Accessory subunits and selected ion channel adapter proteins
| Channel | Subunit | Gene | Candidate S-acylation sites | UniProt ID | References |
| Voltage gated | |||||
| Calcium | CaVβ2a | Cacnb2 | 1MQCCGLVHRRRVRV | Q8CC27 | Chien et al., 1996; Stephens et al., 2000; Heneghan et al., 2009; Mitra-Ganguli et al., 2009 |
| Potassium | KChip2 | Kcnip2 | 34LKQRFLKLLPCCGPQALPSVSE | Q9JJ69 | Takimoto et al., 2002 |
| KChip3 | Kcnip3 | 35PRFTRQALMRCCLIKWILSSAA | Q9QXT8 | Takimoto et al., 2002 | |
| BK β4 | Kcnmb4 | 193VGVLIVVLTICAKSLAVKAEA | Q9JIN6 | Chen et al., 2013 | |
| Adapter proteins that interact with ion channels | PICK1 | Pick1 | 404TGPTDKGGSWCDS-stop | Q62083 | Thomas et al., 2013 |
| Grip1b | Grip1 | 1MPGWKKNIPICLQAEEQERE | Q925T6-2 | Thomas et al., 2012; Yamazaki et al., 2001 | |
| psd-95 | Dlg4 | 1MDCLCIVTTKKYR | Q62108 | Topinka and Bredt, 1998 | |
| S-delphilin | Grid2ip | 1MSCLGIFIPKKH | Q0QWG9-2 | Matsuda et al., 2006 | |
| Ankyrin-G | Ank3 | 60YIKNGVDVNICNQNGLNALHL | F1LNM3 | He et al., 2012 |
| Channel | Subunit | Gene | Candidate S-acylation sites | UniProt ID | References |
| Voltage gated | |||||
| Calcium | CaVβ2a | Cacnb2 | 1MQCCGLVHRRRVRV | Q8CC27 | Chien et al., 1996; Stephens et al., 2000; Heneghan et al., 2009; Mitra-Ganguli et al., 2009 |
| Potassium | KChip2 | Kcnip2 | 34LKQRFLKLLPCCGPQALPSVSE | Q9JJ69 | Takimoto et al., 2002 |
| KChip3 | Kcnip3 | 35PRFTRQALMRCCLIKWILSSAA | Q9QXT8 | Takimoto et al., 2002 | |
| BK β4 | Kcnmb4 | 193VGVLIVVLTICAKSLAVKAEA | Q9JIN6 | Chen et al., 2013 | |
| Adapter proteins that interact with ion channels | PICK1 | Pick1 | 404TGPTDKGGSWCDS-stop | Q62083 | Thomas et al., 2013 |
| Grip1b | Grip1 | 1MPGWKKNIPICLQAEEQERE | Q925T6-2 | Thomas et al., 2012; Yamazaki et al., 2001 | |
| psd-95 | Dlg4 | 1MDCLCIVTTKKYR | Q62108 | Topinka and Bredt, 1998 | |
| S-delphilin | Grid2ip | 1MSCLGIFIPKKH | Q0QWG9-2 | Matsuda et al., 2006 | |
| Ankyrin-G | Ank3 | 60YIKNGVDVNICNQNGLNALHL | F1LNM3 | He et al., 2012 |
Common channel abbreviation and subunit as well as gene names are given. Candidate S-acylation sites: experimentally determined cysteine residues (bold) with flanking 10 amino acids. Underlines indicate predicted transmembrane domains. Amino acid numbering corresponds to the UniProt ID. References: selected original supporting citations.