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In an early step of N-glycoprotein biosynthesis, high-mannose type glycans are attached to nascent polypeptides in the endoplasmic reticulum. Subsequently, the glycopolypeptides adopt the correct folding conformations, after which glycans are converted to complex type glycans in the Golgi apparatus. During these processes, over 30% of nascent glycoproteins exist in either misfolded or unfolded forms, therefore proper folding of these proteins is essential for efficient N-glycoprotein biosynthesis. Furthermore, elimination of misfolded glycoproteins from the endoplasmic reticulum via cytoplasmic degradation is essential for maintenance of cellular homeostasis. Through these sorting processes, various glycan-recognizing proteins, such as glycosyltransferases, glycosidases, and lectins, contribute to the conversion of nascent glycoproteins into a variety of glycoforms. Some glycans are believed to be signals for the folding, secretion, and degradation of glycoproteins that are partially folded, correctly folded, and misfolded, respectively. Since targets of the glycan-recognizing proteins are diverse within the body, some of the lectin and glycan processing enzymes may be bifunctional, characterised by dual recognition of both glycan and aglycone moieties. In fact, uridine 5’-diphosphate glucose: glycoprotein glucosyltransferase, which localises in the endoplasmic reticulum, has been known to have both, glucose transfer activity and the ability to sense improperly folded proteins. Similar dual recognition properties have been reported, particularly in glycan-recognizing proteins, with regards to glycoprotein folding, sorting, and degradation processes. However, there have not been any review articles highlighting the bifunctionality of glycan-recognizing proteins thus far. In this review, we summarise several examples of the bifunctionality of glycan-recognizing proteins involved in N-glycoprotein biosynthesis.