The immunopeptidome comprises the suite of human leukocyte antigen (HLA)-bound peptides that are presented at the cell surface for recognition by patrolling T cells. A variety of glycosylated peptides have been shown to be presented by HLA molecules, emphasising the importance of the antigen processing pathway in continuously monitoring intracellular protein states. However, little is known about the nature or extent to which glycosylated peptides represent a yet-to-be-explored component of the immunopeptidome, in part due to technical challenges for direct characterisation of sequence and glycan. To tackle these challenges, we have developed a program for the rapid analysis and characterisation of immunoglycopeptides in mass spectrometry data by harnessing the presence of signature oxonium ions. These methods include quantifying oxonium ion intensities to differentiate between N-linked and O-linked immunoglycopeptides, determining glycan makeup by comparing mass shifts between spectral peaks, and identifying the unmodified precursor peptide (Y0 ion) fragment in order to elucidate the composition of the attached glycan mass. By employing these techniques in tandem, immunoglycopeptides can be detected and characterised accurately and quickly, with analysis being completed in minutes on datasets containing tens to hundreds of thousands of spectra. This program provides not only a valuable method for rapid immunopeptidomic and proteomic interrogation but can also serve as a basis for more tailored downstream search strategies and analysis or to inform subsequent experimental design. These capabilities make it an ideal tool for exploring novel glycosylation events in the immunopeptidome, opening a new window into cell health and antigen presentation.