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Details on Person UniProt:P06865 HEXA

Class:Id	ReferenceGeneProduct:56472
_chainChangeLog	signal peptide:1-22 added on Fri February 6 2015;propeptide:23-88 added on Fri February 6 2015;chain:89-529 added on Fri February 6 2015
_displayName	UniProt:P06865 HEXA
_timestamp	2026-02-20 21:49:42
chain	signal peptide:1-22 propeptide:23-88 chain:89-529
checksum	DACB3E3992E57A47
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 S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2 (PubMed:11707436). 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).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.SUBUNIT There are 3 beta-hexosaminidase isozymes: isozyme A (hexosaminidase A) is a heterodimer composed of one subunit alpha and one subunit beta (chain A and B); isozyme B (hexosaminidase B) is a homodimer of two beta subunits (two chains A and B); isozyme S (hexosaminidase S) is a homodimer of two alpha subunits (PubMed:16698036). 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 glycan at Asn-115 consists of Man(3)-GlcNAc(2) (Probable) (PubMed:1533633, PubMed:16698036, PubMed:19159218). N-linked glycan at Asn-157 consists of either GlcNAc or GlcNAc(2)-Man(7-9). N-linked glycan at Asn-295 consists of either GlcNAc, GlcNAc-Fuc, or GlcNAc(2)-Man(4) (Probable).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="47"Beta-hexosaminidase subunit alpha ecNumber evidence="1 31 35 44"3.2.1.52 alternativeName: Beta-N-acetylhexosaminidase subunit alpha shortName: Hexosaminidase subunit A alternativeName: N-acetyl-beta-glucosaminidase subunit alpha
geneName	HEXA
identifier	P06865
isSequenceChanged	FALSE
keyword	3D-structure Alternative splicing 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 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
name	HEXA
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8958600] ENSEMBL:ENSG00000213614 HEXA [Homo sapiens]
secondaryIdentifier	HEXA_HUMAN B4DKE7 E7ENH7 Q53HS8 Q6AI32
sequenceLength	529
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:8972431] UniProt:P06865-1 HEXA [Homo sapiens] [ReferenceIsoform:8972432] UniProt:P06865-2 HEXA [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:1605799] HEXA(88-528) [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:3700918] HEXA Y427Ifs*5 [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:8957942] HEXA [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:9842401] HEXA(23-73) [lysosomal lumen] [Homo sapiens]
(referenceSequence)	[ReplacedResidue:3700880] L-tyrosine 427 replaced with L-isoleucine [ReplacedResidue:3700906] glycine 428 replaced with L-leucine [ReplacedResidue:3700933] L-aspartic acid 430 replaced with L-proline [ReplacedResidue:3700965] L-proline 429 replaced with L-tryptophan [FragmentReplacedModification:3769425] Replacement of residues 427 to 430 by ILWP [InterChainCrosslinkedResidue:9842374] Inter-chain Crosslink via L-cystine (cross-link) at 104 and 58 [InterChainCrosslinkedResidue:9842376] Inter-chain Crosslink via L-cystine (cross-link) at 58 and 104
(secondReferenceSequence)	[InterChainCrosslinkedResidue:9842374] Inter-chain Crosslink via L-cystine (cross-link) at 104 and 58 [InterChainCrosslinkedResidue:9842376] Inter-chain Crosslink via L-cystine (cross-link) at 58 and 104
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No pathways have been reviewed or authored by UniProt:P06865 HEXA (56472)