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Literature summary for 2.4.1.41 extracted from

  • Shan, A.; Lu, J.; Xu, Z.; Li, X.; Xu, Y.; Li, W.; Liu, F.; Yang, F.; Sato, T.; Narimatsu, H.; Zhang, Y.
    Polypeptide N-acetylgalactosaminyltransferase 18 non-catalytically regulates the ER homeostasis and O-glycosylation (2019), Biochim. Biophys. Acta, 1863, 870-882 .
    View publication on PubMed
Search for more literature for 2.4.1.41

Protein Variants

Protein Variants Comment Organism
H253D catalytically dead Mn2+ binding site mutant Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum predominant localization Homo sapiens 5783
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q6P9A2 isoform Galnt18
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein full length GalNAc-T18 carries high-mannose N-glycan Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
A-549 cell
-
 Homo sapiens
-
PC-12 cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
GalNAc-T18
-
 Homo sapiens
Galnt18
-
 Homo sapiens
NM_001079884
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function GalNAc-T18 silencing in cells decreases O-glycosylation levels and activates ER stress leading to apoptosis. After treatment with chaperone 4-phenylbutyric acid or forced expression of GalNAc-T18 in the GalNAc-T18 knockdown cell, these defects can be significantly alleviated. GalNAc-T18 exerts its functions in O-glycosylation and ER stress via a non-catalytic mechanism. Both wild-type GalNT18 and mutant H253D show no catalytic activity in vitro, but both of them can rescue the O-glycosylation defect of GalNAc-T18 knockdown cells Homo sapiens