{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/diaParameters.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_18_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_16_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_14_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_11_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_12_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_19_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_20_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_15_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_13_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_10_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_1_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_9_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_7_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_3_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_2_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_6_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_4_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_5_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_8_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/6016_Exp1_110IS_DIA_400-800_17_01.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/cRAP_iRT_240507.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/UniProtKB_Human_can_20240529.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD067002/240604_main_search.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["zdrahal@sci.muni.cz"],"submitter":["Katerina Hanakova"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Dishevelled","Interactome","Turboid","Proximity labeling"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067002"],"tissue":["Cell Culture"],"sample_protocol":["Expression of the fusion proteins was induced by 1 µg/ml doxycycline. After 24 hours, cells were supplemented with 50 µM Biotin for 30 minutes, washed with PBS and lysed using sonication. Biotinylated proteins were isolated by Streptavidin Sepharose beads. Bead bound protein complexes were processed and digested as describe elsewhere1,2. Digested peptides were evaporated completely in SpeedVac concentrator (Thermo Fisher Scientific). Resulting peptides were analysed by LC-MS/MS. LC-MS/MS analyses were done using RSLCnano system connected to Orbitrap Exploris 480 spectrometer (Thermo Fisher Scientific) with EASY Spray ion source (Thermo Fisher Scientific) installed. Prior to LC separation, tryptic digests were online concentrated and desalted using trapping column (300 μm × 5 mm, μPrecolumn, 5μm particles, Acclaim PepMap Neo C18, Thermo Fisher Scientific). After washing of trapping column with 0.1% FA, the peptides were eluted (flow 300 nl/min) from the trapping column onto Aurora C18 (75 μm × 250 mm, 1.7 μm particles, heated to 50°C, Ion Opticks) by 98 min long gradient (mobile phase A: 0.1% FA in water; mobile phase B: 0.1% FA in 80% acetonitrile). Data were acquired in a data-independent acquisition mode (DIA). The survey scan covered m/z range of 350-1400 at a resolution of 60,000 (at m/z 200) and a maximum injection time of 55 ms (normalized AGC target 300%). HCD MS/MS (27% relative fragmentation energy) were acquired in the range of m/z 200-2000 at 30,000 resolution (maximum injection time 55 ms, normalized AGC target 1000%). Overlapping windows scheme in the precursor m/z range from 400 to 800 were used as isolation window placements."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["DIA data were processed in DIA-NN2 (version 1.8.1) against iRT database (11 sequences in total) and UniProtKB Human (number of protein sequences: 20,590). No optional, carbamidomethylation as fixed modification and trypsin/P enzyme with 1 allowed missed cleavages and peptide length 7-30 were set during the library preparation. False discovery rate (FDR) control was set to 1% FDR. MS1 and MS2 accuracies as well as scan window parameters were set based on the initial test searches (median value from all samples ascertained parameter values). MBR was switched on.  Reported protein intensities were further processed using the software container environment (https://github.com/OmicsWorkflows). Processing workflow is available upon request. Briefly, it covered: a) removal of low-quality precursors and contaminant protein groups, b) precursor intensities normalization by loessF algorithm, c) precursor intensities imputation by global quantile (0.001), d) protein group MaxLFQ intensities calculation using iq R package and log2 transformation, and e) differential expression analysis using LIMMA statistical test."],"omics_type":["Proteomics"],"labhead":["Zbynek Zdrahal"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Proteomics Core Facility and Research Group Proteomics, CEITEC-MU, Masaryk University, Brno, Czech Republic"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["katerina.hanak@gmail.com"],"submitter_affiliation":["CEITEC MU"],"submitter_country":["Czech Republic"],"additional_accession":[]},"is_claimable":false,"name":"Interactome analysis of DVL3 S/T cluster mutants using proximity labeling","description":"When WNT binds to its receptor Frizzled (FZD) to activate the signalling, Dishevelled (DVL), the central component of Wnt signalling, is phosphorylated by redundant Casein kinase 1 (CK1) isoforms ε or δ, to transduce the signal downstream. Here, we mutated key serine/threonine residues in the intrinsically disordered region (IDR) between the PDZ and DEP domains. Either to alanine to prevent phosphorylation, or to glutamic acid to mimic phosphorylation, or we deleted these residues altogether. We investigated the impact of these mutations on DVL’s interactome using proximity labeling with TurboID-tagged fusion proteins at N-terminus of 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