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Browse result for O-linked glycosylation

※ introduction

    O-linked glycosylation is the attachment of a sugar molecule to an oxygen atom in an amino acid residue in a protein. O-linked glycosylation is a form of glycosylation that occurs in the Golgi apparatus in eukaryotes. It also occurs in archaea and bacteria. The sugar molecule attached to protein includes, O-N-acetylgalactosamine (O-GalNAc), O-fucose, O-glucose, O-N-acetylglucosamine (O-GlcNAc) and O-mannose. In biology glycosylation mainly refers in particular to the enzymatic process that attaches glycans to proteins, lipids, or other organic molecules. This enzymatic process produces one of the fundamental biopolymers found in cells (along with DNA, RNA, and proteins). Glycosylation is a form of co-translational and post-translational modification. Glycans serve a variety of structural and functional roles in membrane and secreted proteins.

Reference
Wiki: O-linked glycosylation



UniProt ACEntrez IDGene NameProtein NameOrganism
O152948473
OGT
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Homo sapiens
P081741604
CD55
Complement decay-accelerating factor
Homo sapiens
P106364137
MAPT
Microtubule-associated protein tau
Homo sapiens
P319433187
HNRNPH1
Heterogeneous nuclear ribonucleoprotein H [Cleaved into: Heterogeneous nuclear ribonucleoprotein H, N-terminally processed]
Homo sapiens
Q0VAM2153020
RASGEF1B
Ras-GEF domain-containing family member 1B
Homo sapiens