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EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein - 31018, 31029
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein 30% Asp-linked carbohydrates, no glycolipid anchor 31023
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein 30% oligosaccharides 31026
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein about 18% carbohydrates, mostly N-linked sugars 31019
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein complex-type glycosylation -, 31024
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein highly glycosylated -, 31021
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein nine out of ten potential glycoslytation sites are glycosylated. Removal of two glycans at N234 and N270, as well as removal of glycan at N452, decrease the chemical and thermal stability of the homooligomer without affecting quarternary structure 669507
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein no sialic acid -, 31031
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18glycoprotein the enzyme is highly glycosylated -, 733947
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.18proteolytic modification activation of recombinant zymogen enzyme by trypsin -, 734296
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