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Reviewed, UniProtKB/Swiss-Prot P20060 (HEXB_MOUSE)

Last modified November 3, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-hexosaminidase subunit beta
    EC=3.2.1.52
Alternative name(s):
    N-acetyl-beta-glucosaminidase subunit beta
    Beta-N-acetylhexosaminidase subunit beta
      Short name=Hexosaminidase subunit B
Gene names
Name: Hexb
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcellular calcium ion homeostasis

Inferred from genetic interaction. Source: MGI

cellular protein metabolic process

Inferred from mutant phenotype. Source: MGI

ganglioside catabolic process

Inferred from mutant phenotype. Source: MGI

glycosaminoglycan metabolic process

Inferred from genetic interaction. Source: MGI

lipid storage

Inferred from mutant phenotype. Source: MGI

locomotory behavior

Inferred from mutant phenotype. Source: MGI

lysosome organization

Inferred from mutant phenotype. Source: MGI

male courtship behavior

Inferred from mutant phenotype. Source: MGI

myelination

Inferred from genetic interaction. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype. Source: MGI

oligosaccharide catabolic process

Inferred from mutant phenotype. Source: MGI

oogenesis

Inferred from mutant phenotype. Source: MGI

penetration of zona pellucida

Inferred from mutant phenotype. Source: MGI

phospholipid biosynthetic process

Inferred from mutant phenotype. Source: MGI

regulation of cellular metabolic process

Inferred from mutant phenotype. Source: MGI

sensory perception of sound

Inferred from genetic interaction. Source: MGI

skeletal system development

Inferred from genetic interaction. Source: MGI

   Cellular componentacrosomal vesicle

Inferred from direct assay. Source: MGI

lysosome

Inferred from direct assay. Source: MGI

membrane

Inferred from direct assay. Source: MGI

   Molecular functionbeta-N-acetylhexosaminidase activity

Inferred from direct assay. Source: MGI

cation binding

Inferred from electronic annotation. Source: InterPro

protein homodimerization activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 536505Beta-hexosaminidase subunit beta
PRO_0000012006

Sites

Active site3341Proton donor By similarity

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation3061N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 116 By similarity
Disulfide bond288 ↔ 339 By similarity
Disulfide bond513 ↔ 530 By similarity

Sequences

Sequence LengthMass (Da)Tools
P20060-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 579BBEEE9CB508BC

FASTA53661,116
        10         20         30         40         50         60 
MPQSPRSAPG LLLLQALVSL VSLALVAPAR LQPALWPFPR SVQMFPRLLY ISAEDFSIDH 

        70         80         90        100        110        120 
SPNSTAGPSC SLLQEAFRRY YNYVFGFYKR HHGPARFRAE PQLQKLLVSI TLESECESFP 

       130        140        150        160        170        180 
SLSSDETYSL LVQEPVAVLK ANSVWGALRG LETFSQLVYQ DSFGTFTINE SSIADSPRFP 

       190        200        210        220        230        240 
HRGILIDTSR HFLPVKTILK TLDAMAFNKF NVLHWHIVDD QSFPYQSTTF PELSNKGSYS 

       250        260        270        280        290        300 
LSHVYTPNDV RMVLEYARLR GIRVIPEFDT PGHTQSWGKG QKNLLTPCYN QKTKTQVFGP 

       310        320        330        340        350        360 
VDPTVNTTYA FFNTFFKEIS SVFPDQFIHL GGDEVEFQCW ASNPNIQGFM KRKGFGSDFR 

       370        380        390        400        410        420 
RLESFYIKKI LEIISSLKKN SIVWQEVFDD KVELQPGTVV EVWKSEHYSY ELKQVTGSGF 

       430        440        450        460        470        480 
PAILSAPWYL DLISYGQDWK NYYKVEPLNF EGSEKQKQLV IGGEACLWGE FVDATNLTPR 

       490        500        510        520        530 
LWPRASAVGE RLWSPKTVTD LENAYKRLAV HRCRMVSRGI AAQPLYTGYC NYENKI 

« Hide

References

[1]"Cloning and sequence analysis of a cDNA encoding the beta-subunit of mouse beta-hexosaminidase."
Bapat B., Ethier M., Neote K., Mahuran D., Gravel R.A.
FEBS Lett. 237:191-195(1988) [PubMed: 2971567] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure and expression of the mouse beta-hexosaminidase genes, Hexa and Hexb."
Yamanaka S., Johnson O.N., Norflus F., Boles D.J., Proia R.L.
Genomics 21:588-596(1994) [PubMed: 7959736] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6 X CBA.
Tissue: Liver.
[3]"Characterization of the murine beta-hexosaminidase (HEXB) gene."
Triggs-Raine B.L., Benoit G., Salo T.J., Trasler J.M., Gravel R.A.
Biochim. Biophys. Acta 1227:79-86(1994) [PubMed: 7918686] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
+Additional computationally mapped references.

Cross-references

Sequence databases

Y00964 mRNA. Translation: CAA68781.1.
U07633 mRNA. Translation: AAA18776.1.
U07049 expand/collapse EMBL AC list , U07036, U07037, U07038, U07039, U07040, U07041, U07042, U07043, U07044, U07045, U07046, U07047, U07048 Genomic DNA. Translation: AAA74738.1.
U07742 expand/collapse EMBL AC list , U07722, U07723, U07724, U07725, U07726, U07727, U07728, U07737, U07738, U07739, U07740, U07741 Genomic DNA. Translation: AAB60667.1.
IPIIPI00115530.
PIRB54745.
RefSeqNP_034552.1.
UniGeneMm.27816

3D structure databases

HSSPHSSP built from PDB template 1NOW based on UniProtKB P07686.
SMRP20060. Positions 34-531.
ModBaseSearch...

Protein-protein interaction databases

STRINGP20060.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PRIDEP20060.

Genome annotation databases

EnsemblENSMUST00000022169; ENSMUSP00000022169; ENSMUSG00000021665; Mus musculus. [Genome view]
GeneID15212.
KEGGmmu:15212.
UCSCuc007roc.1. mouse.

Organism-specific databases

CTD15212.
MGIMGI:96074. Hexb.

Phylogenomic databases

HOGENOMP20060.
HOVERGENP20060.
OMAPWYLDWI.

Enzyme and pathway databases

BRENDA3.2.1.52. 244.

Gene expression databases

ArrayExpressP20060.
BgeeP20060.
CleanExMM_HEXB.
GenevestigatorP20060.
GermOnlineENSMUSG00000021665. Mus musculus.

Family and domain databases

InterProIPR001540. Glyco_hydro_20.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_sg_catalytic.
IPR015882. HexNAc-like_b.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR22600. Glyco_hydro_20. 1 hit.
PfamPF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSPR00738. GLHYDRLASE20.
ProtoNetSearch...

Other Resources

NextBio287781.
SOURCESearch...

Entry information

Entry nameHEXB_MOUSE
AccessionPrimary (citable) accession number: P20060
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: November 3, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents