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ProteomicsData files for site specific S-acylation
Raw data files for site specific S-acylation identification.
ORGANISM(S): Mus <mouse, Genus> (ncbitaxon:10088) Homo Sapiens (ncbitaxon:9606) 
2023-05-31 | MSV000092063 | MassIVE
ProteomicsRif1 S-acylation mediates DNA double-strand break repair at the inner nuclear membrane
Rif1 is involved in telomere homeostasis, DNA replication timing, and DNA double-strand break (DSB) repair pathway choice from yeast to human. The molecular mechanisms that enable Rif1 to fulfill its diverse roles remain to be determined. Here, we demonstrate that Rif1 is S-acylated within its conse...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2019-04-15 | PXD012137 | Pride
Non-homologous end-joining Dna double-strand break repair Palmitoylation Yeast Rif1 s-acylation 
ProteomicsA rapid and convenient sample treatment method based on the dissolvable polyacrylamide gel for S-acylation proteomics
S-acylation, dissolvable gel, sample treatment, proteomics
ORGANISM(S): Mus Musculus 
PXD052808 |
ProteomicsOptimization of a method to quantify S-acylation
HeLa cells were lysed and free cysteines were alkylated with an alkyne-tagged light probe (IAA-BnL or IAA-PrL). S-acylation was hydrolysed with hydroxylamine and newly revealed Cys allowed to react with the heavy probe (IAA-BnL or IAA-PrL). Proteins were clicked with azido-biotin, Adadps-biotin, Aaz...
ORGANISM(S): Homo sapiens (Human) 
2026-06-29 | PXD063994 | Pride
Hela S-acylation 
ProteomicsDirect analysis of IFITM3 S-fatty-acylation, part 2
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and anothe...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008401 | Pride
Ifitm3 S-fatty-acylation Site identification S-palmitoylation 
ProteomicsDirect analysis of IFITM3 S-fatty-acylation, part 1
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and another ...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008400 | Pride
Post translational modifications Modification site identification S-fatty-acylation Ifitm3 S-palmitoylation 
ProteomicsA palmitoyl transferase chemical genetic system to map ZDHHC-specific S-acylation
ZDHHC S-acyltransferases catalyze the transfer of fatty acyl groups, primarily palmitate, to cysteine residues of substrate proteins in all eukaryotes. The 23 human ZDHHCs are known to S-acylate an extensive network of proteins essential to normal physiology, including many which are dysregulated in...
ORGANISM(S): Homo sapiens (Human) 
2023-10-08 | PXD032378 | Pride
Turboid S-acylation Chemical proteomics Click chemistry Zdhhc Zdhhc20 
ProteomicsQuantification of S-acylation sites in autophagy
HeLa cells were lysed and free cysteines were alkylated with the IAA-Bn light probe. S-acylation was hydrolysed with hydroxylamine and newly revealed Cys allowed to react with the IAA-Bn heavy probe. Proteins were clicked with AdadpsB, digested with trypsin, enriched on neutravidin beads and analyse...
ORGANISM(S): Homo sapiens (Human) 
2026-06-29 | PXD062195 | Pride
Faims Autophagy S-acylation 
ProteomicsA palmitoyl transferase chemical genetic system to map ZDHHC-specific S-acylation
ZDHHC S-acyltransferases catalyze the transfer of fatty acyl groups, primarily palmitate, to cysteine residues of substrate proteins in all eukaryotes. The 23 human ZDHHCs are known to S-acylate an extensive network of proteins essential to normal physiology, including many which are dysregulated in...
ORGANISM(S): Homo sapiens (Human) 
2023-10-08 | PXD032373 | Pride
Chemical genetics Zdhhc15 Zdhhc7 S-acylation Chemical proteomics Click chemistry Zdhhc Zdhhc20 
ProteomicsLong-chain S-acylation is a key modulator during the macrophage inflammatory response
Long-chain S-acylation is a reversible lipid modification critical for regulating protein localization, stability, and signaling, yet its role in macrophage-mediated inflammation remains incompletely understood. Here, we combine stable isotope labeling by amino acids in cell culture (SILAC) with sit...
ORGANISM(S): Homo sapiens (Human) 
2026-06-10 | PXD066221 | Pride
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