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ubiquitin-like proteins (ubls); dna repair; dna double-strand breaks (dsbs); non-homologous end-joining (nhej); xrcc4; genetic code expansion; photo-crosslinking; proximity labelling","proximity labelling","xrcc4","genetic code expansion","non-homologous end-joining (nhej)","photo-crosslinking","dna repair","Ufm1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069136"],"sample_protocol":["UFM1 interactors screen: HEK293T cells were harvested 30 min after exposure to IR (10 Gy) and lysed in PBS (137 mM NaCl, 2.7 mM KCl, 10 mM Na₂HPO₄, 1.8 mM KH₂PO₄, pH 7.4) containing 1 × cOmplete EDTA-free protease inhibitors (Roche), using three cycles of sonication (30 s on/off, 30% power). 20 µM singly C-terminally biotinylated UFM1 containing BpF at amino acid position F35 (UFM1*) was incubated with 2-10 mg/mL HEK293T cell extracts for 30 min at 4 °C in 0.2 mL thin-walled polypropylene PCR tubes (Greiner Bio-One). Samples were then irradiated for 2 h with long-wave UV light (λ = 365 nm; Herolab UV-16 L, 8 W) at a 6 mm distance. Aliquots were collected before and after UV exposure. Proteins crosslinked to UFM1 were enriched via streptavidin sepharose pulldown (Cytiva, 17-5113-01). Beads were washed five times with 500 µL of each of the following buffers using spin columns (Pierce Micro-Spin, cat#10510824): buffer A (8 M urea, 2% SDS, 100 mM Tris-HCl pH 8, 200 mM NaCl), buffer B (8 M urea, 0.2% SDS, 10% ethanol, 10% isopropanol, 100 mM Tris-HCl pH 8, 1.2 M NaCl), buffer C (same as buffer B, pH 5), buffer D (same as buffer B, pH 9), buffer E (100 mM Tris-HCl pH 8, 200 mM NaCl), and buffer F (50 mM NH₄HCO₃). Streptavidin beads were transferred to protein LoBind tubes (Eppendorf) and bound proteins eluted with 2 × SDS Laemmli buffer (120 mM Tris-HCl pH 6.8, 4% SDS, 20% glycerol, 0.02% bromophenol blue and 2.5%-mercaptoethanol) for SDS-PAGE analysis. Samples were excised from fully resolved SDS-PAGE gels, subjected to in-gel tryptic digestion.  UFM1 CX-MS: 20 µM UFM1 F35-BpF proteins were incubated with 20 µM UFM1 receptor proteins in PBS for 30 min at 4 °C in 0.2 ml thin-walled polypropylene PCR tubes (Greiner Bio-One). Samples were irradiated for 2 h with long-wave UV light (λ = 365 nm; Herolab UV-16 L, 8 W) at a 6 mm distance. Aliquots were collected before and after UV exposure for SDS-PAGE analysis. The crosslinked proteins were subjected to solution or in-gel tryptic digestion of bands excised from an SDS-PAGE gel.  Ku UFMylation: the reaction was fully resolved by 15% SDS-PAGE with ± ATP samples from two repeats separated by empty lanes. Following brief staining with Coomassie Brilliant Blue, bands were excised at ~70-100 kDa (for Ku70/80) and >100 kDa (for DNA-PKcs). Gel pieces were dehydrated and re-hydrated 5 times with HPLC-grade acetonitrile and HPLC-grade water, respectively, before drying to completeness in a vacuum centrifuge. Gel slices were rehydrated in 40 µl 50 mM TEAB (#catT7408, Sigma) and sequencing-grade trypsin was added at 20 ng/µl and incubated at RT for 20 min without shaking, before 100 µL 50 mM TEAB (#catT7408, Sigma) was added and incubated at 37 °C with shaking for 18 h. Overnight digests were acidified by the addition of formic acid to a final concentration of 0.2% (v/v) and dried to completeness in a vacuum centrifuge. Peptide digests were finally resuspended in 5 µL of 0.2% formic acid immediately prior to LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["UFM1 interactors screen: DIA data was processed using Spectronaut 17 (Biognosys) in direct DIA mode using oxidation (M), deamidation (NQ) and acetylation (N-terminal) as variable modifications in a search against a human Uniprot database and only high-confidence matches were retained for downstream analysis. Gene ontology analyses were carried out for the most significantly enriched proteins (log2 fold change ≥ 0.58) using ShinyGO 0.80 and KEGG.  UFM1 CX-MS: Raw files were analysed directly using pLink2.0 to identify crosslinked peptides. BpF was manually input as an amino acid (designated “X”) and the UV-inducible BpF crosslinker was manually input as crosslinking X to any other canonical amino acid with a crosslink or monolink mass of zero. Met oxidation, Gln/Asn deamidation, and N-terminal acetylation were included as variable modifications. Search parameters included a peptide length 3-100 and peptide mass of 400-10,000 Da, a maximum of 3 missed cleavages allowed, and a precursor and fragment mass tolerance of 20 ppm. An FDR of <1 % was used to filter out low-confidence crosslinks. Fasta files containing the amino acid sequences of the relevant protein constructs were used. For experiments with UFM1-UBA5, trypsin was combined with elastase digestion in tandem while for UFM1-XRCC4 experiments, trypsin was combined with chymotrypsin. The resulting high-confidence crosslinks were further manually inspected using pLabel to assess spectral evidence.  Ku UFMylation: Data was analysed using Scaffold PTM v 4.0.2 (Proteome Software) with VG or DRVG as a variable modification on K residues to detect UFMylated sites."],"omics_type":["Proteomics"],"labhead":["Christine Schmidt"],"instrument_platform":[""],"labhead_affiliation":["Manchester Cancer Research Centre, Division of Cancer Sciences, School of Medical Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, UK"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["10.1038/S41467-026-73882-8"],"submitter_mail":["benjamin.foster@manchester.ac.uk"],"submitter_affiliation":["Manchester Cancer Research Centre, Division of Cancer Sciences, Faculty of Biology, Medicine and Health, University of Manchester"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Systematic discovery of UFM1 receptors reveals a regulatory module in DNA repair directing non-homologous end-joining","description":"As the most recently identified UBL, UFM1 is garnering increasing attention for its roles beyond its canonical functions at the endoplasmic reticulum. To address the challenge of defining UFM1 substrate-receptor relationships, we develop a fully functional, photo-crosslinkable UFM1 probe for receptor screening. The approach identifies a broad spectrum of UFM1-interacting proteins, spanning biological processes known to be regulated by UFM1 as well as unknown associations. Notably, several core NHEJ components ranked prominently amongst the candidates. Using additional biochemical and biophysical techniques, including crosslinking mass spectrometry (CX-MS), we validate and characterise non-canonical UFM1-binding regions on several NHEJ proteins, including XRCC4. In addition, using recombinant reagents, we have identified potential UFMylation sites of Ku70 and Ku80 through identification of VG-K remnant peptides following trypsin digestion.","dates":{"publication":"2026-06-25","submission":"2025-10-05"},"accession":"PXD069136","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: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:2086595","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:3357","NEWT:111225","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: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: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: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:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:1122981","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:1380096","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:299467","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","N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