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Cellulases are important glycosyl hydrolases (GHs) that hydrolyze cellulose poly-mers into smaller oligosaccharides by breaking the cellulose β (1→4) bonds,and they are widely used to produce cellulosic ethanol from the plant biomass.N-linked and O-linked glycosylations were proposed to impact the catalytic efficiency,cel-lulose binding affinity and the stability of cellulases based on observations of in-dividual cellulases.As far as we know,there has not been any systematic analysis of the distributions of N-linked and O-linked glycosylated residues in cellulases,mainly due to the limited annotations of the relevant functional domains and the glycosylated residues.We have computationally annotated the functional domains and glycosylated residues in cellulases,and conducted a systematic analysis of the distributions of the N-linked and O-linked glycosylated residues in these enzymes.Many N-linked glycosylated residues were known to be in the GH domains of cel-lulases,but they are there probably just by chance,since the GH domain usually occupies more than half of the sequence length of a cellulase.Our analysis indicates that the O-linked glycosylated residues are significantly enriched in the linker re-gions between the carbohydrate binding module (CBM) domains and GH domains of cellulases.Possible mechanisms are discussed.