GALNT6

Polypeptide N-acetylgalactosaminyltransferase 6 is an enzyme that in humans is encoded by the GALNT6 gene.^[4][5]

GALNT6
Identifiers
Aliases	GALNT6, GALNAC-T6, GalNAcT6, polypeptide N-acetylgalactosaminyltransferase 6
External IDs	OMIM: 605148; MGI: 1891640; HomoloGene: 5218; GeneCards: GALNT6; OMA:GALNT6 - orthologs
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q13.13 Start 51,351,247 bp[1] End 51,392,867 bp[1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland trachea corpus epididymis bronchial epithelial cell pylorus jejunal mucosa duodenum stromal cell of endometrium monocyte corpus callosum n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function carbohydrate binding glycosyltransferase activity metal ion binding transferase activity polypeptide N-acetylgalactosaminyltransferase activity Cellular component membrane perinuclear region of cytoplasm Golgi membrane integral component of membrane Golgi apparatus Biological process O-glycan processing protein O-linked glycosylation protein glycosylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11226 207839 Ensembl ENSG00000139629 n/a UniProt Q8NCL4 Q8C7U7 RefSeq (mRNA) NM_007210 NM_001161767 NM_001161768 NM_172451 RefSeq (protein) NP_009141 NP_001155239 NP_001155240 NP_766039 Location (UCSC) Chr 12: 51.35 – 51.39 Mb n/a PubMed search [2] [3]
Wikidata
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This gene encodes a member of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi apparatus by catalyzing the transfer of GalNAc to serine and threonine residues on target proteins. They are characterized by an N-terminal transmembrane domain, a stem region, a lumenal catalytic domain containing a GT1 motif and Gal/GalNAc transferase motif, and a C-terminal ricin/lectin-like domain. GalNAc-Ts have different, but overlapping, substrate specificities and patterns of expression. The encoded protein is capable of glycosylating fibronectin peptide in vitro and is expressed in a fibroblast cell line, indicating that it may be involved in the synthesis of oncofetal fibronectin.^[5]