“…Furthermore, the extremely limited types of glycan structures on glycoproteins and relatively glycoprotein-specific glycosylation, such as observed for alpha-dystroglycan, N-CAM, PSGL-1, collagens, glycogenin, pituitary hormones, membrane transporters such as the erythrocyte band 3 anion exchanger, and the dozen or so proteoglycans, along with Skp1 in slime molds, may represent more of the normal situation, rather than the exception, in animal cell glycoconjugates. Rare and unusual forms of protein glycosylation are being found at a rapid pace (Lafite and Daniellou 2012) and 9 of the 20 amino acids are known to be glycosylated (Cummings and Pierce 2014), similar to what is known for protein phosphorylation. Thus, new perspectives and paradigms are needed and will undoubtedly arise as the field continues its ascension.…”