Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-hexosaminidase subunit beta

Gene

HEXB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei355Proton donorBy similarity1

GO - Molecular functioni

  • acetylglucosaminyltransferase activity Source: UniProtKB
  • beta-N-acetylhexosaminidase activity Source: Reactome
  • N-acetyl-beta-D-galactosaminidase activity Source: UniProtKB-EC
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:HS00629-MONOMER
BRENDAi3.2.1.52 2681
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

Protein family/group databases

CAZyiGH20 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:
Gene namesi
Name:HEXB
ORF Names:HCC7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000049860.13
HGNCiHGNC:4879 HEXB
MIMi606873 gene
neXtProtiNX_P07686

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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.
See also OMIM:268800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00324762S → L in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs820878EnsemblClinVar.1
Natural variantiVAR_011704255S → R in GM2G2. 1 Publication1
Natural variantiVAR_003250309C → Y in GM2G2; adult type; severe. 1 Publication1
Natural variantiVAR_003251417P → L in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs28942073EnsemblClinVar.1
Natural variantiVAR_003252456Y → S in GM2G2. 1 Publication1
Natural variantiVAR_011705504P → S in GM2G2. 1 Publication1
Natural variantiVAR_003253505R → Q in GM2G2. 2 Publications1
Natural variantiVAR_003254534C → Y in GM2G2; infantile type. 1 Publication1
Natural variantiVAR_011706543A → T in GM2G2. 1 Publication1

Keywords - Diseasei

Disease mutation, Gangliosidosis, Neurodegeneration

Organism-specific databases

DisGeNETi3074
MalaCardsiHEXB
MIMi268800 phenotype
Orphaneti309169 Sandhoff disease, adult form
309155 Sandhoff disease, infantile form
309162 Sandhoff disease, juvenile form
PharmGKBiPA29257

Chemistry databases

ChEMBLiCHEMBL5877

Polymorphism and mutation databases

BioMutaiHEXB
DMDMi123081

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 42Sequence analysisAdd BLAST42
PropeptideiPRO_000001200243 – 1212 PublicationsAdd BLAST79
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
Glycosylationi84N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi91 ↔ 137
Glycosylationi142N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi190N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi309 ↔ 360
Glycosylationi323N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi327N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi534 ↔ 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 keyPosition(s)DescriptionActionsGraphical viewLength
Sitei497Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP07686
MaxQBiP07686
PaxDbiP07686
PeptideAtlasiP07686
PRIDEiP07686
ProteomicsDBi52022
TopDownProteomicsiP07686

2D gel databases

UCD-2DPAGEiP07686

PTM databases

iPTMnetiP07686
PhosphoSitePlusiP07686
SwissPalmiP07686
UniCarbKBiP07686

Expressioni

Gene expression databases

BgeeiENSG00000049860
CleanExiHS_HEXB
ExpressionAtlasiP07686 baseline and differential
GenevisibleiP07686 HS

Organism-specific databases

HPAiHPA055409
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

WithEntry#Exp.IntActNotes
HEXAP068652EBI-7133736,EBI-723519

GO - Molecular functioni

  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi109323, 35 interactors
ComplexPortaliCPX-502 Beta-hexosaminidase A complex
CPX-686 Beta-hexosaminidase B complex
CORUMiP07686
ELMiP07686
IntActiP07686, 13 interactors
MINTiP07686
STRINGi9606.ENSP00000261416

Chemistry databases

BindingDBiP07686

Structurei

Secondary structure

1556
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 71Combined sources11
Helixi74 – 76Combined sources3
Beta strandi78 – 81Combined sources4
Beta strandi83 – 86Combined sources4
Helixi92 – 105Combined sources14
Beta strandi126 – 131Combined sources6
Beta strandi149 – 153Combined sources5
Beta strandi155 – 164Combined sources10
Helixi165 – 178Combined sources14
Beta strandi187 – 196Combined sources10
Beta strandi201 – 212Combined sources12
Helixi216 – 228Combined sources13
Beta strandi233 – 237Combined sources5
Helixi253 – 258Combined sources6
Beta strandi259 – 261Combined sources3
Beta strandi262 – 264Combined sources3
Helixi268 – 280Combined sources13
Beta strandi284 – 294Combined sources11
Helixi298 – 301Combined sources4
Beta strandi306 – 308Combined sources3
Beta strandi318 – 322Combined sources5
Helixi327 – 343Combined sources17
Beta strandi346 – 352Combined sources7
Helixi359 – 362Combined sources4
Helixi365 – 373Combined sources9
Helixi380 – 397Combined sources18
Beta strandi401 – 405Combined sources5
Helixi406 – 410Combined sources5
Beta strandi420 – 423Combined sources4
Helixi429 – 438Combined sources10
Beta strandi443 – 445Combined sources3
Helixi447 – 449Combined sources3
Beta strandi450 – 453Combined sources4
Beta strandi455 – 457Combined sources3
Helixi460 – 465Combined sources6
Helixi475 – 479Combined sources5
Beta strandi481 – 488Combined sources8
Helixi490 – 492Combined sources3
Turni495 – 497Combined sources3
Helixi498 – 502Combined sources5
Helixi505 – 514Combined sources10
Helixi522 – 538Combined sources17
Beta strandi546 – 548Combined sources3

3D structure databases

ProteinModelPortaliP07686
SMRiP07686
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07686

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2499 Eukaryota
COG3525 LUCA
HOGENOMiHOG000157972
HOVERGENiHBG005961
InParanoidiP07686
KOiK12373
OrthoDBiEOG091G04NA
PhylomeDBiP07686
TreeFamiTF313036

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
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

Sequencei

Sequence statusi: Complete.

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

P07686-1 [UniParc]FASTAAdd 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

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 keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00324762S → L in GM2G2. 1 PublicationCorresponds to variant dbSNP:rs820878EnsemblClinVar.1
Natural variantiVAR_003248121K → R. Corresponds to variant dbSNP:rs11556045EnsemblClinVar.1
Natural variantiVAR_003249207I → V Probable polymorphism. 2 PublicationsCorresponds to variant dbSNP:rs10805890EnsemblClinVar.1
Natural variantiVAR_011704255S → R in GM2G2. 1 Publication1
Natural variantiVAR_003250309C → Y in GM2G2; adult type; severe. 1 Publication1
Natural variantiVAR_003251417P → L in GM2G2. 2 PublicationsCorresponds to variant dbSNP:rs28942073EnsemblClinVar.1
Natural variantiVAR_003252456Y → S in GM2G2. 1 Publication1
Natural variantiVAR_011705504P → S in GM2G2. 1 Publication1
Natural variantiVAR_003253505R → Q in GM2G2. 2 Publications1
Natural variantiVAR_003254534C → Y in GM2G2; infantile type. 1 Publication1
Natural variantiVAR_011706543A → T in GM2G2. 1 Publication1

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 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
CCDSiCCDS4022.1
PIRiA31250
RefSeqiNP_000512.1, NM_000521.3
NP_001278933.1, NM_001292004.1
UniGeneiHs.69293

Genome annotation databases

EnsembliENST00000261416; ENSP00000261416; ENSG00000049860
GeneIDi3074
KEGGihsa:3074
UCSCiuc003kdf.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiHEXB_HUMAN
AccessioniPrimary (citable) accession number: P07686
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1991
Last modified: July 18, 2018
This is version 200 of the entry and version 3 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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 polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health