UniProtKB - P07686 (HEXB_HUMAN)
Beta-hexosaminidase subunit beta
HEXB
Functioni
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:9694901, PubMed:8672428, PubMed:8123671).
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:9694901, PubMed:8672428, PubMed:8123671).
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).
By similarity4 PublicationsCatalytic activityi
- H2O + N-acetyl-β-D-galactosaminyl-(1→4)-β-D-3-sulfogalactosyl-(1→4)-β-D-glucosyl-(1↔1ʼ)-ceramide = a β-D-3-sulfogalactosyl-(1→4)-β-D-glucosyl-(1↔1ʼ)-ceramide + N-acetyl-β-D-galactosamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- ganglioside GM2 (d18:1(4E)) + H2O = ganglioside GM3 (d18:1(4E)) + N-acetyl-β-D-galactosamine3 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- β-D-GalNAc-(1→4)-α-L-IdoA-(1→3)-β-D-GalNAc-4-sulfate-(1→4)-α-L-IdoA-(1→3)-D-GalNAc-4-sulfate + H2O = α-L-IdoA-(1→3)-β-D-GalNAc-4-sulfate-(1→4)-α-L-IdoA-(1→3)-D-GalNAc-4-sulfate + N-acetyl-D-galactosamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- H2O + N-acetyl-β-D-6-sulfogalactosaminyl-(1→4)-α-L-iduronyl-(1→3)-N-acetyl-D-6-sulfogalactosamine = α-L-iduronyl-(1→3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6-sulfogalactosamine1 PublicationThis reaction proceeds in the forward1 Publication direction.
- Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.4 Publications EC:3.2.1.52
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 355 | Proton donorBy similarity | 1 |
GO - Molecular functioni
- acetylglucosaminyltransferase activity Source: UniProtKB
- beta-N-acetylhexosaminidase activity Source: UniProtKB
- identical protein binding Source: MGI
- N-acetyl-beta-D-galactosaminidase activity Source: UniProtKB-EC
GO - Biological processi
- astrocyte cell migration Source: Ensembl
- cellular calcium ion homeostasis Source: Ensembl
- cellular protein metabolic process Source: Ensembl
- ganglioside catabolic process Source: UniProtKB
- glycosaminoglycan metabolic process Source: ComplexPortal
- lipid storage Source: Ensembl
- locomotory behavior Source: Ensembl
- lysosome organization Source: Ensembl
- male courtship behavior Source: Ensembl
- myelination Source: Ensembl
- neuromuscular process controlling balance Source: Ensembl
- oligosaccharide catabolic process Source: Ensembl
- oogenesis Source: Ensembl
- penetration of zona pellucida Source: Ensembl
- phospholipid biosynthetic process Source: Ensembl
- positive regulation of transcription by RNA polymerase II Source: Ensembl
- regulation of cell shape Source: Ensembl
- sensory perception of sound Source: Ensembl
- single fertilization Source: UniProtKB
- skeletal system development Source: Ensembl
Keywordsi
Molecular function | Glycosidase, Hydrolase |
Biological process | Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 3.2.1.52, 2681 |
PathwayCommonsi | P07686 |
Reactomei | R-HSA-1660662, Glycosphingolipid metabolism R-HSA-2022857, Keratan sulfate degradation R-HSA-2024101, CS/DS degradation R-HSA-2160916, Hyaluronan uptake and degradation R-HSA-3656248, Defective HEXB causes GM2G2 R-HSA-6798695, Neutrophil degranulation |
SABIO-RKi | P07686 |
SignaLinki | P07686 |
Protein family/group databases
CAZyi | GH20, Glycoside Hydrolase Family 20 |
Names & Taxonomyi
Protein namesi | Recommended name: Beta-hexosaminidase subunit betaCurated (EC:3.2.1.524 Publications)Alternative name(s): Beta-N-acetylhexosaminidase subunit beta Short name: Hexosaminidase subunit B Cervical cancer proto-oncogene 7 protein Short name: HCC-7 N-acetyl-beta-glucosaminidase subunit beta Cleaved into the following 2 chains: |
Gene namesi | Name:HEXBImported ORF Names:HCC7 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:4879, HEXB |
MIMi | 606873, gene |
neXtProti | NX_P07686 |
VEuPathDBi | HostDB:ENSG00000049860 |
Subcellular locationi
Lysosome
- Lysosome 1 Publication
Other locations
- Cortical granule By similarity
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
- extracellular region Source: Reactome
Lysosome
- azurophil granule Source: UniProtKB
- azurophil granule lumen Source: Reactome
- lysosomal lumen Source: Reactome
- lysosome Source: GO_Central
Other locations
- acrosomal vesicle Source: Ensembl
- beta-N-acetylhexosaminidase complex Source: ComplexPortal
- cortical granule Source: UniProtKB
- membrane Source: UniProtKB
Keywords - Cellular componenti
Cytoplasmic vesicle, LysosomePathology & Biotechi
Involvement in diseasei
GM2-gangliosidosis 2 (GM2G2)10 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_003247 | 62 | L → S in GM2G2. 8 PublicationsCorresponds to variant dbSNP:rs820878EnsemblClinVar. | 1 | |
Natural variantiVAR_011704 | 255 | S → R in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs1554035829Ensembl. | 1 | |
Natural variantiVAR_003250 | 309 | C → Y in GM2G2; adult type; severe. 1 PublicationCorresponds to variant dbSNP:rs1554036641Ensembl. | 1 | |
Natural variantiVAR_003251 | 417 | P → L in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs28942073EnsemblClinVar. | 1 | |
Natural variantiVAR_003252 | 456 | Y → S in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907982EnsemblClinVar. | 1 | |
Natural variantiVAR_011705 | 504 | P → S in GM2G2; decreases the isozyme A transport out of the endoplasmic reticulum. Lowers its heat stability. Affects the ability of isozyme A to hydrolyze GM2 ganglioside. 1 PublicationCorresponds to variant dbSNP:rs121907985EnsemblClinVar. | 1 | |
Natural variantiVAR_003253 | 505 | R → Q in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs121907983EnsemblClinVar. | 1 | |
Natural variantiVAR_003254 | 534 | C → Y in GM2G2; infantile type. 1 PublicationCorresponds to variant dbSNP:rs727503960Ensembl. | 1 | |
Natural variantiVAR_011706 | 543 | A → T in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907984EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 211 | R → K: Does not affect the native conformation of the isozyme A. Does not affect hydrolysis of GM2 ganglioside by the isozyme A. 1 Publication | 1 |
Keywords - Diseasei
Disease variant, Gangliosidosis, NeurodegenerationOrganism-specific databases
DisGeNETi | 3074 |
MalaCardsi | HEXB |
MIMi | 268800, phenotype |
Orphaneti | 309169, Sandhoff disease, adult form 309155, Sandhoff disease, infantile form 309162, Sandhoff disease, juvenile form |
PharmGKBi | PA29257 |
Miscellaneous databases
Pharosi | P07686, Tchem |
Chemistry databases
ChEMBLi | CHEMBL5877 |
DrugBanki | DB03861, (2R,3R,4S,5R)-2-acetamido-3,4-dihydroxy-5-hydroxymethyl-piperidine DB02813, 2-Acetamido-2-Deoxy-D-Glucono-1,5-Lactone DB09301, Chondroitin sulfate DB03747, N-Acetyl-glucosamine thiazoline DB00205, Pyrimethamine |
DrugCentrali | P07686 |
Genetic variation databases
BioMutai | HEXB |
DMDMi | 123081 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 42 | Sequence analysisAdd BLAST | 42 | |
PropeptideiPRO_0000012002 | 43 – 121 | 2 PublicationsAdd BLAST | 79 | |
ChainiPRO_0000012003 | 122 – 556 | Beta-hexosaminidase subunit betaAdd BLAST | 435 | |
ChainiPRO_0000012004 | 122 – 311 | Beta-hexosaminidase subunit beta chain BAdd BLAST | 190 | |
ChainiPRO_0000012005 | 315 – 556 | Beta-hexosaminidase subunit beta chain AAdd BLAST | 242 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 84 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 91 ↔ 137 | |||
Glycosylationi | 142 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 190 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 309 ↔ 360 | |||
Glycosylationi | 327 | N-linked (GlcNAc...) asparagine3 Publications | 1 | |
Disulfide bondi | 534 ↔ 551 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 497 | Not glycosylated1 Publication | 1 |
Keywords - PTMi
Disulfide bond, Glycoprotein, ZymogenProteomic databases
CPTACi | CPTAC-78 CPTAC-79 |
EPDi | P07686 |
jPOSTi | P07686 |
MassIVEi | P07686 |
MaxQBi | P07686 |
PaxDbi | P07686 |
PeptideAtlasi | P07686 |
PRIDEi | P07686 |
ProteomicsDBi | 52022 |
TopDownProteomicsi | P07686 |
2D gel databases
UCD-2DPAGEi | P07686 |
PTM databases
GlyConnecti | 1039, 4 N-Linked glycans (3 sites) |
GlyGeni | P07686, 7 sites, 13 N-linked glycans (4 sites), 1 O-linked glycan (1 site) |
iPTMneti | P07686 |
MetOSitei | P07686 |
PhosphoSitePlusi | P07686 |
SwissPalmi | P07686 |
Expressioni
Gene expression databases
Bgeei | ENSG00000049860, Expressed in placenta and 238 other tissues |
ExpressionAtlasi | P07686, baseline and differential |
Genevisiblei | P07686, HS |
Organism-specific databases
HPAi | ENSG00000049860, Low tissue specificity |
Interactioni
Subunit structurei
There are 3 forms of beta-hexosaminidase: hexosaminidase A is an heterodimer composed of one subunit alpha and one subunit beta (chain A and B); hexosaminidase B is an 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).
By similarity1 PublicationBinary interactionsi
P07686
GO - Molecular functioni
- identical protein binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 109323, 41 interactors |
ComplexPortali | CPX-502, Beta-hexosaminidase A complex CPX-686, Beta-hexosaminidase B complex |
CORUMi | P07686 |
ELMi | P07686 |
IntActi | P07686, 36 interactors |
MINTi | P07686 |
STRINGi | 9606.ENSP00000261416 |
Chemistry databases
BindingDBi | P07686 |
Miscellaneous databases
RNActi | P07686, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P07686 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07686 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG2499, Eukaryota |
HOGENOMi | CLU_007082_0_3_1 |
InParanoidi | P07686 |
OrthoDBi | 545162at2759 |
PhylomeDBi | P07686 |
TreeFami | TF313036 |
Family and domain databases
Gene3Di | 3.30.379.10, 1 hit |
InterProi | View protein in InterPro IPR025705, Beta_hexosaminidase_sua/sub IPR015883, Glyco_hydro_20_cat IPR017853, Glycoside_hydrolase_SF IPR029018, Hex-like_dom2 IPR029019, HEX_eukaryotic_N |
PANTHERi | PTHR22600, PTHR22600, 1 hit |
Pfami | View protein in Pfam PF00728, Glyco_hydro_20, 1 hit PF14845, Glycohydro_20b2, 1 hit |
PIRSFi | PIRSF001093, B-hxosamndse_ab_euk, 1 hit |
PRINTSi | PR00738, GLHYDRLASE20 |
SUPFAMi | SSF51445, SSF51445, 1 hit SSF55545, SSF55545, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MELCGLGLPR PPMLLALLLA TLLAAMLALL TQVALVVQVA EAARAPSVSA
60 70 80 90 100
KPGPALWPLP LLVKMTPNLL HLAPENFYIS HSPNSTAGPS CTLLEEAFRR
110 120 130 140 150
YHGYIFGFYK WHHEPAEFQA KTQVQQLLVS ITLQSECDAF PNISSDESYT
160 170 180 190 200
LLVKEPVAVL KANRVWGALR GLETFSQLVY QDSYGTFTIN ESTIIDSPRF
210 220 230 240 250
SHRGILIDTS RHYLPVKIIL KTLDAMAFNK FNVLHWHIVD DQSFPYQSIT
260 270 280 290 300
FPELSNKGSY SLSHVYTPND VRMVIEYARL RGIRVLPEFD TPGHTLSWGK
310 320 330 340 350
GQKDLLTPCY SRQNKLDSFG PINPTLNTTY SFLTTFFKEI SEVFPDQFIH
360 370 380 390 400
LGGDEVEFKC WESNPKIQDF MRQKGFGTDF KKLESFYIQK VLDIIATINK
410 420 430 440 450
GSIVWQEVFD DKAKLAPGTI VEVWKDSAYP EELSRVTASG FPVILSAPWY
460 470 480 490 500
LDLISYGQDW RKYYKVEPLD FGGTQKQKQL FIGGEACLWG EYVDATNLTP
510 520 530 540 550
RLWPRASAVG ERLWSSKDVR DMDDAYDRLT RHRCRMVERG IAAQPLYAGY
CNHENM
Computationally mapped potential isoform sequencesi
There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketQ5URX0 | Q5URX0_HUMAN | Beta-N-acetylhexosaminidase | HEXB HEL-248, HEL-S-111 | 331 | Annotation score: | ||
H0YA83 | H0YA83_HUMAN | Beta-N-acetylhexosaminidase | HEXB | 170 | Annotation score: | ||
H0Y9B6 | H0Y9B6_HUMAN | Beta-N-acetylhexosaminidase | HEXB | 202 | Annotation score: | ||
D6REQ8 | D6REQ8_HUMAN | Beta-hexosaminidase subunit beta | HEXB | 35 | Annotation score: | ||
H0Y9M3 | H0Y9M3_HUMAN | Beta-hexosaminidase subunit beta | HEXB | 52 | Annotation score: |
Sequence cautioni
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_003247 | 62 | L → S in GM2G2. 8 PublicationsCorresponds to variant dbSNP:rs820878EnsemblClinVar. | 1 | |
Natural variantiVAR_003248 | 121 | K → R. Corresponds to variant dbSNP:rs11556045EnsemblClinVar. | 1 | |
Natural variantiVAR_003249 | 207 | I → V2 PublicationsCorresponds to variant dbSNP:rs10805890EnsemblClinVar. | 1 | |
Natural variantiVAR_011704 | 255 | S → R in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs1554035829Ensembl. | 1 | |
Natural variantiVAR_003250 | 309 | C → Y in GM2G2; adult type; severe. 1 PublicationCorresponds to variant dbSNP:rs1554036641Ensembl. | 1 | |
Natural variantiVAR_003251 | 417 | P → L in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs28942073EnsemblClinVar. | 1 | |
Natural variantiVAR_003252 | 456 | Y → S in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907982EnsemblClinVar. | 1 | |
Natural variantiVAR_011705 | 504 | P → S in GM2G2; decreases the isozyme A transport out of the endoplasmic reticulum. Lowers its heat stability. Affects the ability of isozyme A to hydrolyze GM2 ganglioside. 1 PublicationCorresponds to variant dbSNP:rs121907985EnsemblClinVar. | 1 | |
Natural variantiVAR_003253 | 505 | R → Q in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs121907983EnsemblClinVar. | 1 | |
Natural variantiVAR_003254 | 534 | C → Y in GM2G2; infantile type. 1 PublicationCorresponds to variant dbSNP:rs727503960Ensembl. | 1 | |
Natural variantiVAR_011706 | 543 | A → T in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907984EnsemblClinVar. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M13519 mRNA Translation: AAA51828.1 Frameshift. M23294 , M23282, M23283, M23284, M23285, M23286, M23287, M23288, M23290, M23291, M23292, M23293 Genomic DNA Translation: AAA52645.1 M19735 mRNA Translation: AAA68620.1 AF378118 mRNA Translation: AAM46114.1 BT009919 mRNA Translation: AAP88921.1 AC026405 Genomic DNA No translation available. AC093214 Genomic DNA No translation available. BC017378 mRNA Translation: AAH17378.1 M34906 mRNA Translation: AAA51829.1 |
CCDSi | CCDS4022.1 |
PIRi | A31250 |
RefSeqi | NP_000512.1, NM_000521.3 NP_001278933.1, NM_001292004.1 |
Genome annotation databases
Ensembli | ENST00000261416; ENSP00000261416; ENSG00000049860 |
GeneIDi | 3074 |
KEGGi | hsa:3074 |
MANE-Selecti | ENST00000261416.12; ENSP00000261416.7; NM_000521.4; NP_000512.2 |
UCSCi | uc003kdf.4, human |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M13519 mRNA Translation: AAA51828.1 Frameshift. M23294 , M23282, M23283, M23284, M23285, M23286, M23287, M23288, M23290, M23291, M23292, M23293 Genomic DNA Translation: AAA52645.1 M19735 mRNA Translation: AAA68620.1 AF378118 mRNA Translation: AAM46114.1 BT009919 mRNA Translation: AAP88921.1 AC026405 Genomic DNA No translation available. AC093214 Genomic DNA No translation available. BC017378 mRNA Translation: AAH17378.1 M34906 mRNA Translation: AAA51829.1 |
CCDSi | CCDS4022.1 |
PIRi | A31250 |
RefSeqi | NP_000512.1, NM_000521.3 NP_001278933.1, NM_001292004.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1NOU | X-ray | 2.40 | A/B | 50-556 | [»] | |
1NOW | X-ray | 2.20 | A/B | 50-556 | [»] | |
1NP0 | X-ray | 2.50 | A/B | 50-556 | [»] | |
1O7A | X-ray | 2.25 | A/B/C/D/E/F | 42-556 | [»] | |
2GJX | X-ray | 2.80 | B/C/F/G | 50-556 | [»] | |
2GK1 | X-ray | 3.25 | B/D/F/H | 50-552 | [»] | |
3LMY | X-ray | 2.80 | A/B | 1-556 | [»] | |
5BRO | X-ray | 2.40 | A | 43-556 | [»] | |
SMRi | P07686 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109323, 41 interactors |
ComplexPortali | CPX-502, Beta-hexosaminidase A complex CPX-686, Beta-hexosaminidase B complex |
CORUMi | P07686 |
ELMi | P07686 |
IntActi | P07686, 36 interactors |
MINTi | P07686 |
STRINGi | 9606.ENSP00000261416 |
Chemistry databases
BindingDBi | P07686 |
ChEMBLi | CHEMBL5877 |
DrugBanki | DB03861, (2R,3R,4S,5R)-2-acetamido-3,4-dihydroxy-5-hydroxymethyl-piperidine DB02813, 2-Acetamido-2-Deoxy-D-Glucono-1,5-Lactone DB09301, Chondroitin sulfate DB03747, N-Acetyl-glucosamine thiazoline DB00205, Pyrimethamine |
DrugCentrali | P07686 |
Protein family/group databases
CAZyi | GH20, Glycoside Hydrolase Family 20 |
PTM databases
GlyConnecti | 1039, 4 N-Linked glycans (3 sites) |
GlyGeni | P07686, 7 sites, 13 N-linked glycans (4 sites), 1 O-linked glycan (1 site) |
iPTMneti | P07686 |
MetOSitei | P07686 |
PhosphoSitePlusi | P07686 |
SwissPalmi | P07686 |
Genetic variation databases
BioMutai | HEXB |
DMDMi | 123081 |
2D gel databases
UCD-2DPAGEi | P07686 |
Proteomic databases
CPTACi | CPTAC-78 CPTAC-79 |
EPDi | P07686 |
jPOSTi | P07686 |
MassIVEi | P07686 |
MaxQBi | P07686 |
PaxDbi | P07686 |
PeptideAtlasi | P07686 |
PRIDEi | P07686 |
ProteomicsDBi | 52022 |
TopDownProteomicsi | P07686 |
Protocols and materials databases
Antibodypediai | 24338, 266 antibodies from 34 providers |
DNASUi | 3074 |
Genome annotation databases
Ensembli | ENST00000261416; ENSP00000261416; ENSG00000049860 |
GeneIDi | 3074 |
KEGGi | hsa:3074 |
MANE-Selecti | ENST00000261416.12; ENSP00000261416.7; NM_000521.4; NP_000512.2 |
UCSCi | uc003kdf.4, human |
Organism-specific databases
CTDi | 3074 |
DisGeNETi | 3074 |
GeneCardsi | HEXB |
HGNCi | HGNC:4879, HEXB |
HPAi | ENSG00000049860, Low tissue specificity |
MalaCardsi | HEXB |
MIMi | 268800, phenotype 606873, gene |
neXtProti | NX_P07686 |
Orphaneti | 309169, Sandhoff disease, adult form 309155, Sandhoff disease, infantile form 309162, Sandhoff disease, juvenile form |
PharmGKBi | PA29257 |
VEuPathDBi | HostDB:ENSG00000049860 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG2499, Eukaryota |
HOGENOMi | CLU_007082_0_3_1 |
InParanoidi | P07686 |
OrthoDBi | 545162at2759 |
PhylomeDBi | P07686 |
TreeFami | TF313036 |
Enzyme and pathway databases
BRENDAi | 3.2.1.52, 2681 |
PathwayCommonsi | P07686 |
Reactomei | R-HSA-1660662, Glycosphingolipid metabolism R-HSA-2022857, Keratan sulfate degradation R-HSA-2024101, CS/DS degradation R-HSA-2160916, Hyaluronan uptake and degradation R-HSA-3656248, Defective HEXB causes GM2G2 R-HSA-6798695, Neutrophil degranulation |
SABIO-RKi | P07686 |
SignaLinki | P07686 |
Miscellaneous databases
BioGRID-ORCSi | 3074, 5 hits in 1045 CRISPR screens |
ChiTaRSi | HEXB, human |
EvolutionaryTracei | P07686 |
GeneWikii | HEXB |
GenomeRNAii | 3074 |
Pharosi | P07686, Tchem |
PROi | PR:P07686 |
RNActi | P07686, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000049860, Expressed in placenta and 238 other tissues |
ExpressionAtlasi | P07686, baseline and differential |
Genevisiblei | P07686, HS |
Family and domain databases
Gene3Di | 3.30.379.10, 1 hit |
InterProi | View protein in InterPro IPR025705, Beta_hexosaminidase_sua/sub IPR015883, Glyco_hydro_20_cat IPR017853, Glycoside_hydrolase_SF IPR029018, Hex-like_dom2 IPR029019, HEX_eukaryotic_N |
PANTHERi | PTHR22600, PTHR22600, 1 hit |
Pfami | View protein in Pfam PF00728, Glyco_hydro_20, 1 hit PF14845, Glycohydro_20b2, 1 hit |
PIRSFi | PIRSF001093, B-hxosamndse_ab_euk, 1 hit |
PRINTSi | PR00738, GLHYDRLASE20 |
SUPFAMi | SSF51445, SSF51445, 1 hit SSF55545, SSF55545, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | HEXB_HUMAN | |
Accessioni | P07686Primary (citable) accession number: P07686 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1988 |
Last sequence update: | February 23, 2022 | |
Last modified: | February 23, 2022 | |
This is version 223 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries - Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families