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Literature summary for 2.4.1.41 extracted from

  • Simon, E.J.; Linstedt, A.D.
    Site-specific glycosylation of Ebola virus glycoprotein by human polypeptide GalNAc-transferase 1 induces cell adhesion defects (2018), J. Biol. Chem., 293, 19866-19873 .
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
medicine isoform GalNAc-T1 is largely required for the Ebola virus surface glycoprotein-mediated adhesion defects. Despite its profound effect on surface glycoprotein function, the absence of GalNAc-T1 only modestly reduces the O-glycan mass of surface glycoprotein. A small segment of the mucin-like domain of the surface glycoprotein is critical for function and mutation of five glycan acceptor sites within this segment are sufficient to abrogate surface glycoprotein function Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q10472 isoform GalNAc-T1
-

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293 cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
GalNAc-T1
-
 Homo sapiens
GALNT1
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function isoform GalNAc-T1 is largely required for the Ebola virus surface glycoprotein-mediated adhesion defects. Despite its profound effect on surface glycoprotein function, the absence of GalNAc-T1 only modestly reduces the O-glycan mass of surface glycoprotein. A small segment of the mucin-like domain of the surface glycoprotein is critical for function and mutation of five glycan acceptor sites within this segment are sufficient to abrogate surface glycoprotein function Homo sapiens