HEXB

Functionⁱ

Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.

Catalytic activityⁱ

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	355	Proton donorBy similarity		1

GO - Molecular functionⁱ

acetylglucosaminyltransferase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 25645918
beta-N-acetylhexosaminidase activity Source: Reactome
N-acetyl-beta-D-galactosaminidase activity Source: UniProtKB-EC
protein heterodimerization activity
Source: MGI
Inferred from direct assayⁱ
- 6230359
protein homodimerization activity
Source: MGI
Inferred from direct assayⁱ
- 6230359

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

astrocyte cell migration Source: Ensembl
cellular calcium ion homeostasis Source: Ensembl
cellular protein metabolic process Source: Ensembl
chondroitin sulfate catabolic process Source: Reactome
ganglioside catabolic process Source: Ensembl
glycosphingolipid metabolic process Source: Reactome
hyaluronan catabolic process Source: Reactome
keratan sulfate catabolic process Source: Reactome
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
neutrophil degranulation Source: Reactome
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
skeletal system development Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosidase, Hydrolase

Molecular function

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS00629-MONOMER
BRENDAⁱ	3.2.1.52 2681
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

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GH20 Glycoside Hydrolase Family 20

CAZyⁱ

GH20 Glycoside Hydrolase Family 20

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Beta-hexosaminidase subunit beta (EC:3.2.1.52) 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: Beta-hexosaminidase subunit beta chain B Beta-hexosaminidase subunit beta chain A
Gene namesⁱ	Name:HEXB ORF Names:HCC7
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000049860.13
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4879 HEXB
MIMⁱ	606873 gene
neXtProtⁱ	NX_P07686

Keywords - Cellular componentⁱ

Lysosome

Pathology & Biotechⁱ

Involvement in diseaseⁱ

GM2-gangliosidosis 2 (GM2G2)10 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

Keywords - Diseaseⁱ

Disease mutation, Gangliosidosis, Neurodegeneration

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3074
MalaCards human disease database More...MalaCardsⁱ	HEXB
MIMⁱ	268800 phenotype
Orphanetⁱ	309169 Sandhoff disease, adult form 309155 Sandhoff disease, infantile form 309162 Sandhoff disease, juvenile form
PharmGKBⁱ	PA29257

Chemistry databases

ChEMBLⁱ	CHEMBL5877

ChEMBLⁱ

CHEMBL5877

Polymorphism and mutation databases

BioMutaⁱ	HEXB
DMDMⁱ	123081

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	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	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

N-linked glycans at Asn-142 and Asn-190 consist of Man₃-GlcNAc₂ and Man(5 to 7)-GlcNAc₂, respectively.3 Publications

The beta-A and beta-B chains are produced by proteolytic processing of the precursor beta chain.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	497	Not glycosylated1 Publication		1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDⁱ	P07686
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P07686
PaxDbⁱ	P07686
PeptideAtlas More...PeptideAtlasⁱ	P07686
PRIDEⁱ	P07686
ProteomicsDBⁱ	52022
TopDownProteomicsⁱ	P07686

2D gel databases

UCD-2DPAGEⁱ	P07686

UCD-2DPAGEⁱ

P07686

PTM databases

GlyConnectⁱ	1039
iPTMnetⁱ	P07686
PhosphoSitePlusⁱ	P07686
SwissPalmⁱ	P07686
UniCarbKBⁱ	P07686

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000049860 Expressed in 227 organ(s), highest expression level in placenta
CleanExⁱ	HS_HEXB
ExpressionAtlasⁱ	P07686 baseline and differential
Genevisibleⁱ	P07686 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA055409 HPA056010

HPAⁱ

HPA055409
HPA056010

Interactionⁱ

Subunit structureⁱ

There are 3 forms of beta-hexosaminidase: hexosaminidase A is a trimer composed of one subunit alpha, one subunit beta chain A and one subunit beta chain B; hexosaminidase B is a tetramer of two subunit beta chains A and two subunit beta chains B; hexosaminidase S is a homodimer of two alpha subunits. The two beta chains are derived from the cleavage of the beta subunit.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
HEXA	P06865	2	EBI-7133736,EBI-723519

With

Entry

#Exp.

IntAct

Notes

HEXA

P06865

2

EBI-7133736,EBI-723519

GO - Molecular functionⁱ

protein heterodimerization activity
Source: MGI
Inferred from direct assayⁱ
- 6230359
protein homodimerization activity
Source: MGI
Inferred from direct assayⁱ
- 6230359

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109323, 35 interactors
ComplexPortalⁱ	CPX-502 Beta-hexosaminidase A complex CPX-686 Beta-hexosaminidase B complex
CORUMⁱ	P07686
ELMⁱ	P07686
IntActⁱ	P07686, 13 interactors
Molecular INTeraction database More...MINTⁱ	P07686
STRINGⁱ	9606.ENSP00000261416

Chemistry databases

BindingDBⁱ

P07686

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	61 – 71	Combined sources	11
Helixⁱ	74 – 76	Combined sources	3
Beta strandⁱ	78 – 81	Combined sources	4
Beta strandⁱ	83 – 86	Combined sources	4
Helixⁱ	92 – 105	Combined sources	14
Beta strandⁱ	126 – 131	Combined sources	6
Beta strandⁱ	149 – 153	Combined sources	5
Beta strandⁱ	155 – 164	Combined sources	10
Helixⁱ	165 – 178	Combined sources	14
Beta strandⁱ	187 – 196	Combined sources	10
Beta strandⁱ	201 – 212	Combined sources	12
Helixⁱ	216 – 228	Combined sources	13
Beta strandⁱ	233 – 237	Combined sources	5
Helixⁱ	253 – 258	Combined sources	6
Beta strandⁱ	259 – 261	Combined sources	3
Beta strandⁱ	262 – 264	Combined sources	3
Helixⁱ	268 – 280	Combined sources	13
Beta strandⁱ	284 – 294	Combined sources	11
Helixⁱ	298 – 301	Combined sources	4
Beta strandⁱ	306 – 308	Combined sources	3
Beta strandⁱ	318 – 322	Combined sources	5
Helixⁱ	327 – 343	Combined sources	17
Beta strandⁱ	346 – 352	Combined sources	7
Helixⁱ	359 – 362	Combined sources	4
Helixⁱ	365 – 373	Combined sources	9
Helixⁱ	380 – 397	Combined sources	18
Beta strandⁱ	401 – 405	Combined sources	5
Helixⁱ	406 – 410	Combined sources	5
Beta strandⁱ	420 – 423	Combined sources	4
Helixⁱ	429 – 438	Combined sources	10
Beta strandⁱ	443 – 445	Combined sources	3
Helixⁱ	447 – 449	Combined sources	3
Beta strandⁱ	450 – 453	Combined sources	4
Beta strandⁱ	455 – 457	Combined sources	3
Helixⁱ	460 – 465	Combined sources	6
Helixⁱ	475 – 479	Combined sources	5
Beta strandⁱ	481 – 488	Combined sources	8
Helixⁱ	490 – 492	Combined sources	3
Turnⁱ	495 – 497	Combined sources	3
Helixⁱ	498 – 502	Combined sources	5
Helixⁱ	505 – 514	Combined sources	10
Helixⁱ	522 – 538	Combined sources	17
Beta strandⁱ	546 – 548	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P07686
SMRⁱ	P07686
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P07686

EvolutionaryTraceⁱ

P07686

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	KOG2499 Eukaryota COG3525 LUCA
HOGENOMⁱ	HOG000157972
HOVERGENⁱ	HBG005961
InParanoidⁱ	P07686
KEGG Orthology (KO) More...KOⁱ	K12373
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G04NA
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
Pfam protein domain database More...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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show all Align All

P07686-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MELCGLGLPR PPMLLALLLA TLLAAMLALL TQVALVVQVA EAARAPSVSA 
        60         70         80         90        100
KPGPALWPLP LSVKMTPNLL 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

Length:556

Mass (Da):63,111

Last modified:February 1, 1991 - v3

Checksum:ⁱB3A0A36594F62536

GO

Computationally mapped potential isoform sequencesⁱ

There are 5 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

Q5URX0	Q5URX0_HUMAN	Beta-hexosaminidase subunit beta Beta-hexosaminidase subunit beta (ENC-1AS) (Epididymis luminal protein 248) (Epididymis secretory protein Li 111)	HEXB HEL-248, HEL-S-111	331	Annotation score:
H0YA83	H0YA83_HUMAN	Beta-hexosaminidase subunit beta Beta-hexosaminidase subunit beta	HEXB	170	Annotation score:
H0Y9B6	H0Y9B6_HUMAN	Beta-hexosaminidase subunit beta Beta-hexosaminidase subunit beta	HEXB	202	Annotation score:
H0Y9M3	H0Y9M3_HUMAN	Beta-hexosaminidase subunit beta Beta-hexosaminidase subunit beta	HEXB	52	Annotation score:
D6REQ8	D6REQ8_HUMAN	Beta-hexosaminidase subunit beta Beta-hexosaminidase subunit beta	HEXB	35	Annotation score:

Sequence cautionⁱ

The sequence AAA51828 differs from that shown. Reason: Frameshift at position 21.Curated

The sequence AAA68620 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_003247	62	S → L in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs820878EnsemblClinVar.	1
Natural variantⁱVAR_003248	121	K → R. Corresponds to variant dbSNP:rs11556045EnsemblClinVar.	1
Natural variantⁱVAR_003249	207	I → V Probable polymorphism. 2 PublicationsCorresponds to variant dbSNP:rs10805890EnsemblClinVar.	1
Natural variantⁱVAR_011704	255	S → R in GM2G2. 1 Publication	1
Natural variantⁱVAR_003250	309	C → Y in GM2G2; adult type; severe. 1 Publication	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 Publication	1
Natural variantⁱVAR_011705	504	P → S in GM2G2. 1 Publication	1
Natural variantⁱVAR_003253	505	R → Q in GM2G2. 2 Publications	1
Natural variantⁱVAR_003254	534	C → Y in GM2G2; infantile type. 1 Publication	1
Natural variantⁱVAR_011706	543	A → T in GM2G2. 1 Publication	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M13519 mRNA Translation: AAA51828.1 Frameshift. M23294 M23293 Genomic DNA Translation: AAA52645.1 M19735 mRNA Translation: AAA68620.1 Different initiation. 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4022.1
PIRⁱ	A31250
NCBI Reference Sequences More...RefSeqⁱ	NP_000512.1, NM_000521.3 NP_001278933.1, NM_001292004.1
UniGeneⁱ	Hs.69293

Genome annotation databases

Ensemblⁱ	ENST00000261416; ENSP00000261416; ENSG00000049860
GeneIDⁱ	3074
KEGGⁱ	hsa:3074
UCSC genome browser More...UCSCⁱ	uc003kdf.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P07686	Beta-hexosaminidase		HUMAN		556	UniRef100_P07686
Beta-hexosaminidase subunit beta		HUMAN		35
Beta-hexosaminidase subunit beta		HUMAN		331
UPI00001E2D3F		HUMAN		515
UPI0000185C76		HUMAN		507
+3

Protein	Similar proteins		Species	Score	Length	Source
P07686	Beta-hexosaminidase		HUMAN		556	UniRef90_P07686
Beta-hexosaminidase		COLAP		557
Beta-hexosaminidase		PANTR		557
Beta-hexosaminidase		CERAT		557
Beta-hexosaminidase		PAPAN		557
+37

Protein	Similar proteins		Species	Score	Length	Source
P07686	Beta-hexosaminidase subunit beta		RAT		537	UniRef50_P07686
Beta-hexosaminidase		HUMAN		556
Beta-hexosaminidase		CERAT		557
Beta-hexosaminidase		COLAP		557
Beta-hexosaminidase		PANTR		557
+72

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M13519 mRNA Translation: AAA51828.1 Frameshift. M23294 M23293 Genomic DNA Translation: AAA52645.1 M19735 mRNA Translation: AAA68620.1 Different initiation. 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
UniGeneⁱ	Hs.69293

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
	1QBD	model	-	A	122-556	[»]
	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	[»]
ProteinModelPortalⁱ	P07686
SMRⁱ	P07686
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109323, 35 interactors
ComplexPortalⁱ	CPX-502 Beta-hexosaminidase A complex CPX-686 Beta-hexosaminidase B complex
CORUMⁱ	P07686
ELMⁱ	P07686
IntActⁱ	P07686, 13 interactors
MINTⁱ	P07686
STRINGⁱ	9606.ENSP00000261416

Chemistry databases

BindingDBⁱ	P07686
ChEMBLⁱ	CHEMBL5877

Protein family/group databases

CAZyⁱ	GH20 Glycoside Hydrolase Family 20

CAZyⁱ

GH20 Glycoside Hydrolase Family 20

PTM databases

GlyConnectⁱ	1039
iPTMnetⁱ	P07686
PhosphoSitePlusⁱ	P07686
SwissPalmⁱ	P07686
UniCarbKBⁱ	P07686

Polymorphism and mutation databases

BioMutaⁱ	HEXB
DMDMⁱ	123081

2D gel databases

UCD-2DPAGEⁱ	P07686

UCD-2DPAGEⁱ

P07686

Proteomic databases

EPDⁱ	P07686
MaxQBⁱ	P07686
PaxDbⁱ	P07686
PeptideAtlasⁱ	P07686
PRIDEⁱ	P07686
ProteomicsDBⁱ	52022
TopDownProteomicsⁱ	P07686

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	3074
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000261416; ENSP00000261416; ENSG00000049860
GeneIDⁱ	3074
KEGGⁱ	hsa:3074
UCSCⁱ	uc003kdf.4 human

Organism-specific databases

CTDⁱ	3074
DisGeNETⁱ	3074
EuPathDBⁱ	HostDB:ENSG00000049860.13
GeneCardsⁱ	HEXB
HGNCⁱ	HGNC:4879 HEXB
HPAⁱ	HPA055409 HPA056010
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
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2499 Eukaryota COG3525 LUCA
HOGENOMⁱ	HOG000157972
HOVERGENⁱ	HBG005961
InParanoidⁱ	P07686
KOⁱ	K12373
OrthoDBⁱ	EOG091G04NA
PhylomeDBⁱ	P07686
TreeFamⁱ	TF313036

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS00629-MONOMER
BRENDAⁱ	3.2.1.52 2681
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

Miscellaneous databases

ChiTaRSⁱ	HEXB human
EvolutionaryTraceⁱ	P07686
GeneWikiⁱ	HEXB
GenomeRNAiⁱ	3074
Protein Ontology More...PROⁱ	PR:P07686
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000049860 Expressed in 227 organ(s), highest expression level in placenta
CleanExⁱ	HS_HEXB
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
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
ProtoNetⁱ	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 1, 1991
	Last modified:	November 7, 2018
	This is version 203 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
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
Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM
Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P07686 (HEXB_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Beta-hexosaminidase subunit beta

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Lysosome

Extracellular region or secreted

Lysosome

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ