{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_2_20250215001252.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_4_20250215035802.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_1_20250214222023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/AP310125_AI_5_20250215055016.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015673.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015670.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015694.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015678.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015676.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015667.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015691.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015695.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015680.dat","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD076837/F015693.dat"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["arne.ittner@flinders.edu.au"],"submitter":["Arne Ittner"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Phosphoproteomics","Tau","Engram","Hippocampus","Fear conditioning"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD076837"],"tissue":["Brain"],"sample_protocol":["Tau protein was immunoprecipitated from hippocampal tissue extracts adjusted to a total protein concentration of 6 µg/µl. Extracts were incubated with 60 μl Pierce Anti-HA Magnetic Beads (no. 88836, Thermo Scientific) for 4 h at 4 °C with gentle rotation. Beads were washed three times with RIPA buffer for 5 min at 4 °C, followed by one rinse and one wash with 20 mM Tris‑HCl (pH 7.4), 2 mM CaCl₂, and 150 mM NaCl. To eliminate residual detergent and protease inhibitors, beads were transferred to a new tube and washed twice with the same Tris‑based buffer, followed by three washes with freshly prepared 20 mM ammonium bicarbonate containing 150 mM NaCl. Beads were then resuspended in 1× trypsin digestion buffer (V5111, Promega). On‑bead proteins were reduced with 1 mM tris(2‑carboxyethyl)phosphine (TCEP) for 10 min at 56 °C and alkylated with 10 mM iodoacetamide (I1149, Sigma‑Aldrich) for 30 min at ambient temperature in the dark. Proteolytic digestion was performed on‑bead using sequencing‑grade trypsin (V5111, Promega) at a 1:25 (w/w) enzyme‑to‑protein ratio for 16 h at 37 °C, supplemented with ProteaseMAX surfactant (V2072, Promega). Phosphopeptides were enriched using TiO₂ spin tips (GL Sciences) according to the manufacturer’s instructions. Trifluoroacetic acid (TFA) was added to the enriched samples to a final concentration of 0.1%. Peptides were desalted using tC18 cartridges (WAT036805, Waters), which were conditioned sequentially with 100% acetonitrile, 50% acetonitrile containing 0.5% acetic acid, and 0.1% TFA. After sample loading, cartridges were washed with 0.1% TFA and 0.5% acetic acid, and phosphopeptides were eluted with 80% acetonitrile containing 0.5% acetic acid. Eluted peptides were dried by vacuum centrifugation (Eppendorf) for 45 min at 45 °C and resuspended in 0.2% heptafluorobutyric acid containing 1% formic acid. Samples were stored at –80 °C until analysis. Phosphopeptides were analysed by LC‑MS/MS using an Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific) equipped with a FAIMS Pro Duo ion source and coupled to a Vanquish Neo UHPLC system (Thermo Electron). Peptides (3–6 µg injected in 1–7 µl) were first captured on a PepMap Neo C18 trap cartridge (300 µm, 5 µm; Thermo Scientific) and separated on a C18 reverse‑phase analytical column (~25 cm; ReproSil‑Pur, 1.9 µm, 200 Å; Dr. Maisch GmbH) housed in a column oven maintained at 45 °C (Sonation). Peptides were eluted over a 40‑min linear water–acetonitrile gradient containing 0.1% formic acid at a flow rate of 200 nl/min."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peak lists were generated using MASCOT Distiller and searched with the MASCOT search engine (versions v3.0.0 and v3.1.0; Matrix Science). Searches were performed against the Swiss‑Prot protein sequence database (release 19 January 2024; 570,420 sequences; 206,321,560 residues) restricted to Mammalia taxonomy.  Database searches were conducted using the MS/MS ion search type with semi‑tryptic enzyme specificity, allowing up to three missed cleavages. Carbamidomethylation of cysteine residues was specified as a fixed modification, while acetylation of asparagine, oxidation of methionine, and phosphorylation of serine, threonine, and tyrosine residues were included as variable modifications. Precursor ion mass tolerance was set to ±5 ppm and fragment ion mass tolerance to ±0.05 Da. The default Mascot minimum peptide length (7 amino acid residues) was applied."],"omics_type":["Proteomics"],"labhead":["Arne Ittner"],"instrument_platform":[""],"labhead_affiliation":["Flinders Health and Medical Research Institute, College of Medicine and Public Health, Flinders University, Adelaide, Australia"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)","Mus Musculus (mouse)"],"submitter_mail":["arne.ittner@flinders.edu.au"],"publication":["Not available"],"submitter_affiliation":["Flinders University"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"Phosphoproteomics of tau from tau knockout mice expressing tau or phospho-deficient tauT205A in active hippocampal cells upon fear conditioning","description":"This dataset describes the mass spectrometric identification of tau phosphorylation sites in hippocampal neurons active during fear memory encoding. Tau knockout (tau‑/‑) mice were used as a background to selectively express human 2N4R tau variants in behaviourally activated neuronal populations.  Tau‑/‑ mice received bilateral injections into the dorsal and ventral hippocampus with doxycycline‑regulated AAV vectors under control of the robust activity‑marking (RAM) promoter. Experimental groups expressed either wild‑type human 2N4R tau (tauWT; n = 4), a phosphorylation‑deficient tau mutant (tauT205A; n = 4), or eGFP as a negative control (n = 2). Following postoperative recovery, mice underwent fear conditioning. Hippocampal tissue was collected 120 minutes after conditioning, prior to induction of transgene expression.  Temporal control of tau, tauT205A, or eGFP expression was achieved by doxycycline withdrawal, allowing expression during a defined 20‑hour window corresponding to neuronal activity associated with fear memory encoding. Tau protein was subsequently immunoprecipitated from hippocampal lysates and subjected to bottom‑up phosphoproteomic analysis.  Immunoprecipitated tau was reduced, alkylated, and digested with trypsin, followed by enrichment of phosphopeptides using titanium dioxide (TiO₂) affinity chromatography. Enriched phosphopeptides were buffer‑exchanged, dried by vacuum centrifugation, resuspended, and analysed by liquid chromatography–tandem mass spectrometry (LC‑MS/MS). This dataset enables comparative analysis of tau phosphorylation patterns associated with neuronal activation during fear learning and provides insight into the role of the T205 phosphorylation site in activity‑dependent tau 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