HEXB
entrez
3074
canonical
uniprot
P07686
canonical
ensembl
ENSG00000049860
resolver
ensp
ENSP00000261416
resolver
ensp
ENSP00000426285
resolver
enst
ENST00000261416
resolver
enst
ENST00000511181
resolver
genesymbol
HEL-S-111
resolver
genesymbol
HEXB
resolver
genesymbol_syn
HEL-248
resolver
hgnc
HGNC:4879
resolver
uniprot
A0A024RAJ6
resolver
uniprot
F6RVC2
resolver
uniprot
Q5URX0
resolver
uniprot_entry
A0A024RAJ6_HUMAN
resolver
uniprot_entry
F6RVC2_HUMAN
resolver
uniprot_entry
HEXB_HUMAN
resolver
uniprot_entry
Q5URX0_HUMAN
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
MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLLVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM
uniprot
proteins
disease_involvement
DISEASE: GM2-gangliosidosis 2 (GM2G2) [MIM:268800]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. Clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula. {ECO:0000269|PubMed:1531140, ECO:0000269|PubMed:1720305, ECO:0000269|PubMed:7557963, ECO:0000269|PubMed:7626071, ECO:0000269|PubMed:7633435, ECO:0000269|PubMed:8357844, ECO:0000269|PubMed:8950198, ECO:0000269|PubMed:9401004, ECO:0000269|PubMed:9694901, ECO:0000269|PubMed:9856491}. 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: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). {ECO:0000250|UniProtKB:P20060, ECO:0000269|PubMed:11707436, ECO:0000269|PubMed:8123671, ECO:0000269|PubMed:8672428, ECO:0000269|PubMed:9694901}.
uniprot
proteins
mass_dalton
63137
uniprot
proteins
mutagenesis
MUTAGEN 211; /note="R->K: Does not affect the native conformation of the isozyme A. Does not affect hydrolysis of GM2 ganglioside by the isozyme A."; /evidence="ECO:0000269|PubMed:8672428"; MUTAGEN 241; /note="D->N: 2.7-fold reduction in substrate affinity. 39-fold reduction in catalytic efficiency."; /evidence="ECO:0000269|PubMed:11329289"; MUTAGEN 354; /note="D->N: No effect on substrate affinity. 1750-fold reduction in catalytic efficiency."; /evidence="ECO:0000269|PubMed:11329289"; MUTAGEN 355; /note="E->Q: 1.5-fold increase in substrate affinity. 2300-fold reduction in catalytic efficiency. Reduces optimal pH to 3-3.5."; /evidence="ECO:0000269|PubMed:11329289"; MUTAGEN 491; /note="E->Q: No effect on substrate affinity and on catalytic efficiency."; /evidence="ECO:0000269|PubMed:11329289
uniprot
proteins
post_translational_modification
PTM: N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-GlcNAc(2) and Man(5 to 7)-GlcNAc(2), respectively. {ECO:0000269|PubMed:11447134, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218}.; PTM: The beta-A and beta-B chains are produced by proteolytic processing of the precursor beta chain.
uniprot
proteins
protein_family
Glycosyl hydrolase 20 family
uniprot
proteins
pubmed
11329289
uniprot
proteins
pubmed
11447134
uniprot
proteins
pubmed
11707436
uniprot
proteins
pubmed
12662933
uniprot
proteins
pubmed
12706724
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
1531140
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1720305
uniprot
proteins
pubmed
1825792
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2139028
uniprot
proteins
pubmed
2147427
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2525487
uniprot
proteins
pubmed
2579389
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2964638
uniprot
proteins
pubmed
2965147
uniprot
proteins
pubmed
2966076
uniprot
proteins
pubmed
2971039
uniprot
proteins
pubmed
2971395
uniprot
proteins
pubmed
2977375
uniprot
proteins
pubmed
3013851
uniprot
proteins
pubmed
7557963
uniprot
proteins
pubmed
7626071
uniprot
proteins
pubmed
7633435
uniprot
proteins
pubmed
8123671
uniprot
proteins
pubmed
8357844
uniprot
proteins
pubmed
8672428
uniprot
proteins
pubmed
8673609
uniprot
proteins
pubmed
8950198
uniprot
proteins
pubmed
9401004
uniprot
proteins
pubmed
9694901
uniprot
proteins
pubmed
9856491
uniprot
proteins
sequence_length
556
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9694901}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:P20060}.
uniprot
proteins