{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set1_ion.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set2_ion.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set1_peptide.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set1_psm.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set2_ion.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set2_peptide.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set2_psm.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set2_peptide.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set2_protein.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set1_protein.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set2_protein.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set1_protein.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set1_peptide.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_Set1_ion.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set2_psm.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_Set1_psm.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_annotation.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_log_2024-08-26_09-46-17.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_annotation.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_log_2024-08-26_09-29-00.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_metadata.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_metadata.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Zelda_240822_P3457_JS_BL_Myc_set1_TMT12_1out30_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Zelda_240822_P3457_JS_BL_HA_set1_TMT12_1out30_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Zelda_240822_P3457_JS_BL_Myc_set2_TMT12_1out30_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Zelda_240822_P3457_JS_BL_HA_set2_TMT12_1out30_R1.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/2024-08-26-decoys-contam-UP000005640_HomoSapiens_ID9606_20594entries_26102022_dl11012023.fasta.fas","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/UP000005640_HomoSapiens_ID9606_20594entries_26102022_dl11012023.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_fragpipe-files.fp-manifest","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_FragPipe_workflow.workflow","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/HAtag_fragpipe-files.fp-manifest","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD072359/Myctag_FragPipe_workflow.workflow"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Urszula.Mcclurg@liverpool.ac.uk"],"submitter":["Frank Stein"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Breast Cancer"],"software":[""],"submitter_keywords":["proximity labeling","Sycp1","bioid","Sycp1; bioid; proximity labeling"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072359"],"tissue":["Epithelial Cell","Cell Culture"],"sample_protocol":["Cells expressing either N-terminal Myc-tagged or C-terminal HA-tagged SYCP1 constructs were cultured under standard conditions and subjected to BioID proximity labelling. Biotinylated proteins were enriched using streptavidin-based affinity purification, and enriched protein lysates were collected for mass spectrometry analysis. Protein samples were subjected to the SP3 protocol (PMID 25358341) conducted on the KingFisher Apex™ platform (Thermo Fisher). For digestion, trypsin was used in a 1:20 ratio (protease:protein) in 50 mM N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid (HEPES) supplemented with 5 mM Tris(2-carboxyethyl)phosphine hydrochloride (TCEP) and 20 mM 2-chloroacetamide (CAA). Digestion was carried out for 5 hours at 37°C.  Peptides were labeled using TMTpro™ 16plex reagent as previously described (PMID: 31738517). Briefly, 0.5 mg of TMT reagent was dissolved in 45 µL of 100% acetonitrile. Subsequently, 4 µL of this solution was added to each peptide sample, followed by incubation at room temperature for 1 hour. The labeling reaction was quenched by adding 4 µL of a 5% aqueous hydroxylamine solution and incubating for an additional 15 minutes at room temperature. Labeled samples were then combined for multiplexing, desalted using an Oasis® HLB µElution Plate (Waters) according to the manufacturer's instructions, and dried by vacuum centrifugation. An UltiMate 3000 RSLCnano LC system (Thermo Fisher Scientific) equipped with a trapping cartridge (µ-Precolumn C18 PepMap™ 100, 300 µm i.d. × 5 mm, 5 µm particle size, 100 Å pore size; Thermo Fisher Scientific) and an analytical column (nanoEase™ M/Z HSS T3, 75 µm i.d. × 250 mm, 1.8 µm particle size, 100 Å pore size; Waters). Samples were trapped at a constant flow rate of 30 µL/min using 0.05% trifluoroacetic acid (TFA) in water for 6 minutes. After switching in-line with the analytical column, which was pre-equilibrated with solvent A (3% dimethyl sulfoxide [DMSO], 0.1% formic acid in water), the peptides were eluted at a constant flow rate of 0.3 µL/min using a gradient of increasing solvent B concentration (3% DMSO, 0.1% formic acid in acetonitrile).  Peptides were introduced into an Orbitrap Fusion™ Lumos™ Tribrid™ mass spectrometer (Thermo Fisher Scientific) via a Pico-Tip emitter (360 µm OD × 20 µm ID; 10 µm tip, CoAnn Technologies) using an applied spray voltage of 2.2 kV. The capillary temperature was maintained at 275 °C. Full MS scans were acquired in profile mode over an m/z range of 375–1,500, with a resolution of 120,000 at m/z 200 in the Orbitrap. The maximum injection time was set to 50 ms, and the AGC target limit was set to ‘standard’. The instrument was operated in data-dependent acquisition (DDA) mode, with MS/MS scans acquired in the Orbitrap at a resolution of 30,000. The maximum injection time was set to 94 ms, with an AGC target of 200%. Fragmentation was performed using higher-energy collisional dissociation (HCD) with a normalized collision energy of 34%, and MS2 spectra were acquired in profile mode. The quadrupole isolation window was set to 0.7 m/z, and dynamic exclusion was enabled with a duration of 60 seconds. Only precursor ions with charge states 2–7 were selected for fragmentation."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Raw files were converted to mzML format using MSConvert from ProteoWizard, using peak picking, 64-bit encoding and zlib compression, and filtering for the 1000 most intense peaks. Files were then searched using MSFragger (v4.0) in FragPipe (21.1) against the FASTA database of homo sapiens (UP000005640; ID9606; 20594 entries; October 2022) containing common contaminants and reversed sequences. The following modifications were included into the search parameters: Carbamidomethylation (C, 57.0215), TMTpro (K, 304.2072) as fixed modifications; Oxidation (M, 15.9949), Acetylation (protein N-terminus, 42.0106), TMTpro (peptide N-terminus, 304.2072) as variable modifications. For the full scan (MS1) a mass error tolerance of 20 PPM and for MS/MS (MS2) spectra of 20 PPM was set. For protein digestion, 'stricttrypsin' was used as protease with an allowance of maximum 2 missed cleavages requiring a minimum peptide length of 7 amino acids. The false discovery rate on peptide and protein level was set to 0.01."],"omics_type":["Proteomics"],"labhead":["Dr. Urszula McClurg"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["University Of Liverpool"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["frank.stein@embl.de"],"submitter_affiliation":["EMBL"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"BioID2 interactome of wild-type SYCP1 versus the D918–942 mutant","description":"This dataset comprises a tandem mass tag (TMT)–based quantitative proteomic analysis of proteins proximal to SYCP1 identified using BioID proximity labelling. Two independent BioID experiments were performed using distinct SYCP1 constructs: an N-terminal Myc-tagged SYCP1 and a C-terminal HA-tagged SYCP1. For each construct, full-length wild-type SYCP1, a SYCP1 deletion mutant lacking amino acids 918–942, and a SYCP1 knockout negative control were analysed in MCF7 cells. Biotinylated proteins were enriched by streptavidin-based affinity purification, and the resulting protein lysates were submitted to the EMBL Proteomics Core Facility for downstream processing and LC–MS/MS analysis, enabling quantitative comparison of SYCP1-associated proteins across constructs and 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