A protein arginine N-methyltransferase 7 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NVM4]
EC 2.1.1.321;
Histone-arginine N-methyltransferase PRMT7;
[Myelin basic protein]-arginine N-methyltransferase PRMT7
| 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 | 1 (50.00) | 24.3611 |
| 2020's | 1 (50.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| s-adenosylhomocysteine | Homo sapiens (human) | IC50 | 25.0550 | 2 | 2 |
| epz004777 | Homo sapiens (human) | IC50 | 7.5000 | 1 | 1 |
This protein enables 10 target(s):
| Target | Category | Definition |
|---|---|---|
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| S-adenosylmethionine-dependent methyltransferase activity | molecular function | Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to a substrate. [GOC:mah] |
| 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 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 binding | molecular function | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. [GOC:jl, PMID:16209651, PMID:30212449, PMID:9305837] |
| 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] |
| histone H4 methyltransferase activity | molecular function | Catalysis of the reaction: Catalysis of the reaction: S-adenosyl-L-methionine + a histone H4 = S-adenosyl-L-homocysteine + a methylated histone H4. Histone methylation generally occurs on either an arginine or a lysine residue. [PMID:28450737] |
| 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] |
| 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] |
This protein is located in 4 target(s):
| Target | Category | Definition |
|---|---|---|
| fibrillar center | cellular component | A structure found most metazoan nucleoli, but not usually found in lower eukaryotes; surrounded by the dense fibrillar component; the zone of transcription from multiple copies of the pre-rRNA genes is in the border region between these two structures. [PMID:10754561] |
| 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] |
| 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] |
This protein is involved in 6 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] |
| peptidyl-arginine methylation | biological process | The addition of a methyl group to an arginine residue in a protein. [GOC:mah] |
| regulation of protein binding | biological process | Any process that modulates the frequency, rate or extent of protein binding. [GOC:go_curators] |
| genomic imprinting | biological process | The establishment of epigenetic modifications (imprints) during gametogenesis, and propagation of these imprints during the organism's life. Genomic imprinting leads to an asymmetry between the maternal and paternal alleles and differential expression of the corresponding alleles. This can happen through heterochromatin formation or differential chromatin loop formation. [PMID:24492710, PMID:31896690, PMID:31965998] |
| 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] |