Palmitoyltransferase, DHHC domain
IPR001594
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, catalyse this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterised by the presence of 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 [[cite:PMID:23034182], [cite:PMID:26224664]]. Some of the proteins containing a DHHC domain are listed below: Drosophila DNZ1 protein PMID:10231582 Mouse Abl-philin 2 (Aph2) protein. Interacts with c-Abl. May play a role in apoptosis PMID:12021275 Mammalian ZDHHC9, an integral membrane protein PMID:16000296 Yeast ankyrin repeat-containing protein AKR1 PMID:12370247 Yeast Erf2 protein. This protein localizes to the endoplasmic reticulum and seems to be important for Ras function PMID:10490616 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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