{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_pep.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/Codex.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_pro.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/checksum.txt"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_.msfView","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_.msf"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_13.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_.pdResult","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_.pdStudy.bak","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_.pdStudy","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD065107/0143_.pdResultView"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["wangsa@qibebt.ac.cn"],"submitter":["Ruilin Huang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Xanthophyllomyces dendrorhous","E3 ubiquitin ligase"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065107"],"sample_protocol":["In brief, proteins were extracted from 50 h cell cultures s with Tris-saturated phenol and SDS lysis buffer containing PMSF (Beyotime, China), quantified via bicinchoninic acid (BCA) assay (Beyotime, China), then alkylated with iodoacetamide, and finally digested into peptides with trypsin. The peptides were labelled using TMT system (Thermo Fisher, USA) according to the manufacturer’s protocol.  Labeled peptides were separated using an Agilent 1100 HPLC system with an Agilent Zorbax Extend-C18 column. The mobile phase consisted of 2% acetonitrile in water (solvent A) and 90% acetonitrile in water (solvent B). A linear gradient was applied at 300 μL/min as follows: initial 98% A maintained until 8 min, decreasing to 95% A at 8.01 min, then to 75% A at 48 min, next to 60% A at 60 min, followed by a rapid ramp to 10% A at 60.01 min, which was maintained until 70 min, finally to 98% B at 70.01 with a hold until 75 min. Peptide fractions were collected from 8 to 60 min using 15 sequential centrifuge tubes, with each tube capturing eluent at one-minute intervals. All collected fractions were immediately freeze-dried under vacuum and stored at −80 °C prior to downstream LC-MS/MS analysis. Mass spectrometry analyses were performed by a Q-Exactive HF-X mass spectrometer (ThermoFisher) coupled to an EASY-nLCTM 1200 (Thermo Fisher). Peptides were loaded onto an Acclaim PepMap100 C18 trap column (100 μm × 2 cm, 5 μm particles) and separated on an Acclaim PepMap RSLC analytical column (75 μm × 15 cm, 2 μm particles). The mobile phase consisted of 0.1% formic acid in water (solvent A) and 0.1% formic acid in 80% acetonitrile (solvent B). A linear gradient was applied at 300 nL/min as follows: initial 5% B, increasing to 30% B at 40 min, then to 50% B at 54 min, followed by a rapid ramp to 100% B at 55 min, which was maintained until 60 min. Full MS scans (300 – 1600 m/z) were acquired at 70000 mass resolution and 1e6 automatic gain control (AGC). The top 10 most intense precursors in MS were fragmented with higher-energy collisional dissociation (HCD) at 32% normal collision energy (NCE). MS/MS spectra were run under positive mode, and collected at 17500 resolution, 2e5 AGC and 80 ms max injection time with 30.0 s dynamic exclusion window."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Proteome Discoverer v2.2 (Thermo Scientific) was used to search all of the raw data thoroughly against the X. dendrorhous UniProt database. Proteins with Score Sequest HT > 0, the number of unique peptides > 1, and without empty expression values were then analyzed their expression levels."],"omics_type":["Proteomics"],"labhead":["Shi'an Wang"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["1. Key Laboratory of Photoelectric Conversion and Utilization of Solar Energy, Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China. 2. Shandong Energy Institute, Qingdao 266101, China. 3. Qingdao New Energy Shandong Laboratory, Qingdao 266101, China."],"species":["Phaffia Rhodozyma"],"publication":["10.1073/PNAS.2530496123"],"submitter_mail":["huangrl@qibebt.ac.cn"],"submitter_affiliation":["Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Evolutionarily conserved E3 ubiquitin ligase modulates carotenoid, sterol and lipid crosstalk","description":"After disrupting the E3 ligase PTR1 in Xanthophyllomyces dendrorhous CBS 6938 (Xd-ptr1), we observed a quadrupling of astaxanthin production, accompanied by increased levels of ergosterol and stellasterol. This disruption also resulted in a reduction of total lipids, a shift in fatty acid composition toward polyunsaturated species, and a decrease in triglyceride levels. To elucidate the mechanism by which PTR1 regulates carotenoid, sterol, and lipid metabolism, we conducted proteomic 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