{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/CombineAnnotation--Z.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/CombineAnnotation--M.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/CombineAnnotation--J.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kj2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mj1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mz2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mj2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mm2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mk5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_km10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mk1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kz1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kz2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mz1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kj10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mm3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mj3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mk2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mj4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kz5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mz4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mm4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kj5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kz10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_kj1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mm1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD064647/ace_mz3.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["guoyajing0817@163.com"],"submitter":["Tao Li"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Crohn's Disease"],"software":[""],"submitter_keywords":["Signaling pathways","Crohn","Immune response","Protein acetylation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064647"],"tissue":["Intestine"],"sample_protocol":["Two-month-old male NOD2 rats were used to prepare animal models of CD with reference to the internationally recognized Morris method. Two rats were randomly selected from each group, and the rats were cut off their necks under anesthesia, and the tissue damage of the modeled rats was scored by taking the intestines, and the intestinal tissues of the normal rats were compared to evaluate the success of the CD model. After one week of acclimatization, 24 rats were randomly divided into two groups for experiments: normal control group (n=12); In the model group (n=12,), all rats were euthanized by cervical dislocation under ether anesthesia, and intestinal tissue samples from different parts were collected for subsequent analysis. Frozen rat intestinal tissue is homogenized in lysis buffer containing 1% acetylase inhibitor to extract total tissue protein. The Bradford (Beyotime) method was used to determine the protein concentration. The sample containing 1 mg of protein was incubated with 10 mM DTT at room temperature for 30 min, the protein disulfide bond was reduced, the alkylation was incubated at room temperature at 25 mM IAM, trypsin was added overnight at 37°C for enzymatic hydrolysis, and then trypsin was added for secondary enzymatic hydrolysis according to the mass ratio. The digest was acidified by formic acid and desalted using an HLB solid-phase extraction column. Samples were fractionated using an LC-15AC chromatograph with a high pH C18RP column. Add loading buffer using Anti-Diglycine Lysine magnetic beads and mix well with the sample to be enriched, and incubate for 20 minutes at room temperature. After incubation, retain the supernatant for later use. The acetyl peptide was eluted with 5% NH4OH, washed and incubated with 0.1 M FeCl3/6% acetic acid in rotation. Add buffer to prepare a 50% slurry. Resuspend the dried peptide in the slurry at a concentration of 1 μg/μl and incubate with vigorous shaking. After incubation, leave the supernatant for later use. The Anti-Diglycine Lysine-enriched eluate was mixed and vacuum freeze-dried for mass spectrometry analysis after desalting."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The purified peptides were re-dissolved and analyzed by LC-MS/MS using the Ultimate 3000 RSLCnano System (Thermo Fisher Scientific), which was connected in-line to a Q Exactive HF Mass Spectrometer (Thermo Fisher Scientific) equipped with a Nanospray Flex ion source (Thermo Fisher Scientific). Samples were loaded onto a 150 mm analytical column (homemade, 75 μm I.D., 3 μm C18 Reprosil-HD resisin, Dr. Maisch). Peptides were eluted by a nonlinear solvent gradient with a 70-minute increase in the ratio of solvent B (0.1% formic acid in water/acetonitrile (2:8, v/v)) from 2% to 56% at a constant flow rate of 300 nl/min, followed by a 20-minute rinse of 99% solvent B and re-equilibration to solvent A (0.1% formic acid in water/acetonitrile (2:8, v/v)). The mass spectrometer uses a data-dependent acquisition mode that automatically switches between MS and MS/MS scans, capturing 16 of the strongest ion peaks per MS spectrum. Full-scan MS spectra (400-1800 m/z) were acquired in the Orbitrap analyzer at 60,000 resolution with a cumulative target value of 3×10⁶. MS/MS spectra (100-2000 m/z) were acquired in the Orbitrap analyzer at 15,000 resolution. Data analysis was performed using MaxQuant Software (version 2.0.3.1) with the Andromeda search engine, using default search parameter settings, including a 5% false positive rate for peptide and protein levels. Mass spectrometry data were indexed against rat proteins in the UniProt/Swiss-Prot database. The mass tolerances for precursor and fragment ions in the main search phase were set to 6 ppm and 20 ppm, respectively. The digestion specificity was set to C-terminal cleavage of lysine, and the maximum missed cleavage sites were 2. Aminoacetylation (K) of lysine is set as a fixed modification. The inter-run matching function is enabled, and the matching time window is set to 1 minute and the alignment time window is set to 20 minutes. Use WebLogo (https://weblogo.berkeley.edu/) to analyze and visualize the amino acid sequence around the Kac site. A sequence window containing 11 amino acids around the Kac site was constructed. The pLogo (https://plogo.uconn.edu/)33 tool was used to identify statistically overexpressed Kac motifs in identified Kac loci. The sequence windows containing 6 amino acids upstream and downstream of the Kac site were extracted from the database and submitted to the Motif-X platform for Kac motif extraction."],"omics_type":["Proteomics"],"labhead":["Yajing Guo"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Henan University of Chinese Medicine"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["litao@mass-hub.com"],"submitter_affiliation":["17765116266"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Differences in protein acetylation in different parts of Crohn's gut","description":"Lysine acetylation is a rich post-translational modification in prokaryotes that regulates multiple immune response pathways, and its importance has been overlooked. Crohn's disease is a subtype of inflammatory bowel disease characterized by chronic inflammation involving the entire gastrointestinal tract. CD-induced intestinal damage and subsequent disability is a growing global health problem. However, the pathophysiology of this disease is not fully understood, and the level of protein acetylation in Crohn's gut tissue is not well understood.To determine the level of protein acetylation in different intestinal sites of CD and changes in intestinal immune response after colonic protein acetylation. Colon, cecum, and rectal tissues of Crohn's disease and healthy control mice were detected by acetylation proteomics. ResultsThe analysis determined that there were up to 624 acetylated proteins and 1809 acetylation sites in intestinal tissue, which were different in the disease and control groups, and the acetylated proteins were enriched in immunomodulatory signaling pathways such as NF-κB, MAPK, and 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