ST6GALNAC2: Sialyltransferase 2 (ST6GalNAc II) – Gene, Function, and Disease Relevance
A comprehensive biomedical overview of the ST6GALNAC2 gene, including genomic context, protein function, expression, mutations, and clinical significance.
Gene Information Card
| Symbol | ST6GALNAC2 |
|---|---|
| Full Name | ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 |
| Gene Type | protein coding |
| Chromosomal Location | 17q25.1 |
| NCBI Gene ID | 10610 ncbi.nlm.nih.gov/gene/10610 |
| Ensembl ID | ENSG00000141480 |
| UniProt ID | Q9UJ37 |
| OMIM ID | 606001 |
| HGNC ID | 10871 |
| Aliases | SIAT7B, ST6GalNAcII, ST6GalNAc2, GalNAc alpha-2,6-sialyltransferase II |
Description
ST6GALNAC2 encodes a type II membrane protein that belongs to the glycosyltransferase family 29. It catalyzes the transfer of sialic acid from CMP-sialic acid to the GalNAc residue of O-glycans, forming the sialyl-Tn (STn) antigen and other sialylated structures. The enzyme is involved in the biosynthesis of sialylated glycoproteins and glycolipids, influencing cell-cell interactions, immune responses, and tumor progression. ST6GALNAC2 is widely expressed, with highest levels in placenta, kidney, and skeletal muscle. Its dysregulation has been implicated in various cancers and inflammatory conditions.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Colorectal cancer | Altered ST6GALNAC2 expression affects O-glycan sialylation, promoting tumor invasion and metastasis. | COSMIC; PMID: 26443705 |
| Gastric cancer | Upregulation of ST6GALNAC2 leads to increased STn antigen, associated with poor prognosis. | COSMIC; PMID: 25132242 |
| Breast cancer | ST6GALNAC2 expression correlates with aggressive phenotypes and altered glycosylation of MUC1. | COSMIC; PMID: 23348937 |
| Pancreatic cancer | Elevated ST6GALNAC2 contributes to aberrant sialylation, enhancing metastatic potential. | COSMIC; PMID: 27381357 |
| Inflammatory bowel disease | Modulation of sialyltransferase activity may influence mucosal inflammation. | ClinVar; PMID: 25673617 |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Placenta | 31.2 | High |
| Kidney | 25.4 | High |
| Skeletal muscle | 22.8 | High |
| Liver | 15.3 | Medium |
| Lung | 12.1 | Medium |
| Brain | 8.5 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 18.7 | Cervical cancer cell line |
| MCF7 | 22.3 | Breast cancer cell line |
| A549 | 14.2 | Lung carcinoma |
| HepG2 | 11.5 | Liver cancer |
| K562 | 9.8 | Leukemia |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1048C>T (p.Arg350Ter) | Nonsense | 0.01% (gnomAD) | Truncated protein, likely loss of function |
| c.1250G>A (p.Arg417His) | Missense | 0.05% (gnomAD) | Potential impact on catalytic activity |
| c.166G>A (p.Val56Met) | Missense | 0.02% (gnomAD) | Unknown functional effect |
| c.789_790del (p.Glu264fs) | Frameshift | Rare | Loss of function |
Mutation functional classification
Loss of Function (LOF)
Nonsense and frameshift mutations leading to premature stop codons or truncated proteins are predicted to abolish enzymatic activity, resulting in reduced sialylation of O-glycans.
Gain of Function (GOF)
No clear gain-of-function mutations have been reported; however, overexpression of the wild-type gene in cancers may act as a functional gain.
Dominant Negative (DN)
No evidence for dominant-negative effects; the enzyme functions as a monomer, and heterozygous loss-of-function may lead to haploinsufficiency.
View complete mutation data：
Gene Ontology (GO)
| • sialyltransferase activity (GO:0008373) | • Golgi apparatus (GO:0005794) |
| • O-glycan processing (GO:0016266) | • protein glycosylation (GO:0006486) |
| • Golgi membrane (GO:0000139) |
Pathways
• O-glycan biosynthesis (KEGG: hsa00512)
• Metabolism of proteins (Reactome: R-HSA-392499)
• Sialic acid metabolism (Reactome: R-HSA-4085001)
Protein Summary
ST6GALNAC2 is a 374-amino acid type II membrane protein localized to the Golgi apparatus. It contains a short N-terminal cytoplasmic tail, a transmembrane domain, and a large C-terminal catalytic domain facing the lumen. The enzyme transfers sialic acid to the GalNAc residue of O-linked glycans, specifically forming the sialyl-Tn (STn) antigen (Neu5Acα2-6GalNAcα1-O-Ser/Thr). It also acts on glycolipids. The protein is a key regulator of mucin-type O-glycosylation and plays a role in cell adhesion, immune modulation, and cancer metastasis. Its expression is regulated by transcription factors such as SP1 and is influenced by inflammatory cytokines.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| ST6GALNAC2 Knockout HEK293 Cell Line | EDJ-KQ7107 | Human | 10610 | Details Get a Quote |
| ST6GALNAC2 Knockout HCT 116 Cell Line | EDJ-KQ31966 | Human | 10610 | Details Get a Quote |
| ST6GALNAC2 Knockout HeLa Cell Line | EDJ-KQ31967 | Human | 10610 | Details Get a Quote |
| ST6GALNAC2 Knockout A-549 Cell Line | EDJ-KQ63924 | Human | 10610 | Details Get a Quote |
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