Reviewed,
UniProtKB/Swiss-Prot P06865 (HEXA_HUMAN)
Last modified
October 13, 2009.
Version 121.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Beta-hexosaminidase subunit alpha EC=3.2.1.52 Alternative name(s): N-acetyl-beta-glucosaminidase subunit alpha Beta-N-acetylhexosaminidase subunit alpha Short name=Hexosaminidase subunit A | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 529 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. The form B is active against certain oligosaccharides. The form S has no measurable activity. |
| Catalytic activity | Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. |
| Subunit structure | 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 an homodimer of two alpha subunits. The two beta chains are derived from the cleavage of the beta subunit. |
| Subcellular location | |
| Post-translational modification | N-linked glycan at Asn-115 consists of Man(3)-GlcNAc2. |
| Involvement in disease | Defects in HEXA are the cause of GM2-gangliosidosis type 1 (GM2G1) [MIM:272800]; also known as Tay-Sachs disease. GM2-gangliosidosis is an autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. GM2G1 is characterized by GM2 gangliosides accumulation in the absence of HEXA activity, leading to neurodegeneration and, in the infantile form, death in early childhood. GM2G1 has an increased incidence among Ashkenazi Jews and French Canadians in eastern Quebec. It exists in several forms: infantile (most common and most severe), juvenile and adult (late onset). Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 |
| Sequence similarities | Belongs to the glycosyl hydrolase 20 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Lysosome |
| Coding sequence diversity | Polymorphism |
| Disease | Disease mutation Gangliosidosis |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC cation bindingInferred from electronic annotation. Source: InterPro protein heterodimerization activityInferred from direct assay. Source: MGI |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ABL1 | P00519 | 1 | EBI-723519,EBI-375543 | |
| CRK | P46108 | 1 | EBI-723519,EBI-886 | |
| FYN | P06241 | 1 | EBI-723519,EBI-515315 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Ref.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Propeptide | 23 – 88 | 66 | PRO_0000011993 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 89 – 529 | 441 | Beta-hexosaminidase subunit alpha | PRO_0000011994 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 323 | 1 | Proton donor By similarity | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 115 | 1 | N-linked (GlcNAc...) Ref.10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 157 | 1 | N-linked (GlcNAc...) Ref.10 Ref.13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Glycosylation | 295 | 1 | N-linked (GlcNAc...) Ref.10 Ref.13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 58 ↔ 104 | By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 277 ↔ 328 | By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 505 ↔ 522 | By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 25 | 1 | P → S in GM2G1; late infantile. Ref.28 | VAR_003202 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 39 | 1 | L → R in GM2G1; infantile. | VAR_003203 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 127 | 1 | L → F in GM2G1. Ref.35 | VAR_022439 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 127 | 1 | L → R in GM2G1; infantile. | VAR_003204 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 166 | 1 | R → G in GM2G1; late infantile. Ref.32 | VAR_003205 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 170 | 1 | R → Q in GM2G1; infantile; inactive or unstable protein. Ref.36 | VAR_003206 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 170 | 1 | R → W in GM2G1; infantile. Ref.23 | VAR_003207 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 178 | 1 | R → C in GM2G1; infantile; inactive protein. | VAR_003208 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 178 | 1 | R → H in GM2G1; infantile; inactive protein. | VAR_003209 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 178 | 1 | R → L in GM2G1; infantile. | VAR_003210 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 180 | 1 | Y → H in GM2G1. Ref.34 | VAR_003211 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 192 | 1 | V → L in GM2G1; infantile. | VAR_003212 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 196 | 1 | N → S in GM2G1. Ref.31 | VAR_003213 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 197 | 1 | K → T in GM2G1. | VAR_003214 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 200 | 1 | V → M in GM2G1. dbSNP rs1800429. | VAR_003215 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 204 | 1 | H → R in GM2G1; infantile. | VAR_003216 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 210 | 1 | S → F in GM2G1; infantile. Ref.20 | VAR_003217 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 211 | 1 | F → S in GM2G1; infantile. | VAR_003218 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 226 | 1 | S → F in GM2G1. Ref.35 | VAR_022440 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 247 | 1 | R → W in HEXA pseudodeficiency. Ref.22 | VAR_003219 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 249 | 1 | R → W in HEXA pseudodeficiency. Ref.5 Ref.26 | VAR_003220 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 250 | 1 | G → D in GM2G1; juvenile. Ref.24 | VAR_003221 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 250 | 1 | G → S in GM2G1. Ref.31 | VAR_003222 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 252 | 1 | R → H in GM2G1. | VAR_003223 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 252 | 1 | R → L in GM2G1. Ref.40 | VAR_017188 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 258 | 1 | D → H in GM2G1; infantile. Ref.23 | VAR_003224 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 269 | 1 | G → D in GM2G1. Ref.35 | VAR_022441 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 269 | 1 | G → S in GM2G1; late onset; inhibited subunit dissociation. Ref.18 | VAR_003225 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 279 | 1 | S → P in GM2G1; late infantile. Ref.38 | VAR_003226 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 293 | 1 | S → I: dbSNP rs1054374. | VAR_058477 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 295 | 1 | N → S in GM2G1. Ref.40 | VAR_017189 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 301 | 1 | M → R in GM2G1; infantile. | VAR_003227 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 304 | 1 | Missing in GM2G1; infantile; Moroccan Jewish. | VAR_003228 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 314 | 1 | D → V in GM2G1. Ref.35 | VAR_022442 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 320 | 1 | Missing in GM2G1; late infantile. | VAR_003229 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 335 | 1 | I → F in GM2G1. Ref.29 | VAR_003230 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 347 – 352 | 6 | Missing in GM2G1. | VAR_003231 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 391 | 1 | V → M in GM2G1; mild; associated with spinal muscular atrophy. Ref.33 | VAR_003232 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 399 | 1 | N → D: dbSNP rs1800430. Ref.21 | VAR_003233 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 420 | 1 | W → C in GM2G1; infantile; inactive protein. Ref.19 Ref.40 | VAR_003234 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 436 | 1 | V → I: dbSNP rs1800431. Ref.21 | VAR_003235 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 454 | 1 | G → S in GM2G1; infantile. | VAR_003236 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 455 | 1 | G → R in GM2G1; late infantile. Ref.37 | VAR_003237 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 458 | 1 | C → Y in GM2G1; infantile. Ref.30 | VAR_003238 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 474 | 1 | W → C in GM2G1; subacute. Ref.39 | VAR_003239 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 482 | 1 | E → K in GM2G1; infantile. Ref.17 Ref.36 | VAR_003240 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 484 | 1 | L → Q in GM2G1; infantile. Ref.30 | VAR_003241 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 485 | 1 | W → R in GM2G1; infantile. Ref.25 | VAR_003242 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 499 | 1 | R → C in GM2G1; infantile. Ref.40 | VAR_003243 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 499 | 1 | R → H in GM2G1; juvenile. Ref.40 | VAR_003244 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 504 | 1 | R → C in GM2G1; infantile. Ref.20 | VAR_003245 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 504 | 1 | R → H in GM2G1; juvenile; inhibited subunit dissociation. | VAR_003246 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 331 | 1 | S → P in BAD96222. Ref.4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 168 – 175 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 177 – 179 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 183 – 195 | 13 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 200 – 204 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 219 – 223 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 224 – 226 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 227 – 231 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 236 – 249 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 252 – 262 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 264 – 269 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 284 – 286 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 295 – 311 | 17 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 318 – 320 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 333 – 340 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 348 – 350 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 351 – 365 | 15 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 371 – 373 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 374 – 377 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 388 – 391 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 395 – 398 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 400 – 409 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 413 – 416 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 426 – 429 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 431 – 436 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 454 – 459 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 466 – 473 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 476 – 485 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 2933746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [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: 2952641] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [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: 1833974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [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]. Tissue: Adipose tissue. |
| [5] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PSEUDODEFICIENCY TRP-249. |
| [6] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Eye. |
| [7] | "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: 3013851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-529. |
| [8] | "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: 2965147] [Abstract] Cited for: PROTEIN SEQUENCE OF 89-99. |
| [9] | "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: 2971395] [Abstract] Cited for: PROTEIN SEQUENCE OF 96-105, STRUCTURE OF CARBOHYDRATES. |
| [10] | "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: 1533633] [Abstract] Cited for: GLYCOSYLATION AT ASN-115; ASN-157 AND ASN-295, MUTAGENESIS OF ASN-115; ASN-157 AND ASN-295. |
| [11] | "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: 8652542] [Abstract] Cited for: ACTIVE SITES. |
| [12] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157 AND ASN-295, MASS SPECTROMETRY. 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: 8673609] [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: 1825792] [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: 9090523] [Abstract] Cited for: REVIEW ON VARIANTS. |
| [17] | "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: 2970528] [Abstract] Cited for: VARIANT GM2G1 LYS-482. |
| [18] | "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: 2522679] [Abstract] Cited for: VARIANT GM2G1 SER-269. |
| [19] | "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: 2144098] [Abstract] Cited for: VARIANT GM2G1 CYS-420. |
| [20] | "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: 1837283] [Abstract] Cited for: VARIANTS GM2G1 PHE-210 AND CYS-504. |
| [21] | "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: 1532289] [Abstract] Cited for: VARIANT GM2G1 GLY-320 DEL, VARIANTS ASP-399 AND ILE-436. |
| [22] | "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: 1384323] [Abstract] Cited for: VARIANT PSEUDODEFICIENCY TRP-247. |
| [23] | "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: 1302612] [Abstract] Cited for: VARIANTS GM2G1 TRP-170 AND HIS-258. |
| [24] | "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: 1301189] [Abstract] Cited for: VARIANT GM2G1 ASP-250. |
| [25] | "Novel Tay-Sachs disease mutations from China." Akalin N., Shi H.-P., Vavougios G., Hechtman P., Lo W., Scriver C.R., Mahuran D., Kaplan F. Hum. Mutat. 1:40-46(1992) [PubMed: 1301190] [Abstract] Cited for: VARIANT GM2G1 ARG-485. |
| [26] | "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: 7902672] [Abstract] Cited for: VARIANT PSEUDODEFICIENCY TRP-249. |
| [27] | "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: 8490625] [Abstract] Cited for: VARIANTS GM2G1. |
| [28] | "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: 8445615] [Abstract] Cited for: VARIANT GM2G1 SER-25. |
| [29] | "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: 7951261] [Abstract] Cited for: VARIANTS GM2G1 PHE-335 AND 347-ASP--GLU-352 DEL. |
| [30] | "Molecular genetics of Tay-Sachs disease in Japan." Tanaka A., Sakazaki H., Murakami H., Isshiki G., Suzuki K. J. Inherit. Metab. Dis. 17:593-600(1994) [PubMed: 7837766] [Abstract] Cited for: VARIANTS GM2G1 TYR-458 AND GLN-484. |
| [31] | "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: 7717398] [Abstract] Cited for: VARIANTS GM2G1 SER-196 AND SER-250. |
| [32] | "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: 8581357] [Abstract] Cited for: VARIANT GM2G1 GLY-166. |
| [33] | "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: 7898712] [Abstract] Cited for: VARIANT GM2G1 MET-391. |
| [34] | "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: 8757036] [Abstract] Cited for: VARIANT GM2G1 HIS-180. |
| [35] | "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: 9150157] [Abstract] Cited for: VARIANTS GM2G1 PHE-127; PHE-226; ASP-269 AND VAL-314. |
| [36] | "Tay-Sachs disease and HEXA mutations among Moroccan Jews." Kaufman M., Grinshpun-Cohen J., Karpati M., Peleg L., Goldman B., Akstein E., Adam A., Navon R. Hum. Mutat. 10:295-300(1997) [PubMed: 9338583] [Abstract] Cited for: VARIANTS GM2G1 GLN-170; PHE-304 DEL AND LYS-482. |
| [37] | "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: 9375850] [Abstract] Cited for: VARIANT GM2G1 ARG-455. |
| [38] | "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: 9401008] [Abstract] Cited for: VARIANT GM2G1 PRO-279. |
| [39] | "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: 9603435] [Abstract] Cited for: VARIANT GM2G1 CYS-474. |
| [40] | "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: 14566483] [Abstract] Cited for: VARIANTS GM2G1 LEU-252; SER-295; CYS-420; CYS-499 AND HIS-499. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
M16424 M16423 Genomic DNA. Translation: AAB00965.1. S62076 S62072 Genomic DNA. Translation: AAD13932.1. AK222502 mRNA. Translation: BAD96222.1. CR627386 mRNA. Translation: CAH10482.1. BC018927 mRNA. Translation: AAH18927.1. BC084537 mRNA. Translation: AAH84537.1. M13520 mRNA. Translation: AAA51827.1. | |||||||||||||||||||||||||
| IPI | IPI00941167. | ||||||||||||||||||||||||
| PIR | AOHUBA. A23561. | ||||||||||||||||||||||||
| RefSeq | NP_000511.2. | ||||||||||||||||||||||||
| UniGene | Hs.604479 Hs.709495 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| |||||||||||||||||||||||||
| SMR | P06865. Positions 23-528. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | P06865. 4 interactions. | ||||||||||||||||||||||||
| STRING | P06865. | ||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||
| CAZy | GH20. Glycoside Hydrolase Family 20. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PeptideAtlas | P06865. | ||||||||||||||||||||||||
| PRIDE | P06865. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENST00000268097; ENSP00000268097; ENSG00000213614; Homo sapiens. [Genome view] ENST00000423001; ENSP00000388226; ENSG00000213614; Homo sapiens. [Genome view] ENST00000429918; ENSP00000416187; ENSG00000213614; Homo sapiens. [Genome view] ENST00000457859; ENSP00000398026; ENSG00000213614; Homo sapiens. [Genome view] | ||||||||||||||||||||||||
| GeneID | 3073. | ||||||||||||||||||||||||
| KEGG | hsa:3073. | ||||||||||||||||||||||||
| UCSC | uc002aun.2. human. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 3073. | ||||||||||||||||||||||||
| GeneCards | GC15M070422. | ||||||||||||||||||||||||
| H-InvDB | HIX0012407. | ||||||||||||||||||||||||
| HGNC | HGNC:4878. HEXA. | ||||||||||||||||||||||||
| MIM | 272800. phenotype. 606869. gene. | ||||||||||||||||||||||||
| Orphanet | 845. Tay-Sachs disease. | ||||||||||||||||||||||||
| PharmGKB | PA29256. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | P06865. | ||||||||||||||||||||||||
| HOVERGEN | P06865. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BRENDA | 3.2.1.52. 247. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P06865. | ||||||||||||||||||||||||
| Bgee | P06865. | ||||||||||||||||||||||||
| CleanEx | HS_HEXA. | ||||||||||||||||||||||||
| Genevestigator | P06865. | ||||||||||||||||||||||||
| GermOnline | ENSG00000140488. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR001540. Glyco_hydro_20. IPR015883. Glyco_hydro_20_cat-core. IPR013781. Glyco_hydro_sg_catalytic. IPR015882. HexNAc-like_b. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. | ||||||||||||||||||||||||
| PANTHER | PTHR22600. Glyco_hydro_20. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR00738. GLHYDRLASE20. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | HEXA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P06865 Secondary accession number(s): Q53HS8, Q6AI32 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| Human chromosome 15 Human chromosome 15: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


