{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/IgG_control_IP_S2.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_shared_IP_S2.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/MP1_FLAG_IP_S3.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_shared_IP_S3.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_unique_IP_S3.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/Outcomp_control_IP_S3.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/MP1_FLAG_IP_S1.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/IgG_control_IP_S3.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/MP1_FLAG_IP_S2.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/Outcomp_control_IP_S2.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/Outcomp_control_IP_S1.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_unique_IP_S2.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_shared_IP_S1.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_unique_IP_S1.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/IgG_control_IP_S1.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/Outcomp_control_IP_S2_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/Outcomp_control_IP_S1_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/MP1_FLAG_IP_S2_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/Outcomp_control_IP_S3_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/MP1_FLAG_IP_S3_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_shared_IP_S2_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_shared_IP_S3_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_shared_IP_S1_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/MP1_FLAG_IP_S1_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_unique_IP_S3_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/IgG_control_IP_S2_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/IgG_control_IP_S3_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_unique_IP_S2_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/APC1_unique_IP_S1_RAW.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070186/IgG_control_IP_S1_RAW.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sabapat@nccs.res.in"],"submitter":["Amruta Jadhav"],"technology_type":["Mass Spectrometry","Top-down proteomics","Bottom-up proteomics"],"disease":["Malignant Neoplasm Of Ovary"],"software":[""],"submitter_keywords":["Human","Ip-ms","Anapc1","Ovarian cancer","Mp1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070186"],"tissue":["Epithelial Cell","Cell Culture"],"sample_protocol":["Protein samples obtained from the RNA pull-down assay were processed for LC–MS/MS analysis using a combination of ultrafiltration-based cleanup, in-solution digestion, and peptide desalting.  1. Amicon Ultra 3 kDa MWCO Cleanup and Buffer Exchange  Protein samples were concentrated and buffer-exchanged using Amicon Ultra 0.5 mL centrifugal filters (3 kDa MWCO). Filters were pre-equilibrated twice with 500 µL Milli-Q water by centrifugation at 14,000 × g for 15 min at 4 °C. Samples were loaded onto the filters and centrifuged under the same conditions, followed by sequential washes with Milli-Q water and 100 mM ammonium bicarbonate (ABC). The concentrated protein retentate was recovered by inverting the filter unit into a clean tube and centrifuging at 1,000 × g for 3 min at 4 °C.  2. In-Solution Digestion (TFE-Assisted)  Approximately 50 µg of protein was mixed with 100 mM ABC, trifluoroethanol (TFE), and DTT, and reduced for 45 minutes at room temperature. Cysteine residues were alkylated with iodoacetamide (IAA) for 1 hour in the dark, followed by an additional brief reduction step with DTT. The sample was then diluted with Milli-Q water and 100 mM ABC to maintain a pH between 7.5 and 8.5. Proteins were digested overnight at 37 °C using trypsin (Porcine pancreas, Sigma, Cat. No. T6567) at an enzyme-to-substrate ratio of 1:25 (w/w). Digestion was quenched by adding trifluoroacetic acid (TFA) to a final concentration of 0.5%, and peptides were dried using a SpeedVac concentrator.  3. Peptide Desalting Using C18 ZipTips  Peptides were desalted using C18 ZipTip pipette tips (Millipore, Cat. No. ZTC18S960). Tips were conditioned with acetonitrile (ACN) + 0.1% TFA, equilibrated with 0.1% TFA in water, and the peptide solution was repeatedly aspirated and dispensed to bind the peptides. Bound peptides were washed with 0.1% TFA in water and eluted using a 50:50 mixture of ACN and water containing 0.1% TFA. The eluted peptides were dried again in a SpeedVac prior to LC–MS/MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw LC-MS/MS data were processed using Proteome Discoverer (Thermo Fisher Scientific, version ≥2.x). Spectra were searched against the Uniprot Human reference proteome (with common contaminants included) using the Sequest HT search engine.  Search Parameters:  Enzyme: Trypsin (Full)  Maximum missed cleavages: 2  Precursor mass tolerance: 10 ppm  Fragment mass tolerance: 0.02 Da (Orbitrap MS2 detection)  Fixed modification: Carbamidomethylation (Cys)  Variable modifications: Oxidation (Met); Acetylation (Protein N-terminus)  Peptide-spectrum matches were scored using Percolator, and identifications were filtered to achieve a 1% FDR at both PSM and protein levels. Protein grouping was performed using the default parsimony rules.  Quantification  Label-free quantification (LFQ) was performed using the Precursor Ion Quantification workflow with intensity-based normalization applied across all samples. Only proteins identified with at least one unique peptide were retained for downstream comparative analysis. Missing intensity values were handled using the software’s default settings for feature alignment and match-between-runs."],"omics_type":["Proteomics"],"labhead":["Dr. Sharmila A. Bapat"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["BRIC-National Centre for Cell Science, Inside Pune Univesrity, Ganeshkhind, Pune, India, 411007"],"species":["Homo Sapiens (human)"],"publication":["42049239 Jadhav AR, Sahoo S, Kuber YL, Hatwar K, Varanwal A, Tanwar K, Palwankar S, Chatrasal G, Mali AM, Bapat SA. Emergence and evolution of chimeric pseudogenes (φgenes) contribute to genetic and functional diversity of the human genome. Nucleic Acids Res. 2026 54(8):gkag375 10.1093/nar/gkag375"],"submitter_mail":["amrutaj355@gmail.com"],"submitter_affiliation":["National centre for cell science, Pune, India"],"submitter_country":["India"],"pubmed_abstract":["Genome evolution through rearrangements and selection drives the emergence of new genes, gene families, and species. Although pseudogenes (φgenes) are often regarded as \"dead on arrival\" due to disruptive mutations or loss of regulatory elements, our earlier work revealed that several φgenes remain transcriptionally active, challenging this assumption. Here, we show that segmental duplications at proximal loci can generate chimeric φgenes comprising contiguous sequences from two or more genes, occasionally through intron fusions. These fused introns and flanking exons appear to have co-evolved from ancestral parent genes. Co-opting of 5' regulatory elements from the upstream parent likely drives chimeric φgene activation, while 3' modifications enhance transcript stability. Some chimeric φgenes retain strong coding potential, producing novel or truncated proteins that preserve parental domains. Notably, their expression is restricted to human tissues and exhibits signatures of purifying selection. Functional analysis identifies ANAPC1P2 (vA-202) as a coding-noncoding (cnc) RNA that regulates p53 stability and translation, while HYDIN2 knockdown impairs neuronal differentiation, underscoring the regulatory significance of these chimeric φgenes. Collectively, our findings suggest that chimeric φgenes and their emergent functions contribute to human-specific traits, speciation, and adaptive evolution."],"pubmed_title":["Emergence and evolution of chimeric pseudogenes (φgenes) contribute to genetic and functional diversity of the human genome."],"pubmed_authors":["Jadhav Amruta R AR, Sahoo Sushmita S, Kuber Yash L YL, Hatwar Krutika K, Varanwal Avinash A, Tanwar Khushi K, Palwankar Shubhankar S, Chatrasal Gauri G, Mali Avinash M AM, Bapat Sharmila A SA"],"additional_accession":[]},"is_claimable":false,"name":"IP-MS Profiling of ANAPC1 and MP1 Interaction Networks in OVCAR3 Cells","description":"We identified a pseudogene-derived chimeric transcript, vA-202, which encodes a partial ANAPC1-derived protein (MP1). To characterize its protein interaction network, we transiently expressed FLAG-tagged MP1 in OVCAR3 cells and performed immunoprecipitation using an anti-FLAG antibody. For comparison with the parental protein, endogenous ANAPC1 was immunoprecipitated using two antibodies: one specific to ANAPC1 alone and another recognizing an epitope shared with MP1. Corresponding IgG and peptide competition controls were included to eliminate nonspecific interactions. Immunoprecipitated protein complexes were subjected to LC-MS/MS analysis to identify interacting partners of both ANAPC1 and MP1.","dates":{"publication":"2026-05-25","submission":"2025-11-01"},"accession":"PXD070186","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: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:2587410","NEWT:207340","NEWT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