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As control, HEK Flp-In T-REx 293 cells without any integrated construct were used. Medium was removed, the cells were put on ice and were washed once with ice-cold PBS. The cells were resuspended by adding ice-cold PBS and pipetting several times up and down. The cells were pelleted at 1000 g, 4 °C for 1 min. The supernatant was completely removed and the pellet was resuspended in a small volume of lysis buffer (30 mM HEPES pH 7.3, 100 mM KCl, 5 mM MgCl2, 104 µM AEBSF, 1.0 % NP-40, 10 % Glycerol). The crude lysate was rotated at 18 rpm for 30 min at 4 °C and then pelleted at 21100 g, 4 °C for 10 min. The cleared lysate (supernatant) was transferred into a new tube and the total protein concentration was measured with a Bradford assay. All lysates were diluted to the same concentration with lysis buffer. Anti-FLAG M2 magnetic beads (Sigma, M8823) were equilibrated by washing them three times with 1 mL ice-cold lysis buffer. For binding, the prepared lysates were added to the beads and incubated for 2 h at 4 °C rotating at 18 rpm. Equal amounts of beads as well as lysate was used for each sample. A small volume of lysate was not added to the beads and kept as input sample. After the binding, the beads were collected with a magnetic separator and the supernatant was removed. The beads were washed eight times with 1 mL ice-cold detergent- and AEBSF-free lysis buffer. The beads were resuspended in 30 µL 2 M urea and 50 mM ammonium bicarbonate. The beads were digested with 150 ng LysC (mass spectrometry grade, FUJIFILM Wako chemicals) at room temperature for 90 minutes. The supernatant was transferred to a new tube. The beads were rinsed with 30µL 50mM ammonium bicarbonate and combined with the supernatant. Disulfide bonds were reduced with 2.4 µL of 250 mM dithiothreitol (DTT) for 30 min at room temperature before adding 2.4 µL of 500 mM iodoacetamide and incubating for 30 min at room temperature in the dark. The remaining iodoacetamide was quenched with 1.2 µL of 250 mM DTT for 10 min. Proteins were digested with 150 ng trypsin (Trypsin Gold, Promega) in 1.5 µL 50 mM ammonium bicarbonate overnight. The digest was stopped by the addition of trifluoroacetic acid (TFA) to a final concentration of 0.5%, and the peptides were desalted using C18 Stagetips. LC-MS analysis was performed on an UltiMate 3000 RSLCnano LC system (Thermo Scientific) coupled to a timsTOF HT (Bruker). The system was equipped with a CaptiveSpray ion source (Bruker), and a Butterfly Portfolio Heater (Phoenix S&T). Peptides were loaded onto a trap column (Acclaim PepMap 100 C18 HPLC Column, 5 mm × 0.3 mm, 5 μm particle size, Thermo Scientific) using 0.1% TFA as mobile phase, and separated on an analytical column (Aurora Ultimate XT C18, 25 cm × 75 µm, 1.7 µm particle size, IonOpticks), applying a linear gradient starting with a mobile phase of 98% solvent A (0.1% FA) and 2% solvent B (80% acetonitrile, 0.08% FA), increasing to 35% solvent B over 60 min at a flow rate of 300 nl/min. The analytical column was heated to 50°C  The mass spectrometer was operated in data-independent acquisition (DIA) parallel accumulation serial fragmentation (PASEF) mode. MS2 data were acquired with eight PASEF scans per duty cycle, each containing three m/z windows. The m/z window widths were adjusted based on the expected precursor density, covering a total range of 300–1200 m/z. The ion mobility range was set to 0.64-1.42 V*s/cm, and the accumulation and ramp time was set to 100 ms. TIMS elution voltages were calibrated linearly to obtain the reduced ion mobility coefficients (1/K0) using three Agilent ESI-L Tuning Mix ions (m/z 622, 922 and 1,222). Collision energy for fragmentation was scaled linearly with precursor mobility (1/K0), ranging from 20 eV (at 1/K0 = 0.6 V*s/cm) to 59 eV at (at 1/K0 = 1.6 V*s/cm)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS raw data were converted to htrms format using HTRMS converter (Biognosys). Then it was searched with Spectronaut(19.1, Biognosys) in directDIA+ mode against the Uniprot human reference proteome (version 2024_01, www.uniprot.org), as well as a database of most common contaminants (version 2023_03, https://github.com/maxperutzlabs-ms/perutz-ms-contaminants ). The search was performed with full trypsin specificity and a maximum of two missed cleavages at a protein and peptide spectrum match false discovery rate of 1%. Carbamidomethylation of cysteine residues was set as fixed, oxidation of methionine, and N-terminal acetylation as variable modifications. The cross-run normalization was turned off and all other settings were left as default.  Computational analysis was performed using Python and the in-house developed Python library MsReport (version 0.0.25). LFQ protein intensities reported by Spectronaut were log2-transformed and normalized across samples using the ModeNormalizer from MsReport. The missing normalized LFQ intensity values were imputed by drawing random values from a normal distribution after filtering out contaminants, proteins with less than 2 peptides and less than 2 quantified values in at least one group. Differences between groups were statistically evaluated using the LIMMA 3.52.1  at 5% FDR (Benjamini-Hochberg)."],"omics_type":["Proteomics"],"labhead":["Javier Martinez"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Max Perutz Labs, Medical University of Vienna, Dr. Bohr-Gasse 9/2, 1030 Vienna, Austria"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["proteomics@maxperutzlabs.ac.at"],"submitter_affiliation":["Max Perutz Labs, Mass Spectrometry Facility, Vienna Biocenter Campus (VBC), Dr. Bohr-Gasse 9, Vienna, Austria"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"Anti-FLAG co-immunoprecipitation of N- or C-terminally FLAG-HA-tagged FAM98A, FAM98B and FAM98C, from HEK Flp-In T-REx 293 cells.","description":"Determination of the interactome of different human FLAG-HA-tagged FAM98 paralogs (FAM98A, FAM98B and FAM98C) by co-immunoprecipitation/MS. Two expression constructs were used per paralog: one with an N-terminal and one with a C-terminal FLAG-HA-tag. Expression constructs were stably integrated into HEK Flp-In T-REx 293 cells and induced by addition of doxycycline. HEK Flp-In T-REx 293 cells without any integrated construct were used as control.","dates":{"publication":"2026-06-08","submission":"2026-04-07"},"accession":"PXD076703","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:1126","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1367493","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:46429","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:2736291","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:166340","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:2767846","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:468822","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:99802","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:709964","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:156974","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:199225","NEWT:1549675","NEWT:177437","NEWT:717966","NEWT:9014","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:29022","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:96795","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:1883426","NEWT:8165","NEWT:96794","NEWT:10401","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:215451","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:329032","NEWT:56636","NEWT:2499525","NEWT:55307","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:2830","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:141469","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:1578","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:291146","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:1092586","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:911022","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:1255232","NEWT:11723","NEWT:445","NEWT:153009","NEWT:1004879","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","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