Proteins > Protein arginine N-methyltransferase 5
Page last updated: 2024-08-07 21:03:29
Protein arginine N-methyltransferase 5
A protein arginine N-methyltransferase 5 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O14744]
Synonyms
PRMT5;
EC 2.1.1.320;
72 kDa ICln-binding protein;
Histone-arginine N-methyltransferase PRMT5;
Jak-binding protein 1;
Shk1 kinase-binding protein 1 homolog;
SKB1 homolog;
SKB1Hs
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 | 11 (73.33) | 24.3611 |
2020's | 4 (26.67) | 2.80 |
Compounds (12)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
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 of new potent protein arginine methyltransferase 5 (PRMT5) inhibitors by assembly of key pharmacophores from known inhibitors.Bioorganic & medicinal chemistry letters, , 12-15, Volume: 28, Issue:23-24, 2018
Identification of a novel selective small-molecule inhibitor of protein arginine methyltransferase 5 (PRMT5) by virtual screening, resynthesis and biological evaluations.Bioorganic & medicinal chemistry letters, , 05-15, Volume: 28, Issue:9, 2018
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
Discovery of a Dual PRMT5-PRMT7 Inhibitor.ACS medicinal chemistry letters, , Apr-09, Volume: 6, Issue:4, 2015
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
Structure-Aided Design, Synthesis, and Biological Evaluation of Potent and Selective Non-Nucleoside Inhibitors Targeting Protein Arginine Methyltransferase 5.Journal of medicinal chemistry, , 06-09, Volume: 65, Issue:11, 2022
Fragment-Based Discovery of MRTX1719, a Synthetic Lethal Inhibitor of the PRMT5•MTA Complex for the Treatment of Journal of medicinal chemistry, , 02-10, Volume: 65, Issue:3, 2022
Discovery of a First-in-Class Inhibitor of the PRMT5-Substrate Adaptor Interaction.Journal of medicinal chemistry, , 08-12, Volume: 64, Issue:15, 2021
Discovery of First-in-Class Protein Arginine Methyltransferase 5 (PRMT5) Degraders.Journal of medicinal chemistry, , 09-10, Volume: 63, Issue:17, 2020
Discovery of 2-substituted-N-(3-(3,4-dihydroisoquinolin-2(1H)-yl)-2-hydroxypropyl)-1,2,3,4-tetrahydroisoquinoline-6-carboxamide as potent and selective protein arginine methyltransferases 5 inhibitors: Design, synthesis and biological evaluation.European journal of medicinal chemistry, , Feb-15, Volume: 164, 2019
Identification of a novel selective small-molecule inhibitor of protein arginine methyltransferase 5 (PRMT5) by virtual screening, resynthesis and biological evaluations.Bioorganic & medicinal chemistry letters, , 05-15, Volume: 28, Issue:9, 2018
Discovery of new potent protein arginine methyltransferase 5 (PRMT5) inhibitors by assembly of key pharmacophores from known inhibitors.Bioorganic & medicinal chemistry letters, , 12-15, Volume: 28, Issue:23-24, 2018
Protein Arginine Methyltransferase 5 (PRMT5) as an Anticancer Target and Its Inhibitor Discovery.Journal of medicinal chemistry, , 11-08, Volume: 61, Issue:21, 2018
Structure and Property Guided Design in the Identification of PRMT5 Tool Compound EPZ015666.ACS medicinal chemistry letters, , Feb-11, Volume: 7, Issue:2, 2016
Enables
This protein enables 15 target(s):
Target | Category | Definition |
p53 binding | molecular function | Binding to one of the p53 family of proteins. [GOC:hjd] |
transcription corepressor activity | molecular function | A transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. [GOC:txnOH-2018, PMID:10213677, PMID:16858867] |
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] |
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] |
protein-arginine omega-N symmetric methyltransferase activity | molecular function | Catalysis of the addition of a second methyl group to methylated peptidyl-arginine. Methylation is on the terminal nitrogen (omega nitrogen) residue that is not already methylated, resulting in symmetrical peptidyl-N(omega),N'(omega)-dimethyled arginine residues. [EC:2.1.1.320, PMID:14705965, RESID:AA0067, RESID:AA0069] |
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] |
ribonucleoprotein complex binding | molecular function | Binding to a complex of RNA and protein. [GOC:bf, GOC:go_curators, GOC:vk] |
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] |
protein heterodimerization activity | molecular function | Binding to a nonidentical protein to form a heterodimer. [GOC:ai] |
E-box binding | molecular function | Binding to an E-box, a DNA motif with the consensus sequence CANNTG that is found in the promoters of a wide array of genes expressed in neurons, muscle and other tissues. [GOC:BHF, GOC:vk, PMID:11812799] |
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 arginine N-methyltransferase activity | molecular function | Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-arginine = S-adenosyl-L-homocysteine + (histone)-N-methyl-arginine. [PMID:8002954] |
Located In
This protein is located in 5 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] |
Golgi apparatus | cellular component | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. [ISBN:0198506732] |
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] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
Active In
This protein is active in 2 target(s):
Target | Category | Definition |
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] |
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 3 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] |
chromatin | cellular component | The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome. [GOC:elh, PMID:20404130] |
histone methyltransferase complex | cellular component | A multimeric complex that is able to catalyze the addition of methyl groups to histone proteins. [GOC:bf] |
Involved In
This protein is involved in 18 target(s):
Target | Category | Definition |
spliceosomal snRNP assembly | biological process | The aggregation, arrangement and bonding together of one or more snRNA and multiple protein components to form a ribonucleoprotein complex that is involved in formation of the spliceosome. [GOC:krc, GOC:mah, ISBN:0879695897] |
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] |
DNA-templated transcription termination | biological process | The completion of transcription: the RNA polymerase pauses, the RNA-DNA hybrid dissociates, followed by the release of the RNA polymerase from its DNA template. [GOC:txnOH, PMID:15020047, PMID:18280161, PMID:30978344] |
regulation of mitotic nuclear division | biological process | Any process that modulates the frequency, rate or extent of mitosis. [GOC:go_curators] |
peptidyl-arginine methylation | biological process | The addition of a methyl group to an arginine residue in a protein. [GOC:mah] |
circadian regulation of gene expression | biological process | Any process that modulates the frequency, rate or extent of gene expression such that an expression pattern recurs with a regularity of approximately 24 hours. [GOC:mah] |
endothelial cell activation | biological process | The change in morphology and behavior of an endothelial cell resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. [GOC:mgi_curators, ISBN:0781735149, PMID:12851652, PMID:14581484] |
negative regulation of gene expression via chromosomal CpG island methylation | biological process | An epigenetic gene regulation mechanism that negatively regulates gene expression by methylation of cytosine residues in chromosomal CpG islands. CpG islands are genomic regions that contain a high frequency of the CG dinucleotide associated with the transcription start site of genes. [PMID:11898023, Wikipedia:Cpg_island] |
negative regulation of cell differentiation | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell differentiation. [GOC:go_curators] |
negative regulation of DNA-templated transcription | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
positive regulation of mRNA splicing, via spliceosome | biological process | Any process that activates or increases the rate or extent of mRNA splicing via a spliceosomal mechanism. [GOC:jid] |
positive regulation of oligodendrocyte differentiation | biological process | Any process that activates or increases the frequency, rate or extent of oligodendrocyte differentiation. [GOC:vp, PMID:15139015] |
regulation of ERK1 and ERK2 cascade | biological process | Any process that modulates the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. [GOC:add, ISBN:0121245462, ISBN:0896039986] |
Golgi ribbon formation | biological process | The formation of a continuous ribbon of interconnected Golgi stacks of flat cisternae. [GOC:ascb_2009, GOC:dph, GOC:tb] |
liver regeneration | biological process | The regrowth of lost or destroyed liver. [GOC:gap, PMID:19447520] |
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] |
positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway | biological process | Any process that activates or increases the frequency, rate or extent of adenylate cyclase-inhibiting dopamine receptor signaling pathway. [GO_REF:0000058, GOC:kmv, GOC:TermGenie, PMID:26554819] |
regulation of DNA-templated transcription | biological process | Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |