Target type: molecularfunction
Catalysis of the reaction: L-lysyl20-[histone H4] + S-adenosyl-L-methionine = H+ + N6-methyl-L-lysyl20-[histone H4] + S-adenosyl-L-homocysteine. This reaction is the addition of a methyl group to the unmethylated lysine residue at position 20 of histone H4, producing histone H4K20me. [RHEA:60344]
Histone H4K20 monomethyltransferase activity refers to the enzymatic ability to catalyze the transfer of a single methyl group from a donor molecule, such as S-adenosyl methionine (SAM), to the lysine residue at position 20 (K20) of histone H4. This methylation event is a critical epigenetic modification, playing a crucial role in regulating chromatin structure and gene expression.
Histone H4K20 monomethylation is primarily associated with heterochromatin formation, a condensed and transcriptionally inactive state of chromatin. The addition of a methyl group at this specific lysine residue contributes to the compaction of chromatin by facilitating interactions with other chromatin-associated proteins. These interactions can lead to the silencing of genes located within these condensed regions.
Furthermore, histone H4K20 monomethylation has been implicated in other cellular processes, including DNA repair, DNA replication, and the maintenance of genomic stability. It can influence the recruitment of specific proteins to chromatin, thereby affecting the recruitment and function of DNA repair machinery.
The precise molecular mechanism underlying the role of histone H4K20 monomethylation in these processes is still under investigation. However, it is clear that this specific epigenetic modification plays a pivotal role in maintaining proper genomic function.'
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Protein | Definition | Taxonomy |
---|---|---|
N-lysine methyltransferase KMT5A | An N-lysine methyltransferase KMT5A that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NQR1] | Homo sapiens (human) |
Histone-lysine N-methyltransferase KMT5C | A histone-lysine N-methyltransferase KMT5C that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q86Y97] | Homo sapiens (human) |
Histone-lysine N-methyltransferase KMT5B | A histone-lysine N-methyltransferase KMT5B that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q4FZB7] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
nsc 663284 | NSC 663284: structure in first source | quinolone | |
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 |
2-methyl-5-(4-methylanilino)-1,3-benzothiazole-4,7-dione | aminotoluene | ||
bvt.948 | |||
unc 0321 | 7-(2-(2-(dimethylamino)ethoxy)ethoxy)-6-methoxy-2-(4-methyl-1,4-diazepan-1-yl)-N-(1-methylpiperidin-4-yl)quinazolin-4-amine: a G9a antagonist; structure in first source | quinazolines | |
6,7-dimethoxy-2-(pyrrolidin-1-yl)-n-(5-(pyrrolidin-1-yl)pentyl)quinazolin-4-amine | 6,7-dimethoxy-2-(pyrrolidin-1-yl)-N-(5-(pyrrolidin-1-yl)pentyl)quinazolin-4-amine: a SETD8 inhibitor; structure in first source |