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protein O-[N-acetyl]-glucosylation

The most abundant type of O glycosylation in proteins is the GalNAc-type, where : CPD-3604 is linked to : SER or : THR residues in the protein chain by an alpha-glycosidic linkage. In most cases other sugars are added to this galactosamine residue, resulting in glycosidic chains of variable lengths. Among O-GalNAc glycosylated proteins, mucins are the most ubiquitous. That type of glycosylation is described in other pathways, such as : PWY-7433 and : PWY-7435. However, it has been subsequently found that in all eukaryotic systems : SER or : THR residues of some proteins are also modified with a beta-linked : CPD-12541 that is not elongated to more complex structures . This type of glycosylation is ubiquitous and abundant on nuclear and cytoskeletal proteins of virtually all eukaryotes, including protozoans and fungi . More than 400 proteins are known to be modified in this manner, including RNA polymerase II and its transcription factors, nuclear pore proteins, viral proteins, cytoskeletal proteins, tumor suppressor proteins, and oncoproteins . The O-[N-acetyl]-glucosylation is highly dynamic, with turnover rates much higher than those of the the protein backbones . In addition, the glucosylation is often associated with phosphorylation, and sometimes the phosphate groups and the NAcGlc groups occupy the same hydroxyl groups . These observations lead to the conclusion that O-[N-acetyl]-glucosylation serves a regulatory role, controlling protein phosphorylation and protein multimerization . Glycosylation generally promotes the associations with other proteins, while phosphorylation favor disassociation. The modified proteins, which are involved in regulation processes of the cell, can exhibit reciprocal O-GlcNAc glycosylation and phosphorylation during the cell cycle, cell stimulation, and/or cell growth . Glycosylation appears to be involved in mediating cytoskeletal assembly and organization . The enzyme that attaches the : CPD-12541 moiety to the proteins is : EC-2.4.1.255. Deletion of the : HS07403 gene that encodes it is lethal . The N-acetylglucosamine residues are not extended into longer structures, and are removed from the modified proteins by : EC-3.2.1.169. While there may be multiple proteins that catalyze this activity, it has been well documented as one of the activities of the : HS03036-MONOMER .

from BIOCYC source record: HUMAN_PWY-7437
Type: pathway
Taxonomic scope
:
organism-specific biosystem
Organism
:
Homo sapiens
BSID:
1108787

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