ST6GALNAC3 — ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 3
ST6GALNAC3 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
ST6GALNAC3's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Lymphatic endothelial | Polarized Vesicle Trafficking migration & adhesion | ELMO1, EXOC4, EXOC6B, IMMP2L, L3MBTL4, LRBA, LRMDA, MYO9A +5 more | View in SCUBA |
| Neutrophils | Cytoskeletal Remodeling Cytoskeletal | ARB2A, ASAP1, ATXN1, GTDC1, HDAC4, MTMR3, NFAT5, SVIL +2 more |
About the gene
| Synonyms | SIAT7C |
|---|---|
| Chromosome | 1: 76074746-76634603 |
| Predicted location | Intracellular, Membrane |
| Essential gene | No |
| Protein class | Enzymes, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins |
| Molecular function | Glycosyltransferase, Transferase |
| Biological process | Lipid metabolism |
Function
Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal- beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.