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Polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6)
- Target
- GALNT6
- Molecular classification
- Enzyme, Glycosyltransferase (specifically, glycosyltransferase 2 family, GalNAc-T subfamily), Protein modifier (catalyzes post-translational protein modification via glycosylation)
01
Overview
Polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6) is a member of the glycosyltransferase 2 family and the GalNAc-T subfamily. It catalyzes the first step in mucin-type O-linked glycosylation in the Golgi apparatus by transferring N-acetylgalactosamine to serine and threonine residues on proteins. GALNT6 plays roles in normal tissue glycosylation and has been implicated in cancer biology through the modification of proteins such as fibronectin, MUC1A, MUC2, EA2, and FGF23. Aberrant expression or activity of GALNT6 alters glycoprotein profiles and may contribute to oncogenic transformation and tumor progression. Its main molecular domains include an N-terminal transmembrane region, a catalytic domain with GT1 and Gal/GalNAc transferase motifs, and a C-terminal ricin-like lectin domain that confers glycopeptide specificity
- Other names
- GalNAc-T6Polypeptide GalNAc transferase 6UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 6UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6pp-GaNTase 6GALT6 (less used)
02
Mechanism of action
Inhibition of GALNT6 would block mucin-type O-linked glycosylation initiation, potentially affecting glycoprotein maturation and cell surface properties, which may influence tumor growth and metastasis
03
Biological functions
Initiation of mucin-type O-linked glycosylationProtein modification (attachment of GalNAc sugars to polypeptides)Synthesis of oncofetal fibronectinGlycosylation of fibronectin, MUC1A, MUC2, EA2 peptides, and FGF23May impact cell-cell communication and tumor progression (via glycosylation changes)
04
Disease associations
Cancer (especially luminal breast carcinoma A)Oncology relevance (through aberrant glycosylation)Potential implication in other processes where O-glycosylation is altered
05
Safety considerations
Risk of off-target effects, as GALNT6 is involved in normal glycosylation processes essential for multiple tissuesPotential for altered protein function, cell adhesion, or immune recognition due to broad glycosylation changes
06
Interacting drugs
No well-characterized small molecule inhibitors or approved drugs directly targeting GALNT6 are documented in standard sources; research compounds may exist but are not widely established
1 more in the full profile.
07
Biomarkers
Expression of GALNT6 protein or mRNA may serve as a biomarker for certain cancers (e.g., breast cancer subtypes)Glycosylation status (altered O-linked glycoprotein expression) in tumors
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