HEXB — Hexosaminidase subunit beta
HEXB belongs to a gene co-expression module in 3 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.
HEXB's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Gamma-delta T cells | ER Glycoprotein Quality Control Protein processing & ER | APOL2, BAG6, CALR, ELP3, GBP1, GBP2, GBP4, HSP90B1 +9 more | |
| Macrophages | ER Protein Processing Housekeeping | ACTR1A, ANXA7, ATP6AP1, ATP6AP2, ATP6V0B, ATP6V0E1, AUP1, BCAP31 +41 more | View in SCUBA |
| Smooth muscle cells | Lysosomal Glycoprotein Catabolism Protein processing & ER | AKR7A2, CERCAM, CPQ, FCGRT, GRN, LTBP1, MRGPRF, PPIC | View in SCUBA |
About the gene
| Chromosome | 5: 74640023-74722647 |
|---|---|
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins |
| Molecular function | Glycosidase, Hydrolase |
| Biological process | Lipid metabolism |
Function
Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A. During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity).
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.