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Protein posttranslational modifications (PTMs), by covalent addition of chemical groups or peptide chains, or by proteolytic cleavage, directly alter the structure, activity, electrical charge, thermal stability, and function of immune\u2010related proteins. Here, we enumerate the main PTMs in the immune system and highlight their global regulatory roles across innate immunity, T\u2010cell\u2010mediated cellular immunity, and B\u2010cell\u2010mediated humoral immunity, including phosphorylation, ubiquitination, SUMOylation, acetylation, methylation, glycosylation, and other new types. We focus on how these modifications regulate antigen presentation and recognition, immune signal transduction, antibody production and class switching, immune contraction, immune memory establishment, as well as immune tolerance and homeostasis. Critically, dysregulation of host protein PTMs disrupts immune homeostasis, which in turn induces numerous immune\u2010related diseases, including cancer, autoimmune diseases, and infectious diseases. By integrating mechanistic insights with emerging therapeutic strategies, this review provides a comprehensive PTM network that elucidates the molecular basis of immune\u2010related diseases and highlights promising immunotherapeutic strategies targeting these modifications.<\/jats:p>","DOI":"10.1002\/mco2.70951","type":"journal-article","created":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T06:42:03Z","timestamp":1788158523000},"source":"Crossref","is-referenced-by-count":0,"title":["Protein Posttranslational Modifications in Immunity: Molecular Mechanisms and Therapeutic Targets"],"prefix":"10.1002","volume":"7","author":[{"given":"Yuxing","family":"Yao","sequence":"first","affiliation":[{"name":"School of Materia Medica Beijing University of Chinese Medicine  Beijing China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinxiu","family":"Qian","sequence":"additional","affiliation":[{"name":"School of Materia Medica Beijing University of Chinese Medicine  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