Protein arginine N-methyltransferase 6

A protein arginine N-methyltransferase 6 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q96LA8]

Synonyms

EC 2.1.1.319;
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 6;
Histone-arginine N-methyltransferase PRMT6

Research

Bioassay Publications (3)

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	3 (100.00)	24.3611
2020's	0 (0.00)	2.80

Compounds (4)

Drugs with Inhibition Measurements

Drug	Taxonomy	Measurement	Average (mM)	Bioassay(s)	Publication(s)
sulfathiazole	Homo sapiens (human)	IC50	430.0000	1	1
c.i. direct red 23	Homo sapiens (human)	IC50	39.2000	1	1
furamidine	Homo sapiens (human)	IC50	283.0000	1	1
stilbamidine	Homo sapiens (human)	IC50	173.0000	1	1

Enables

This protein enables 12 target(s):

Target	Category	Definition
chromatin binding	molecular function	Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. [GOC:jl, ISBN:0198506732, PMID:20404130]
protein binding	molecular function	Binding to a protein. [GOC:go_curators]
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]
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 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]
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]
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 H3R2 methyltransferase activity	molecular function	Catalysis of the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 2) = S-adenosyl-L-homocysteine + (histone H3)-N-methyl-arginine (position 2). This reaction is the addition of a methyl group to the arginine residue at position 2 of histone H3. [GOC:mah, PMID:17898714]
histone H2AR3 methyltransferase activity	molecular function	Catalysis of the reaction: S-adenosyl-L-methionine + (histone H2A)-arginine (position 3) = S-adenosyl-L-homocysteine + (histone H2A)-N-methyl-arginine (position 3). This reaction is the addition of a methyl group to the arginine residue at position 3 of histone H2A. [GOC:mah, PMID:17898714, PMID:23451136]
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]

Located In

This protein is located in 3 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]
nucleolus	cellular component	A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. [ISBN:0198506732]

Involved In

This protein is involved in 12 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]
base-excision repair	biological process	In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. [ISBN:0815316194]
regulation of mitochondrion organization	biological process	Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of a mitochondrion. [GOC:dph, GOC:tb]
methylation	biological process	The process in which a methyl group is covalently attached to a molecule. [GOC:mah]
protein modification process	biological process	The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). [GOC:bf, GOC:jl]
regulation of megakaryocyte differentiation	biological process	Any process that modulates the frequency, rate or extent of megakaryocyte 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]
cellular senescence	biological process	A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest. [GOC:BHF, PMID:28682291]
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]
negative regulation of ubiquitin-dependent protein catabolic process	biological process	Any process that stops, prevents, or reduces the frequency, rate or extent of ubiquitin-dependent protein catabolic process. [GOC:BHF]
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]
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]