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Hartl"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Mapk pathway","Ras/raf/mek/erk","Ap-ms","Hek293t","Proximity dependent labeling","Mek1","Mek2","Turboid","Protein-protein interactions","Disease mutations"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079313"],"tissue":["Cell Culture"],"sample_protocol":["Stable HEK293T cell lines containing Dox-inducible versions MEK2 WT and MEK1 in wild-type (WT), constitutively active (CA), or inactive (CI)) tagged to V5-BirA* TbID were generated.  Cells were kept at a young passage (max. passage 5) and grown in 10cm cell culture dishes to approx. 80-90% confluency. Expression was induced by addition of Doxycycline overnight. Biotin was added to the cell dishes to a final concentration of 500µM for 10 min before washing.  Dishes were washed 3x with ice-cold PBS. Cells were lysed in RIPA lysis buffer containing 50 mM TrisHCl (pH 8.0), 150 mM NaCl, 1% NP-40, 0.1% SDS, 0.5% sodium deoxycholate supplemented with  1 mM Na3VO4, 50 mM NaF, 2 mM PMSF, and protein inhibitor cocktail (Roche). Samples were rotated at 4oC for 10 minutes. Lysates were cleared by centrifugation at 20000g for 15min at 4oC. Cleared lysate was saved and protein concentrations were determined by BCA assay. For enrichment, lysates were subjected to MagReSyn Streptavidin MS Beads. After the incubation, beads were washed 3 times with lysis buffer, followed by 6 washes with PBS.  The beads were resuspended in 50 µL 1 M urea and 50 mM ammonium bicarbonate. Disulfide bonds were reduced with 2 µL of 250 mM dithiothreitol (DTT) for 30 min at room temperature before adding 2 µL of 500 mM iodoacetamide and incubating for 30 min at room temperature in the dark. The remaining iodoacetamide was quenched with 1 µL of 250 mM DTT for 10 min. Proteins were digested with 150 ng LysC (mass spectrometry grade, FUJIFILM Wako chemicals) in 1.5 µL 50 mM ammonium bicarbonate at 25°C overnight. The supernatant without beads was digested with 150 ng trypsin (Trypsin Gold, Promega) in 1.5 µL 50 mM ammonium bicarbonate followed by incubation at 37°C for 5 hours. 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 an Orbitrap Exactive HF-X mass spectrometer (Thermo Scientific). The system was equipped with a Nanospray Flex ion source (Thermo Scientific), coated emitter tips (PepSep, MSWil), and a Butterfly Portfolio Heater (Phoenix S&T). Peptides were loaded onto a trap column (PepMap C18 5mm × 300 µm, 5 μm particle size, Thermo Scientific) using 0.1% TFA as mobile phase, and separated on an analytical column (Acclaim PepMap 100 C18 HPLC Column, 50 cm × 75 µm, 2 μm particle size, Thermo Scientific, 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 120 min at a flow rate of 230 nl/min. The analytical column was heated to 30°C.  The mass spectrometer was operated in data-dependent acquisition (DDA) mode. Survey scans were acquired from 375-1500 m/z, AGC target of 3E6, resolution of 120,000. The most intense 8 precursor ions (charge states +2 to +6) were selected for fragmentation using an isolation window of 1.6 m/z with 0.2 m/z offset. Selected ions were analyzed with a maximum fill time of 250 ms, AGC target of 1e5, and resolution of 30,000 after HCD fragmentation with normalized collision energy of 28%. Monoisotopic precursor selection (MIPS) was set to “peptide” mode, the intensity threshold to 4E4, and selected precursors were dynamically excluded for 30 seconds with isotope exclusion enabled."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["MS data were analyzed using the MaxQuant software package (version 1.6.17.0) and the Uniprot human reference proteome (version 2020_01, www.uniprot.org ),  as well as a database of most common contaminants, and the target protein sequences. 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 were set as fixed, oxidation of methionine and N-terminal acetylation as variable modifications. For label-free quantification the “match between runs” feature and the LFQ function were activated - all other parameters were left at default. MaxQuant output tables were further processed in Cassiopeia_LFQ (https://github.com/maxperutzlabs-ms/Cassiopeia_LFQ) Reverse database identifications, contaminant proteins, protein groups identified only by a modified peptide, protein groups with less than two quantitative values in one experimental group, and protein groups with less than 2 razor peptides were removed for further analysis. Missing values were replaced by randomly drawing data points from a normal distribution model on the whole dataset (data mean shifted by -1.8 standard deviations, a width of the distribution of 0.3 standard deviations). Differences between groups were statistically evaluated using the LIMMA 3.52.1 with batch correction at 5% FDR (Benjamini-Hochberg)."],"omics_type":["Proteomics"],"labhead":["Prof. Dr. Manuela Baccarini"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Max Perutz Labs, Department of Microbiology, Immunobiology and Genetics, Center for Molecular Biology, University of Vienna"],"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":"Systematic mapping of MEK (MEK1, MEK2) interactomes, in WT, inactive, clinically relevant and functional mutations","description":"This dataset provides a comprehensive proteomic map of the MEK1 and MEK2 interactomes, utilizing two complementary mass spectrometry (MS) approaches to capture both stable and transient protein-protein interactions (PPIs).  A total of 8 functional and clinical mutations of MEK1 was used as bait in addition to the WT. For MEK2, only the WT was used.","dates":{"publication":"2026-07-10","submission":"2026-06-05"},"accession":"PXD079313","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","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:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:595495","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:74426","NEWT:443906","NEWT:1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