Reviewed, UniProtKB/Swiss-Prot P06865 (HEXA_HUMAN)

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

Name:

HEXA

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	Lysosome.
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 binding Inferred from electronic annotation. Source: InterPro protein heterodimerization activity Inferred 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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

529

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	P06865-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 42F0BD9202FB9559	FASTA	529	60,689
	10 20 30 40 50 60 MTSSRLWFSL LLAAAFAGRA TALWPWPQNF QTSDQRYVLY PNNFQFQYDV SSAAQPGCSV 70 80 90 100 110 120 LDEAFQRYRD LLFGSGSWPR PYLTGKRHTL EKNVLVVSVV TPGCNQLPTL ESVENYTLTI 130 140 150 160 170 180 NDDQCLLLSE TVWGALRGLE TFSQLVWKSA EGTFFINKTE IEDFPRFPHR GLLLDTSRHY 190 200 210 220 230 240 LPLSSILDTL DVMAYNKLNV FHWHLVDDPS FPYESFTFPE LMRKGSYNPV THIYTAQDVK 250 260 270 280 290 300 EVIEYARLRG IRVLAEFDTP GHTLSWGPGI PGLLTPCYSG SEPSGTFGPV NPSLNNTYEF 310 320 330 340 350 360 MSTFFLEVSS VFPDFYLHLG GDEVDFTCWK SNPEIQDFMR KKGFGEDFKQ LESFYIQTLL 370 380 390 400 410 420 DIVSSYGKGY VVWQEVFDNK VKIQPDTIIQ VWREDIPVNY MKELELVTKA GFRALLSAPW 430 440 450 460 470 480 YLNRISYGPD WKDFYVVEPL AFEGTPEQKA LVIGGEACMW GEYVDNTNLV PRLWPRAGAV 490 500 510 520 AERLWSNKLT SDLTFAYERL SHFRCELLRR GVQAQPLNVG FCEQEFEQT

References

	« Hide 'large scale' referencesShow '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.

Web resources

HEXAdb

HEXA mutation database

GeneDis

Tay Sachs disease website

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
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

PDBPDBe

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	[»]

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

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	October 13, 2009
This is version 121 of the entry and version 1 of the sequence. [Complete 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.