Target intelligence / Profile preview

Protein lysine residue

Molecular classification
Amino acid residue, Post-translational modification site, Other
01

Overview

Lysine residues are the basic, positively charged amino acids located at various positions within proteins. Their ε-amino group is highly reactive and serves as both a structural and functional anchor for numerous critical post-translational modifications, including acetylation, methylation, ubiquitination, and SUMOylation. These modifications regulate protein activity, stability, localization, and interactions, playing vital roles in gene regulation, cell signaling, and metabolic processes. Altered lysine modification status has been implicated in various diseases, highlighting the biological importance of targeted lysine residue study—but "protein lysine residues" itself does not correspond to a singular therapeutic target, receptor, or molecule.

Other names
Lysine residue in proteinprotein lysyl residue
02

Mechanism of action

Inhibition or modulation of enzymes that modify lysine residues (e.g., acetylation, methylation, ubiquitination, SUMOylation)

03

Biological functions

Protein structure stabilizationSignal transductionEpigenetic regulationEnzyme catalysisCell adhesion
04

Disease associations

Cancer (via epigenetic dysregulation)Neurodegenerative diseasesMetabolic disordersOther
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Safety considerations

Non-specific targeting or broad modulation of protein lysine residues in all proteins is likely toxic due to widespread roles in protein functionoff-target modulation of lysine-modifying enzymes can disrupt essential cellular processes
06

Interacting drugs

histone deacetylase inhibitors (HDACi)

1 more in the full profile.

07

Biomarkers

Modified lysine residues on histones or other proteins (acetyl-lysine, methyl-lysine, ubiquitin-lysine) are commonly used as biomarkers in epigenetics and disease

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