{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/Wang_etal_2026_S1_WT_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/Wang_etal_2026_S7_upl3_upl4_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/Wang_etal_2026_S3_WT_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/Wang_etal_2026_S9_upl3_upl4_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/Wang_etal_2026_S2_WT_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/Wang_etal_2026_S8_upl3_upl4_2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD072854/Wang_etal_2026_WT_upl3_upl4.7z"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Steven.Spoel@ed.ac.uk"],"submitter":["Christos Spanos"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Lumos dda","Ubiquitome","Upl3","Upl4","Ubiquitin-proteasome sydtem (ups)","Ubiquitin ligases"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072854"],"tissue":["Cell Culture"],"sample_protocol":["The HALO-Ubiquilin fusion protein was expressed in E. coli and immobilised onto HaloTag magnetic affinity beads (Promega). 2-week-old Arabidopsis seedlings were ground in liquid nitrogen, and homogenised in extraction buffer (1x PBS, 0.05% NP-40, 0.05% Triton, 10 mM NEM, 40 μM MG132, protease inhibitor cocktail, and PPI3). Protein extracts were centrifuged at 13,000 rpm for 20 min at 4°C and supernatant was incubated with the prepared HaloTag magnetic affinity beads overnight at 4°C with rotation. Subsequently, the beads were washed three times with the extraction buffer, followed by three additional washes with 1x PBS.Protein samples from all biological replicates were processed at the same time and with using the same digestion protocol without any deviations. They were subjected for MS analysis under the same conditions. Protein and peptide lists generated using the same software and the same parameters. Specifically, proteins were digested on beads according to the following protocol. Beads were isolated on a magnetic rack and the elution, from the IP buffer, was substituted by 50µL of 8M urea in 50mM ammonium bicarbonate (ABC). Proteins were then reduced in 100mM dithiothreitol (Sigma Aldrich, UK) for 30 min at room temperature with constant shaking and alkylated in 100mM chlorodoacetamide (Sigma Aldrich, UK) for 30 min at ambient temperature in the dark (also with constant shaking). Following alkylation, proteins were digested for 4 hours with LysC (FujiFilm Wako, Japan) (1:50 protease:protein ratio). The samples were then diluted with 50mM ABC to reduce the concentration of urea below 2M and digested overnight at ambient temperature and constant shaking with trypsin (Pierce Scientific, UK), with the same protease:protein ratio as with LysC. Following digestion, samples were diluted with equal volume of 0.1% TFA and spun onto StageTips as described by Rappsilber et al (2007). Peptides were eluted in 40 μL of 80% acetonitrile in 0.1% TFA and concentrated down to 1 μL by vacuum centrifugation (Concentrator 5301, Eppendorf, UK). They were then prepared for LC-MS/MS analysis by diluting it to 5 μL by 0.1% TFA. LC-MS-analyses were performed on an Orbitrap Fusion™ Lumos™ Tribrid™ Mass Spectrometer (Thermo Scientific, UK) coupled on-line, to an Ultimate 3000 RSLCnano Systems (Dionex, Thermo Fisher Scientific, UK). Peptides were separated on a 50 cm EASY-Spray column (Thermo Scientific, UK), which was assembled on an EASY-Spray source (Thermo Scientific, UK) and operated at 55°C. Mobile phase A consisted of 0.1% formic acid in LC-MS grade water and mobile phase B consisted of 80% acetonitrile and 0.1% formic acid. Peptides were loaded onto the column at a flow rate of 0.3 μL min-1 and eluted at a flow rate of 0.25 μL min-1 according to the following gradient: 2 to 40% mobile phase B in 150 min and then to 95% in 11 min. Mobile phase B was retained at 95% for 5 min and returned back to 2% a minute after until the end of the run (190 min). FTMS spectra were recorded at 120,000 resolution (scan range 350-1500 m/z) with an ion target of 7.0×105. MS2 was performed in the ion trap with ion target of 1.0×104 and HCD fragmentation (Olsen et al. 2007) with normalized collision energy of 27. The isolation window in the quadrupole was 1.4 Thomson. Only ions with charge between 2 and 7 were selected for MS2."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The MaxQuant software platform (Cox and Mann 2008) version 1.6.1.0 was used to process the raw files and search was conducted against the Arabidopsis thaliana complete/reference proteome (Uniprot, released in August, 2019), using the Andromeda search engine (Cox et al. 2011). For the first search, peptide tolerance was set to 20 ppm while for the main search peptide tolerance was set to 4.5 pm. Isotope mass tolerance was 2 ppm and maximum charge to 7. Digestion mode was set to specific with trypsin allowing maximum of two missed cleavages. Carbamidomethylation of cysteine was set as fixed modification. Oxidation of methionine, and the DiGly residue on lysine were set as variable modifications. Absolute protein quantification was performed as described in Schwanhüusser et al. 2011. Peptide and protein identifications were filtered to 1% FDR."],"omics_type":["Proteomics"],"labhead":["Steven Spoel"],"instrument_platform":[""],"labhead_affiliation":["University of Edinburgh"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["Not available"],"submitter_mail":["spanos.christos@gmail.com"],"submitter_affiliation":["University of Edinburgh"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Identification of the ubiquitination landscape in Arabidopsis upl3 upl4 mutants","description":"The ubiquitin-proteasome system (UPS) serves as the primary pathway regulating cellular homeostasis and environmental responses in eukaryotes. In this pathway, E3 ubiquitin ligases catalyse substrate ubiquitination, thereby marking targets for proteasomal degradation. UPL3 and UPL4 are proteasome-associated HECT-type ubiquitin ligases known to remodel substrate-attached ubiquitin chains at the proteasome, ensuring processive degradation. To investigate the role of UPL3/4 in regulating cellular ubiquitination, we enriched ubiquitinated proteins from wild-type and upl3 upl4 mutant seedlings using a Ubiquilin UBA domain tetramer. The purified ubiquitome was subsequently analysed by liquid chromatography-mass spectrometry (LC-MS).","dates":{"publication":"2026-08-06","submission":"2026-01-09"},"accession":"PXD072854","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","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:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:112509","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","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:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","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:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","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:37919","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:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:177437","NEWT:717966","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:9006","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:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","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: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:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","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:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","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:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:10804","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","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