Target type: molecularfunction
Catalysis of the reaction: S-adenosyl-L-methionine + (histone H3)-arginine (position 17) = S-adenosyl-L-homocysteine + (histone H3)-N-methyl-arginine (position 17). This reaction is the addition of a methyl group to the arginine residue at position 17 of histone H3. [GOC:sp, PMID:11341840]
Histone H3R17 methyltransferase activity is a specific type of enzymatic activity that catalyzes the transfer of a methyl group from a methyl donor, such as S-adenosyl methionine (SAM), to the arginine residue at position 17 (R17) of histone H3. This modification is crucial for regulating chromatin structure and gene expression. Histone H3R17 methylation plays a significant role in various cellular processes, including transcription, DNA replication, and repair.
The methyltransferase enzymes responsible for this modification, known as histone H3R17 methyltransferases, recognize specific amino acid sequences and structural features within the histone H3 tail. The methylation process involves a complex interplay between the methyltransferase, the histone substrate, and the surrounding DNA.
Histone H3R17 methylation can occur in different states, ranging from mono-methylation (me1) to di-methylation (me2) to tri-methylation (me3). Each methylation state is associated with distinct biological functions. For instance, H3R17me2 is linked to gene silencing and transcriptional repression, while H3R17me3 is associated with active gene expression.
The precise molecular mechanisms by which H3R17 methylation influences gene expression remain under investigation. However, studies have suggested that this modification can alter chromatin accessibility, affect the recruitment of transcription factors, and influence the activity of chromatin remodeling complexes.
The dysregulation of H3R17 methyltransferase activity has been implicated in various diseases, including cancer and neurodevelopmental disorders. Understanding the molecular function of H3R17 methyltransferase activity is crucial for developing targeted therapies and diagnostic tools for these conditions.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Histone-arginine methyltransferase CARM1 | A histone-arginine methyltransferase CARM1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q86X55] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| furamidine | furamidine: RN given refers to parent cpd; WR 199385 refers to di-HCl; pafuramidine is a prodrug of this | ||
| s-adenosylhomocysteine | S-adenosyl-L-homocysteine : An organic sulfide that is the S-adenosyl derivative of L-homocysteine. S-Adenosylhomocysteine: 5'-S-(3-Amino-3-carboxypropyl)-5'-thioadenosine. Formed from S-adenosylmethionine after transmethylation reactions. | adenosines; amino acid zwitterion; homocysteine derivative; homocysteines; organic sulfide | cofactor; EC 2.1.1.72 [site-specific DNA-methyltransferase (adenine-specific)] inhibitor; EC 2.1.1.79 (cyclopropane-fatty-acyl-phospholipid synthase) inhibitor; epitope; fundamental metabolite |
| stilbamidine | stilbamidine: RN given refers to parent cpd | ||
| gsk343 | GSK343 : A member of the class of indazoles that is 1-isopropyl-1H-indazole-4-carboxamide in which the nitrogen of the carboxamide group is substituted by a (6-methyl-2-oxo-4-propyl-1,2-dihydropyridin-3-yl)methyl group and in which the indazole ring is substituted at position 6 by a 2-(4-methylpiperazin-1-yl)pyridin-4-yl group. A highly potent and selective EZH2 inhibitor (IC50 = 4 nM). GSK343: an EZH2 methyltransferase inhibitor | aminopyridine; indazoles; N-alkylpiperazine; N-arylpiperazine; pyridone; secondary carboxamide | antineoplastic agent; apoptosis inducer; EC 2.1.1.43 (enhancer of zeste homolog 2) inhibitor |