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Covalent attachment of fatty acid palmitate to cysteine residues, affects protein membrane association and signaling pathways.

Attachment of carbohydrate chains to proteins, essential for proper protein folding and stability; involved in cell-cell recognition.

Attachment of ubiquitin molecules to a protein, typically signals for protein degradation via the proteasome.

Addition of a phosphate group (PO4) to an amino acid, often leads to changes in protein function and signal transduction.

Addition of an acetyl group to the N-terminus of a protein or at lysine residues, often modulates protein function and interaction.

Addition of a nitric oxide group to cysteine residues, critical for regulating protein function and cell signaling.

Addition of methyl groups to amino acids like lysine and arginine, can affect gene expression and protein interactions.

Attachment of SUMO (Small Ubiquitin-like Modifier) proteins to other proteins, regulates protein localization, stability, and activity.

Addition of hydroxyl groups (OH) to amino acids like proline and lysine, important for collagen stability and oxygen sensing.