DHHC palmitoyltransferase
PF01529
Definition
This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases PMID:15603741. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein PMID:23034182PMID:26224664. Some proteins containing a DHHC domain include Drosophila DNZ1 protein PMID:10231582, Mouse Abl-philin 2 (Aph2) protein PMID:12021275, Mammalian ZDHHC9 PMID:16000296, Yeast ankyrin repeat-containing protein AKR1 PMID:12370247, Yeast Erf2 protein PMID:10490616, and Arabidopsis thaliana tip growth defective 1 PMID:16100337.
24 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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