Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06865

- HEXA_HUMAN

UniProt

P06865 - HEXA_HUMAN

Protein

Beta-hexosaminidase subunit alpha

Gene

HEXA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. The form B is active against certain oligosaccharides. The form S has no measurable activity.

    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 sitei323 – 3231Proton donorBy similarity

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC
    2. protein heterodimerization activity Source: MGI

    GO - Biological processi

    1. adult walking behavior Source: Ensembl
    2. carbohydrate metabolic process Source: Reactome
    3. cell death Source: UniProtKB-KW
    4. cell morphogenesis involved in neuron differentiation Source: Ensembl
    5. chondroitin sulfate catabolic process Source: Reactome
    6. chondroitin sulfate metabolic process Source: Reactome
    7. ganglioside catabolic process Source: Ensembl
    8. glycosaminoglycan metabolic process Source: Reactome
    9. glycosphingolipid metabolic process Source: Reactome
    10. hyaluronan catabolic process Source: Reactome
    11. hyaluronan metabolic process Source: Reactome
    12. keratan sulfate catabolic process Source: Reactome
    13. keratan sulfate metabolic process Source: Reactome
    14. lipid storage Source: Ensembl
    15. lysosome organization Source: Ensembl
    16. myelination Source: Ensembl
    17. neuromuscular process controlling balance Source: Ensembl
    18. neuromuscular process controlling posture Source: Ensembl
    19. sensory perception of sound Source: Ensembl
    20. sexual reproduction Source: Ensembl
    21. skeletal system development Source: Ensembl
    22. small molecule metabolic process Source: Reactome
    23. sphingolipid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000140495-MONOMER.
    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    REACT_120888. CS/DS degradation.
    REACT_120996. Hyaluronan uptake and degradation.
    REACT_121313. Keratan sulfate degradation.
    SABIO-RKP06865.

    Protein family/group databases

    CAZyiGH20. Glycoside Hydrolase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidase subunit alpha (EC:3.2.1.52)
    Alternative name(s):
    Beta-N-acetylhexosaminidase subunit alpha
    Short name:
    Hexosaminidase subunit A
    N-acetyl-beta-glucosaminidase subunit alpha
    Gene namesi
    Name:HEXA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:4878. HEXA.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. lysosomal lumen Source: Reactome
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    GM2-gangliosidosis 1 (GM2G1) [MIM:272800]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. It is characterized by GM2 gangliosides accumulation in the absence of HEXA activity, leading to neurodegeneration and, in the infantile form, death in early childhood. It exists in several forms: infantile (most common and most severe), juvenile and adult (late-onset).22 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251P → S in GM2G1; late infantile. 1 Publication
    VAR_003202
    Natural varianti39 – 391L → R in GM2G1; infantile.
    VAR_003203
    Natural varianti127 – 1271L → F in GM2G1. 1 Publication
    VAR_022439
    Natural varianti127 – 1271L → R in GM2G1; infantile.
    VAR_003204
    Natural varianti166 – 1661R → G in GM2G1; late infantile. 1 Publication
    VAR_003205
    Natural varianti170 – 1701R → Q in GM2G1; infantile; inactive or unstable protein. 1 Publication
    VAR_003206
    Natural varianti170 – 1701R → W in GM2G1; infantile. 1 Publication
    VAR_003207
    Natural varianti178 – 1781R → C in GM2G1; infantile; inactive protein.
    VAR_003208
    Natural varianti178 – 1781R → H in GM2G1; infantile; inactive protein.
    VAR_003209
    Natural varianti178 – 1781R → L in GM2G1; infantile.
    Corresponds to variant rs28941770 [ dbSNP | Ensembl ].
    VAR_003210
    Natural varianti180 – 1801Y → H in GM2G1. 1 Publication
    Corresponds to variant rs28941771 [ dbSNP | Ensembl ].
    VAR_003211
    Natural varianti192 – 1921V → L in GM2G1; infantile.
    VAR_003212
    Natural varianti196 – 1961N → S in GM2G1. 1 Publication
    VAR_003213
    Natural varianti197 – 1971K → T in GM2G1.
    VAR_003214
    Natural varianti200 – 2001V → M in GM2G1.
    Corresponds to variant rs1800429 [ dbSNP | Ensembl ].
    VAR_003215
    Natural varianti204 – 2041H → R in GM2G1; infantile.
    VAR_003216
    Natural varianti210 – 2101S → F in GM2G1; infantile. 1 Publication
    VAR_003217
    Natural varianti211 – 2111F → S in GM2G1; infantile.
    VAR_003218
    Natural varianti226 – 2261S → F in GM2G1. 1 Publication
    VAR_022440
    Natural varianti250 – 2501G → D in GM2G1; juvenile. 1 Publication
    VAR_003221
    Natural varianti250 – 2501G → S in GM2G1. 1 Publication
    VAR_003222
    Natural varianti252 – 2521R → H in GM2G1.
    VAR_003223
    Natural varianti252 – 2521R → L in GM2G1. 1 Publication
    VAR_017188
    Natural varianti258 – 2581D → H in GM2G1; infantile. 1 Publication
    VAR_003224
    Natural varianti269 – 2691G → D in GM2G1. 1 Publication
    VAR_022441
    Natural varianti269 – 2691G → S in GM2G1; late onset; inhibited subunit dissociation. 1 Publication
    VAR_003225
    Natural varianti279 – 2791S → P in GM2G1; late infantile. 1 Publication
    VAR_003226
    Natural varianti295 – 2951N → S in GM2G1. 1 Publication
    Corresponds to variant rs199578185 [ dbSNP | Ensembl ].
    VAR_017189
    Natural varianti301 – 3011M → R in GM2G1; infantile.
    VAR_003227
    Natural varianti304 – 3041Missing in GM2G1; infantile; Moroccan Jewish. 1 Publication
    VAR_003228
    Natural varianti314 – 3141D → V in GM2G1. 1 Publication
    VAR_022442
    Natural varianti320 – 3201Missing in GM2G1; late infantile. 1 Publication
    VAR_003229
    Natural varianti335 – 3351I → F in GM2G1. 1 Publication
    VAR_003230
    Natural varianti347 – 3526Missing in GM2G1.
    VAR_003231
    Natural varianti391 – 3911V → M in GM2G1; mild; associated with spinal muscular atrophy. 1 Publication
    VAR_003232
    Natural varianti420 – 4201W → C in GM2G1; infantile; inactive protein. 2 Publications
    VAR_003234
    Natural varianti454 – 4541G → S in GM2G1; infantile.
    VAR_003236
    Natural varianti455 – 4551G → R in GM2G1; late infantile. 1 Publication
    VAR_003237
    Natural varianti458 – 4581C → Y in GM2G1; infantile. 1 Publication
    VAR_003238
    Natural varianti474 – 4741W → C in GM2G1; subacute. 1 Publication
    VAR_003239
    Natural varianti482 – 4821E → K in GM2G1; infantile. 2 Publications
    VAR_003240
    Natural varianti484 – 4841L → Q in GM2G1; infantile. 1 Publication
    VAR_003241
    Natural varianti485 – 4851W → R in GM2G1; infantile. 1 Publication
    VAR_003242
    Natural varianti499 – 4991R → C in GM2G1; infantile. 1 Publication
    VAR_003243
    Natural varianti499 – 4991R → H in GM2G1; juvenile. 1 Publication
    VAR_003244
    Natural varianti504 – 5041R → C in GM2G1; infantile. 1 Publication
    Corresponds to variant rs28942071 [ dbSNP | Ensembl ].
    VAR_003245
    Natural varianti504 – 5041R → H in GM2G1; juvenile; inhibited subunit dissociation.
    VAR_003246

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi115 – 1151N → Q: No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-157 and Q-295. 1 Publication
    Mutagenesisi157 – 1571N → Q: No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-115 and Q-295. 1 Publication
    Mutagenesisi295 – 2951N → Q: No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-115 and Q-157. 1 Publication

    Keywords - Diseasei

    Disease mutation, Gangliosidosis, Neurodegeneration

    Organism-specific databases

    MIMi272800. phenotype.
    Orphaneti309192. Tay-Sachs disease, B variant, adult form.
    309178. Tay-Sachs disease, B variant, infantile form.
    309185. Tay-Sachs disease, B variant, juvenile form.
    309239. Tay-Sachs disease, B1 variant.
    PharmGKBiPA29256.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Propeptidei23 – 88661 PublicationPRO_0000011993Add
    BLAST
    Chaini89 – 529441Beta-hexosaminidase subunit alphaPRO_0000011994Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 1041 Publication
    Glycosylationi115 – 1151N-linked (GlcNAc...)2 Publications
    Glycosylationi157 – 1571N-linked (GlcNAc...)3 Publications
    Disulfide bondi277 ↔ 3281 Publication
    Glycosylationi295 – 2951N-linked (GlcNAc...)3 Publications
    Disulfide bondi505 ↔ 5221 Publication

    Post-translational modificationi

    N-linked glycan at Asn-115 consists of Man(3)-GlcNAc2.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP06865.
    PaxDbiP06865.
    PeptideAtlasiP06865.
    PRIDEiP06865.

    PTM databases

    PhosphoSiteiP06865.

    Expressioni

    Gene expression databases

    ArrayExpressiP06865.
    BgeeiP06865.
    CleanExiHS_HEXA.
    GenevestigatoriP06865.

    Organism-specific databases

    HPAiHPA054583.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005191EBI-723519,EBI-375543
    CRKP461081EBI-723519,EBI-886
    FYNP062411EBI-723519,EBI-515315

    Protein-protein interaction databases

    BioGridi109322. 25 interactions.
    IntActiP06865. 6 interactions.
    MINTiMINT-1393072.
    STRINGi9606.ENSP00000268097.

    Structurei

    Secondary structure

    1
    529
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 314
    Beta strandi36 – 394
    Turni41 – 433
    Beta strandi45 – 484
    Helixi59 – 7315
    Beta strandi93 – 1008
    Beta strandi104 – 1063
    Beta strandi116 – 1238
    Beta strandi125 – 1317
    Helixi132 – 14514
    Beta strandi146 – 1483
    Beta strandi154 – 1574
    Beta strandi159 – 1635
    Beta strandi168 – 1758
    Turni176 – 1783
    Helixi183 – 19513
    Beta strandi200 – 2045
    Beta strandi216 – 2183
    Helixi220 – 2256
    Beta strandi226 – 2283
    Turni229 – 2313
    Helixi236 – 24813
    Beta strandi252 – 2565
    Beta strandi260 – 2623
    Turni264 – 2696
    Beta strandi274 – 29017
    Helixi295 – 31117
    Beta strandi314 – 3185
    Helixi327 – 3315
    Helixi333 – 3419
    Helixi349 – 36416
    Turni365 – 3673
    Beta strandi369 – 3735
    Helixi374 – 3785
    Beta strandi388 – 3914
    Beta strandi394 – 3985
    Helixi400 – 40910
    Beta strandi413 – 4164
    Beta strandi426 – 4283
    Helixi431 – 4366
    Helixi446 – 4494
    Beta strandi452 – 4598
    Turni466 – 4683
    Helixi469 – 4735
    Helixi476 – 48510
    Helixi493 – 50917
    Beta strandi517 – 5193

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QBCmodel-A109-529[»]
    2GJXX-ray2.80A/D/E/H23-529[»]
    2GK1X-ray3.25A/C/E/G23-529[»]
    ProteinModelPortaliP06865.
    SMRiP06865. Positions 23-528.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06865.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni423 – 4242Critical for hydrolyzis GM2 gangliosides

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3525.
    HOGENOMiHOG000157972.
    HOVERGENiHBG005961.
    InParanoidiP06865.
    KOiK12373.
    OrthoDBiEOG7KDFB6.
    PhylomeDBiP06865.
    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.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06865-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTSSRLWFSL LLAAAFAGRA TALWPWPQNF QTSDQRYVLY PNNFQFQYDV    50
    SSAAQPGCSV LDEAFQRYRD LLFGSGSWPR PYLTGKRHTL EKNVLVVSVV 100
    TPGCNQLPTL ESVENYTLTI NDDQCLLLSE TVWGALRGLE TFSQLVWKSA 150
    EGTFFINKTE IEDFPRFPHR GLLLDTSRHY LPLSSILDTL DVMAYNKLNV 200
    FHWHLVDDPS FPYESFTFPE LMRKGSYNPV THIYTAQDVK EVIEYARLRG 250
    IRVLAEFDTP GHTLSWGPGI PGLLTPCYSG SEPSGTFGPV NPSLNNTYEF 300
    MSTFFLEVSS VFPDFYLHLG GDEVDFTCWK SNPEIQDFMR KKGFGEDFKQ 350
    LESFYIQTLL DIVSSYGKGY VVWQEVFDNK VKIQPDTIIQ VWREDIPVNY 400
    MKELELVTKA GFRALLSAPW YLNRISYGPD WKDFYIVEPL AFEGTPEQKA 450
    LVIGGEACMW GEYVDNTNLV PRLWPRAGAV AERLWSNKLT SDLTFAYERL 500
    SHFRCELLRR GVQAQPLNVG FCEQEFEQT 529
    Length:529
    Mass (Da):60,703
    Last modified:November 2, 2010 - v2
    Checksum:iDACB3E3992E57A47
    GO
    Isoform 2 (identifier: P06865-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-192: Missing.
         359-360: LL → YP
         361-529: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:168
    Mass (Da):19,326
    Checksum:i58E9CE3F7F778082
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti331 – 3311S → P in BAD96222. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251P → S in GM2G1; late infantile. 1 Publication
    VAR_003202
    Natural varianti39 – 391L → R in GM2G1; infantile.
    VAR_003203
    Natural varianti127 – 1271L → F in GM2G1. 1 Publication
    VAR_022439
    Natural varianti127 – 1271L → R in GM2G1; infantile.
    VAR_003204
    Natural varianti166 – 1661R → G in GM2G1; late infantile. 1 Publication
    VAR_003205
    Natural varianti170 – 1701R → Q in GM2G1; infantile; inactive or unstable protein. 1 Publication
    VAR_003206
    Natural varianti170 – 1701R → W in GM2G1; infantile. 1 Publication
    VAR_003207
    Natural varianti178 – 1781R → C in GM2G1; infantile; inactive protein.
    VAR_003208
    Natural varianti178 – 1781R → H in GM2G1; infantile; inactive protein.
    VAR_003209
    Natural varianti178 – 1781R → L in GM2G1; infantile.
    Corresponds to variant rs28941770 [ dbSNP | Ensembl ].
    VAR_003210
    Natural varianti180 – 1801Y → H in GM2G1. 1 Publication
    Corresponds to variant rs28941771 [ dbSNP | Ensembl ].
    VAR_003211
    Natural varianti192 – 1921V → L in GM2G1; infantile.
    VAR_003212
    Natural varianti196 – 1961N → S in GM2G1. 1 Publication
    VAR_003213
    Natural varianti197 – 1971K → T in GM2G1.
    VAR_003214
    Natural varianti200 – 2001V → M in GM2G1.
    Corresponds to variant rs1800429 [ dbSNP | Ensembl ].
    VAR_003215
    Natural varianti204 – 2041H → R in GM2G1; infantile.
    VAR_003216
    Natural varianti210 – 2101S → F in GM2G1; infantile. 1 Publication
    VAR_003217
    Natural varianti211 – 2111F → S in GM2G1; infantile.
    VAR_003218
    Natural varianti226 – 2261S → F in GM2G1. 1 Publication
    VAR_022440
    Natural varianti247 – 2471R → W in HEXA pseudodeficiency. 1 Publication
    Corresponds to variant rs121907970 [ dbSNP | Ensembl ].
    VAR_003219
    Natural varianti249 – 2491R → W in HEXA pseudodeficiency. 2 Publications
    VAR_003220
    Natural varianti250 – 2501G → D in GM2G1; juvenile. 1 Publication
    VAR_003221
    Natural varianti250 – 2501G → S in GM2G1. 1 Publication
    VAR_003222
    Natural varianti252 – 2521R → H in GM2G1.
    VAR_003223
    Natural varianti252 – 2521R → L in GM2G1. 1 Publication
    VAR_017188
    Natural varianti258 – 2581D → H in GM2G1; infantile. 1 Publication
    VAR_003224
    Natural varianti269 – 2691G → D in GM2G1. 1 Publication
    VAR_022441
    Natural varianti269 – 2691G → S in GM2G1; late onset; inhibited subunit dissociation. 1 Publication
    VAR_003225
    Natural varianti279 – 2791S → P in GM2G1; late infantile. 1 Publication
    VAR_003226
    Natural varianti293 – 2931S → I.
    Corresponds to variant rs1054374 [ dbSNP | Ensembl ].
    VAR_058477
    Natural varianti295 – 2951N → S in GM2G1. 1 Publication
    Corresponds to variant rs199578185 [ dbSNP | Ensembl ].
    VAR_017189
    Natural varianti301 – 3011M → R in GM2G1; infantile.
    VAR_003227
    Natural varianti304 – 3041Missing in GM2G1; infantile; Moroccan Jewish. 1 Publication
    VAR_003228
    Natural varianti314 – 3141D → V in GM2G1. 1 Publication
    VAR_022442
    Natural varianti320 – 3201Missing in GM2G1; late infantile. 1 Publication
    VAR_003229
    Natural varianti335 – 3351I → F in GM2G1. 1 Publication
    VAR_003230
    Natural varianti347 – 3526Missing in GM2G1.
    VAR_003231
    Natural varianti391 – 3911V → M in GM2G1; mild; associated with spinal muscular atrophy. 1 Publication
    VAR_003232
    Natural varianti399 – 3991N → D.1 Publication
    Corresponds to variant rs1800430 [ dbSNP | Ensembl ].
    VAR_003233
    Natural varianti420 – 4201W → C in GM2G1; infantile; inactive protein. 2 Publications
    VAR_003234
    Natural varianti436 – 4361I → V.9 Publications
    Corresponds to variant rs1800431 [ dbSNP | Ensembl ].
    VAR_003235
    Natural varianti454 – 4541G → S in GM2G1; infantile.
    VAR_003236
    Natural varianti455 – 4551G → R in GM2G1; late infantile. 1 Publication
    VAR_003237
    Natural varianti458 – 4581C → Y in GM2G1; infantile. 1 Publication
    VAR_003238
    Natural varianti474 – 4741W → C in GM2G1; subacute. 1 Publication
    VAR_003239
    Natural varianti482 – 4821E → K in GM2G1; infantile. 2 Publications
    VAR_003240
    Natural varianti484 – 4841L → Q in GM2G1; infantile. 1 Publication
    VAR_003241
    Natural varianti485 – 4851W → R in GM2G1; infantile. 1 Publication
    VAR_003242
    Natural varianti499 – 4991R → C in GM2G1; infantile. 1 Publication
    VAR_003243
    Natural varianti499 – 4991R → H in GM2G1; juvenile. 1 Publication
    VAR_003244
    Natural varianti504 – 5041R → C in GM2G1; infantile. 1 Publication
    Corresponds to variant rs28942071 [ dbSNP | Ensembl ].
    VAR_003245
    Natural varianti504 – 5041R → H in GM2G1; juvenile; inhibited subunit dissociation.
    VAR_003246

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 192192Missing in isoform 2. 1 PublicationVSP_056657Add
    BLAST
    Alternative sequencei359 – 3602LL → YP in isoform 2. 1 PublicationVSP_056658
    Alternative sequencei361 – 529169Missing in isoform 2. 1 PublicationVSP_056659Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16424
    , M16411, M16412, M16413, M16414, M16415, M16416, M16417, M16418, M16419, M16420, M16421, M16422, M16423 Genomic DNA. Translation: AAB00965.1.
    S62076
    , S62047, S62049, S62051, S62053, S62055, S62057, S62059, S62061, S62063, S62066, S62068, S62070, S62072 Genomic DNA. Translation: AAD13932.1.
    AK296528 mRNA. Translation: BAG59159.1.
    AK222502 mRNA. Translation: BAD96222.1.
    CR627386 mRNA. Translation: CAH10482.1.
    AC009690 Genomic DNA. No translation available.
    BC018927 mRNA. Translation: AAH18927.1.
    BC084537 mRNA. Translation: AAH84537.1.
    M13520 mRNA. Translation: AAA51827.1.
    CCDSiCCDS10243.1.
    PIRiA23561. AOHUBA.
    RefSeqiNP_000511.2. NM_000520.4.
    UniGeneiHs.604479.
    Hs.709495.

    Genome annotation databases

    EnsembliENST00000268097; ENSP00000268097; ENSG00000213614.
    ENST00000457859; ENSP00000398026; ENSG00000213614.
    GeneIDi3073.
    KEGGihsa:3073.
    UCSCiuc002aun.4. human.

    Polymorphism databases

    DMDMi311033393.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    HEXAdb

    HEXA mutation database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16424
    , M16411 , M16412 , M16413 , M16414 , M16415 , M16416 , M16417 , M16418 , M16419 , M16420 , M16421 , M16422 , M16423 Genomic DNA. Translation: AAB00965.1 .
    S62076
    , S62047 , S62049 , S62051 , S62053 , S62055 , S62057 , S62059 , S62061 , S62063 , S62066 , S62068 , S62070 , S62072 Genomic DNA. Translation: AAD13932.1 .
    AK296528 mRNA. Translation: BAG59159.1 .
    AK222502 mRNA. Translation: BAD96222.1 .
    CR627386 mRNA. Translation: CAH10482.1 .
    AC009690 Genomic DNA. No translation available.
    BC018927 mRNA. Translation: AAH18927.1 .
    BC084537 mRNA. Translation: AAH84537.1 .
    M13520 mRNA. Translation: AAA51827.1 .
    CCDSi CCDS10243.1.
    PIRi A23561. AOHUBA.
    RefSeqi NP_000511.2. NM_000520.4.
    UniGenei Hs.604479.
    Hs.709495.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QBC model - A 109-529 [» ]
    2GJX X-ray 2.80 A/D/E/H 23-529 [» ]
    2GK1 X-ray 3.25 A/C/E/G 23-529 [» ]
    ProteinModelPortali P06865.
    SMRi P06865. Positions 23-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109322. 25 interactions.
    IntActi P06865. 6 interactions.
    MINTi MINT-1393072.
    STRINGi 9606.ENSP00000268097.

    Chemistry

    BindingDBi P06865.
    ChEMBLi CHEMBL3038485.

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    PTM databases

    PhosphoSitei P06865.

    Polymorphism databases

    DMDMi 311033393.

    Proteomic databases

    MaxQBi P06865.
    PaxDbi P06865.
    PeptideAtlasi P06865.
    PRIDEi P06865.

    Protocols and materials databases

    DNASUi 3073.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268097 ; ENSP00000268097 ; ENSG00000213614 .
    ENST00000457859 ; ENSP00000398026 ; ENSG00000213614 .
    GeneIDi 3073.
    KEGGi hsa:3073.
    UCSCi uc002aun.4. human.

    Organism-specific databases

    CTDi 3073.
    GeneCardsi GC15M072635.
    GeneReviewsi HEXA.
    H-InvDB HIX0012407.
    HGNCi HGNC:4878. HEXA.
    HPAi HPA054583.
    MIMi 272800. phenotype.
    606869. gene.
    neXtProti NX_P06865.
    Orphaneti 309192. Tay-Sachs disease, B variant, adult form.
    309178. Tay-Sachs disease, B variant, infantile form.
    309185. Tay-Sachs disease, B variant, juvenile form.
    309239. Tay-Sachs disease, B1 variant.
    PharmGKBi PA29256.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3525.
    HOGENOMi HOG000157972.
    HOVERGENi HBG005961.
    InParanoidi P06865.
    KOi K12373.
    OrthoDBi EOG7KDFB6.
    PhylomeDBi P06865.
    TreeFami TF313036.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000140495-MONOMER.
    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_120888. CS/DS degradation.
    REACT_120996. Hyaluronan uptake and degradation.
    REACT_121313. Keratan sulfate degradation.
    SABIO-RK P06865.

    Miscellaneous databases

    EvolutionaryTracei P06865.
    GeneWikii HEXA.
    GenomeRNAii 3073.
    NextBioi 12155.
    PROi P06865.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06865.
    Bgeei P06865.
    CleanExi HS_HEXA.
    Genevestigatori P06865.

    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. "Human beta-hexosaminidase alpha chain: coding sequence and homology with the beta chain."
      Myerowitz R., Piekarz R., Neufeld E.F., Shows T.B., Suzuki K.
      Proc. Natl. Acad. Sci. U.S.A. 82:7830-7834(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-436.
    2. "Organization of the gene encoding the human beta-hexosaminidase alpha-chain."
      Proia R.L., Soravia E.
      J. Biol. Chem. 262:5677-5681(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-436.
    3. "Sequence of DNA flanking the exons of the HEXA gene, and identification of mutations in Tay-Sachs disease."
      Triggs-Raine B.L., Akerman B.R., Clarke J.T.R., Gravel R.A.
      Am. J. Hum. Genet. 49:1041-1054(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-436.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Thalamus.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-436.
      Tissue: Adipose tissue.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PSEUDODEFICIENCY TRP-249 AND VAL-436.
    7. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1), VARIANT VAL-436.
      Tissue: Brain and Eye.
    9. "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] OF 40-529 (ISOFORM 1), VARIANT VAL-436.
    10. "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 89-99.
    11. "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: PROTEIN SEQUENCE OF 96-105, STRUCTURE OF CARBOHYDRATES.
    12. "Analysis of the glycosylation and phosphorylation of the alpha-subunit of the lysosomal enzyme, beta-hexosaminidase A, by site-directed mutagenesis."
      Weitz G., Proia R.L.
      J. Biol. Chem. 267:10039-10044(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-115; ASN-157 AND ASN-295, MUTAGENESIS OF ASN-115; ASN-157 AND ASN-295.
    13. "Identification of an active acidic residue in the catalytic site of beta-hexosaminidase."
      Tse R., Vavougios G., Hou Y., Mahuran D.J.
      Biochemistry 35:7599-7607(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES.
    14. "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-157 AND ASN-295.
      Tissue: Liver.
    15. "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.
    16. "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.
    17. "Tay-Sachs disease-causing mutations and neutral polymorphisms in the Hex A gene."
      Myerowitz R.
      Hum. Mutat. 9:195-208(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    18. "Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis."
      Lemieux M.J., Mark B.L., Cherney M.M., Withers S.G., Mahuran D.J., James M.N.
      J. Mol. Biol. 359:913-929(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-529 IN COMPLEX WITH HEXB, GLYCOSYLATION AT ASN-115; ASN-157 AND ASN-295, DISULFIDE BONDS.
    19. "A point mutation in the coding sequence of the beta-hexosaminidase alpha gene results in defective processing of the enzyme protein in an unusual GM2-gangliosidosis variant."
      Nakano T., Muscillo M., Ohno K., Hoffman A.J., Suzuki K.
      J. Neurochem. 51:984-987(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 LYS-482.
    20. "The mutations in Ashkenazi Jews with adult GM2 gangliosidosis, the adult form of Tay-Sachs disease."
      Navon R., Proia R.L.
      Science 243:1471-1474(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 SER-269.
    21. "A new point mutation in the beta-hexosaminidase alpha subunit gene responsible for infantile Tay-Sachs disease in a non-Jewish Caucasian patient (a Kpn mutant)."
      Tanaka A., Punnett H.H., Suzuki K.
      Am. J. Hum. Genet. 47:568-574(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 CYS-420.
    22. "Seven novel Tay-Sachs mutations detected by chemical mismatch cleavage of PCR-amplified cDNA fragments."
      Akli S., Lacorte J.-M., Poenaru L., Khan A.
      Genomics 11:124-134(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GM2G1 PHE-210 AND CYS-504.
    23. "Six novel deleterious and three neutral mutations in the gene encoding the alpha-subunit of hexosaminidase A in non-Jewish individuals."
      Mules E.H., Hayflick S., Miller C.S., Reynolds L.W., Thomas G.H.
      Am. J. Hum. Genet. 50:834-841(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 GLY-320 DEL, VARIANTS ASP-399 AND VAL-436.
    24. "A pseudodeficiency allele common in non-Jewish Tay-Sachs carriers: implications for carrier screening."
      Triggs-Raine B.L., Mules E.H., Kaback M.M., Lim-Steele J.S.T., Dowling C.E., Akerman B.R., Natowicz M.R., Grebner E.E., Navon R., Welch J.P., Greenberg C.R., Thomas G.H., Gravel R.A.
      Am. J. Hum. Genet. 51:793-801(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PSEUDODEFICIENCY TRP-247.
    25. "A new Tay-Sachs disease B1 allele in exon 7 in two compound heterozygotes each with a second novel mutation."
      Fernandes M., Kaplan F., Natowicz M., Prence E., Kolodny E., Kaback M., Hechtman P.
      Hum. Mol. Genet. 1:759-761(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GM2G1 TRP-170 AND HIS-258.
    26. "A glycine250--> aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family."
      Trop I., Kaplan F., Brown C., Mahuran D., Hechtman P.
      Hum. Mutat. 1:35-39(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 ASP-250.
    27. Cited for: VARIANT GM2G1 ARG-485.
    28. "A second mutation associated with apparent beta-hexosaminidase A pseudodeficiency: identification and frequency estimation."
      Cao Z., Natowicz M.R., Kaback M.M., Lim-Steele J.S.T., Prence E.M., Brown D., Chabot T., Triggs-Raine B.L.
      Am. J. Hum. Genet. 53:1198-1205(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PSEUDODEFICIENCY TRP-249.
    29. "Ten novel mutations in the HEXA gene in non-Jewish Tay-Sachs patients."
      Akli S., Chomel J.-C., Lacorte J.-M., Bachner L., Poenaru A., Poenaru L.
      Hum. Mol. Genet. 2:61-67(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GM2G1.
    30. "Two new mutations in a late infantile Tay-Sachs patient are both in exon 1 of the beta-hexosaminidase alpha subunit gene."
      Harmon D.L., Gardner-Medwin D., Stirling J.L.
      J. Med. Genet. 30:123-128(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 SER-25.
    31. "Three novel beta-hexosaminidase A mutations in obligate carriers of Tay-Sachs disease."
      Tomczak J., Grebner E.E.
      Hum. Mutat. 4:71-72(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GM2G1 PHE-335 AND 347-ASP--GLU-352 DEL.
    32. Cited for: VARIANTS GM2G1 TYR-458 AND GLN-484.
    33. "Mutational analyses of Tay-Sachs disease: studies on Tay-Sachs carriers of French Canadian background living in New England."
      Triggs-Raine B.L., Richard M., Wasel N., Prence E.M., Natowicz M.R.
      Am. J. Hum. Genet. 56:870-879(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GM2G1 SER-196 AND SER-250.
    34. "GM2 gangliosidosis B1 variant: biochemical and molecular characterization of hexosaminidase A."
      Peleg L., Meltzer F., Karpati M., Goldman B.
      Biochem. Mol. Med. 54:126-132(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 GLY-166.
    35. "A new mutation in the HEXA gene associated with a spinal muscular atrophy phenotype."
      Navon R., Khosravi R., Korczyn T., Masson M., Sonnino S., Fardeau M., Eymard B., Lefevre N., Turpin J.C., Rondot P.
      Neurology 45:539-543(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 MET-391.
    36. "Late-onset GM2 gangliosidosis: Ashkenazi Jewish family with an exon 5 mutation (Tyr180-->His) in the Hex A alpha-chain gene."
      de Gasperi R., Gama Sosa M.A., Battistini S., Yeretsian J., Raghavan S., Zelnik N., Leshinsky E., Kolodny E.H.
      Neurology 47:547-552(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 HIS-180.
    37. "Novel mutations and DNA-based screening in non-Jewish carriers of Tay-Sachs disease."
      Akerman B.R., Natowicz M.R., Kaback M.M., Loyer M., Campeau E., Gravel R.A.
      Am. J. Hum. Genet. 60:1099-1106(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GM2G1 PHE-127; PHE-226; ASP-269 AND VAL-314.
    38. Cited for: VARIANTS GM2G1 GLN-170; PHE-304 DEL AND LYS-482.
    39. "Two novel (1334delC and 1363G to A, G455R) mutations in exon 12 of the beta-hexosaminidase alpha-chain gene in two Portuguese patients."
      Ribeiro M.G., Pinto R.A., Suzuki K., Sa Miranda M.C.
      Hum. Mutat. 10:359-360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 ARG-455.
    40. "Two mutated HEXA alleles in a Druze patient with late-infantile Tay-Sachs disease."
      Drucker L., Hemli J.A., Navon R.
      Hum. Mutat. 10:451-457(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 PRO-279.
    41. "W474C amino acid substitution affects early processing of the alpha-subunit of beta-hexosaminidase A and is associated with subacute G(M2) gangliosidosis."
      Petroulakis E., Cao Z., Clarke J.T.R., Mahuran D.J., Lee G., Triggs-Raine B.
      Hum. Mutat. 11:432-442(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GM2G1 CYS-474.
    42. "Different attenuated phenotypes of GM2 gangliosidosis variant B in Japanese patients with HEXA mutations at codon 499, and five novel mutations responsible for infantile acute form."
      Tanaka A., Hoang L.T., Nishi Y., Maniwa S., Oka M., Yamano T.
      J. Hum. Genet. 48:571-574(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GM2G1 LEU-252; SER-295; CYS-420; CYS-499 AND HIS-499.
    43. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHEXA_HUMAN
    AccessioniPrimary (citable) accession number: P06865
    Secondary accession number(s): B4DKE7
    , E7ENH7, Q53HS8, Q6AI32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 175 of the entry and version 2 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 15
      Human chromosome 15: 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

    Dasty 3