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Uliana"],"technology_type":["SRM/MRM","Data-dependent acquisition","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["Phosphorylation","Pka inhibition"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD052971"],"sample_protocol":["Cells were grown in 50 ml of SD media culture, until OD 0.6. Cell grow was quenched with 6.25% (v:v) of 100% trichloroacetic acid purum (TCA) on ice for 10min. Cultures were centrifuged at 1500g for 5min at 4˚C and the pellets were washed twice times with ice-cold acetone. Samples were stored at -80˚C until lysis. Cell pellets were lysed in 0.4 ml of 8M Urea, 100mM ammonium bicarbonate, 5mM EDTA by glass bead beating (using beads with 500µm diameter in an amount equal to the volume of the lysate). The mechanical lysis was performed at 4C using the following settings: 6m/s for 20sec for 5 cycles with fresh lysis buffer, keeping the supernatant for every cycle. Protein amount was estimated by BCA Protein Assay. 3mg of protein extracted were reduced with 5mM TCEP for 30 min at 37C and 12mM IAA at room temperature in the dark.  After diluting Urea to 1M by adding 100mM Ammonium Bicarbonate, proteins were digested by 1:50 sequencing-grade Trypsin (Promega) overnight at 37˚C and 300rpm. Proteolyisis was quenched by adding formic acid to a final volume of 1% and peptide mixture were cleaned up by C18 phase separation (3cc SepPak C18 cartridge) following the manufacture procedure. Peptides were resuspended in 50µl (0.1% formic acid) and 2 µl were further diluted to 1ug/ul and analyzed by LC-MS for the normalization of the phosphorylated level (non-enriched samples). For the phospho enrichment, the remaining peptides (48 µl) were diluted with 350 ul of phospho-enrichment loading buffer. The phospho-enrichment loading buffer was prepared with 50% acetonitrile, 29.2% lactic acid and 0.1% trifuloroacetic (TFA). To enrich the phospho-peptides, 6mg of TiO2 resin (GL Science) was washed twice with 500 ul of methanol and twice with 500 ul of the loading buffer. The TiO2 resin was each time pelleted by centrifugation at 2000g for 1 min and the supernatant discarded. The peptide mixture in the loading buffer was then incubated in presence of the resin in a tube rotator for 1 hour at room temperature. The resin supernatant was then removed by centrifugation at 2000g for 1 min and the resin washed sequentially twice each with 500 ul of loading buffer, 500 ul of 50% acetonitrile, 0.1% TFA and finally 500 ul of 0.1% TFA. The phosphopeptides were then eluted from the resin in two steps with 150µl of 50mM ammonium hydroxide (at pH 10.8). The elution solution was quenched immediately with 4.4ul of 50% TFA. The enriched peptides were then desalted on ultra-micro spin columns (the Nest Group) and dried on a speedvac . For MS measurement, peptides were reconstituted to 1ug/ul in 0.1% formic acid and retention time standard peptide (1:50 iRT, Biognosys) were spiked into the samples before the LC-MS analysis. For the targeted analysis, reference peptides (PEPotec Heavy, Thermo) with arginine [+10] or lysine [+8] residues labeled with heavy amino acids were spiked into the sample mixture to facilitate the identification and quantification of targeted peptides. Samples were acquired in untargeted (DDA) mode and in targeted mode for the quantification of the phospho-peptides : Atg1 S515, Bcy S415, Cdc19 S22, Cdc19 S56, Cdc19 S9, Cdc19 S407, Cdc19 T478, Msn2 S288 and iRT QC peptides (the list of precursors is in Supplementary Table 2). In the experiment, cells were not treated (control) or treated with PKA inhibitor in the following conditions: exponential growth, eight days starvations and heat shock treatment.  For DDA analysis samples were acquired in Orbitrap QE Exactive Plus (Thermo) equipped with a nanoelectrospray ion source coupled to EASY-nLC-1000 liquid chromatography system (Thermo). Peptides were separated using a reverse phase column (75 µm ID x 400 mm New Objective, in-house packed with ReproSil Gold 120 C18, 1.9 µm, Dr. Maisch GmbH) in a gradient of 90min from 3 to 25 and 40% (buffer A: 0.1% (v/v) formic acid; buffer B: 0.1% (v/v) formic acid, 95% (v/v) acetonitrile). The DDA data acquisition mode was set to perform one MS1 scan followed by a 20 MS2 scans for top 20 ion peaks; MS1 scans (R=70’000 at 400 m/z, AGC=3’000’000 and maximum IT= 64ms), HCD fragmentation (NCE=25%), isolation windows (1.4m/z) and MS2 scans (R=35’000 at 400 m/z, AGC=50’000 and maximum IT=110ms). A dynamic exclusion of 30s was applied and charge states lower than two and higher than seven were rejected for the isolation.  For the targeted analysis samples were acquired with the same instrument setup used in the DDA analysis using a shorter gradient (peptides were eluted in 60min from 5 to 40% buffer B). A targeted scheduled method was set up with one MS1 scan (R=70’000 at 400 m/z, normalized AGC = 3’000’000 and max. IT 100ms) and a cycle time of 3s to monitor 69 peptides (R= 35’000, AGC = 50’000 and max. IT 110ms) using an isolation window of 1.8m/z and normalized collision energy 27%."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["DDA analysis. Acquired spectra in the untargeted analysis were searched using the MaxQuant software package version 1.5.2.8 embedded with the Andromeda search engine against Saccharomyces Cerevisiae reference dataset (http://www.uniprot.org/, downloaded on 17.05.2021, 6055 entries) extended with reverse decoy sequences. The search parameters were set to include only full tryptic peptides, maximum two missed cleavage, carbamidomethyl as static peptide modification, oxidation (M), deamidation N terminal, phosphorylation (S, T, Y) as variable modification and “match between runs” option. The MS and MS/MS mass tolerance were set, respectively, to 20 ppm and 0.5 Da. False discovery rate of < 1% was used at the PSM level. Phosphorylation sites identified in the table “Phospho (STY)Sites.txt” were filter for localization (localization score > 0.6) and only phosphosites identified at least in two replicates in at least one conditions were considered (7;152 phosphosites identified). Intensity values of phosphorylation sites identified in the table” was log2 transformed, median normalized and imputed using random sampling from a normal distribution generated from the 1% lower intense values of the whole dataset. ANOVA statistical analysis comparing variance across multiple conditions was performed to identify significatively regulated phosphorylation sites (pvalues were corrected for multiple hypothesis using Benjamin Hochberg method). Significantly downregulated phosphosites (log2FC < (-1) & pvalue BH corrected <0.05) were characterized by gene ontology enrichment analysis and identification of kinase-substrate relationships, performing a hypergeometric test. PRM analysis. For targeted analysis, peptides were manually examined using Skyline daily software. Endogenous phosphorylated peptides were identified by matching the coelution and peak shapes of precursor and product ions with those of the reference peptides. Quantification was carried out using data from the file “Transition_Results_240608.csv,” summing five fragment ions per peptide. The intensity of endogenous peptides was normalized to the intensity of the heavy peptides. After log2 transformation and normalization against the mean phosphorylation intensities in the Exponential condition without treatment, the significance of changes was evaluated using p-values obtained from two-sided, unpaired t-tests."],"omics_type":["Proteomics"],"labhead":["Federico Uliana"],"instrument_platform":[""],"labhead_affiliation":["JGU University Mainz"],"submission_type":["PARTIAL"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"submitter_mail":["fuliana@uni-mainz.de"],"publication":["Not available"],"submitter_affiliation":["JGU"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Identification of PKA dependent phosphorylation sites","description":"Identification of PKA dependent phosphorylation sites in Exponential, starvation (day 8) and heat shock 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