{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/Summary_of_proteomics_experiments_in_cellulo.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/RS-82-1_mix1-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/RS_300825_IAA_treated_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/RS-82-1_mix1-6_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/RS_300825_no_IAA_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/RS_300825_no_IAA_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/RS_300825_IAA_treated_1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/txt_MEF_Probe1_protein_level_enrichment.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD080059/txt_HEK293_Probe1_peptide_level_enrichment.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["r.serwa@imol.edu.pl"],"submitter":["Remigiusz Serwa"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["N8-propargyl spermidine","Chemical probe","Hek293","Hypusination","Mef"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080059"],"tissue":["Mef Cell","Hek-293 Cell"],"sample_protocol":["HEK293 or MEF cells were washed with PBS and incubated with Probe 1 or spermidine (200-400 µM,  1-4 h). Cells were washed with PBS twice, lysed in 2% SDS in PBS, and cysteine residues were reacted or not with 40 mM iodoacetamide for 30 min. Proteins were precipitated by addition of methanol (1 vol.) and chloroform (1/4 vol.). The pellets were washed with methanol, air-dried, and reconstituted in 2% SDS in PBS. The solutions were diluted with PBS (3 vol.) and the protein concentration was adjusted to 1 mg/ml. The samples were subjected to CuAAC ligation. A click reaction mixture was prepared by combining 4 reagents: azido-PEG3-biotin (final conc. 0.2 mM), CuSO4 (final conc. 1 mM), TCEP (final conc.1 mM), THPTA (1 μl, stock 20 mM in water, final conc. 0.2 mM). The samples were vortex-mixed at RT for 1 h. EDTA (final conc. 5 mM), methanol (1 vol.), and chloroform (1/4 vol.) were added to precipitate proteins. The samples were vortexed and centrifuged. The pellets were washed with methanol twice and dried.  For the enrichment of MEF proteins, the pellets were resuspended in 2% SDS in PBS and PBS (3 vol.)  added. The samples were added to NeutrAvidin agarose resin and the enrichment was carried out for 2 h at RT. The supernatants were removed and the beads were washed with 0.5% SDS in PBS (2×), with PBS (2×), and then with 100 mM HEPES pH 8.0 (2×). The beads were suspended in 100 mM HEPES pH 8.0 containing 5 mM TCEP and 10 mM chloroacetamide. Trypsin was added and the samples incubated overnight at 37 °C with 1100 RPM shaking. The solutions were acidified (TFA, final conc. 1%) and peptides labelled with TMT on StageTip. Prior to the LC-MS/MS measurements, the peptide sample was resuspended in 0.1% TFA and 2% acetonitrile in water. The sample was injected twice. Chromatographic separation was performed on an Easy-Spray Acclaim PepMap column (50 cm length × 75 µm inner diameter, Thermo Fisher Scientific) at 55 °C by applying 180 min acetonitrile gradients in 0.1% aqueous formic acid at a flow rate of 300 nl/min. An UltiMate 3000 nano-LC system was coupled to a Q Exactive HF-X mass spectrometer via an easy-spray source (all Thermo Fisher Scientific). The Q Exactive HF-X was operated in TMT mode with survey scans acquired at a resolution of 60,000 at m/z 200. Up to 15 of the most abundant isotope patterns with charges 2-5 from the survey scan were selected with an isolation window of 0.7 m/z and fragmented by higher-energy collision dissociation with normalized collision energies of 32, while the dynamic exclusion was set to 35 s. The maximum ion injection times for the survey scan and dual MS (MS/MS) scans (acquired with a resolution of 30,000 at m/z 200) were 50 and 150 ms, respectively. The ion target value for MS was set to 3e6 and for MS/MS was set to 1e5, and the minimum AGC target was set to 1e3. For the enrichment of HEK293 peptides, the pellet was suspended in 100 mM HEPES pH 8.0 containing 5 mM TCEP and 10 mM chloroacetamide. Trypsin was added and the sample incubated overnight at 37 °C with 1100 RPM shaking. EDTA-free Protease Inhibitor Cocktail (1x, Roche) was added to quench residual trypsin activity. The tryptic peptide sample was centrifuged and clear supernatants added to the NeutrAvidin agarose resin.  The enrichment was carried out for 2 h at RT with 1100 RPM shaking. The supernatant was removed and the beads were washed with 100 mM HEPES (3×), with water (2×), and with 10% acetonitrile in water (2×). Probe-modified peptides were eluted at 37 °C with 0.1% trifluoroacetic acid and 1% formic acid in water (2×15 min). Combined eluates were concentrated using a SpeedVac concentrator. The sample was pre-cleaned using C18 StageTips and resuspended in 0.1% TFA and 2% acetonitrile in water prior to the LC-MS/MS measurement. Chromatographic separation was performed on an Easy-Spray Acclaim PepMap column (15 cm length × 75 µm inner diameter, Thermo Fisher Scientific) at 60 °C by applying 75 min acetonitrile gradients in 0.1% aqueous formic acid at a flow rate of 450 nl/min. An UltiMate 3000 nano-LC system was coupled to a Q Exactive HF-X mass spectrometer via an easy-spray source (all Thermo Fisher Scientific). The Q Exactive HF-X was operated in a data-dependent acquisition mode with survey scans acquired at a resolution of 60,000 at m/z 200. Up to 15 of the most abundant isotope patterns with charges 3-6 from the survey scan were selected with an isolation window of 1.3 m/z and fragmented by higher-energy collision dissociation with normalized collision energies of 27, while the dynamic exclusion was set to 35 s. The maximum ion injection times for the survey scan and MS/MS scans (acquired with a resolution of 15,000 at m/z 200) were 45 and 150 ms, respectively. The ion target value for MS was set to 3e6 and for MS/MS was set to 1e5, and the minimum AGC target was set to 1e3."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For the enrichment of MEF proteins, the data were processed with MaxQuant v. 2.6.7.0 and the peptides were identified from the MS/MS spectra searched against the reviewed UniProt mouse proteome using the built-in Andromeda search engine. Reporter ion MS2-based quantification was applied with reporter mass tolerance = 0.003 Da and min. reporter PIF = 0.75. Cysteine carbamidomethylation was set as a fixed modification and methionine oxidation, asparagine/glutamine deamidatio, and protein N-terminal acetylation were set as variable modifications. For in silico digests of the reference proteome, cleavages of arginine or lysine followed by any amino acid were allowed (trypsin/P), and up to two missed cleavages were allowed. The FDR was set to 0.01 for peptides, proteins and sites. Since two raw files were collected (double injection of the sample), match between runs was enabled. Other parameters were used as pre-set in the software. For the enrichment of HEK293 peptides, the data were processed with MaxQuant v. 2.6.7.0 and the peptides were identified from the MS/MS spectra searched against reference Uniprot Human Proteome using the built-in Andromeda search engine. Cysteine carbamidomethylation, the cysteine-Probe1 thiotriazole adduct (Δmass = 625.3734), and probe 1-derived hypusine (Δmass = 569.2996) or deoxyhypusine (Δmass = 553.3046) carrying the biotinylated triazole tag were set as variable modifications. The maximal number of variable modifications per peptide was set to 2. For in silico digests of the reference proteome, cleavages of arginine or lysine followed by any amino acid were allowed (trypsin/P), and up to two missed cleavages were allowed. The FDR was set to 0.01 for PSMs and proteins. Other parameters were used as pre-set in the software."],"omics_type":["Proteomics"],"labhead":["Remigiusz Serwa"],"instrument_platform":[""],"labhead_affiliation":["IMol, Polish Academy of Sciences, M. Flisa 6, 02-247 Warsaw, Poland"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["r.serwa@imol.edu.pl"],"submitter_affiliation":["The International Institute of Molecular Mechanisms and Machines, Polish Academy of Sciences"],"submitter_country":["Poland"],"additional_accession":[]},"is_claimable":false,"name":"Evaluation of N8-propargyl spermidine (Probe 1) as a substrate of deoxyhypusine synthase in cellulo","description":"Two complementary experiments were performed to evaluate whether N8-propargyl spermidine is a substrate of deoxyhypusine synthase in cells. HEK293 and mouse embryonic fibroblast (MEF) cells were incubated with either N8-propargyl spermidine (Probe 1) or spermidine, lysed, and subjected to CuAAC ligation with azido-PEG3-biotin. In the MEF experiment, biotinylated proteins were enriched on NeutrAvidin agarose resin, digested on-bead with trypsin, and, following TMT labeling and LC-MS/MS analysis, the data were processed in MaxQuant and analyzed for intensity enrichment in samples derived from cells treated with Probe 1 versus spermidine. In the HEK293 experiment, proteins were first digested with trypsin, after which biotinylated peptides were enriched on NeutrAvidin agarose resin and analyzed by LC-MS/MS. During MaxQuant processing, the peptide-level data were searched for Probe 1-derived hypusine and deoxyhypusine modifications carrying the biotinylated triazole tag, as well as for Probe 1-derived thiotriazole adducts on cysteine 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