Human olfactory tract plays a fundamental role in health and disease. Proteomic analysis of the olfactory tract therefore bears fundamental importance for integrative biology and clinical medicine. For example, olfactory dysfunction is one of the earliest findings in neurodegenerative disorders. The objective of the present study was to build the proteome data from human olfactory tract using a mass spectrometry-based approach. We performed a shotgun proteomic analysis of the human olfactory tract obtained from three healthy adult male subjects. The proteomics workflow consisted of fractionation based on high pH reverse phase liquid chromatography and SDS-PAGE, followed by liquid chromatography tandem-mass spectrometry (LC-MS/MS) analysis on high-resolution mass spectrometer. In total, 6055 proteins were identified, which were further subjected to bioinformatics analysis and contextualization to identify the associated biological processes and molecular functions. We found the identified proteins involved in processes and functions related to olfactory perception, cell to cell adhesion, cellular and G-coupled receptor activity, axonal growth, and transportation. Importantly, we report the identification of 83 olfactory tract-restricted proteins, 4 seven-transmembrane proteins, and 14 protein kinases. Pathway analysis of the restricted proteins revealed the enrichment of olfactory transduction, adherens junction, taste transduction, and neurotropic signaling pathways. To the best of our knowledge, this is the first study to report the human olfactory tract proteome. The study contributes to the knowledge of the human brain proteome and forms a crucial knowledge base for future applications in basic and clinical research, especially in olfactory sensation and neurodegenerative human disorders.