{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Yanping Xu"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0019730000"],"submitter_email":["yanpingxu@tongji.edu.cn"],"submitter_affiliation":["Tongji University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"Identification of PD‑1 lysine lactylation sites by immunoprecipitation‑mass spectrometry","description":"This project aims to identify lactylation modification sites on PD‑1 protein. Lactate‑treated MOLT‑4 human T‑lymphoblastic leukemia cells were used for PD‑1 immunoprecipitation, followed by SDS‑PAGE separation and in‑gel digestion. Mass‑spectrometry analysis identified K131 and K135 as major lactylation sites of PD‑1. Further biological experiments demonstrated that AARS1 catalyzes PD‑1 K131 lactylation, which recruits deubiquitinase USP38 to stabilize PD‑1 protein, promoting CD8+ T‑cell exhaustion and tumour immune evasion. Targeting PD‑1 K131 lactylation improves anti‑tumor immunotherapy efficacy.","dates":{"publication":"Fri Sep 18 00:00:00 GMT+01:00 2026"},"accession":"PXD084400","cross_references":{"TAXONOMY":["9606"]}}