Abstract It appears increasingly evident that the oligomannoside type N-glycans play important roles in the fate of newly synthesized glycoproteins in the rough endoplasmic reticulum. The variety of protein-bound oligomannoside isomers are involved in the quality control of glycoprotein, in their transport into the Golgi and probably as a degradation signal. A prerequisite of the degradation in the cytosol by the proteasome pathway is the release of the glycans as free oligomannosides. These oligomannosides are further processed in the cytosol into a peculiar isomer of Man 5GlcNAc 1which enters into the lysosome to be further degraded into monosaccharides. In this review, we will illustrate how the different species of N-linked and free oligomannosides either are involved or are markers of the quality control and fate of newly synthesized glycoproteins.