{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Final_main_output.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_HOW_01_01.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_BSK_02_01.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_BSK_03_01.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_BSK_01_01.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_HOW_03_01.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_HOW_02_01.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_HOW_02_01.raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_HOW_01_01.raw.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_BSK_01_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_BSK_02_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_BSK_03_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_Ecl01_Karl_DIA_TRAP_50cm_120min_HOW_03_01.raw.zip"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD070902/24254_FASTA_prep_drosphila.pipeline"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["j.aspden@leeds.ac.uk"],"submitter":["Julie Aspden"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["How(s)","Drosophila"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070902"],"tissue":["Early Embryonic Cell"],"sample_protocol":["S-TRAPTM Digestion Complex cell lysates suspended in sample buffer and then subjected to S-TRAPTM digestion, as per the instructions (PROTIFI, NY, USA). Briefly, Samples were initially reduced and alkylated using 20mM DTT for 10minutes and 40mM IAA for 30minutes respectively followed by acidification of samples using 5.5% phosphoric acid. Acidified samples were then trapped on S-TRAP columns after the addition of sample buffer (100mM TEAB in 90% methanol) and 1µg trypsin. Followed by washing with sample buffer, S-TRAP is covered with trypsin and incubated at 47˚C for one and half hour. Eluted peptides were concentrated in the speedvac concentrator and reconstituted in 0.1% FA.   LC-MS analysis of peptides LC-MS/MS analyses of peptide mixtures were done using Vanquish Neo UHPLC system connected to Orbitrap Eclipse Tribrid mass spectrometer (Thermo Fisher Scientific). Prior to LC separation, tryptic digests were online concentrated and desalted using a trapping column (300 μm × 5 mm, μPrecolumn, 5μm particles, Acclaim PepMap100 C18, Thermo Fisher Scientific) at room temperature. After washing of trapping column with 0.1 % formic acid (FA), the peptides were eluted (flow rate – 0.25 nl/min) from the trapping column onto an analytical column (EASY spray column, Acclaim Pepmap100 C18, 2µm particles, 75 μm × 500 mm, Thermo Fisher Scientific) at 45 ºC by a 120 min linear gradient program (2-50 % of mobile phase B; mobile phase A: 0.1 % FA in water; mobile phase B: 0.1 % FA in 80 % ACN). Equilibration of the trapping column and the analytical column was done prior to sample injection to the sample loop. The analytical column with the emitter was directly connected to the ion source. MS data were acquired in a data-independent strategy (DIA). The survey scan range was set to m/z 400-1000 with the resolution of 60,000 (at m/z 200)   with a standard target value and maximum injection time of 100 ms. HCD MS/MS (30% normalized fragmentation energy) spectra were acquired for maximum injection time of 55 ms and resolution of 15 000 (at m/z 200). The isolation window was set to 15 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometry data analysis The mass spectrometric RAW data files were analyzed using DIA-NN 1.8.1 software. Spectral library was initially generated using cRAP database containing protein contaminants like keratin, trypsin, etc., and UniProtKB protein database for Drosophila melanogaster (taxon: 7227; downloaded 05.2024, version 2024/05, number of protein sequences: 3738). Oxidation of methionine, deamidation (N, Q) and acetylation (protein N-terminus) as optional modification and carbamidomethyl on cysteine as static modification were used. Trypsin (full) enzyme with 2 allowed miss cleavages were set. Mass spectra were searched using precursor ion tolerance 10 ppm and fragment ion tolerance 0.02 Da. Peptides and proteins FDR threshold set to <0.01 and proteins with at least one peptide were taken for further analysis.  Output from the DIA-NN software was further processed using the KNIME software container environment (https://github.com/OmicsWorkflows), version 4.7.7a. Processing workflow is available upon request. Briefly, it covered: a) removal of decoy hits and contaminant protein groups, b) protein group intensities log2 transformation, c) LoessF normalization, and d) differential expression using LIMMA statistical test.  All analysis performed with R v4.4.0. Before any filtering – checks were done to check for RNAi off target effects – The RNAi sequence, including reversing the sequence, complement of the sequence, and reverse complement of the sequence was obtained. All possible transcripts associated with the proteins identified in mass-spec before any filtering were obtained (no pADJ and no LFC filtering performed). Pairwise alignments were performed between the resulting transcripts and the RNAi sequence(s) to look for any off-target effects, while allowing for incomplete alignment (local alignments, global alignments and short indels allowed). No successful alignments determined. Also checked the RNAi sequence against full transcript DB, to ensure nothing missed.   Identification of motifs in Mass Spectrometry hits  The resulting mass-spec data was filtered with a pADJ < 0.05 and absolute log2 fold change of > 1. The remaining identified proteins of interest were mapped to their appropriate transcript IDs with the BioConductor R package AnnotationDbi (Pagès, Carlson et al. 2024) and the genome annotation for fly database. In the case of a protein mapping to multiple transcript IDs, the transcript consisting of the longest 5’ UTR was retained. Both the 5’ UTR and 3’ UTR sequences for all identified transcripts were obtained using the genome fly annotation. DREME from the meme-suite was used on the obtained UTRs with the following flags: -norc, -rna, -m 25 (Bailey, Johnson et al. 2015, Carlson 2019)."],"omics_type":["Proteomics"],"labhead":["Julie Aspden"],"instrument_platform":[""],"labhead_affiliation":["School of Molecular and Cellular Biology, University of Leeds"],"submission_type":["PARTIAL"],"species":["Drosophila Melanogaster (fruit Fly)"],"submitter_mail":["j.aspden@leeds.ac.uk"],"publication":["41526452 Agapiou M, Norris K, Hopes T, Ward E, Hobor F, Bretman A, Edwards TA, Aspden JL. Held out wings RNA binding activity in the cytoplasm during early spermatogenesis. Commun Biol. 2026 10.1038/s42003-025-09435-4"],"submitter_affiliation":["University of Leeds"],"submitter_country":["United Kingdom"],"pubmed_abstract":["Held out wings (HOW) is an RNA-binding protein essential for spermatogenesis in Drosophila melanogaster. HOW is a signal transduction and activation of RNA (STAR) protein, regulating post-transcriptional gene expression. The characteristics of RNA-binding by the conserved short cytoplasmic isoform, HOW(S), are unknown. In vivo RIP-seq identified 121 novel transcripts bound by HOW(S) in germ stem cells and spermatogonia, many with signal transduction functions. (A/G/U)CUAAC motifs were enriched in 3'-UTRs and GCG(A/U)G in 5'-UTRs. HOW binds with high affinity to sites containing CUAAC motifs from lola and hipk mRNAs. The binding of cytoplasmic HOW(S) specifically to CUAAC motifs in 3'-UTRs can result in stabilization or destabilization of mRNAs and translational regulation potentially depending on position of binding, number of sites and interacting partners. This study provides new insight into STAR protein-RNA interactions and functions in spermatogenesis."],"pubmed_title":["Held out wings RNA binding activity in the cytoplasm during early spermatogenesis."],"pubmed_authors":["Agapiou Michaela M, Norris Karl K, Hopes Tayah T, Ward Eilidh E, Hobor Fruzsina F, Bretman Amanda A, Edwards Thomas A TA, Aspden Julie L JL"],"additional_accession":[]},"is_claimable":false,"name":"HOW(S) RNAi in Drosophila S2 sells followed by proteomics","description":"Proteomic analysis of S2 cells subjected to RNAi with either HOW(S) specific RNAi duplex or non-specific 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