EC Number |
Protein Variants |
Reference |
---|
2.3.1.225 | C129S |
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. About 10% of wild-type activity |
736490 |
2.3.1.225 | C132S |
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. Less than 5% of wild-type activity |
736490 |
2.3.1.225 | C133S |
mutation of unconserved cysteine residue of the cysteine-rich domain. About 90% of wild-type activity |
736490 |
2.3.1.225 | C146S |
mutation of highly conserved cysteine residue of the cysteine-rich domain, results in activity deficits and a structural perturbation. About 15% of wild-type activity. Mutation reduces the palmitoylation level of DHHC3 |
736490 |
2.3.1.225 | C157 |
mutation reduces the palmitoylation level of DHHC3 |
736490 |
2.3.1.225 | C157S |
mutation in DHHC motif, mutant is not able to complement a yeast akr1 mutant strain |
737037 |
2.3.1.225 | C157S |
site-directed mutagenesis, inactive mutant |
720055 |
2.3.1.225 | C159S |
the DHHC15 mutant shows reduced activity compared to the wild-type |
720174 |
2.3.1.225 | C164R |
substitution of the conserved cysteine in the DHHC motif. Overexpression of this mutant allows to partially complement an isoform Swf1 gene deletion and to acylate the Swf1 substrates Tlg1, Syn8, and Snc1. Mutant protein is not acylated |
736483 |
2.3.1.225 | C192A |
mutation in the DHHC motif, loss of autoacylation capacity and the ability to complement a yeast akr1 mutant |
736893 |