{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/combined_protein.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/combined_peptide.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/2025_Sample_annotation.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/ARID5B_prot_norm_imputed.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-1_uncalibrated.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-3_uncalibrated.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-1_uncalibrated.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-2_uncalibrated.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-2_uncalibrated.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-3_uncalibrated.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-3.raw"],"Pepxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-3.pepXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-2.pepXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-ARID5B-long-rep-1.pepXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-3.pepXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-1.pepXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/CC_154_HEK-BirA-2.pepXML"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061867/2025-02-06-decoys-contam-uniprotkb_AND_reviewed_true_AND_model_o_2025_02_06.fasta.fas"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["davide.seruggia@ccri.at"],"submitter":["Fabian Frommelt"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Transcriptional repressor complex","Avitag"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD061867"],"tissue":["Kidney Cell"],"sample_protocol":["The murine Arid5b ORF with 5’ N-terminus AviTag and FLAG was synthesized (IDT) and cloned into a lentivector under the EF1a promoter using Gibson Assembly Master Mix (NEB). HEK293T cells constitutively expressing the E.Coli Biotin ligase BirA were transduced with the ARID5B lentivector and selected with Puromycin for 5 days. One-step affinity purification with streptavidin-beads was performed as previously reported (Kim, J. 2009). In brief, nuclear extracts were obtained from approximately 300 million cells using NE-PER Nuclear and Cytoplasmic Extraction Reagents (Thermo Fisher Scientific, #78833) and quantified using the Pierce BCA Protein Assay Kit (Thermo Fisher Scientific, #23225). 5 mg of nuclear extract from HEK293T cells either expressing only BirA (control) or BirA plus biotin-tagged ARID5B were diluted in 10 ml of IP350 buffer (20 mM Tris-HCl (pH 7.5), 0.3% NP-40, 1 mM EDTA, 10% glycerol, 350mM NaCl, 1 mM DTT, 0.2 mM PMSF) supplemented with a Protease Inhibitor Cocktail (Sigma Aldrich, #P8340-5, 1:100). 100 ul Dybabeads MyOne Streptavidin T1 beads (Thermo Fisher Scientific) were added and incubated with rotation overnight at 4°C. Beads were washed four times with 10 ml of IP350 buffer and eluted in 250 µl Buffer II (50mM HEPES (pH 8.0), 150mM NaCl, 5mM EDTA, 2%SDS).  Samples were diluted to equal amounts in lysis buffer (2% SDS, 50 mM HEPES, pH 8, supplemented with 1 mM PMSF and protease inhibitors) up to 100 µL. Next DTT (final concentration of 10 mM DTT) was added, and samples were incubated for 1 h at 56°C. After reduction, cysteine residues were treated with IAA (final concentration of approximately 50 mM) and incubated in the dark for 30 min at room temperature. To each sample 8 µL washed and equilibrated magnetic SP3 beads (SpeedBeads, GE Healthcare) were added, and proteins were precipitated by the addition of Acetonitrile (final concentration of 70% v/v). The samples were incubated for 18 minutes before the beads were immobilized for 2 min and the supernatant was removed. Beads were rinsed twice with 70% (v/v) ethanol, followed by a wash in acetonitrile (ACN). After the final washing step, 100 µL of 50 mM Ammonium-bicarbonate (NH4HCO3) was added to the beads, and proteins were digested by the addition of 1.5 µg of sequencing grade trypsin. Samples were incubated on the shaker with low agitation speed overnight (~ 12 h) at 37 °C. Next, samples were acidified to pH 2-3 with 30% TFA and cleaned up by STAGE-tip C18.  MS-data were acquired on an Orbitrap Fusion Lumos Tribrid mass spectrometer coupled to a Dionex Ultimate 3000 RSLCnano system via a Nanospray Flex Ion Source interface. Peptides were loaded onto the trap column (PepMap 100 C18, 5 µm, 5 × 0.3 mm) and subsequently eluted onto the analytical column (50 cm, 75 mm inner diameter analytical column inhouse packed with ReproSil-Pur 120 C18-AQ, 3 mm, with an ESI emitter (20 µm ID x 7 cm L x 365 µm OD; Orifice ID: 10 µm, CoAnn Technologies) kept at 50°C. A 120 min analytical gradient with 230 nL/min flow rate was used, using as buffer A 0.4% FA in H2O, and as buffer B 0.4% FA in ACN. The gradient had the following scheme: scheme: 0-4 min 4% buffer B, 4-86 min to 24% B, 86-94 to 36% B, 94-95 min increase to 100% B and 101-102 back to 4% B. The MS was operated in positive mode using a data dependent acquisition (DDA) mode with a 3 sec cycle time. The MS1 scan range was set from 375 – 1650 m/z, and the dynamic exclusion was set to 60 seconds with a mass tolerance of 10 ppm. MS1 spectra were recorded in the Orbitrap at a resolution of 120,000, with a maximum injection time of 80 ms and an AGC target value of 2e5. Only peptide precursor charge stages of 2 to 6 were selected for fragmentation. MS2 fragment spectra were recorded at resolution of 15,000 with an automatic gain control target intensity of 5e4. Fragmentation was achieved with higher energy collision energy (HCD) at 30%. The maximum injection time was limited to 100 ms. The isolation width was set to 1.6 m/z and fragments were recorded from 120 – 2000 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS raw files were processed using FragPipe (version 22.0) and MSFragger (version 4.1) (Kong et al., 2017) with the label-free quantification with match-between-runs (LFQ-MBR) workflow. The peptide identification search was conducted against the human protein database downloaded from UniProtKB (consensus sequences, only reviewed, 02/06/2025), which included decoy sequences (reversed protein sequences) and common lab contaminants (e.g., rubber, bovine serum albumin, sheep wool). The default search engine settings of the LFQ-MBR workflow were used for the FragPipe analysis. Briefly, a closed search with the setting “strict trypsin” specificity, N-terminal methionine clipping, and up to two missed cleavages was performed. Up to three variable modifications were allowed, including oxidation on methionine, N-terminal acetylation, and carbamidomethylation of cysteine residues as a static modification. Peptide lengths were set to a minimum of 7 and a maximum of 50 amino acids. MSBooster was enabled, and Percolator was used for PSM validation. ProteinProphet controlled the protein FDR at 0.01. Quantification was performed with IonQuant (Yu et al., 2020) using LFQ with MBR enabled, with advanced options set to default. The peptide-level outputs from FragPipe were further analyzed to determine protein abundance and perform differential analysis using R (version 4.4.1). The raw peptide intensities from each MS-injection were normalized based on the total peptide signal and scaled to the median total signal. Peptides which were sparsely identified peptides in less than three samples were excluded from the dataset. Subsequently, the peptides for each protein were summed and ranked across the entire experiment. The six highest abundant peptides (TOP6) were used to infer protein abundances for each sample. If fewer than six peptides were quantified, the protein abundance was inferred from the remaining peptides. The mean signal of the peptides was used for protein abundance inference. Protein intensities were then log2 transformed, and missing values were imputed by sampling from a normal distribution centered around the lowest 5% quantile of all intensity values. Proteins for which more than 50% of the quantities were imputed were excluded from further analysis. Common lab contaminants (e.g., sheep wool) were also removed. Finally, the log2FC was calculated using the average signal quantified in ARID5B samples compared to the BirA negative controls. To assess enrichment of interaction partners, we applied a linear model to each protein using the limma package (Ritchie et al., 2015). The model estimated the coefficients for each protein, with contrasts between ARID5B and BirA negative controls fitted using empirical Bayes moderation. The resulting statistics were adjusted for multiple testing using the Benjamini-Hochberg method. All proteins with a log2FC larger or equal to 2 and an adjusted p-value of smaller or equal to 0.05 were categorized as interaction partners."],"omics_type":["Proteomics"],"labhead":["Davide Seruggia"],"instrument_platform":[""],"labhead_affiliation":["St. Anna Children's Cancer Research Institute (CCRI), Vienna, Austria; CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Vienna, Austria."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["fabian.frommelt@hotmail.com"],"publication":["Not available"],"submitter_affiliation":["CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"Defining the interactome of ARID5B by AviTag protein pull-down coupled to quantitative mass spectrometry.","description":"Among the strongest associations with pediatric B-cell acute lymphoblastic leukemia (B-ALL) are risk non-coding variants localized in the intron of ARID5B (AT-rich interaction domain 5B), a poorly characterized DNA-binding protein. In this study, we defined the interactome of ARID5B by LC-MS/MS and identified transcriptional repressors HDAC1, HDAC2, MIER1 and C16ORF87 as interactors. Structural predictions revealed that ARID5B and its interactors assemble into a repressor complex. We further validated and characterized the molecular function of the ARID5B repressor complex in B 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