{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_02end.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_03end.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_02.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_06.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_04.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_09.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_03.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_01.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_01.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_05.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_07.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_01end.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_04.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_07.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_02.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_06.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_08.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_05.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_08.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_03.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/sample_description_RBMXL1_Pierre_Tilliole.sdrf.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_02end.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_01end.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_03end.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/240522_PT_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD066823/230427_PT_01.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["godin@igbmc.fr"],"submitter":["Bastien Morlet"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Splicing","Evolution","Neurodevelopmental disorder","Rbmx","Rbmxl1 retrocopy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066823"],"tissue":["Brain","Cell Culture"],"sample_protocol":["Analysis of binding partners. After IP, the proteins retained on the beads were reduced 30 min at 56°C with 5 mM TCEP in Urea 2M (Sigma Aldrich), 0.1M Tris pH8, then alkylated 30 min at RT with 10 mM IAA (iodoacetamide). Trypsin digestion was carried out at 37°C, OVN with 500 ng enzymes. After acidification with Trifluoroacetic acid (TFA) (Sigma Aldrich), the peptide supernatant was desalted on C18 spin column and dried on Speed-Vacuum before LC-MS/MS analysis. Samples were analyzed using an Ultimate 3000 nano-RSLC (Thermo Scientific, San Jose California) coupled in line with a quadrupole - orbitrap Exploris 480 via a nano-electrospray ionization source (Thermo Scientific, San Jose California) and the FAIMS pro interface. The tryptic peptides were loaded on a C18 Acclaim PepMap100 pre-column (75 µm x 2 cm, 3 µm, 100Å, Thermo Fisher Scientific) for 1 minutes at 15 µL/min with 2% Acetonitrile MS grade (ACN) (Sigma Aldrich), 0.1% Formic acid (FA) in H2O and then separated on a C18 PepMap nano-column (75 µm ID x 25 cm, 2.6 µm, 150Å, Thermo Fisher Scientific) with a 23 minutes linear gradient from 7% to 35% buffer B (A: 0.1% FA, in H2O; B: 0.1% FA in 80% ACN) at 400 nl/min followed by a regeneration step at 90% B and a equilibration at 7% B. The total chromatography was 30 minutes. The mass spectrometer was operated in positive ionization mode in Data-Dependent Acquisition (DDA) for one FAIMS compensation voltages (CV = -45V). The DDA cycle consisted of one survey scans or MS1 (300-1500 m/z, 120,000 FWHM) followed by MS² spectra (HCD; 30% normalized energy; 2 m/z window; 30,000 FWMH) in the limit of 1.2 sec. The Automatic Gain Control (AGC target) were set to 3E6 and 1E5 respectively for MS1 and MS2 scans, and the maximum injection time (IT) was set to 50 ms for both scan modes. Unassigned and single charged states were rejected. The exclusion duration was set for 40 s with mass width was ± 10 ppm."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Proteins were identified with Proteome Discoverer 2.5 software (Thermo Fisher Scientific) and Homo Sapiens proteome database (UniProt, reviewed, release 2024_04_03 with 20598 entries). Precursor and fragment mass tolerances were set at 10 ppm and 0.02 Da respectively, and up to 2 missed cleavages were allowed. Oxidation (M) was set as variable modification, and Carbamidomethylation (C) as fixed modification. Peptides were filtered with a false discovery rate (FDR) at 1%, rank 1. Proteins were quantified with a minimum of 1 unique peptide based on the XIC (sum of the Extracted Ion Chromatogram). The quantification values were exported in Perseus for statistical analysis involving a log[2] transform, imputation, normalization47. Gene Ontology (GO) analysis was performed using DAVID tool48 on the top proteins (P-value<0.05) identified by mass spectrometry data. The top 10 categories were selected based on Benjamini–Hochberg-corrected P-values. A correlation plot was generated by calculating the difference in binding (log₂ fold change) between HA-RBMXL1 and HA-RBMX conditions for each shared interactor (P-value<0.05) identified in the mass spectrometry data. Each point represents a shared interactor, plotted according to its log₂ fold change in binding to HA-RBMX (x-axis) and HA-RBMXL1 (y-axis). A linear regression was fitted to the data, and the coefficient of determination (R²) was calculated to assess the strength of the correlation between the two conditions.  Analysis of human RBMX and RBMXL1 protein expression. The same analysis than the one for binding partners was performed, except that it was used with an inclusion mass list. The mass list contains (compound: GLPPSMER, m/z: 443.725; IVELLMK, 472.796; IVEVLLM(-Ox)K, 480.793; VEQATKPSFESGR, 718.362; GLPPSVER, 427.739; IVEVLLIK, 463.817; VEQATKPSFER, 646.335). If no targets of the previous list were found, dependent scan was performed on the most intense ion. For RBMX, all the compounds can be used to detect both RBMX isoforms (NP_002130.2 and NP_001158275.1), but only the following compounds, IVELLMK and IVEVLLM(Ox)K, are found to the isoform NP_001158275.1."],"omics_type":["Proteomics"],"labhead":["Dr Juliette D. Godin"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["IGBMC, Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France, UMR7104, UMR-S 1258."],"species":["Homo Sapiens (human)"],"publication":["42360281 Tilliole P, Mattausch C, Tilly P, Leitão E, Boutaud L, Lehalle D, An I, Argilli E, Aufox S, Callewaert B, Charles P, Cinkornpumin JK, Courtin T, Vecchia MD, Davis EE, Dimitrov BI, Dobyns W, Epifanova E, Grandgirard E, Jung M, Jurgensmeyer Langas S, Kaya S, Keren B, Khan TN, Lejeune E, Li M, Marie Y, Morlet B, Nava C, Pastor WA, Plassard D, Prada CE, Rastetter A, Schwaller N, Sestan N, Sherr E, Temple SL, Tenywa JF, Tielens S, van Haeringen A, Whitley H, Nguyen L, Steenpaß L, Rhinn M, Collins SC, Héron D, Cormier-Daire V, Attie-Bitach T, Yalcin B, Depienne C, Godin JD. RBMX functional retrocopy safeguards brain development in a species-dependent context. Brain. 2026:awag218 10.1093/brain/awag218"],"submitter_mail":["morletb@igbmc.fr"],"submitter_affiliation":["IGBMC - CNRS UMR 7104 - Inserm U1258"],"submitter_country":["France"],"pubmed_abstract":["Retrotransposition has generated thousands of intronless gene copies in mammalian genomes, yet their contribution to brain development and evolution remains largely unexplored. RBMX encodes an X-linked RNA-binding protein involved in pre-mRNA splicing. RBMX has highly similar retrocopies, RBMXL1, which arose independently in primates and rodents, suggesting convergent evolutionary pressure and potential functional compensation. We identified individuals with RBMX variants through exome sequencing and GeneMatcher. We combined transcriptomic profiling, protein-protein and protein-RNA interaction studies both in human cellular models and mouse embryonic cortices to assess the functional redundancy between RBMX and its retrocopy RBMXL1. Finally, we use mouse genetics to dissect RBMX function and its compensation by RBMXL1 in corticogenesis. Hemizygous RBMX variants lead to neurodevelopmental disorders characterized by intellectual disability and variable brain, ocular, and genital malformations. N-terminal variants include missense changes and in-frame deletions, whereas truncating variants clustered in the final exon. RBMX pathogenic variants disrupt cortical development through both partial loss-of function (C-terminal variants) and gain-of-function (N-terminal variants) mechanisms. Despite severe phenotypes in humans, Rbmx-deficient mice display only mild cortical abnormalities. We demonstrate that RBMX and RBMXL1 share protein and RNA partners and act redundantly in brain development, with RBMXL1 buffering the impact of RBMX deficiency. Together, these findings establish RBMXL1 as a functional paralog of RBMX that is likely buffering deleterious variation in a context- and dosage-dependent manner. More broadly, these results identify retrocopies as active contributors to neurodevelopmental robustness and suggest that functional retrocopies may have facilitated the evolutionary diversification of the mammalian brain."],"pubmed_title":["RBMX functional retrocopy safeguards brain development in a species-dependent context."],"pubmed_authors":["Tilliole Pierre P, Mattausch Carolin C, Tilly Peggy P, Leitão Elsa E, Boutaud Lucile L, Lehalle Daphné D, An Isabelle I, Argilli Emanuela E, Aufox Sharon S, Callewaert Bert B, Charles Perrine P, Cinkornpumin Jessica K JK, Courtin Thomas T, Vecchia Marco Dalla MD, Davis Erica E EE, Dimitrov Boyan Ivanov BI, Dobyns William W, Epifanova Ekaterina E, Grandgirard Erwan E, Jung Matthieu M, Jurgensmeyer Langas Sarah S, Kaya Sabine S, Keren Boris B, Khan Tahir N TN, Lejeune Elodie E, Li Mingfeng M, Marie Yannick Y, Morlet Bastien B, Nava Caroline C, Pastor William A WA, Plassard Damien D, Prada Carlos E CE, Rastetter Agnès A, Schwaller Noémie N, Sestan Nenad N, Sherr Elliott E, Temple Suzanna L SL, Tenywa Jude-Felix JF, Tielens Sylvia S, van Haeringen Arie A, Whitley Helen H, Nguyen Laurent L, Steenpaß Laura L, Rhinn Muriel M, Collins Stephan C SC, Héron Delphine D, Cormier-Daire Valerie V, Attie-Bitach Tania T, Yalcin Binnaz B, Depienne Christel C, Godin Juliette D JD"],"additional_accession":[]},"is_claimable":false,"name":"Dual molecular mechanisms and functional compensation by RBMXL1 retrocopy underlie RBMX-associated neurodevelopmental syndrome","description":"Genetic variants in RBMX may cause X-linked neurodevelopmental syndromes, but their pathogenicity and mechanisms remain unclear. Here, we provide definitive evidence from nine unrelated families that RBMX variants lead to neurodevelopmental disorders characterised by intellectual disability, brain malformations, microcephaly, and microphthalmia. Combining in vitro and in vivo experiments in human and mouse models, we show that RBMX pathogenic variants disrupt cortical development through both loss- and gain-of-function mechanisms. Despite severe phenotypes in humans, Rbmx-deficient mice display only mild cortical abnormalities, which we attribute to partial compensation by Rbmxl1, a retrocopy that arose independently in mice and humans. We demonstrate that RBMX and RBMXL1 share protein and RNA partners and act redundantly during brain development, with RBMXL1 buffering the effect of RBMX loss. Our findings reveal that RBMX-related neurodevelopmental syndromes result from the interplay of opposing molecular mechanisms and retrocopy compensation, highlighting a previously unrecognized role for retrocopies in modulating disease severity.","dates":{"publication":"2026-07-28","submission":"2025-07-31"},"accession":"PXD066823","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:123606","NEWT:291146","NEWT:29466","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:476","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:265619","NEWT:11294","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NE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