2.3.1.225: protein S-acyltransferase
This is an abbreviated version!
For detailed information about protein S-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.225
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2.3.1.225
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palmitoylation
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palmitate
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s-acylation
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huntingtin
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palmitoylation-dependent
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huntingtin-interacting
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2-bromopalmitate
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s-acyltransferases
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medicine
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autoacylation
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16-carbon
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snap25
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acyl-acyl
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palmitoylation-deficient
- 2.3.1.225
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palmitoylation
- palmitate
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s-acylation
- huntingtin
-
palmitoylation-dependent
-
huntingtin-interacting
- 2-bromopalmitate
-
s-acyltransferases
- medicine
-
autoacylation
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16-carbon
- snap25
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acyl-acyl
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palmitoylation-deficient
Reaction
Synonyms
Akr1, Akr1p, APT1, Asp-His-His-Cys motif palmitoyl transferase, At3g51390, DHHC palmitoyl transferase, DHHC protein, DHHC protein acyltransferase, DHHC-2, DHHC-21, DHHC-21 palmitoyl transferase, DHHC-3, DHHC-3 palmitoyl transferase, DHHC-7, DHHC-8, DHHC-CRD S-acyltransferase, DHHC16, DHHC17, DHHC2, DHHC3, DHHC4, DHHC5, Erf2, Erf2p, G-protein palmitoyltransferase, HIP14, palmitoyl acyltransferase, Pat, PAT10, PAT14, PAT15, PAT21, PAT24, PAT4, Pfa3, Pfa4, PFA5, protein acyl transferase, protein acyltransferase, protein S-acyl transferase 4, Ras PAT, S-protein acyltransferase, SEC18p, Swf1, ZDHHC3, ZDHHC5
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Engineering
Engineering on EC 2.3.1.225 - protein S-acyltransferase
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C157S
mutation in DHHC motif, mutant is not able to complement a yeast akr1 mutant strain
C192A
mutation in the DHHC motif, loss of autoacylation capacity and the ability to complement a yeast akr1 mutant
C159S
the DHHC15 mutant shows reduced activity compared to the wild-type
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
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
C133S
mutation of unconserved cysteine residue of the cysteine-rich domain. About 90% of wild-type activity
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
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
H162Q
substitution in the DHHC motif, mutant is partially active
H162Q/C164R
substitutions in the DHHC motif, mutant is inactive
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
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complementation of the Vac8 protein localization to the vacuolar membrane in mutant yeast cells by Arabidopsis PATs
additional information
generation of tip1-1, tip1-2, and tip1-3 mutants, overview. Several stable transformants carrying Pro35S:TIP1 have significantly longer root hairs than does the wild-type, phenotype, overview
additional information
DHHC2 targeting with siRNA leads to Lck partial delocalization from the membranes and moving to the cytosol
additional information
DHHC2 targeting with siRNA leads to Lck partial delocalization from the membranes and moving to the cytosol
additional information
DHHC2 targeting with siRNA leads to Lck partial delocalization from the membranes and moving to the cytosol
additional information
DHHC4 targeting with siRNA leads to Lck partial delocalization from the membranes and moving to the cytosol
additional information
DHHC4 targeting with siRNA leads to Lck partial delocalization from the membranes and moving to the cytosol
additional information
DHHC4 targeting with siRNA leads to Lck partial delocalization from the membranes and moving to the cytosol
additional information
substitution of the conserved cysteine in the DHHC motif to DHHA or DHHR still allows for acylation of substrate Chs3. Mutant protein is not acylated
additional information
substitution of the conserved cysteine in the DHHC motif to DHHA or DHHR still allows for acylation of substrate Chs3. Mutant protein is not acylated