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P07686 (HEXB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:HEXB
ORF Names:HCC7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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.

Subcellular location

Lysosome.

Post-translational modification

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

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

Involvement in disease

GM2-gangliosidosis 2 (GM2G2) [MIM:268800]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. Clinically indistinguishable from GM2-gangliosidosis type 1, presenting startle reactions, early blindness, progressive motor and mental deterioration, macrocephaly and cherry-red spots on the macula.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Sequence caution

The sequence AAA51828.1 differs from that shown. Reason: Frameshift at position 21.

The sequence AAA68620.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Gangliosidosis
Neurodegeneration
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processastrocyte cell migration

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Inferred from electronic annotation. Source: Ensembl

chondroitin sulfate catabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

ganglioside catabolic process

Inferred from electronic annotation. Source: Ensembl

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

glycosphingolipid metabolic process

Traceable author statement. Source: Reactome

hyaluronan catabolic process

Traceable author statement. Source: Reactome

hyaluronan metabolic process

Traceable author statement. Source: Reactome

keratan sulfate catabolic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

lipid storage

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

lysosome organization

Inferred from electronic annotation. Source: Ensembl

male courtship behavior

Inferred from electronic annotation. Source: Ensembl

myelination

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

oligosaccharide catabolic process

Inferred from electronic annotation. Source: Ensembl

oogenesis

Inferred from electronic annotation. Source: Ensembl

penetration of zona pellucida

Inferred from electronic annotation. Source: Ensembl

phospholipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

lysosomal lumen

Traceable author statement. Source: Reactome

membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbeta-N-acetylhexosaminidase activity

Traceable author statement PubMed 8663217. Source: ProtInc

protein heterodimerization activity

Inferred from direct assay PubMed 6230359. Source: MGI

protein homodimerization activity

Inferred from direct assay PubMed 6230359. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 Potential
Propeptide43 – 12179
PRO_0000012002
Chain122 – 556435Beta-hexosaminidase subunit beta
PRO_0000012003
Chain122 – 311190Beta-hexosaminidase subunit beta chain B
PRO_0000012004
Chain315 – 556242Beta-hexosaminidase subunit beta chain A
PRO_0000012005

Sites

Active site3551Proton donor By similarity
Site4971Not glycosylated (PubMed:11447134)

Amino acid modifications

Glycosylation841N-linked (GlcNAc...) Ref.17 Ref.18
Glycosylation1421N-linked (GlcNAc...) Ref.17
Glycosylation1901N-linked (GlcNAc...) Ref.17
Glycosylation3231N-linked (GlcNAc...) Ref.18
Glycosylation3271N-linked (GlcNAc...) Ref.16 Ref.17 Ref.18
Disulfide bond91 ↔ 137 Ref.17 Ref.21 Ref.22
Disulfide bond309 ↔ 360 Ref.17 Ref.21 Ref.22
Disulfide bond534 ↔ 551 Ref.17 Ref.21 Ref.22

Natural variations

Natural variant621S → L in GM2G2. Ref.29
Corresponds to variant rs820878 [ dbSNP | Ensembl ].
VAR_003247
Natural variant1211K → R.
Corresponds to variant rs11556045 [ dbSNP | Ensembl ].
VAR_003248
Natural variant2071I → V Probable polymorphism. Ref.24 Ref.30
Corresponds to variant rs10805890 [ dbSNP | Ensembl ].
VAR_003249
Natural variant2551S → R in GM2G2. Ref.32
VAR_011704
Natural variant3091C → Y in GM2G2; adult type; severe; almost complete absence of activity. Ref.28
VAR_003250
Natural variant4171P → L in GM2G2. Ref.25 Ref.28
Corresponds to variant rs28942073 [ dbSNP | Ensembl ].
VAR_003251
Natural variant4561Y → S in GM2G2. Ref.24
VAR_003252
Natural variant5041P → S in GM2G2. Ref.33
VAR_011705
Natural variant5051R → Q in GM2G2. Ref.26 Ref.30
VAR_003253
Natural variant5341C → Y in GM2G2; infantile type. Ref.27
VAR_003254
Natural variant5431A → T in GM2G2. Ref.31
VAR_011706

Secondary structure

................................................................................. 556
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07686 [UniParc].

Last modified February 1, 1991. Version 3.
Checksum: B3A0A36594F62536

FASTA55663,111
        10         20         30         40         50         60 
MELCGLGLPR PPMLLALLLA TLLAAMLALL TQVALVVQVA EAARAPSVSA KPGPALWPLP 

        70         80         90        100        110        120 
LSVKMTPNLL HLAPENFYIS HSPNSTAGPS CTLLEEAFRR YHGYIFGFYK WHHEPAEFQA 

       130        140        150        160        170        180 
KTQVQQLLVS ITLQSECDAF PNISSDESYT LLVKEPVAVL KANRVWGALR GLETFSQLVY 

       190        200        210        220        230        240 
QDSYGTFTIN ESTIIDSPRF SHRGILIDTS RHYLPVKIIL KTLDAMAFNK FNVLHWHIVD 

       250        260        270        280        290        300 
DQSFPYQSIT FPELSNKGSY SLSHVYTPND VRMVIEYARL RGIRVLPEFD TPGHTLSWGK 

       310        320        330        340        350        360 
GQKDLLTPCY SRQNKLDSFG PINPTLNTTY SFLTTFFKEI SEVFPDQFIH LGGDEVEFKC 

       370        380        390        400        410        420 
WESNPKIQDF MRQKGFGTDF KKLESFYIQK VLDIIATINK GSIVWQEVFD DKAKLAPGTI 

       430        440        450        460        470        480 
VEVWKDSAYP EELSRVTASG FPVILSAPWY LDLISYGQDW RKYYKVEPLD FGGTQKQKQL 

       490        500        510        520        530        540 
FIGGEACLWG EYVDATNLTP RLWPRASAVG ERLWSSKDVR DMDDAYDRLT RHRCRMVERG 

       550 
IAAQPLYAGY CNHENM 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of cDNA clones coding for the alpha-subunit of human beta-hexosaminidase. Extensive homology between the alpha- and beta-subunits and studies on Tay-Sachs disease."
Korneluk R.G., Mahuran D.J., Neote K., Klavins M.H., O'Dowd B.F., Tropak M., Willard H.F., Anderson M.-J., Lowden J.A., Gravel R.A.
J. Biol. Chem. 261:8407-8413(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of the human HEXB gene encoding lysosomal beta-hexosaminidase."
Neote K., Bapat B., Dumbrille-Ross A., Troxel C., Schuster S.M., Mahuran D.J., Gravel R.A.
Genomics 3:279-286(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Gene encoding the human beta-hexosaminidase beta chain: extensive homology of intron placement in the alpha- and beta-chain genes."
Proia R.L.
Proc. Natl. Acad. Sci. U.S.A. 85:1883-1887(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Identification of a new proto-oncogene in human cancers."
Kim J.W.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[8]"Synthesis and assembly of a catalytically active lysosomal enzyme, beta-hexosaminidase B, in a cell-free system."
Sonderfeld-Fresko S., Proia R.L.
J. Biol. Chem. 263:13463-13469(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-67.
[9]"Translation initiation in the HEXB gene encoding the beta-subunit of human beta-hexosaminidase."
Neote K., Brown C.A., Mahuran D.J., Gravel R.A.
J. Biol. Chem. 265:20799-20806(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
[10]"Localization of the pro-sequence within the total deduced primary structure of human beta-hexosaminidase B."
Stirling J., Leung A., Gravel R.A., Mahuran D.
FEBS Lett. 231:47-50(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 43-57 AND 122-151.
[11]"Characterization of human placental beta-hexosaminidase I2. Proteolytic processing intermediates of hexosaminidase A."
Mahuran D.J.
J. Biol. Chem. 265:6794-6799(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-54 AND 315-324.
[12]"The amino-terminal sequences in the pro-alpha and -beta polypeptides of human lysosomal beta-hexosaminidase A and B are retained in the mature isozymes."
Hubbes M., Callahan J., Gravel R., Mahuran D.
FEBS Lett. 249:316-320(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 50-59.
[13]"Proteolytic processing of pro-alpha and pro-beta precursors from human beta-hexosaminidase. Generation of the mature alpha and beta a beta b subunits."
Mahuran D.J., Neote K., Klavins M.H., Leung A., Gravel R.A.
J. Biol. Chem. 263:4612-4618(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 122-151 AND 315-340.
[14]"Isolation of cDNA clones coding for the beta subunit of human beta-hexosaminidase."
O'Dowd B.F., Quan F., Willard H.F., Lamhonwah A.-M., Korneluk R.G., Lowden J.A., Gravel R.A., Mahuran D.J.
Proc. Natl. Acad. Sci. U.S.A. 82:1184-1188(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-283.
[15]"Oligosaccharide structure and amino acid sequence of the major glycopeptides of mature human beta-hexosaminidase."
O'Dowd B.F., Cumming D.A., Gravel R.A., Mahuran D.J.
Biochemistry 27:5216-5226(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[16]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-327.
[17]"Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS."
Schuette C.G., Weisgerber J., Sandhoff K.
Glycobiology 11:549-556(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, GLYCOSYLATION AT ASN-84; ASN-142; ASN-190 AND ASN-327.
[18]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-323 AND ASN-327.
Tissue: Liver.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease."
Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S., Vorgias C.E.
Nat. Struct. Biol. 3:638-648(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[21]"Crystal structure of human beta-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease."
Mark B.L., Mahuran D.J., Cherney M.M., Zhao D., Knapp S., James M.N.
J. Mol. Biol. 327:1093-1109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 50-556, DISULFIDE BONDS.
[22]"The X-ray crystal structure of human beta-hexosaminidase B provides new insights into Sandhoff disease."
Maier T., Strater N., Schuette C.G., Klingenstein R., Sandhoff K., Saenger W.
J. Mol. Biol. 328:669-681(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 42-556, DISULFIDE BONDS.
[23]"The biochemistry of HEXA and HEXB gene mutations causing GM2 gangliosidosis."
Mahuran D.J.
Biochim. Biophys. Acta 1096:87-94(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[24]"Molecular basis of an adult form of beta-hexosaminidase B deficiency with motor neuron disease."
Banerjee P., Siciliano L., Oliveri D., McCabe N.R., Boyers M.J., Horwitz A.L., Li S.-C., Dawson G.
Biochem. Biophys. Res. Commun. 181:108-115(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 SER-456, VARIANT VAL-207.
[25]"A novel exon mutation in the human beta-hexosaminidase beta subunit gene affects 3' splice site selection."
Wakamatsu N., Kobayashi H., Miyatake T., Tsuji S.
J. Biol. Chem. 267:2406-2413(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 LEU-417.
[26]"Molecular basis of an adult form of Sandhoff disease: substitution of glutamine for arginine at position 505 of the beta-chain of beta-hexosaminidase results in a labile enzyme."
Bolhuis P.A., Ponne N.J., Bikker H., Baas F., Vianney de Jong J.M.B.
Biochim. Biophys. Acta 1182:142-146(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 GLN-505.
[27]"A novel missense mutation (C522Y) is present in the beta-hexosaminidase beta-subunit gene of a Japanese patient with infantile Sandhoff disease."
Kuroki Y., Itoh K., Nadaoka Y., Tanaka T., Sakuraba H.
Biochem. Biophys. Res. Commun. 212:564-571(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 TYR-534.
[28]"A common beta hexosaminidase gene mutation in adult Sandhoff disease patients."
Gomez-Lira M., Sangalli A., Mottes M., Perusi C., Pignatti P.F., Rizzuto N., Salviati A.
Hum. Genet. 96:417-422(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GM2G2 TYR-309 AND LEU-417.
[29]"A second, large deletion in the HEXB gene in a patient with infantile Sandhoff disease."
Zhang Z.-X., Wakamatsu N., Akerman B.R., Mules E.H., Thomas G.H., Gravel R.A.
Hum. Mol. Genet. 4:777-780(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 LEU-62.
[30]"Significance of two point mutations present in each HEXB allele of patients with adult GM2 gangliosidosis (Sandhoff disease) homozygosity for the Ile207-->Val substitution is not associated with a clinical or biochemical phenotype."
Redonnet-Vernhet I., Mahuran D.J., Salvayre R., Dubas F., Levade T.
Biochim. Biophys. Acta 1317:127-133(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 GLN-505, VARIANT VAL-207.
[31]"Molecular basis of heat labile hexosaminidase B among Jews and Arabs."
Narkis G., Adam A., Jaber L., Pennybacker M., Proia R.L., Navon R.
Hum. Mutat. 10:424-429(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 THR-543.
[32]"Two mutations remote from an exon/intron junction in the beta-hexosaminidase beta-subunit gene affect 3'-splice site selection and cause Sandhoff disease."
Fujimaru M., Tanaka A., Choeh K., Wakamatsu N., Sakuraba H., Isshiki G.
Hum. Genet. 103:462-469(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 ARG-255.
[33]"A Pro504 --> Ser substitution in the beta-subunit of beta-hexosaminidase A inhibits alpha-subunit hydrolysis of GM2 ganglioside, resulting in chronic Sandhoff disease."
Hou Y., McInnes B., Hinek A., Karpati G., Mahuran D.
J. Biol. Chem. 273:21386-21392(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GM2G2 SER-504.
+Additional computationally mapped references.

Web resources

HEXBdb

HEXB mutation database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13519 mRNA. Translation: AAA51828.1. Frameshift.
M23294 expand/collapse EMBL AC list , 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.
PIRA31250.
RefSeqNP_000512.1. NM_000521.3.
UniGeneHs.69293.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
1QBDmodel-A122-556[»]
2GJXX-ray2.80B/C/F/G50-556[»]
2GK1X-ray3.25B/D/F/H50-552[»]
3LMYX-ray2.80A/B1-556[»]
ProteinModelPortalP07686.
SMRP07686. Positions 54-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109323. 20 interactions.
IntActP07686. 1 interaction.
MINTMINT-4528380.
STRING9606.ENSP00000261416.

Chemistry

BindingDBP07686.
ChEMBLCHEMBL5877.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

PTM databases

PhosphoSiteP07686.

Polymorphism databases

DMDM123081.

2D gel databases

UCD-2DPAGEP07686.

Proteomic databases

PaxDbP07686.
PeptideAtlasP07686.
PRIDEP07686.

Protocols and materials databases

DNASU3074.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261416; ENSP00000261416; ENSG00000049860.
GeneID3074.
KEGGhsa:3074.
UCSCuc003kdd.3. human.

Organism-specific databases

CTD3074.
GeneCardsGC05P073935.
HGNCHGNC:4879. HEXB.
HPAHPA055409.
HPA056010.
MIM268800. phenotype.
606873. gene.
neXtProtNX_P07686.
Orphanet309169. Sandhoff disease, adult form.
309155. Sandhoff disease, infantile form.
309162. Sandhoff disease, juvenile form.
PharmGKBPA29257.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3525.
HOGENOMHOG000157972.
HOVERGENHBG005961.
InParanoidP07686.
KOK12373.
OrthoDBEOG7KDFB6.
PhylomeDBP07686.
TreeFamTF313036.

Enzyme and pathway databases

BioCycMetaCyc:HS00629-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP07686.

Gene expression databases

ArrayExpressP07686.
BgeeP07686.
CleanExHS_HEXB.
GenevestigatorP07686.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

ChiTaRSHEXB. human.
EvolutionaryTraceP07686.
GeneWikiHEXB.
GenomeRNAi3074.
NextBio12159.
PROP07686.
SOURCESearch...

Entry information

Entry nameHEXB_HUMAN
AccessionPrimary (citable) accession number: P07686
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

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