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P07686

- HEXB_HUMAN

UniProt

P07686 - HEXB_HUMAN

Protein

Beta-hexosaminidase subunit beta

Gene

HEXB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (01 Feb 1991)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei355 – 3551Proton donorBy similarity
    Sitei497 – 4971Not glycosylated (PubMed:11447134)1 Publication

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: ProtInc
    2. protein heterodimerization activity Source: MGI
    3. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. astrocyte cell migration Source: Ensembl
    2. carbohydrate metabolic process Source: Reactome
    3. cell death Source: UniProtKB-KW
    4. cellular calcium ion homeostasis Source: Ensembl
    5. cellular protein metabolic process Source: Ensembl
    6. chondroitin sulfate catabolic process Source: Reactome
    7. chondroitin sulfate metabolic process Source: Reactome
    8. ganglioside catabolic process Source: Ensembl
    9. glycosaminoglycan metabolic process Source: Reactome
    10. glycosphingolipid metabolic process Source: Reactome
    11. hyaluronan catabolic process Source: Reactome
    12. hyaluronan metabolic process Source: Reactome
    13. keratan sulfate catabolic process Source: Reactome
    14. keratan sulfate metabolic process Source: Reactome
    15. lipid storage Source: Ensembl
    16. locomotory behavior Source: Ensembl
    17. lysosome organization Source: Ensembl
    18. male courtship behavior Source: Ensembl
    19. myelination Source: Ensembl
    20. neuromuscular process controlling balance Source: Ensembl
    21. oligosaccharide catabolic process Source: Ensembl
    22. oogenesis Source: Ensembl
    23. penetration of zona pellucida Source: Ensembl
    24. phospholipid biosynthetic process Source: Ensembl
    25. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    26. regulation of cell shape Source: Ensembl
    27. sensory perception of sound Source: Ensembl
    28. skeletal system development Source: Ensembl
    29. small molecule metabolic process Source: Reactome
    30. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00629-MONOMER.
    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    REACT_120888. CS/DS degradation.
    REACT_120996. Hyaluronan uptake and degradation.
    REACT_121313. Keratan sulfate degradation.
    SABIO-RKP07686.

    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
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4879. HEXB.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. lysosomal lumen Source: Reactome
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    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.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621S → L in GM2G2. 1 Publication
    Corresponds to variant rs820878 [ dbSNP | Ensembl ].
    VAR_003247
    Natural varianti255 – 2551S → R in GM2G2. 1 Publication
    VAR_011704
    Natural varianti309 – 3091C → Y in GM2G2; adult type; severe; almost complete absence of activity. 1 Publication
    VAR_003250
    Natural varianti417 – 4171P → L in GM2G2. 2 Publications
    Corresponds to variant rs28942073 [ dbSNP | Ensembl ].
    VAR_003251
    Natural varianti456 – 4561Y → S in GM2G2. 1 Publication
    VAR_003252
    Natural varianti504 – 5041P → S in GM2G2. 1 Publication
    VAR_011705
    Natural varianti505 – 5051R → Q in GM2G2. 2 Publications
    VAR_003253
    Natural varianti534 – 5341C → Y in GM2G2; infantile type. 1 Publication
    VAR_003254
    Natural varianti543 – 5431A → T in GM2G2. 1 Publication
    VAR_011706

    Keywords - Diseasei

    Disease mutation, Gangliosidosis, Neurodegeneration

    Organism-specific databases

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4242Sequence AnalysisAdd
    BLAST
    Propeptidei43 – 121792 PublicationsPRO_0000012002Add
    BLAST
    Chaini122 – 556435Beta-hexosaminidase subunit betaPRO_0000012003Add
    BLAST
    Chaini122 – 311190Beta-hexosaminidase subunit beta chain BPRO_0000012004Add
    BLAST
    Chaini315 – 556242Beta-hexosaminidase subunit beta chain APRO_0000012005Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi84 – 841N-linked (GlcNAc...)2 Publications
    Disulfide bondi91 ↔ 137
    Glycosylationi142 – 1421N-linked (GlcNAc...)1 Publication
    Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
    Disulfide bondi309 ↔ 360
    Glycosylationi323 – 3231N-linked (GlcNAc...)1 Publication
    Glycosylationi327 – 3271N-linked (GlcNAc...)3 Publications
    Disulfide bondi534 ↔ 551

    Post-translational modificationi

    N-linked glycans at Asn-142 and Asn-190 consist of Man(3)-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.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP07686.
    PaxDbiP07686.
    PeptideAtlasiP07686.
    PRIDEiP07686.

    2D gel databases

    UCD-2DPAGEP07686.

    PTM databases

    PhosphoSiteiP07686.

    Expressioni

    Gene expression databases

    ArrayExpressiP07686.
    BgeeiP07686.
    CleanExiHS_HEXB.
    GenevestigatoriP07686.

    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.

    Protein-protein interaction databases

    BioGridi109323. 20 interactions.
    IntActiP07686. 1 interaction.
    MINTiMINT-4528380.
    STRINGi9606.ENSP00000261416.

    Structurei

    Secondary structure

    1
    556
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi61 – 7111
    Helixi74 – 763
    Beta strandi78 – 814
    Beta strandi83 – 864
    Helixi92 – 10514
    Beta strandi126 – 1316
    Beta strandi149 – 1535
    Beta strandi155 – 16410
    Helixi165 – 17814
    Beta strandi187 – 19610
    Beta strandi201 – 21212
    Helixi216 – 22813
    Beta strandi233 – 2375
    Helixi253 – 2586
    Beta strandi259 – 2613
    Beta strandi262 – 2643
    Helixi268 – 28013
    Beta strandi284 – 29411
    Helixi298 – 3014
    Beta strandi306 – 3083
    Beta strandi318 – 3225
    Helixi327 – 34317
    Beta strandi346 – 3527
    Helixi359 – 3624
    Helixi365 – 3739
    Helixi380 – 39718
    Beta strandi401 – 4055
    Helixi406 – 4105
    Beta strandi420 – 4234
    Helixi429 – 43810
    Beta strandi443 – 4453
    Helixi447 – 4493
    Beta strandi450 – 4534
    Beta strandi455 – 4573
    Helixi460 – 4656
    Helixi475 – 4795
    Beta strandi481 – 4888
    Helixi490 – 4923
    Turni495 – 4973
    Helixi498 – 5025
    Helixi505 – 51410
    Helixi522 – 53817
    Beta strandi546 – 5483

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP07686.
    SMRiP07686. Positions 54-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07686.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3525.
    HOGENOMiHOG000157972.
    HOVERGENiHBG005961.
    InParanoidiP07686.
    KOiK12373.
    OrthoDBiEOG7KDFB6.
    PhylomeDBiP07686.
    TreeFamiTF313036.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view]
    PfamiPF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view]
    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

    MELCGLGLPR PPMLLALLLA TLLAAMLALL TQVALVVQVA EAARAPSVSA    50
    KPGPALWPLP LSVKMTPNLL HLAPENFYIS HSPNSTAGPS CTLLEEAFRR 100
    YHGYIFGFYK WHHEPAEFQA KTQVQQLLVS ITLQSECDAF PNISSDESYT 150
    LLVKEPVAVL KANRVWGALR GLETFSQLVY QDSYGTFTIN ESTIIDSPRF 200
    SHRGILIDTS RHYLPVKIIL KTLDAMAFNK FNVLHWHIVD DQSFPYQSIT 250
    FPELSNKGSY SLSHVYTPND VRMVIEYARL RGIRVLPEFD TPGHTLSWGK 300
    GQKDLLTPCY SRQNKLDSFG PINPTLNTTY SFLTTFFKEI SEVFPDQFIH 350
    LGGDEVEFKC WESNPKIQDF MRQKGFGTDF KKLESFYIQK VLDIIATINK 400
    GSIVWQEVFD DKAKLAPGTI VEVWKDSAYP EELSRVTASG FPVILSAPWY 450
    LDLISYGQDW RKYYKVEPLD FGGTQKQKQL FIGGEACLWG EYVDATNLTP 500
    RLWPRASAVG ERLWSSKDVR DMDDAYDRLT RHRCRMVERG IAAQPLYAGY 550
    CNHENM 556
    Length:556
    Mass (Da):63,111
    Last modified:February 1, 1991 - v3
    Checksum:iB3A0A36594F62536
    GO

    Sequence cautioni

    The sequence AAA51828.1 differs from that shown. Reason: Frameshift at position 21.
    The sequence AAA68620.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621S → L in GM2G2. 1 Publication
    Corresponds to variant rs820878 [ dbSNP | Ensembl ].
    VAR_003247
    Natural varianti121 – 1211K → R.
    Corresponds to variant rs11556045 [ dbSNP | Ensembl ].
    VAR_003248
    Natural varianti207 – 2071I → V Probable polymorphism. 2 Publications
    Corresponds to variant rs10805890 [ dbSNP | Ensembl ].
    VAR_003249
    Natural varianti255 – 2551S → R in GM2G2. 1 Publication
    VAR_011704
    Natural varianti309 – 3091C → Y in GM2G2; adult type; severe; almost complete absence of activity. 1 Publication
    VAR_003250
    Natural varianti417 – 4171P → L in GM2G2. 2 Publications
    Corresponds to variant rs28942073 [ dbSNP | Ensembl ].
    VAR_003251
    Natural varianti456 – 4561Y → S in GM2G2. 1 Publication
    VAR_003252
    Natural varianti504 – 5041P → S in GM2G2. 1 Publication
    VAR_011705
    Natural varianti505 – 5051R → Q in GM2G2. 2 Publications
    VAR_003253
    Natural varianti534 – 5341C → Y in GM2G2; infantile type. 1 Publication
    VAR_003254
    Natural varianti543 – 5431A → T in GM2G2. 1 Publication
    VAR_011706

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiHs.69293.

    Genome annotation databases

    EnsembliENST00000261416; ENSP00000261416; ENSG00000049860.
    GeneIDi3074.
    KEGGihsa:3074.
    UCSCiuc003kdd.3. human.

    Polymorphism databases

    DMDMi123081.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    HEXBdb

    HEXB mutation database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4022.1.
    PIRi A31250.
    RefSeqi NP_000512.1. NM_000521.3.
    UniGenei Hs.69293.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P07686.
    SMRi P07686. Positions 54-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109323. 20 interactions.
    IntActi P07686. 1 interaction.
    MINTi MINT-4528380.
    STRINGi 9606.ENSP00000261416.

    Chemistry

    BindingDBi P07686.
    ChEMBLi CHEMBL5877.

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    PTM databases

    PhosphoSitei P07686.

    Polymorphism databases

    DMDMi 123081.

    2D gel databases

    UCD-2DPAGE P07686.

    Proteomic databases

    MaxQBi P07686.
    PaxDbi P07686.
    PeptideAtlasi P07686.
    PRIDEi P07686.

    Protocols and materials databases

    DNASUi 3074.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261416 ; ENSP00000261416 ; ENSG00000049860 .
    GeneIDi 3074.
    KEGGi hsa:3074.
    UCSCi uc003kdd.3. human.

    Organism-specific databases

    CTDi 3074.
    GeneCardsi GC05P073935.
    HGNCi HGNC:4879. HEXB.
    HPAi HPA055409.
    HPA056010.
    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.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3525.
    HOGENOMi HOG000157972.
    HOVERGENi HBG005961.
    InParanoidi P07686.
    KOi K12373.
    OrthoDBi EOG7KDFB6.
    PhylomeDBi P07686.
    TreeFami TF313036.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00629-MONOMER.
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_120888. CS/DS degradation.
    REACT_120996. Hyaluronan uptake and degradation.
    REACT_121313. Keratan sulfate degradation.
    SABIO-RK P07686.

    Miscellaneous databases

    ChiTaRSi HEXB. human.
    EvolutionaryTracei P07686.
    GeneWikii HEXB.
    GenomeRNAii 3074.
    NextBioi 12159.
    PROi P07686.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07686.
    Bgeei P07686.
    CleanExi HS_HEXB.
    Genevestigatori P07686.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProi IPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view ]
    Pfami PF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
    PRINTSi PR00738. GLHYDRLASE20.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiHEXB_HUMAN
    AccessioniPrimary (citable) accession number: P07686
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 of the sequence. [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

    External Data

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