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Literature summary for 2.4.1.41 extracted from

  • Goth, C.K.; Tuhkanen, H.E.; Khan, H.; Lackman, J.J.; Wang, S.; Narimatsu, Y.; Hansen, L.H.; Overall, C.M.; Clausen, H.; Schjoldager, K.T.; Petaejae-Repo, U.E.
    Site-specific O-glycosylation by polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) co-regulates beta1-adrenergic receptor N-terminal cleavage (2017), J. Biol. Chem., 292, 4714-4726 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.41

Organism

Organism UniProt Comment Textmining
Homo sapiens Q10471
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5 UDP-N-acetyl-alpha-D-galactosamine + beta1-adrenergic receptor
-
 Homo sapiens 5 UDP + (N-acetyl-alpha-D-galactosaminyl)5-beta1-adrenergic receptor
-
 ?

Synonyms

Synonyms Comment Organism
GalNAc-transferase T2
-
 Homo sapiens
GALNT2
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function polypeptide GalNAc-transferase 2 specifically O-glycosylates beta1-adrenergic receptor at five residues in the extracellular N-terminus, including the Ser49 residue at the location of the common S49G single-nucleotide polymorphism. GalNAc-T2 coregulates the metalloproteinase-mediated limited proteolysis of beta1-adrenergic receptor. Impaired O-glycosylation and enhanced proteolysis lead to attenuated receptor signaling Homo sapiens