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A comprehensive landscape of human organ N-glycoproteome

ABSTRACT: N-glycosylation, as a common post-translational modification with enormous structures, plays key roles in protein folding, cellular recognition and signaling pathways. State-of-the-art mass spectrometry-based N-glycoproteomics has enabled deep N-glycoproteome characterization of various human organs. However, a comprehensive N-glycoproteome landscape of human organs remains lacking. Here we present a systematic human N-glycoproteome atlas spanning 18 organs/tissues with identification of 31,003 intact N-glycopeptides, corresponding to 14,043 N-glycan monosaccharide compositions on 5,539 N-glycosites of 3,681 N-glycoproteins. Tissue-specific glycosylation patterns, novel glycoforms and crosstalk between sialylation and fucosylation are observed. This atlas, complemented by a unified multi-software analysis framework, provides insights into organ-specific glycobiology and establishes a fundamental reference for understanding physiological glycosylation characteristics of human tissues.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Whole Body

SUBMITTER: hu xiaoyu

LAB HEAD: Zhixin Tian

PROVIDER: PXD070547 | Pride | 2026-05-13

REPOSITORIES: Pride

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			Action	DRS
	Adrenal_gland1_TR1_240615.raw	Raw
	Adrenal_gland1_TR2_240615.raw	Raw
	Adrenal_gland1_TR3_240615.raw	Raw
	Adrenal_gland2_TR1_250705.raw	Raw
	Adrenal_gland2_TR2_250706.raw	Raw

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