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Details on Person UniProt:P07686 HEXB
| Class:Id | ReferenceGeneProduct:56474 |
|---|---|
| _chainChangeLog | signal peptide:1-42 added on Fri February 6 2015;propeptide:43-121 added on Fri February 6 2015;chain:122-556 added on Fri February 6 2015;chain:122-311 added on Fri February 6 2015;chain:315-556 added on Fri February 6 2015 |
| _displayName | UniProt:P07686 HEXB |
| _timestamp | 2025-02-21 18:37:14 |
| chain | signal peptide:1-42 propeptide:43-121 chain:122-556 chain:122-311 chain:315-556 |
| checksum | 2267BF1453EA50EF |
| comment | 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).CATALYTIC ACTIVITY Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.CATALYTIC ACTIVITY N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H2O = a beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N-acetyl-beta-D-galactosamineCATALYTIC ACTIVITY a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GM3 (d18:1(4E)) + N-acetyl-beta-D-galactosamineCATALYTIC ACTIVITY a ganglioside GM2 + H2O = a ganglioside GM3 + N-acetyl-beta-D-galactosamineCATALYTIC ACTIVITY beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha-L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + N-acetyl-D-galactosamineCATALYTIC ACTIVITY N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + H2O = alpha-L-iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-sulfogalactosamineACTIVITY REGULATION Addition of GM2A stimulates the hydrolysis of sulfated glycosphingolipid SM2 and the ganglioside GM2.BIOPHYSICOCHEMICAL PROPERTIES Optimum pH is 4.SUBUNIT There are 3 forms of beta-hexosaminidase: hexosaminidase A is a heterodimer composed of one subunit alpha and one subunit beta (chain A and B); hexosaminidase B is a homodimer of two beta subunits (two chains A and B); hexosaminidase S is a homodimer of two alpha subunits (By similarity). The composition of the dimer (isozyme A versus isozyme S) has a significant effect on the substrate specificity of the alpha subunit active site (PubMed:8672428).INTERACTION N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-GlcNAc(2) and Man(5 to 7)-GlcNAc(2), respectively.PTM The beta-A and beta-B chains are produced by proteolytic processing of the precursor beta chain.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the glycosyl hydrolase 20 family. |
| description | recommendedName: fullName evidence="30"Beta-hexosaminidase subunit beta ecNumber evidence="4 6 21 23 26"3.2.1.52 alternativeName: Beta-N-acetylhexosaminidase subunit beta shortName: Hexosaminidase subunit B alternativeName: Cervical cancer proto-oncogene 7 protein shortName: HCC-7 alternativeName: N-acetyl-beta-glucosaminidase subunit beta component recommendedName: Beta-hexosaminidase subunit beta chain B /component component recommendedName: Beta-hexosaminidase subunit beta chain A /component |
| geneName | HEXB HCC7 |
| identifier | P07686 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Cytoplasmic vesicle Direct protein sequencing Disease variant Disulfide bond Gangliosidosis Glycoprotein Glycosidase Hydrolase Lipid metabolism Lysosome Neurodegeneration Proteomics identification Reference proteome Signal Zymogen |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 |
| name | HEXB |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8958230] ENSEMBL:ENSG00000049860 HEXB [Homo sapiens] |
| secondaryIdentifier | HEXB_HUMAN |
| sequenceLength | 556 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:1605605] HEXB(316-556) [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:1605777] HEXB(122-311) [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:3700843] HEXB M26Cfs*5 [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:3700889] HEXB I322Kfs*5 [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:3700901] HEXB S62L [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:3700930] HEXB R284* [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:6799125] HEXB(122-311) [azurophil granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:6799134] HEXB(315-556) [azurophil granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:6806188] HEXB(315-556) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:6806190] HEXB(122-311) [extracellular region] [Homo sapiens] |
| (referenceSequence) | [ReplacedResidue:3700841] L-asparagine 323 replaced with L-threonine [ReplacedResidue:3700854] L-isoleucine 322 replaced with L-lysine [ReplacedResidue:3700861] L-proline 324 replaced with L-leucine [NonsenseMutation:3700875] Nonsense mutation at L-arginine 284 [ReplacedResidue:3700897] L-threonine 325 replaced with L-leucine [ReplacedResidue:3700909] L-alanine 28 replaced with L-arginine [ReplacedResidue:3700911] L-serine 62 replaced with L-leucine [ReplacedResidue:3700940] L-leucine 29 replaced with L-cysteine [ReplacedResidue:3700967] L-leucine 27 replaced with L-tryptophan [ReplacedResidue:3700970] L-methionine 26 replaced with L-cysteine |
| (secondReferenceSequence) | [InterChainCrosslinkedResidue:9842373] Inter-chain Crosslink via L-cystine (cross-link) at 360 and 309 [InterChainCrosslinkedResidue:9842375] Inter-chain Crosslink via L-cystine (cross-link) at 93 and 137 [InterChainCrosslinkedResidue:9842377] Inter-chain Crosslink via L-cystine (cross-link) at 309 and 360 [InterChainCrosslinkedResidue:9842379] Inter-chain Crosslink via L-cystine (cross-link) at 137 and 93 |
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No pathways have been reviewed or authored by UniProt:P07686 HEXB (56474)
