{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065503/AFletcher_190130_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065503/AFletcher_190130_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065503/AFletcher_190130_01.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065503/txt_Maxquant_UBE2L3_ABP_AFletcher_190130_02.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065503/txt_Maxquant_UBE2D3_ABP_AFletcher_190130_04.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD065503/txt_Maxquant_No_ABP_AFletcher_190130_01.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["s.s.virdee@dundee.ac.uk"],"submitter":["Satpal Virdee"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"disease":["Acute Leukemia"],"software":[""],"submitter_keywords":["Activity-based probes","Silac"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065503"],"tissue":["Leukocyte"],"sample_protocol":["Heavy and light SILAC labelled THP-1 cells were treated with interferon alpha-1 or vehicle, respectively. Combined lysates were treated with biotinylated UBE2D3 or UBE2L3 derived E2~Ub activity-based probes ABPs. A control experiment was included where ABP was omitted. Probe labelled proteins were enriched against streptavidin beads which were then digested by trypsin. Peptides were analysed on an Orbitrap Velos mass spectrometer."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Differential signals were quantified by two channel processing (light vs.Arg10/Lys8) of the raw data file with Maxquant (version 1.6.5.0). Variable modifications included methione oxidation and N-terminal acetylation whereas carbamidomethylation of cysteine was considered a fixed modification. The human Swiss-Prot protein database (UP000005640) was searched with a peptide and protein false discovery rate of 0.01 and minimum peptide length of 7. Quantified protein groups with less than 1 unique peptide were manually excluded in the data presented in the associated manuscript."],"omics_type":["Proteomics"],"labhead":["Satpal Virdee"],"instrument_platform":[""],"labhead_affiliation":["MRC Protein phosphorylation and ubiquitylation unit, University of Dundee"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41861786 Squair DR, Rivers E, Sowar H, Balci A, Harmo R, Wright DJ, Beniwal G, Soetens M, Mathur S, Tollervey A, Wood NT, Pao KC, Stanton C, Fletcher AJ, Virdee S. ZNFX1 uses two-component ubiquitin circuitry to quarantine viral RNA. Mol Cell. 2026 86(6):1164-1181.e12 10.1016/j.molcel.2026.02.015"],"submitter_mail":["s.s.virdee@dundee.ac.uk"],"submitter_affiliation":["University of Dundee"],"submitter_country":["United Kingdom"],"pubmed_abstract":["The detection of viral RNA inside cells triggers a diverse range of antiviral responses, including global translation inhibition, interferon secretion, and RNA sequestration. Mutations in the gene zinc-finger NFX1-type containing 1 (ZNFX1) cause severe pediatric immunodeficiencies, including chronic viral infection and autoinflammation. Here, we show that ZNFX1 is an RNA helicase with cryptic and unusual bifurcating E3 ubiquitin ligase activity. Nucleotide-dependent RNA binding stimulates ZNFX1 to generate complex ubiquitin chains via a two-component ubiquitin circuit wired in parallel, with ubiquitin flux occurring via two competing paths. One route produces K63-linked polyubiquitin that drives RNA entrapment within self-propagating ZNFX1 aggregates, and the other route produces K48-linked polyubiquitin that drives ZNFX1 turnover. RNA entrapment restricts RNA virus replication and is reversible by deubiquitination. Pathogenic ZNFX1 variants are defective for viral restriction, linking RNA entrapment to antiviral immunity in vivo."],"pubmed_title":["ZNFX1 uses two-component ubiquitin circuitry to quarantine viral RNA."],"pubmed_authors":["Squair Daniel R DR, Rivers Eilidh E, Sowar Hanna H, Balci Arda A, Harmo Roosa R, Wright David J DJ, Beniwal Gaurav G, Soetens Mathieu M, Mathur Sunil S, Tollervey Aidan A, Wood Nicola T NT, Pao Kuan-Chuan KC, Stanton Callum C, Fletcher Adam J AJ, Virdee Satpal S"],"additional_accession":[]},"is_claimable":false,"name":"SILAC E3 ligase activity-based profiling of interferon-stimulated THP-1 cells","description":"Activity-based probes that covalently label proteins with transthiolating E3 ligase activity were used to determine differential changes in E3 ligase activity upon interferon stimulation of monocytic THP-1 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