Literature summary for 2.4.1.41 extracted from

Lackman, J.J.; Goth, C.K.; Halim, A.; Vakhrushev, S.Y.; Clausen, H.; Petaejae-Repo, U.E.
Site-specific O-glycosylation of N-terminal serine residues by polypeptide GalNAc-transferase 2 modulates human delta-opioid receptor turnover at the plasma membrane (2018), Cell. Signal., 42, 184-193 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q10471	isoform GalNAc-T2	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
GalNAc-T2	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	isoform GalNAc-T2 is the specific regulator of O-glycosylation of Ser6, Ser25 and Ser29 in the N-terminal ectodomain of the receptor. Single-nucleotide polymorphism F27C of the receptor alters O-glycosylation of the receptor in efficiency as well as in glycosite usage. The absence of O-glycans results in decreased receptor levels at the plasma membrane due to enhanced turnover. Mutation of the identified O-glycosylation sites leads to a decrease in the number of ligand binding competent receptors and impaired agonist-mediated inhibition of cyclic AMP accumulation in HEK-293 cells	Homo sapiens

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Release 2023.1 (January 2023)