{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Shisheng Sun"],"species":["Mus Musculus"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0011732000"],"submitter_email":["suns@nwu.edu.cn"],"submitter_affiliation":["Northwest University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["The mouse is a key model in biomedical research, yet its tissue-specific glycoproteome remains incompletely characterized due to glycan complexity and microheterogeneity. Here, we present a comprehensive N-glycoproteomic atlas across 24 mouse tissues, comprising 3045 N-glycans with distinct structural features attached at 8681 glycosites on 74,277 glycopeptides and 5026 glycoproteins. Among these glycans, 2687 (88.2%) meet the high-confidence threshold through an integrative confidence-estimation framework. Overall glycan structural patterns show enormous tissue-specific diversities, acting as superior molecular signatures of tissue identity and system origins. Notably, even commonly expressed glycoproteins undergo tissue-dependent glycan remodeling, suggesting that glycosylation may fine-tune protein functions to meet specialized biological demands. These patterns are further shaped by subcellular localization, which constrains glycan variabilities across compartments. Co-occurrence network analyses also expose substructural biases and non-random microheterogeneities among glycans attached at the same glycosites. The dataset serves as a valuable database resource for advancing the structural and functional understanding of glycoproteins."],"pubmed_title":["A comprehensive N-glycoproteome atlas reveals tissue-specific glycan remodeling but non-random structural microheterogeneities."],"pubmed_authors":["Wu Yongqi Y, Yang Muyao M, Xu Yongchao Y, Jia Li L, Li Jun J, Wang Xiaohan X, Zhao Jiayu J, Cai Yinli Y, Zhang Yiwen Y, Sun Shisheng S"],"additional_accession":[]},"is_claimable":false,"name":"A Tissue-Specific Atlas of Mouse N-Glycoproteome","description":"In this study, we employed StrucGP to generate the first high-resolution and site-specific N- glycoproteomic atlas across 24 diverse mouse tissues. This comprehensive dataset provides an unprecedented insight into the tissue-specific landscape of N-glycosylation, revealing how distinct glycan structures and site-specific modifications contribute to tissue identity and specialization.","dates":{"publication":"Wed May 07 00:00:00 BST 2025"},"accession":"PXD063701","cross_references":{"TAXONOMY":["10090"],"pubmed":["41530124"]}}