, GOC:vw, PMID:12042764, PMID:12697820] |
heart development | biological process | The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood. [GOC:jid, UBERON:0000948] |
negative regulation of cell population proliferation | biological process | Any process that stops, prevents or reduces the rate or extent of cell proliferation. [GOC:go_curators] |
peptidyl-lysine monomethylation | biological process | The methylation of peptidyl-lysine to form peptidyl-N6-methyl-L-lysine. [RESID:AA0076] |
peptidyl-lysine dimethylation | biological process | The methylation of peptidyl-lysine to form peptidyl-N6,N6-dimethyl-L-lysine. [RESID:AA0075] |
regulation of DNA damage response, signal transduction by p53 class mediator | biological process | Any process that modulates the frequency, rate or extent of the cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage. [GOC:jl] |
regulation of signal transduction by p53 class mediator | biological process | Any process that modulates the frequency, rate or extent of signal transduction by p53 class mediator. [GOC:TermGenie] |