{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_ONLYBEADS_SET3_021121.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_P_XEF_SET2_221021.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_FL_RA_SET2_221021_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_FL_RA_SET1_20082021.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_ONLYBEADS_SET1_021121.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_ONLYBEADS_SET2_221021.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_P_XEF_SET1_060122.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_FLRA_SET3_221021_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/BAPAT_P_XEF_SET3_021121.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD070150/vA202_RNApullDown_MaxQuant_SearchResults.zip"]},"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"],"disease":["Malignant Neoplasm Of Ovary"],"software":[""],"submitter_keywords":["Human","Rna pull down","Orbutrap ms"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070150"],"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"],"modification":[""],"quantification_method":[""],"data_protocol":["Raw mass spectrometry data acquired on an Orbitrap mass spectrometer were processed using MaxQuant (v1.6.17.0) with default parameters unless stated otherwise. The UniProt reference human proteome was used as the search database for peptide and protein identification. Enzyme specificity was set to trypsin/P and trypsin, allowing a maximum of two missed cleavages. Label-free quantification (LFQ) was enabled to estimate relative protein abundances, using a minimum ratio count of 1. The “Match between runs” option was activated to transfer identifications across different orbitrap runs based on retention time alignment, enhancing identification and quantification coverage. All other settings were maintained at their default values. The resulting proteinGroups.txt file was imported into Perseus (v1.6.14.0) for downstream statistical analysis. Proteins identified as reverse hits, potential contaminants, and proteins identified only by site were excluded from the dataset. LFQ intensity values were log₂-transformed to achieve normal distribution. Proteins with missing intensity values across replicates were filtered to retain only those quantified in at least two out of three replicates in at least one condition. Subsequent statistical analyses, including comparative expression profiling and significance testing, were performed within Perseus to identify differentially abundant proteins across experimental conditions. From the resulting dataset, proteins detected in control samples were filtered out—only-beads controls were used for RNA pull-down experiments, only-beads and IgG controls for APC1 immunoprecipitation, and only-beads and out competition controls for MP1 Flag immunoprecipitation. The remaining proteins were considered as the specific interactome for each respective experiment."],"omics_type":["Proteomics"],"labhead":["Dr. Sharmila A. Bapat"],"instrument_platform":[""],"labhead_affiliation":["National Centre for Cell Science, SPPU, Pune, India."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["amrutaj355@gmail.com"],"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_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":"RNA pull down experiment for vA-202 (ANAPC1P2) lncRNA","description":"This study aimed to identify protein interaction partners of the lncRNA vA-202 using an RNA pull-down approach followed by mass spectrometry. Biotinylated vA-202 RNA was generated by in vitro transcription incorporating biotin-14-CTP. For each pull-down reaction, 400 µg of whole-cell lysate (in a total volume of 100 µL) was incubated with 1 µg of biotinylated RNA in the presence of protease inhibitor cocktail (PIC), RNaseOUT, and 2× TENT buffer (20 mM Tris-HCl pH 8.0, 2 mM EDTA, 500 mM NaCl, 0.5% Tween-20), supplemented with IP lysis buffer (25 mM Tris-HCl pH 7.4, 150 mM NaCl, 1 mM EDTA, 1% NP-40, 5% glycerol). The mixture was rotated at 4 °C for 2 hours. In parallel, streptavidin magnetic beads were washed three times with PBST (PBS + 0.1% Tween-20) and maintained on ice.  The RNA-protein complexes were captured by adding the reaction mixture to the pre-washed magnetic beads and incubated for an additional 2 hours at 4 °C. Beads were then washed five times with PBST and twice with 100 mM ammonium bicarbonate. Bound proteins were eluted by incubating the beads in 0.1% RapiGest supplemented with 5 mM DTT at 60 °C for 30 minutes. The eluates were collected for downstream proteomic processing and LC-MS/MS analysis.  Two controls were included: (i) a pull-down using an unrelated RNA (p-XEF) and (ii) a beads-only control (no RNA). All pull-down experiments were performed in 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