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UniProtKB - P07686 (HEXB_HUMAN)

Entry version 223 (23 Feb 2022)
Sequence version 4 (23 Feb 2022)
Previous versions | rss
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Protein

Beta-hexosaminidase subunit beta

Gene

HEXB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Addition of GM2A stimulates the hydrolysis of sulfated glycosphingolipid SM2 and the ganglioside GM2.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei355Proton donorBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processLipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.2.1.52, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P07686

Reactome - a knowledgebase of biological pathways and processes

More...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-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P07686

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P07686

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GH20, Glycoside Hydrolase Family 20

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
Beta-hexosaminidase subunit beta chain B
Beta-hexosaminidase subunit beta chain A
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HEXBImported
ORF Names:HCC7
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:4879, HEXB

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606873, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P07686

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000049860

<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

Keywords - Cellular componenti

Cytoplasmic vesicle, Lysosome

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

GM2-gangliosidosis 2 (GM2G2)10 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00324762L → S in GM2G2. 8 PublicationsCorresponds to variant dbSNP:rs820878EnsemblClinVar.1
Natural variantiVAR_011704255S → R in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs1554035829Ensembl.1
Natural variantiVAR_003250309C → Y in GM2G2; adult type; severe. 1 PublicationCorresponds to variant dbSNP:rs1554036641Ensembl.1
Natural variantiVAR_003251417P → L in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs28942073EnsemblClinVar.1
Natural variantiVAR_003252456Y → S in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907982EnsemblClinVar.1
Natural variantiVAR_011705504P → 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_003253505R → Q in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs121907983EnsemblClinVar.1
Natural variantiVAR_003254534C → Y in GM2G2; infantile type. 1 PublicationCorresponds to variant dbSNP:rs727503960Ensembl.1
Natural variantiVAR_011706543A → T in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907984EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi211R → K: Does not affect the native conformation of the isozyme A. Does not affect hydrolysis of GM2 ganglioside by the isozyme A. 1 Publication1

Keywords - Diseasei

Disease variant, Gangliosidosis, Neurodegeneration

Organism-specific databases

DisGeNET

More...DisGeNETi		3074

MalaCards human disease database

More...MalaCardsi		HEXB
MIMi268800, phenotype

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		309169, Sandhoff disease, adult form
309155, Sandhoff disease, infantile form
309162, Sandhoff disease, juvenile form

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29257

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P07686, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5877

Drug and drug target database

More...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

DrugCentral

More...DrugCentrali		P07686

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HEXB

Domain mapping of disease mutations (DMDM)

More...DMDMi		123081

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 42Sequence analysisAdd BLAST42
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000001200243 – 1212 PublicationsAdd BLAST79
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000012003122 – 556Beta-hexosaminidase subunit betaAdd BLAST435
ChainiPRO_0000012004122 – 311Beta-hexosaminidase subunit beta chain BAdd BLAST190
ChainiPRO_0000012005315 – 556Beta-hexosaminidase subunit beta chain AAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi84N-linked (GlcNAc...) asparagine2 Publications1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi91 ↔ 137
Glycosylationi142N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi190N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi309 ↔ 360
Glycosylationi327N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi534 ↔ 551

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei497Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-78
CPTAC-79

Encyclopedia of Proteome Dynamics

More...EPDi		P07686

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P07686

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P07686

MaxQB - The MaxQuant DataBase

More...MaxQBi		P07686

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P07686

PeptideAtlas

More...PeptideAtlasi		P07686

PRoteomics IDEntifications database

More...PRIDEi		P07686

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		52022

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P07686

2D gel databases

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P07686

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1039, 4 N-Linked glycans (3 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P07686, 7 sites, 13 N-linked glycans (4 sites), 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P07686

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P07686

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P07686

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P07686

<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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000049860, Expressed in placenta and 238 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P07686, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P07686, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000049860, Low tissue specificity

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		109323, 41 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-502, Beta-hexosaminidase A complex
CPX-686, Beta-hexosaminidase B complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P07686

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P07686

Protein interaction database and analysis system

More...IntActi		P07686, 36 interactors

Molecular INTeraction database

More...MINTi		P07686

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000261416

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P07686

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P07686, protein

<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

1556
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P07686

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P07686

<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

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2499, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_007082_0_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07686

Database of Orthologous Groups

More...OrthoDBi		545162at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P07686

TreeFam database of animal gene trees

More...TreeFami		TF313036

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.379.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

The PANTHER Classification System

More...PANTHERi		PTHR22600, PTHR22600, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00728, Glyco_hydro_20, 1 hit
PF14845, Glycohydro_20b2, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001093, B-hxosamndse_ab_euk, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00738, GLHYDRLASE20

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51445, SSF51445, 1 hit
SSF55545, SSF55545, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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 allAlign All

P07686-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:556
Mass (Da):63,137
Last modified:February 23, 2022 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2267BF1453EA50EF
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5URX0Q5URX0_HUMAN
Beta-N-acetylhexosaminidase
HEXB HEL-248, HEL-S-111
331Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YA83H0YA83_HUMAN
Beta-N-acetylhexosaminidase
HEXB
170Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y9B6H0Y9B6_HUMAN
Beta-N-acetylhexosaminidase
HEXB
202Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6REQ8D6REQ8_HUMAN
Beta-hexosaminidase subunit beta
HEXB
35Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y9M3H0Y9M3_HUMAN
Beta-hexosaminidase subunit beta
HEXB
52Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<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

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00324762L → S in GM2G2. 8 PublicationsCorresponds to variant dbSNP:rs820878EnsemblClinVar.1
Natural variantiVAR_003248121K → R. Corresponds to variant dbSNP:rs11556045EnsemblClinVar.1
Natural variantiVAR_003249207I → V2 PublicationsCorresponds to variant dbSNP:rs10805890EnsemblClinVar.1
Natural variantiVAR_011704255S → R in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs1554035829Ensembl.1
Natural variantiVAR_003250309C → Y in GM2G2; adult type; severe. 1 PublicationCorresponds to variant dbSNP:rs1554036641Ensembl.1
Natural variantiVAR_003251417P → L in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs28942073EnsemblClinVar.1
Natural variantiVAR_003252456Y → S in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907982EnsemblClinVar.1
Natural variantiVAR_011705504P → 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_003253505R → Q in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs121907983EnsemblClinVar.1
Natural variantiVAR_003254534C → Y in GM2G2; infantile type. 1 PublicationCorresponds to variant dbSNP:rs727503960Ensembl.1
Natural variantiVAR_011706543A → T in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs121907984EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M13519 mRNA Translation: AAA51828.1 Frameshift.
M23294 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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4022.1

Protein sequence database of the Protein Information Resource

More...PIRi		A31250

NCBI Reference Sequences

More...RefSeqi		NP_000512.1, NM_000521.3
NP_001278933.1, NM_001292004.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000261416; ENSP00000261416; ENSG00000049860

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3074

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3074

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000261416.12; ENSP00000261416.7; NM_000521.4; NP_000512.2

UCSC genome browser

More...UCSCi		uc003kdf.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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
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
CCDSiCCDS4022.1
PIRiA31250
RefSeqiNP_000512.1, NM_000521.3
NP_001278933.1, NM_001292004.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
1NOUX-ray2.40A/B50-556[»]
1NOWX-ray2.20A/B50-556[»]
1NP0X-ray2.50A/B50-556[»]
1O7AX-ray2.25A/B/C/D/E/F42-556[»]
2GJXX-ray2.80B/C/F/G50-556[»]
2GK1X-ray3.25B/D/F/H50-552[»]
3LMYX-ray2.80A/B1-556[»]
5BROX-ray2.40A43-556[»]
SMRiP07686
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi109323, 41 interactors
ComplexPortaliCPX-502, Beta-hexosaminidase A complex
CPX-686, Beta-hexosaminidase B complex
CORUMiP07686
ELMiP07686
IntActiP07686, 36 interactors
MINTiP07686
STRINGi9606.ENSP00000261416

Chemistry databases

BindingDBiP07686
ChEMBLiCHEMBL5877
DrugBankiDB03861, (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
DrugCentraliP07686

Protein family/group databases

CAZyiGH20, Glycoside Hydrolase Family 20

PTM databases

GlyConnecti1039, 4 N-Linked glycans (3 sites)
GlyGeniP07686, 7 sites, 13 N-linked glycans (4 sites), 1 O-linked glycan (1 site)
iPTMnetiP07686
MetOSiteiP07686
PhosphoSitePlusiP07686
SwissPalmiP07686

Genetic variation databases

BioMutaiHEXB
DMDMi123081

2D gel databases

UCD-2DPAGEiP07686

Proteomic databases

CPTACiCPTAC-78
CPTAC-79
EPDiP07686
jPOSTiP07686
MassIVEiP07686
MaxQBiP07686
PaxDbiP07686
PeptideAtlasiP07686
PRIDEiP07686
ProteomicsDBi52022
TopDownProteomicsiP07686

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		24338, 266 antibodies from 34 providers

The DNASU plasmid repository

More...DNASUi		3074

Genome annotation databases

EnsembliENST00000261416; ENSP00000261416; ENSG00000049860
GeneIDi3074
KEGGihsa:3074
MANE-SelectiENST00000261416.12; ENSP00000261416.7; NM_000521.4; NP_000512.2
UCSCiuc003kdf.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3074
DisGeNETi3074

GeneCards: human genes, protein and diseases

More...GeneCardsi		HEXB
HGNCiHGNC:4879, HEXB
HPAiENSG00000049860, Low tissue specificity
MalaCardsiHEXB
MIMi268800, phenotype
606873, gene
neXtProtiNX_P07686
Orphaneti309169, Sandhoff disease, adult form
309155, Sandhoff disease, infantile form
309162, Sandhoff disease, juvenile form
PharmGKBiPA29257
VEuPathDBiHostDB:ENSG00000049860

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2499, Eukaryota
HOGENOMiCLU_007082_0_3_1
InParanoidiP07686
OrthoDBi545162at2759
PhylomeDBiP07686
TreeFamiTF313036

Enzyme and pathway databases

BRENDAi3.2.1.52, 2681
PathwayCommonsiP07686
ReactomeiR-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-RKiP07686
SignaLinkiP07686

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		3074, 5 hits in 1045 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		HEXB, human
EvolutionaryTraceiP07686

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HEXB

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		3074
PharosiP07686, Tchem

Protein Ontology

More...PROi		PR:P07686
RNActiP07686, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000049860, Expressed in placenta and 238 other tissues
ExpressionAtlasiP07686, baseline and differential
GenevisibleiP07686, HS

Family and domain databases

Gene3Di3.30.379.10, 1 hit
InterProiView 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
PANTHERiPTHR22600, PTHR22600, 1 hit
PfamiView protein in Pfam
PF00728, Glyco_hydro_20, 1 hit
PF14845, Glycohydro_20b2, 1 hit
PIRSFiPIRSF001093, B-hxosamndse_ab_euk, 1 hit
PRINTSiPR00738, GLHYDRLASE20
SUPFAMiSSF51445, SSF51445, 1 hit
SSF55545, SSF55545, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHEXB_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07686
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human entries with genetic variants
    List of human entries with genetic variants
  4. Human variants curated from literature reports
    Index of human variants curated from literature reports
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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