Proteins > Protein arginine N-methyltransferase 1
Page last updated: 2024-08-07 13:42:42
Protein arginine N-methyltransferase 1
A protein arginine N-methyltransferase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q99873]
Synonyms
EC 2.1.1.319;
Histone-arginine N-methyltransferase PRMT1;
Interferon receptor 1-bound protein 4
Research
Bioassay Publications (16)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (12.50) | 29.6817 |
| 2010's | 11 (68.75) | 24.3611 |
| 2020's | 3 (18.75) | 2.80 |
Compounds (19)
Drugs with Inhibition Measurements
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| furamidine | Homo sapiens (human) | Kii | 26.0000 | 1 | 1 |
| furamidine | Homo sapiens (human) | Kis | 2.6000 | 1 | 1 |
Fascinating Transformation of SAM-Competitive Protein Methyltransferase Inhibitors from Nucleoside Analogues to Non-Nucleoside Analogues.Journal of medicinal chemistry, , 02-10, Volume: 65, Issue:3, 2022
Discovery of Decamidine as a New and Potent PRMT1 Inhibitor.MedChemComm, , Feb-01, Volume: 8, Issue:2, 2017
Discovery and mechanistic study of a class of protein arginine methylation inhibitors.Journal of medicinal chemistry, , Aug-26, Volume: 53, Issue:16, 2010
Small molecule inhibitors of histone arginine methyltransferases: homology modeling, molecular docking, binding mode analysis, and biological evaluations.Journal of medicinal chemistry, , Mar-22, Volume: 50, Issue:6, 2007
Fascinating Transformation of SAM-Competitive Protein Methyltransferase Inhibitors from Nucleoside Analogues to Non-Nucleoside Analogues.Journal of medicinal chemistry, , 02-10, Volume: 65, Issue:3, 2022
Discovery of Decamidine as a New and Potent PRMT1 Inhibitor.MedChemComm, , Feb-01, Volume: 8, Issue:2, 2017
Pharmacophore-based virtual screening and biological evaluation of small molecule inhibitors for protein arginine methylation.Journal of medicinal chemistry, , Sep-27, Volume: 55, Issue:18, 2012
Discovery and mechanistic study of a class of protein arginine methylation inhibitors.Journal of medicinal chemistry, , Aug-26, Volume: 53, Issue:16, 2010
Pharmacophore-based screening of diamidine small molecule inhibitors for protein arginine methyltransferases.RSC medicinal chemistry, , Jan-01, Volume: 12, Issue:1, 2021
Discovery of Decamidine as a New and Potent PRMT1 Inhibitor.MedChemComm, , Feb-01, Volume: 8, Issue:2, 2017
Diamidine compounds for selective inhibition of protein arginine methyltransferase 1.Journal of medicinal chemistry, , Mar-27, Volume: 57, Issue:6, 2014
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
Design and synthesis of novel PRMT1 inhibitors and investigation of their binding preferences using molecular modelling.Bioorganic & medicinal chemistry letters, , 10-15, Volume: 27, Issue:20, 2017
Exploration of cyanine compounds as selective inhibitors of protein arginine methyltransferases: synthesis and biological evaluation.Journal of medicinal chemistry, , Feb-12, Volume: 58, Issue:3, 2015
Discovery and structure-activity analysis of 4-((5-nitropyrimidin-4-yl)amino)benzimidamide derivatives as novel protein arginine methyltransferase 1 (PRMT1) inhibitors.Bioorganic & medicinal chemistry letters, , Nov-15, Volume: 25, Issue:22, 2015
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
Pharmacophore-based screening of diamidine small molecule inhibitors for protein arginine methyltransferases.RSC medicinal chemistry, , Jan-01, Volume: 12, Issue:1, 2021
Discovery of Decamidine as a New and Potent PRMT1 Inhibitor.MedChemComm, , Feb-01, Volume: 8, Issue:2, 2017
Diamidine compounds for selective inhibition of protein arginine methyltransferase 1.Journal of medicinal chemistry, , Mar-27, Volume: 57, Issue:6, 2014
Discovery and mechanistic study of a class of protein arginine methylation inhibitors.Journal of medicinal chemistry, , Aug-26, Volume: 53, Issue:16, 2010
Target-based approach to inhibitors of histone arginine methyltransferases.Journal of medicinal chemistry, , May-17, Volume: 50, Issue:10, 2007
Enables
This protein enables 16 target(s):
| Target | Category | Definition |
|---|
| RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| methyltransferase activity | molecular function | Catalysis of the transfer of a methyl group to an acceptor molecule. [ISBN:0198506732] |
| N-methyltransferase activity | molecular function | Catalysis of the transfer of a methyl group to the nitrogen atom of an acceptor molecule. [GOC:ai] |
| protein methyltransferase activity | molecular function | Catalysis of the transfer of a methyl group (CH3-) to a protein. [GOC:jl] |
| methyl-CpG binding | molecular function | Binding to a methylated cytosine/guanine dinucleotide. [GOC:jl, PMID:11746232] |
| protein-arginine N-methyltransferase activity | molecular function | Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine. [GOC:mah, PMID:12351636, PMID:31284549] |
| enzyme binding | molecular function | Binding to an enzyme, a protein with catalytic activity. [GOC:jl] |
| protein-arginine omega-N monomethyltransferase activity | molecular function | Catalysis of the addition of a methyl group to either of the unmethylated terminal nitrogen atoms (also called omega nitrogen) in peptidyl-arginine to form an omega-N-G-monomethylated arginine residue. The reaction is S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine. [EC:2.1.1.321, PMID:14705965, RESID:AA0069] |
| protein-arginine omega-N asymmetric methyltransferase activity | molecular function | Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the same terminal nitrogen (omega nitrogen) residue that was previously methylated, resulting in asymmetrical peptidyl-N(omega),N(omega)-dimethylated arginine residues. [PMID:14705965] |
| 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] |
| identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
| histone H4R3 methyltransferase activity | molecular function | Catalysis of the reaction: S-adenosyl-L-methionine + (histone H4)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H4)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to the arginine residue at position 3 of histone H4, producing histone H4R3me. [GOC:mah, PMID:17898714] |
| mitogen-activated protein kinase p38 binding | molecular function | Binding to mitogen-activated protein kinase p38, an enzyme that catalyzes the transfer of phosphate from ATP to hydroxyl side chains on proteins in response to mitogen activation. [GOC:curators, PMID:17827184] |
| GATOR1 complex binding | molecular function | Binding to a GATOR1 complex. [PMID:28199306] |
| S-adenosyl-L-methionine binding | molecular function | Binding to S-adenosyl-L-methionine. [GO_REF:0000067, GOC:BHF, GOC:hal, GOC:TermGenie, PMID:22985361] |
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 2 target(s):
| Target | Category | Definition |
|---|
| lysosomal membrane | cellular component | The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm. [GOC:ai] |
| 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 |
|---|
| methylosome | cellular component | A large (20 S) protein complex that possesses protein arginine methyltransferase activity and modifies specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins, thereby targeting these proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein (snRNP) core particles. Proteins found in the methylosome include the methyltransferase JBP1 (PRMT5), pICln (CLNS1A), MEP50 (WDR77), and unmethylated forms of SM proteins that have RG domains. [PMID:11713266, PMID:11756452] |
Involved In
This protein is involved in 24 target(s):
| Target | Category | Definition |
|---|
| in utero embryonic development | biological process | The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus. [GOC:go_curators, GOC:mtg_sensu] |
| protein methylation | biological process | The addition of a methyl group to a protein amino acid. A methyl group is derived from methane by the removal of a hydrogen atom. [GOC:ai] |
| DNA damage response | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. [GOC:go_curators] |
| cell surface receptor signaling pathway | biological process | The series of molecular signals initiated by an extracellular ligand binding to a receptor located on the cell surface. The pathway ends with regulation of a downstream cellular process, e.g. transcription. [GOC:signaling] |
| positive regulation of cell population proliferation | biological process | Any process that activates or increases the rate or extent of cell proliferation. [GOC:go_curators] |
| RNA splicing | biological process | The process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA. [GOC:krc, GOC:mah] |
| peptidyl-arginine methylation | biological process | The addition of a methyl group to an arginine residue in a protein. [GOC:mah] |
| viral protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. [GOC:bf, GOC:jl, ISBN:0781702534] |
| regulation of BMP signaling pathway | biological process | Any process that modulates the frequency, rate or extent of the activity of any BMP receptor signaling pathway. [GOC:mah] |
| neuron projection development | biological process | The process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites). [GOC:mah] |
| positive regulation of erythrocyte differentiation | biological process | Any process that activates or increases the frequency, rate or extent of erythrocyte differentiation. [GOC:go_curators] |
| regulation of megakaryocyte differentiation | biological process | Any process that modulates the frequency, rate or extent of megakaryocyte differentiation. [GOC:go_curators] |
| negative regulation of megakaryocyte differentiation | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of megakaryocyte differentiation. [GOC:go_curators] |
| positive regulation of translation | biological process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. [GOC:dph, GOC:go_curators, GOC:tb] |
| negative regulation of JNK cascade | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the JNK cascade. [GOC:bf] |
| positive regulation of hemoglobin biosynthetic process | biological process | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of hemoglobin, an oxygen carrying, conjugated protein containing four heme groups and globin. [GOC:ai] |
| cardiac muscle tissue development | biological process | The process whose specific outcome is the progression of cardiac muscle over time, from its formation to the mature structure. [GOC:dph, GOC:jid, GOC:lm] |
| protein homooligomerization | biological process | The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. [GOC:ai] |
| cellular response to methionine | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a methionine stimulus. [GOC:dph, PMID:7891681] |
| positive regulation of p38MAPK cascade | biological process | Any process that activates or increases the frequency, rate or extent of p38MAPK cascade. [GOC:TermGenie] |
| positive regulation of TORC1 signaling | biological process | Any process that activates or increases the frequency, rate or extent of TORC1 signaling. [GO_REF:0000058, GOC:TermGenie, PMID:25366275] |
| positive regulation of double-strand break repair via homologous recombination | biological process | Any process that activates or increases the frequency, rate or extent of double-strand break repair via homologous recombination. [GO_REF:0000058, GOC:TermGenie, PMID:12023299] |
| 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] |
| peptidyl-arginine methylation, to asymmetrical-dimethyl arginine | biological process | The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine. [RESID:AA0068, RESID:AA0069] |