NDST1 — N-deacetylase and N-sulfotransferase 1
NDST1 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.
NDST1's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Endothelial | Basement Membrane Assembly ECM remodeling | COL15A1, COL4A1, COL4A2, HSPG2, KIFC3, MGAT4A, NOL4L, ORAI2 +4 more | View in SCUBA |
| Pericytes | BMP-SMAD Signaling Developmental | CTSH, ETS2, EXOC3L2, IL3RA, ITM2A, MCF2L, PDE2A, SCARB1 +3 more | View in SCUBA |
About the gene
| Synonyms | HSST, NST1 |
|---|---|
| Chromosome | 5: 150485818-150558211 |
| Predicted location | Intracellular, Membrane |
| Essential gene | No |
| Protein class | Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins |
| Molecular function | Hydrolase, Multifunctional enzyme, Transferase |
| Biological process | Inflammatory response |
Function
Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response (By similarity). Required for the exosomal release of SDCBP, CD63 and syndecan. Lacks both N-deacetylase and N-sulfotransferase activities. Acts as a dominant negative on isoform 1, likely by changing the composition of enzyme complexes responsible for elongation and modification of heparan sulfates
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.