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P06865

- HEXA_HUMAN

UniProt

P06865 - HEXA_HUMAN

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Protein

Beta-hexosaminidase subunit alpha

Gene
HEXA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. 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 donor By 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
Complete GO annotation...

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: Ensembl
Complete GO annotation...

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).
Note: The disease is caused by mutations affecting the gene represented in this entry.22 Publications
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 – 8866PRO_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.

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.

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.

Miscellaneous databases

EvolutionaryTraceiP06865.

Family & Domainsi

Region

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

Sequence similaritiesi

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.

Sequencei

Sequence statusi: Complete.

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

P06865-1 [UniParc]FASTAAdd to Basket

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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

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

Sequence conflict

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

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.
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.
GeneIDi3073.
KEGGihsa:3073.
UCSCiuc002aun.4. human.

Polymorphism databases

DMDMi311033393.

Keywords - Coding sequence diversityi

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 .
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 .
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

« Hide 'large scale' publications
  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], 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. 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], VARIANT VAL-436.
    Tissue: Adipose tissue.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS PSEUDODEFICIENCY TRP-249 AND VAL-436.
  6. "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].
  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], VARIANT VAL-436.
    Tissue: Brain and Eye.
  8. "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, VARIANT VAL-436.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. Cited for: VARIANT GM2G1 ARG-485.
  27. "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.
  28. "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.
  29. "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.
  30. "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.
  31. Cited for: VARIANTS GM2G1 TYR-458 AND GLN-484.
  32. "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.
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. Cited for: VARIANTS GM2G1 GLN-170; PHE-304 DEL AND LYS-482.
  38. "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.
  39. "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.
  40. "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.
  41. "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.
  42. 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): Q53HS8, Q6AI32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 2, 2010
Last modified: September 3, 2014
This is version 174 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

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