{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066858/231215_Bobby_F2_5ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066858/231215_Bobby_F1_5ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066858/231215_Bobby_S2_5ul.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066858/231215_Bobby_S1_5ul.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD066858/swisstransfer_b338b8ba-270c-4009-a5ff-17c9a1638a2e.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jes14@st-andrews.ac.uk"],"submitter":["Sally Shirran"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Progressive Muscular Atrophy"],"software":[""],"submitter_keywords":["Proximity biotinylation","Co-immunoprecipitation","Interactomics","Proteomics","Silac","Turboid","Spinal muscular atrophy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD066858"],"sample_protocol":["SILAC Sample Preparation for Mass Spectrometry Analysis Cell Lysis 1. Resuspend cell pellets in up to 1 ml of fresh Low Salt RIPA buCer. 2. Sonicate on ice at 5 microns for 3 x 15 seconds, with 10 seconds of rest on ice between. 3. Measure total protein via Bradford Assay using a Biophotometer. 4. Store lysates at -80°C. FLAG Immunoprecipitation (Co-IP) 1. Pre-clear 2 mg of input protein in up to 0.7 ml of Low Salt Ripa BuCer with 20 μl of Sepharose beads via gentle rotation (15 RPM) for 30 min at 4°C using an end-over-end rotator. 2. Pellet beads and save 40 μg of the supernatant as the “Precleared” sample. 3. Add remaining supernatant to either 30 μl Protein A Beads and 2 μg/ml Invitrogen Mouse Anti-FLAG antibody (Antibody sample) or 30 μl Protein A Beads only (No Antibody sample). 4. Incubate samples at 4°C overnight with gentle rotation (15 RPM). 5. Pellet beads and save 40 μl of the supernatant as the “Bead Unbound” sample. 6. Wash beads in 500 μl of Low Salt RIPA buCer four times. 7. For western blotting, add 4X LDS Sample BuCer with DTT to a final concentration of 50 mM and heat beads for 25 mins at 65°C. 8. For on-bead digestion and mass spectrometry, wash combined bound bead fractions (Heavy/Medium/Light) five times with 50 mM ammonium bicarbonate solution. Streptavidin Pulldown 1. Pre-clear 2 mg of input protein in up to 0.7 ml of Low Salt Ripa BuCer with 20 μl of Sepharose beads via gentle rotation (15 RPM) for 30 min at 4°C using an end-over-end rotator. 2. Pellet beads and save 40 μl of the supernatant as the “Precleared” sample. 3. Wash Magnetic Streptavidin-Agarose Beads three times in Low Salt RIPA buCer. 4. Add 30 μl of beads to remaining precleared cell lysates and mix overnight at 4°C with gentle rotation. 5. Pellet beads using a magnetic rack and save 40 μl as an “Unbound” sample. 6. For western blotting, wash beads four times with Low Salt RIPA buCer and elute proteins using 30 μl of elution buCer (30 mM Biotin in 2% SDS) and 20 μl of 4X LDS BuCer with 50 mM DTT. 7. Heat beads for 25 mins at 65°C to reduce proteins. 8. For on-bead digestion and mass spectrometry, combine the bound bead samples (Heavy/Medium/Light) and wash five times with 50 mM ammonium bicarbonate solution. Mass Spectrometry Analysis Note: Specific MS methodology will depend on the instrumentation available. The following is optimised for the Orbitrap Fusion Lumos. 1. Perform trypsin digestion of beads overnight at 37°C. 2. Reduce final sample volume to 20 μl using a Speedvac. 3. Subject peptides to LC-MS/MS using an Ultimate 3000 RSLC coupled to an Orbitrap Fusion Lumos mass spectrometer with a FAIMS interface. 4. Inject peptides onto a reverse-phase trap for pre-concentration and desalting. 5. Elute peptides from the analytical column using a linear solvent gradient. 6. Operate mass spectrometer in Data Dependent Acquisition (DDA) positive ion mode with a cycle time of 1.5 seconds. 7. Select peptides with charge states 2 to 5 for fragmentation using HCD as collision energy."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data Processing 1. Search raw MS data files against the UniProt Human Proteome database using MaxQuant software (https://www.maxquant.org/) 2. Set peptide tolerance to 10 ppm and select trypsin as the enzyme. 3. Select fixed modification as carboxyamidomethylation of cysteine. 4. Select variable modifications as oxidation of methionine and N-terminal acetylation. 5. Select SILAC labels of Arg6 (R6), Arg10 (R10), Lys4 (K4), and Lys8 (K8). 6. Choose a minimum of 1 unique peptide, minimum ratio count of 2, and quantitation based on razor and unique peptides. 7. Set peptide and protein FDR to 0.01. 8. Run the analysis. Data Analysis 1. Process output data using the ProteinGroups file in Microsoft Excel or Perseus to produce ratios, proportions, and percentages. 2. Account for relevant controls and remove Control-only protein hits from datasets. 3. Charts can be produced using GraphPad Prism 6 or Microsoft Excel. 4. Perform statistical analysis in either Microsoft Excel or Perseus software (https://maxquant.net/perseus/) 5. Select proteins with significant changes in interactivity (P Value < 0.05 and Fold Change < 0.5 and > 1.5) for further analysis. 6. Compare proteomes of Co-IP vs Streptavidin Pulldown to label protein interactors as either stable (present in both Co-IP and Streptavidin Pulldown) or potentially transient (present in Streptavidin Pulldown only)."],"omics_type":["Proteomics"],"labhead":["Judith E. Sleeman"],"instrument_platform":[""],"labhead_affiliation":["School of Biology, University of St Andrews, BMS, North Haugh, St Andrews, KY16 9ST, UK."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["42307322 Beaumont B, Synowsky SA, Shirran SL, Sleeman JE. Investigating the interactomic landscape of survival motor neuron (SMN) and the SMNΔ7 truncated protein. Biotechniques. 2026 78(1-12):207-220 10.1080/07366205.2026.2675476"],"submitter_mail":["ss101@st-andrews.ac.uk"],"submitter_affiliation":["University of St Andrews"],"submitter_country":["United Kingdom"],"pubmed_abstract":["This protocol describes a methodology combining TurboID - a recently developed proximity biotinylation technique - with conventional epitope-tag based co-immunoprecipitation (Co-IP) to analyze protein-protein interactions (PPIs) in cell culture systems. This integrated approach allows the targeted examination of both transient and stable protein interactors, enhancing our understanding of protein dynamics. TurboID captures transient interactions often missed by Co-IP, which captures high affinity, stable interactors. Combination of both techniques enables direct comparison of interaction strengths, providing insights into the dynamic nature of protein interactions within cells. The rapid biotinylation capability of TurboID reduces background noise and false positives while Co-IP enriches stable interactors, together improving data quality and interpretation of the interactomic landscape. Demonstrating the efficacy of this methodology, proteins relevant to the pathology of Spinal Muscular Atrophy were utilized to explore variations at the interactome level. The use of identical starting cell lysates for both TurboID and Co-IP minimized variability and ensured datasets were comparable, allowing for consistency and enhancing the reliability of findings regarding the nature and strength of protein interactions. This novel framework effectively combines both innovative and classical techniques while maintaining consistency in sample handling, advancing our understanding of the intricate networks that govern cellular processes.Full data-set available at https://www.ebi.ac.uk/pride/ reference ID PXD066858."],"pubmed_title":["Investigating the interactomic landscape of survival motor neuron (SMN) and the SMNΔ7 truncated protein."],"pubmed_authors":["Beaumont Bobby B, Synowsky Silvia A SA, Shirran Sally L SL, Sleeman Judith E JE"],"additional_accession":[]},"is_claimable":false,"name":"Investigating the Interactomic Landscape of Survival Motor Neurons (SMN) and the SMN Δ7 truncated protein","description":"This protocol describes a methodology combining TurboID - a recently developed proximity biotinylation technique - with conventional epitope-tag based co-immunoprecipitation (Co-IP) to analyse protein-protein interactions (PPIs) in cell culture systems. This integrated approach allows for the targeted examination of both transient and stable protein interactors, enhancing our understanding of protein dynamics. TurboID captures transient interactions often missed by Co-IP, which captures high aCinity, stable interactors. Combination of both techniques enables direct comparison of interaction strengths, providing insights into the dynamic nature of protein interactions within cells. The rapid biotinylation capability of TurboID reduces background noise and false positives while Co- IP enriches stable interactors, together improving data quality and interpretation of the interactomic landscape. Demonstrating the eCicacy of this methodology, proteins relevant to the pathology of Spinal Muscular Atrophy were utilised to explore variations at the interactome level. The use of identical starting cell lysates for both TurboID and Co-IP minimised variability and ensured datasets were comparable, allowing for consistency and enhancing the reliability of findings regarding the nature and strength of protein interactions. This novel framework eCectively combines both innovative and classical techniques while maintaining consistency in sample handling, advancing our understanding of the intricate networks that govern cellular 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