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Browse result for Palmitoylation

※ introduction

    Palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine and less frequently to serine and threonine residues of proteins, which are typically membrane proteins.[1] The precise function of palmitoylation depends on the particular protein being considered. Palmitoylation enhances the hydrophobicity of proteins and contributes to their membrane association. Palmitoylation also appears to play a significant role in subcellular trafficking of proteins between membrane compartments,[2] as well as in modulating protein-protein interactions.[3] In contrast to prenylation and myristoylation, palmitoylation is usually reversible (because the bond between palmitic acid and protein is often a thioester bond). The reverse reaction is catalysed by palmitoyl protein thioesterases. Because palmitoylation is a dynamic, post-translational process, it is believed to be employed by the cell to alter the subcellular localization, protein-protein interactions, or binding capacities of a protein.

Wiki: Palmitoylation

UniProt ACEntrez IDGene NameProtein NameOrganism
Amyloid-beta A4 protein [Cleaved into: N-APP; Soluble APP-a
Homo sapiens
Brain-derived neurotrophic factor
Homo sapiens
Sodium-dependent serotonin transporter
Homo sapiens
Platelet-activating factor acetylhydrolase IB subunit gamma
Homo sapiens