HEXA
entrez
3073
canonical
uniprot
P06865
canonical
ensembl
ENSG00000213614
resolver
ensp
ENSP00000268097
resolver
ensp
ENSP00000455114
resolver
enst
ENST00000566304
resolver
genesymbol
HEXA
resolver
hgnc
HGNC:4878
resolver
uniprot
A0A0S2Z3W3
resolver
uniprot
B4DKE7
resolver
uniprot
B4DVA7
resolver
uniprot
E7ENH7
resolver
uniprot
H3BP20
resolver
uniprot
Q53HS8
resolver
uniprot
Q6AI32
resolver
uniprot_entry
A0A0S2Z3W3_HUMAN
resolver
uniprot_entry
B4DVA7_HUMAN
resolver
uniprot_entry
H3BP20_HUMAN
resolver
uniprot_entry
HEXA_HUMAN
resolver
uniprot_sec
B4DKE7
resolver
uniprot_sec
E7ENH7
resolver
uniprot_sec
Q53HS8
resolver
uniprot_sec
Q6AI32
resolver
activity_regulation
ACTIVITY REGULATION: Addition of GM2A stimulates the hydrolysis of sulfated glycosphingolipid SM2 and the ganglioside GM2. {ECO:0000269|PubMed:11707436}.
uniprot
proteins
amino_acid_sequence
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
uniprot
proteins
disease_involvement
DISEASE: GM2-gangliosidosis 1 (GM2G1) [MIM:272800]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. It is characterized by GM2 gangliosides accumulation in the absence of HEXA activity, leading to neurodegeneration and, in the infantile form, death in early childhood. It exists in several forms: infantile (most common and most severe), juvenile and adult (late-onset). {ECO:0000269|PubMed:1301189, ECO:0000269|PubMed:1301190, ECO:0000269|PubMed:1302612, ECO:0000269|PubMed:14566483, ECO:0000269|PubMed:1532289, ECO:0000269|PubMed:1837283, ECO:0000269|PubMed:2140574, ECO:0000269|PubMed:2144098, ECO:0000269|PubMed:22723944, ECO:0000269|PubMed:2522679, ECO:0000269|PubMed:27682588, ECO:0000269|PubMed:2970528, ECO:0000269|PubMed:7717398, ECO:0000269|PubMed:7837766, ECO:0000269|PubMed:7898712, ECO:0000269|PubMed:7951261, ECO:0000269|PubMed:8044648, ECO:0000269|PubMed:8445615, ECO:0000269|PubMed:8490625, ECO:0000269|PubMed:8581357, ECO:0000269|PubMed:8730294, ECO:0000269|PubMed:8757036, ECO:0000269|PubMed:9150157, ECO:0000269|PubMed:9338583, ECO:0000269|PubMed:9375850, ECO:0000269|PubMed:9401008, ECO:0000269|PubMed:9603435}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.2.1.52
uniprot
proteins
function
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:16698036, 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). {ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:16698036, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}.
uniprot
proteins
mass_dalton
60703
uniprot
proteins
mutagenesis
MUTAGEN 115; /note="N->Q: No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-157 and Q-295."; /evidence="ECO:0000269|PubMed:1533633"; MUTAGEN 157; /note="N->Q: No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-115 and Q-295."; /evidence="ECO:0000269|PubMed:1533633"; MUTAGEN 295; /note="N->Q: No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-115 and Q-157."; /evidence="ECO:0000269|PubMed:1533633
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000269|PubMed:1533633, ECO:0000269|PubMed:16698036, ECO:0000269|PubMed:19159218, ECO:0000305|PubMed:11707436}.
uniprot
proteins
protein_family
Glycosyl hydrolase 20 family
uniprot
proteins
pubmed
11707436
uniprot
proteins
pubmed
1301189
uniprot
proteins
pubmed
1301190
uniprot
proteins
pubmed
1302612
uniprot
proteins
pubmed
1384323
uniprot
proteins
pubmed
14566483
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1532289
uniprot
proteins
pubmed
1533633
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16698036
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
1825792
uniprot
proteins
pubmed
1833974
uniprot
proteins
pubmed
1837283
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2140574
uniprot
proteins
pubmed
2144098
uniprot
proteins
pubmed
22723944
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2522679
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27682588
uniprot
proteins
pubmed
2933746
uniprot
proteins
pubmed
2952641
uniprot
proteins
pubmed
2965147
uniprot
proteins
pubmed
2970528
uniprot
proteins
pubmed
2971395
uniprot
proteins
pubmed
3013851
uniprot
proteins
pubmed
30988135
uniprot
proteins
pubmed
7717398
uniprot
proteins
pubmed
7837766
uniprot
proteins
pubmed
7898712
uniprot
proteins
pubmed
7902672
uniprot
proteins
pubmed
7951261
uniprot
proteins
pubmed
8044648
uniprot
proteins
pubmed
8123671
uniprot
proteins
pubmed
8445615
uniprot
proteins
pubmed
8490625
uniprot
proteins
pubmed
8581357
uniprot
proteins
pubmed
8652542
uniprot
proteins
pubmed
8672428
uniprot
proteins
pubmed
8673609
uniprot
proteins
pubmed
8730294
uniprot
proteins
pubmed
8757036
uniprot
proteins
pubmed
9090523
uniprot
proteins
pubmed
9150157
uniprot
proteins
pubmed
9338583
uniprot
proteins
pubmed
9375850
uniprot
proteins
pubmed
9401008
uniprot
proteins
pubmed
9603435
uniprot
proteins
pubmed
9694901
uniprot
proteins
sequence_length
529
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000305|PubMed:16698036}.
uniprot
proteins