{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep1_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep3_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep3_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep1_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep2_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep1_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep2_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep1_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep3_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep3_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep3_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep2_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep2_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep2_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/20191213_QEP1_PBE_FC_U2OS_UFC1_APEX_rep3_1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD069185/maxquant_output.zip"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["p.beli@imb-mainz.de"],"submitter":["Petra Beli"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Ufmylation","Nhej","Double-strand break","Proximity proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069185"],"tissue":["Cell Culture"],"sample_protocol":["Samples were alkylated by addition of 5.5 mM chloroacetamide and loaded onto 4-12% gradient Bis-Tris gels. Proteins were separated by SDS-PAGE, stained using a Colloidal Blue Staining Kit (Life Technologies) and in‐gel digested using trypsin. Peptides were extracted from gel and desalted on reversed‐phase C18 StageTips. Peptides were analysed on a quadrupole Orbitrap mass spectrometer (Q Exactive Plus, Thermo Scientific) equipped with a UHPLC system (EASY-nLC 1200, Thermo Scientific) as described previously. The mass spectrometer was operated in data‐dependent mode, automatically switching between MS and MS2 acquisition. Survey full scan MS spectra (m/z 300-1,700) were acquired in the Orbitrap. The 15 most intense ions were sequentially isolated and fragmented by higher energy C‐trap dissociation (HCD). An ion selection threshold of 5,000 was used. Peptides with unassigned charge states, as well as with charge states <+2, were excluded from fragmentation. Fragment spectra were acquired in the Orbitrap mass analyser."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw data files were analysed using MaxQuant software (development version 1.5.2.8). Parent ion and MS2 spectra were searched against a database containing 98,566 human protein sequences obtained from UniProtKB (April 2018 release) using the Andromeda search engine. Spectra were searched with a mass tolerance of 6 ppm in MS mode, 20 ppm in HCD MS2 mode, strict trypsin specificity and allowing up to two miscleavages. Cysteine carbamidomethylation was set as a fixed modification, whilst N-terminal acetylation and oxidation were set as variable modifications. The dataset was filtered based on posterior error probability (PEP) to arrive at a FDR<1% estimated using a target‐decoy approach. Processed data from MaxQuant were analysed in RStudio (R version 4.2.3). Proteins or peptides flagged as “reverse”, “only identified by site” or “potential contaminant” were excluded from downstream analysis. Only proteins identified by no less than two peptides and at least one unique peptide were used in downstream analysis. Statistical significance was assessed using the LIMMA package (limma-v 3.54.2). Gene ontology analyses were carried out for the most significantly enriched proteins (false discovery rate (FDR) ≤ 0.005) using ShinyGO 0.80 and KEGG."],"omics_type":["Proteomics"],"labhead":["Petra Beli"],"instrument_platform":[""],"labhead_affiliation":["Institute of Molecular Biology gGmbH(IMB), Mainz, 55128, Germany  Institute for Developmental Biology and Neurobiology (iDN) University of Mainz, Germany"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["p.beli@imb-mainz.de"],"publication":["42297806 Wang Z, Foster BM, da Costa IC, Wu Y, Behera D, Conte F, Trotter EW, Lopezcolorado FW, Cabello-Lobato MJ, Choudhary S, Wiener R, Beli P, Smith DL, Banks WH, Bagley S, McKee S, Minnis M, Meyer S, Chaplin AK, Dörner W, Mootz HD, Hagan IM, Galanty Y, Stark JM, Larrosa I, Cliff MJ, Schmidt CK. Systematic discovery of UFM1 receptors reveals a regulatory module in DNA repair directing non-homologous end-joining. Nat Commun. 2026 17(1):7574 10.1038/s41467-026-73882-8"],"submitter_affiliation":["Institute of Molecular Biology (IMB), Mainz, Germany"],"submitter_country":["Germany"],"pubmed_abstract":["Posttranslational modifications with ubiquitin-like modifiers (UBLs) are critical for genome maintenance, yet many remain mechanistically uncharacterised. Here, we identify UFM1 as a key regulator of non-homologous end-joining (NHEJ), a major DNA double-strand break repair pathway. Using a structure-guided chemical biology approach, we develop a photo-crosslinkable UFM1 probe and, in combination with NMR, map non-canonical UFM1-binding interfaces in core NHEJ factors, including the disordered XRCC4 tail. Mechanistically, proximity-dependent proteomics and functional assays identify Ku70 as a crucial UFMylation substrate and reveal a UFM1-dependent axis in which XRCC4 engages UFMylated Ku70 to stabilise NHEJ complex assembly on chromatin. Disruption of this molecular mechanism via UFSP2 depletion or a hypomorphic UBA5 variant in patient-derived cells impairs NHEJ function, linking UFMylation defects to compromised genome integrity processes. Our findings define a complete UFM1 signalling module in DNA repair and establish a generalisable framework for dissecting low-affinity UBL networks with broad functional and disease relevance."],"pubmed_title":["Systematic discovery of UFM1 receptors reveals a regulatory module in DNA repair directing non-homologous end-joining."],"pubmed_authors":["Wang Zijuan Z, Foster Benjamin M BM, da Costa Isabelle C IC, Wu Yue Y, Behera Deepak D, Conte Francesca F, Trotter Eleanor W EW, Lopezcolorado Felicia Wednesday FW, Cabello-Lobato Maria Jose MJ, Choudhary Shweta S, Wiener Reuven R, Beli Petra P, Smith Duncan L DL, Banks William H WH, Bagley Steven S, McKee Shane S, Minnis Meenakshi M, Meyer Stefan S, Chaplin Amanda K AK, Dörner Wolfgang W, Mootz Henning D HD, Hagan Iain M IM, Galanty Yaron Y, Stark Jeremy M JM, Larrosa Igor I, Cliff Matthew J MJ, Schmidt Christine K CK"],"additional_accession":[]},"is_claimable":false,"name":"UFMylation orchestrates chromatin engagement of core NHEJ components to promote DNA double-strand break repair","description":"DNA double-strand breaks (DSBs) are highly cytotoxic lesions that – if misrepaired – can lead to genomic instability, cancer, and developmental disorders. While ubiquitin and select ubiquitin-like proteins (UBLs) are established regulators of DSB repair, many UBLs remain understudied. Here, through systematic UBL screening, we identify UFM1 as a novel regulator of non-homologous end-joining (NHEJ). Using a photo-crosslinkable UFM1 probe, we uncover core NHEJ components, including XRCC4, as downstream UFM1 receptors. Complementary proximity screening reveals UFMylated Ku70 as a key upstream target recognised by XRCC4. Mechanistically, UFMylation facilitates chromatin recruitment and assembly of NHEJ factors, establishing a central role in end-joining repair. Our findings link hereditary UFMylation disorders to defective NHEJ processes, contributing to our molecular understanding of diseases biology. Beyond this, our bottom-up screening strategy reveals broader networks of UFM1-regulated factors, featuring diverse roles in genome maintenance and cellular homeostasis.","dates":{"publication":"2026-07-31","submission":"2025-10-07"},"accession":"PXD069185","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:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:1907535","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: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:199225","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:31345","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:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:258741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