Target intelligence / Profile preview

Polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18)

Target
GALNT18
Molecular classification
Enzyme, Glycosyltransferase
01

Overview

Polypeptide N-acetylgalactosaminyltransferase 18 (GALNT18) is a member of the GALNT family of enzymes responsible for initiating O-linked glycosylation of proteins by transferring N-acetyl-D-galactosamine (GalNAc) residues to serine or threonine residues on polypeptides[2][5][6]. This process occurs in the Golgi membrane and plays a critical role in modifying protein function and cellular signaling. GALNT18 exhibits polypeptide N-acetylgalactosaminyltransferase activity and is predicted to have carbohydrate and metal ion binding properties[3]. As of now, there are no drugs or clinical biomarkers specifically connected to GALNT18, nor are there documented safety concerns or direct disease roles. Its broader biological impact may be inferred from general roles of protein O-glycosylation in health and disease[2][5][6].

Other names
GALNT18GALNTL4GalNAc-T18GalNAc-T-like protein 4pp-GaNTase-like protein 4MGC71806GALNT15GalNAc-T15Polypeptide GalNAc transferase 18Polypeptide GalNAc transferase-like protein 4Polypeptide N-acetylgalactosaminyltransferase-like protein 4Protein-UDP acetylgalactosaminyltransferase-like protein 4UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 15UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 18UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-like 4
02

Mechanism of action

No mechanism described for drug action targeting GALNT18; general mechanism is transfer of GalNAc to polypeptides

03

Biological functions

Protein O-linked glycosylationCatalyzes the initial reaction in O-linked oligosaccharide biosynthesisCarbohydrate bindingMetal ion binding
04

Disease associations

Other (No direct disease associations described in primary sources. Enzymes in this family may be implicated in disorders of glycosylation.)

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