Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06865 - HEXA_HUMAN

UniProt

P06865 - HEXA_HUMAN

(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)

Protein

Beta-hexosaminidase subunit alpha

Gene

HEXA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 donorBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. chondroitin sulfate catabolic process Source: Reactome
  3. chondroitin sulfate metabolic process Source: Reactome
  4. glycosaminoglycan metabolic process Source: Reactome
  5. glycosphingolipid metabolic process Source: Reactome
  6. hyaluronan catabolic process Source: Reactome
  7. hyaluronan metabolic process Source: Reactome
  8. keratan sulfate catabolic process Source: Reactome
  9. keratan sulfate metabolic process Source: Reactome
  10. small molecule metabolic process Source: Reactome
  11. 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:4878. HEXA.

Subcellular locationi

Lysosome

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. lysosomal lumen Source: Reactome
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

GM2-gangliosidosis 122 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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).

See also OMIM:272800
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. 1 Publication
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

BgeeiP06865.
CleanExiHS_HEXA.
ExpressionAtlasiP06865. baseline and differential.
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 – 314Combined sources
Beta strandi36 – 383Combined sources
Helixi41 – 433Combined sources
Beta strandi45 – 484Combined sources
Helixi59 – 7214Combined sources
Beta strandi93 – 986Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi125 – 1317Combined sources
Helixi132 – 14514Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi160 – 1634Combined sources
Beta strandi168 – 1758Combined sources
Beta strandi177 – 1793Combined sources
Helixi183 – 19513Combined sources
Beta strandi200 – 2045Combined sources
Beta strandi216 – 2183Combined sources
Helixi220 – 2256Combined sources
Beta strandi226 – 2283Combined sources
Turni229 – 2324Combined sources
Helixi236 – 24813Combined sources
Beta strandi252 – 26211Combined sources
Helixi264 – 2663Combined sources
Turni267 – 2693Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi280 – 29011Combined sources
Helixi295 – 31117Combined sources
Beta strandi314 – 3207Combined sources
Helixi327 – 3315Combined sources
Helixi333 – 3408Combined sources
Turni341 – 3433Combined sources
Helixi349 – 36517Combined sources
Beta strandi369 – 3735Combined sources
Helixi374 – 3785Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi394 – 3985Combined sources
Helixi400 – 40910Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi426 – 4283Combined sources
Helixi431 – 4366Combined sources
Turni446 – 4483Combined sources
Helixi449 – 4513Combined sources
Beta strandi452 – 4598Combined sources
Turni466 – 4683Combined sources
Helixi469 – 4735Combined sources
Helixi476 – 48510Combined sources
Helixi493 – 50917Combined sources
Beta strandi517 – 5193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000008107.
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

        10         20         30         40         50
MTSSRLWFSL LLAAAFAGRA TALWPWPQNF QTSDQRYVLY PNNFQFQYDV 
        60         70         80         90        100
SSAAQPGCSV LDEAFQRYRD LLFGSGSWPR PYLTGKRHTL EKNVLVVSVV 
       110        120        130        140        150
TPGCNQLPTL ESVENYTLTI NDDQCLLLSE TVWGALRGLE TFSQLVWKSA 
       160        170        180        190        200
EGTFFINKTE IEDFPRFPHR GLLLDTSRHY LPLSSILDTL DVMAYNKLNV 
       210        220        230        240        250
FHWHLVDDPS FPYESFTFPE LMRKGSYNPV THIYTAQDVK EVIEYARLRG 
       260        270        280        290        300
IRVLAEFDTP GHTLSWGPGI PGLLTPCYSG SEPSGTFGPV NPSLNNTYEF 
       310        320        330        340        350
MSTFFLEVSS VFPDFYLHLG GDEVDFTCWK SNPEIQDFMR KKGFGEDFKQ 
       360        370        380        390        400
LESFYIQTLL DIVSSYGKGY VVWQEVFDNK VKIQPDTIIQ VWREDIPVNY 
       410        420        430        440        450
MKELELVTKA GFRALLSAPW YLNRISYGPD WKDFYIVEPL AFEGTPEQKA 
       460        470        480        490        500
LVIGGEACMW GEYVDNTNLV PRLWPRAGAV AERLWSNKLT SDLTFAYERL 
       510        520 
SHFRCELLRR GVQAQPLNVG FCEQEFEQT
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. 1 Publication
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:
EMBLi
GenBanki
DDBJi
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. [P06865-1]
PIRiA23561. AOHUBA.
RefSeqiNP_000511.2. NM_000520.4. [P06865-1]
UniGeneiHs.604479.
Hs.709495.

Genome annotation databases

EnsembliENST00000268097; ENSP00000268097; ENSG00000213614. [P06865-1]
GeneIDi3073.
KEGGihsa:3073.
UCSCiuc002aun.4. human. [P06865-1]

Polymorphism databases

DMDMi311033393.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

HEXAdb

HEXA mutation database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P06865-1]
PIRiA23561. AOHUBA.
RefSeqiNP_000511.2. NM_000520.4. [P06865-1]
UniGeneiHs.604479.
Hs.709495.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Chemistry

BindingDBiP06865.
ChEMBLiCHEMBL3038485.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

PTM databases

PhosphoSiteiP06865.

Polymorphism databases

DMDMi311033393.

Proteomic databases

MaxQBiP06865.
PaxDbiP06865.
PeptideAtlasiP06865.
PRIDEiP06865.

Protocols and materials databases

DNASUi3073.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268097; ENSP00000268097; ENSG00000213614. [P06865-1]
GeneIDi3073.
KEGGihsa:3073.
UCSCiuc002aun.4. human. [P06865-1]

Organism-specific databases

CTDi3073.
GeneCardsiGC15M072635.
GeneReviewsiHEXA.
H-InvDBHIX0012407.
HGNCiHGNC:4878. HEXA.
HPAiHPA054583.
MIMi272800. phenotype.
606869. gene.
neXtProtiNX_P06865.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3525.
GeneTreeiENSGT00390000008107.
HOGENOMiHOG000157972.
HOVERGENiHBG005961.
InParanoidiP06865.
KOiK12373.
OrthoDBiEOG7KDFB6.
PhylomeDBiP06865.
TreeFamiTF313036.

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.

Miscellaneous databases

EvolutionaryTraceiP06865.
GeneWikiiHEXA.
GenomeRNAii3073.
NextBioi12155.
PROiP06865.
SOURCEiSearch...

Gene expression databases

BgeeiP06865.
CleanExiHS_HEXA.
ExpressionAtlasiP06865. baseline and differential.
GenevestigatoriP06865.

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.
ProtoNetiSearch...

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] (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].
+Additional computationally mapped references.

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: February 4, 2015
This is version 179 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.