Proteins > Histone-lysine N-methyltransferase, H3 lysine-79 specific
Page last updated: 2024-08-08 00:05:50
Histone-lysine N-methyltransferase, H3 lysine-79 specific
A histone-lysine N-methyltransferase, H3 lysine-79 specific that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q8TEK3]
Synonyms
EC 2.1.1.360;
DOT1-like protein;
Histone H3-K79 methyltransferase;
H3-K79-HMTase;
Lysine N-methyltransferase 4
Research
Bioassay Publications (15)
| 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 | 13 (86.67) | 24.3611 |
| 2020's | 2 (13.33) | 2.80 |
Compounds (11)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
New small molecule inhibitors of histone methyl transferase DOT1L with a nitrile as a non-traditional replacement for heavy halogen atoms.Bioorganic & medicinal chemistry letters, , 09-15, Volume: 26, Issue:18, 2016
A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L.Journal of medicinal chemistry, , Nov-27, Volume: 56, Issue:22, 2013
Bromo-deaza-SAH: a potent and selective DOT1L inhibitor.Bioorganic & medicinal chemistry, , Apr-01, Volume: 21, Issue:7, 2013
A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L.Journal of medicinal chemistry, , Nov-27, Volume: 56, Issue:22, 2013
Synthesis and structure-activity relationship investigation of adenosine-containing inhibitors of histone methyltransferase DOT1L.Journal of medicinal chemistry, , Sep-27, Volume: 55, Issue:18, 2012
Novel non-covalent LSD1 inhibitors endowed with anticancer effects in leukemia and solid tumor cellular models.European journal of medicinal chemistry, , Jul-05, Volume: 237, 2022
Why Some Targets Benefit from beyond Rule of Five Drugs.Journal of medicinal chemistry, , 11-27, Volume: 62, Issue:22, 2019
New small molecule inhibitors of histone methyl transferase DOT1L with a nitrile as a non-traditional replacement for heavy halogen atoms.Bioorganic & medicinal chemistry letters, , 09-15, Volume: 26, Issue:18, 2016
A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L.Journal of medicinal chemistry, , Nov-27, Volume: 56, Issue:22, 2013
Bromo-deaza-SAH: a potent and selective DOT1L inhibitor.Bioorganic & medicinal chemistry, , Apr-01, Volume: 21, Issue:7, 2013
Synthesis and structure-activity relationship investigation of adenosine-containing inhibitors of histone methyltransferase DOT1L.Journal of medicinal chemistry, , Sep-27, Volume: 55, Issue:18, 2012
Identification of DOT1L inhibitors by structure-based virtual screening adapted from a nucleoside-focused library.European journal of medicinal chemistry, , Mar-01, Volume: 189, 2020
New small molecule inhibitors of histone methyl transferase DOT1L with a nitrile as a non-traditional replacement for heavy halogen atoms.Bioorganic & medicinal chemistry letters, , 09-15, Volume: 26, Issue:18, 2016
Selective inhibitors of protein methyltransferases.Journal of medicinal chemistry, , Feb-26, Volume: 58, Issue:4, 2015
A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L.Journal of medicinal chemistry, , Nov-27, Volume: 56, Issue:22, 2013
Bromo-deaza-SAH: a potent and selective DOT1L inhibitor.Bioorganic & medicinal chemistry, , Apr-01, Volume: 21, Issue:7, 2013
Synthesis, Activity and Metabolic Stability of Non-Ribose Containing Inhibitors of Histone Methyltransferase DOT1L.MedChemComm, , May-01, Volume: 4, Issue:5, 2013
Oncoepigenomics: making histone lysine methylation count.European journal of medicinal chemistry, , Volume: 56, 2012
Why Some Targets Benefit from beyond Rule of Five Drugs.Journal of medicinal chemistry, , 11-27, Volume: 62, Issue:22, 2019
Preparation of 5'-deoxy-5'-amino-5'-C-methyl adenosine derivatives and their activity against DOT1L.Bioorganic & medicinal chemistry letters, , 11-15, Volume: 27, Issue:22, 2017
Discovery of Potent, Selective, and Structurally Novel Dot1L Inhibitors by a Fragment Linking Approach.ACS medicinal chemistry letters, , Mar-09, Volume: 8, Issue:3, 2017
Selective inhibitors of protein methyltransferases.Journal of medicinal chemistry, , Feb-26, Volume: 58, Issue:4, 2015
A medicinal chemistry perspective for targeting histone H3 lysine-79 methyltransferase DOT1L.Journal of medicinal chemistry, , Nov-27, Volume: 56, Issue:22, 2013
Enables
This protein enables 7 target(s):
| Target | Category | Definition |
|---|
| nucleic acid binding | molecular function | Binding to a nucleic acid. [GOC:jl] |
| DNA binding | molecular function | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). [GOC:dph, GOC:jl, GOC:tb, GOC:vw] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| histone methyltransferase activity | molecular function | Catalysis of the reaction: S-adenosyl-L-methionine + histone = S-adenosyl-L-homocysteine + methyl-histone. Histone methylation generally occurs on either an arginine or a lysine residue. [GOC:curators] |
| 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 H3K79 trimethyltransferase activity | molecular function | Catalysis of the reaction: L-lysyl79-[histone H3] + 3 S-adenosyl-L-methionine = 3 H+ + N6,N6,N6-trimethyl-L-lysyl79-[histone H3] + 3 S-adenosyl-L-homocysteine. This reaction is the successive addition of up to three methyl group to the lysine residue at position 79 of the histone H3 protein, producing H3K79me3. [PMID:15371351, RHEA:60328] |
| histone H3K79 methyltransferase activity | molecular function | Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 79) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 79). This reaction is the addition of a methyl group to the lysine residue at position 79 of the histone H3 protein. [GOC:mah, PMID:15371351] |
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] |
| intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
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] |
Part Of
This protein is part of 1 target(s):
| Target | Category | Definition |
|---|
| protein-containing complex | cellular component | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah] |
Involved In
This protein is involved in 9 target(s):
| Target | Category | Definition |
|---|
| gene expression | biological process | The process in which a gene's sequence is converted into a mature gene product (protein or RNA). This includes the production of an RNA transcript and its processing, as well as translation and maturation for protein-coding genes. [GOC:txnOH-2018, PMID:25934543, PMID:31580950] |
| heterochromatin formation | biological process | An epigenetic gene silencing mechanism in which chromatin is compacted into heterochromatin, resulting in a chromatin conformation refractory to transcription. This process starts with heterochromatin nucleation, its spreading, and ends with heterochromatin boundary formation. [PMID:25192661, PMID:33827924] |
| telomere organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of telomeres, terminal regions of a linear chromosome that include the telomeric DNA repeats and associated proteins. [GOC:dph, GOC:jl, GOC:mah] |
| methylation | biological process | The process in which a methyl group is covalently attached to a molecule. [GOC:mah] |
| positive regulation of transcription by RNA polymerase II | biological process | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH] |
| regulation of receptor signaling pathway via JAK-STAT | biological process | Any process that modulates the frequency, rate or extent of receptor signaling via JAK-STAT. [GOC:bf] |
| regulation of transcription regulatory region DNA binding | biological process | Any process that modulates the frequency, rate or extent of transcription regulatory region DNA binding. [GOC:obol] |
| DNA repair | biological process | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. [PMID:11563486] |
| DNA damage checkpoint signaling | biological process | A signal transduction process that contributes to a DNA damage checkpoint. [GOC:mah] |