Search Results
Overview
| Uniprot ID | P07686 |
|---|---|
| Protein Name | Beta-hexosaminidase subunit beta |
| Gene Name | HEXB |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 161 | KEPVAVLKANRVWGA |
| 217 | SRHYLPVKIILKTLD |
| 382 | GFGTDFKKLESFYIQ |
| 412 | WQEVFDDKAKLAPGT |
| 465 | QDWRKYYKVEPLDFG |
| 476 | LDFGGTQKQKQLFIG |
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 (PubMed:11707436, PubMed:8123671, PubMed:8672428, PubMed:9694901). The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide (PubMed:11707436). Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (PubMed:8123671, PubMed:8672428, PubMed:9694901). 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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0001669 | acrosomal vesicle |
| Cellular Component | GO:0042582 | azurophil granule |
| Cellular Component | GO:0035578 | azurophil granule lumen |
| Cellular Component | GO:1905379 | beta-N-acetylhexosaminidase complex |
| Cellular Component | GO:0060473 | cortical granule |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0043202 | lysosomal lumen |
| Cellular Component | GO:0005764 | lysosome |
| Cellular Component | GO:0016020 | membrane |
| Molecular Function | GO:0008375 | acetylglucosaminyltransferase activity |
| Molecular Function | GO:0016231 | beta-N-acetylglucosaminidase activity |
| Molecular Function | GO:0004563 | beta-N-acetylhexosaminidase activity |
| Molecular Function | GO:0030246 | carbohydrate binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Biological Process | GO:0043615 | astrocyte cell migration |
| Biological Process | GO:0005975 | carbohydrate metabolic process |
| Biological Process | GO:0030207 | chondroitin sulfate proteoglycan catabolic process |
| Biological Process | GO:0030209 | dermatan sulfate proteoglycan catabolic process |
| Biological Process | GO:0006689 | ganglioside catabolic process |
| Biological Process | GO:0030203 | glycosaminoglycan metabolic process |
| Biological Process | GO:0030214 | hyaluronan catabolic process |
| Biological Process | GO:0006044 | N-acetylglucosamine metabolic process |
| Biological Process | GO:0006491 | N-glycan processing |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0008360 | regulation of cell shape |
| Biological Process | GO:0007338 | single fertilization |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.