AXL, a receptor tyrosine kinase implicated in tumor progression, undergoes post-translational modifications that regulate its activity and stability. In this study, we have analyzed AXL immunoprecipitated from cell lines by liquid chromatography–tandem mass spectrometry (LC-MS/MS)-based glycoproteomics and show that AXL is extensively N-glycosylated in breast and ovarian cancer cells, existing predominantly as two isoforms corresponding to high-mannose and complex-type glycans. The extracellular cleaved soluble form of AXL (sAXL) primarily carries complex N-glycans. LC-MS/MS–based glycoproteomics analysis identified five glycosylation sites (Asn43, Asn157, Asn198, Asn339, and Asn345) with extensive microheterogeneity, including sialylation, fucosylation, and bisecting GlcNAc modifications. Overall, our results demonstrate that N-glycosylation is essential for AXL stability, localization, and oncogenic signaling, offering new insights into how glycosylation regulates receptor tyrosine kinases function in cancer.