P06280 (AGAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-galactosidase A
EC=3.2.1.22

Alternative name(s):
Alpha-D-galactosidase A
Alpha-D-galactoside galactohydrolase
Melibiase
INN=Agalsidase

Gene names

Name:

GLA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	429 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)

Catalytic activity	Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Subunit structure	Homodimer. Ref.12
Subcellular location	Lysosome.
Involvement in disease	Fabry disease (FD) [MIM:301500]: Rare X-linked sphingolipidosis disease where glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaoslyceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Clinical recognition in males results from characteristic skin lesions (angiokeratomas) over the lower trunk. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease. Heterozygous females may exhibit the disorder in an attenuated form, they are more likely to show corneal opacities. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 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 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53
Pharmaceutical use	Available under the names Replagal (Transkaryotic Therapies) and Fabrazyme (Genzyme). Used as a long-term enzyme replacement therapy in patients with a confirmed diagnosis of Fabry disease.
Sequence similarities	Belongs to the glycosyl hydrolase 27 family.
RNA editing	Edited at position 396. Partially edited. Ref.9

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	RNA editing
Disease	Disease mutation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	glycoside catabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome glycosylceramide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of nitric oxide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of nitric-oxide synthase activity Inferred from sequence or structural similarity. Source: UniProtKB oligosaccharide metabolic process Inferred from direct assay PubMed 39940. Source: UniProtKB phospholipid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Inferred from mutant phenotype PubMed 1332979. Source: UniProtKB extracellular region Inferred from direct assay PubMed 3029062. Source: UniProtKB lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	alpha-galactosidase activity Inferred from direct assay PubMed 39940. Source: UniProtKB galactoside binding Inferred from electronic annotation. Source: Compara protein homodimerization activity Inferred from direct assay PubMed 6256390. Source: UniProtKB raffinose alpha-galactosidase activity Inferred from electronic annotation. Source: EC receptor binding Inferred from direct assay PubMed 1332979. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Chain

32 – 429

398

Alpha-galactosidase A

PRO_0000001004

Regions

Region

203 – 207

5

Substrate binding

Sites

Active site

170

1

Nucleophile By similarity

Active site

231

1

Proton donor By similarity

Amino acid modifications

Glycosylation

139

1

N-linked (GlcNAc...) Ref.12

Glycosylation

192

1

N-linked (GlcNAc...) Ref.12

Glycosylation

215

1

N-linked (GlcNAc...) Ref.10 Ref.12

Glycosylation

408

1

N-linked (GlcNAc...) Potential

Disulfide bond

52 ↔ 94

Disulfide bond

56 ↔ 63

Disulfide bond

142 ↔ 172

Disulfide bond

202 ↔ 223

Disulfide bond

378 ↔ 382

Natural variations

Natural variant

12 – 14

3

Missing in FD; has 4% of wild-type activity.

VAR_062550

Natural variant

20

1

A → P in FD; atypical. Ref.26 Ref.33

VAR_012362

Natural variant

31

1

A → V in FD. Ref.34 Ref.51

VAR_012363

Natural variant

32

1

L → P in FD. Ref.25

VAR_000431

Natural variant

34

1

N → S in FD. Ref.19 Ref.20 Ref.25
Corresponds to variant rs28935192 [ dbSNP | Ensembl ].

VAR_000432

Natural variant

35

1

G → R in FD. Ref.21

VAR_000433

Natural variant

40

1

P → L in FD. Ref.44

VAR_012364

Natural variant

40

1

P → S in FD. Ref.14 Ref.33 Ref.38

VAR_000434

Natural variant

42

1

M → L in FD. Ref.51

VAR_062551

Natural variant

42

1

M → V in FD. Ref.28 Ref.42

VAR_012365

Natural variant

43

1

G → R in FD. Ref.51

VAR_062552

Natural variant

45 – 46

2

LH → RS in FD.

VAR_012366

Natural variant

46

1

H → P in FD; has 36% of wild-type activity. Ref.53

VAR_062553

Natural variant

46

1

H → R in FD. Ref.34

VAR_012367

Natural variant

46

1

H → Y in FD. Ref.46

VAR_012368

Natural variant

47

1

W → G in FD. Ref.46

VAR_012369

Natural variant

49

1

R → L in FD. Ref.21

VAR_000435

Natural variant

49

1

R → P in FD. Ref.46

VAR_012370

Natural variant

49

1

R → S in FD. Ref.28

VAR_012371

Natural variant

52

1

C → R in FD. Ref.30 Ref.31

VAR_000436

Natural variant

52

1

C → S in FD.

VAR_000437

Natural variant

56

1

C → F in FD.

VAR_000438

Natural variant

56

1

C → G in FD. Ref.19
Corresponds to variant rs28935193 [ dbSNP | Ensembl ].

VAR_000439

Natural variant

56

1

C → Y in FD. Ref.28

VAR_012372

Natural variant

59

1

E → K in FD.

VAR_000440

Natural variant

65

1

S → T in FD; does not affect enzyme function. Ref.35 Ref.49

VAR_032290

Natural variant

66

1

E → Q in FD; has 52% of wild-type activity. Ref.18 Ref.23 Ref.33 Ref.53
Corresponds to variant rs28935191 [ dbSNP | Ensembl ].

VAR_000441

Natural variant

72

1

M → V in FD; atypical. Ref.33 Ref.37

VAR_000442

Natural variant

85

1

G → D in FD. Ref.25

VAR_000443

Natural variant

86

1

Y → C in FD. Ref.34

VAR_012373

Natural variant

89

1

L → P in FD. Ref.34

VAR_012374

Natural variant

89

1

L → R in FD.

VAR_000444

Natural variant

91

1

I → T in FD; mild. Ref.34

VAR_012375

Natural variant

92

1

D → H in FD. Ref.28

VAR_012376

Natural variant

92

1

D → Y in FD. Ref.34

VAR_012377

Natural variant

93

1

D → G in FD. Ref.28

VAR_012378

Natural variant

93

1

D → N in FD; has no enzyme activity. Ref.51 Ref.53

VAR_062554

Natural variant

94

1

C → S in FD. Ref.46

VAR_012379

Natural variant

94

1

C → Y in FD. Ref.34

VAR_012380

Natural variant

95

1

W → S in FD. Ref.44 Ref.46

VAR_012381

Natural variant

97

1

A → V in FD. Ref.34

VAR_012382

Natural variant

100

1

R → K in FD.

VAR_000445

Natural variant

100

1

R → T in FD. Ref.34

VAR_012383

Natural variant

112 – 117

6

Missing in FD.

VAR_000446

Natural variant

112

1

R → C in FD. Ref.18 Ref.23 Ref.33 Ref.42 Ref.44 Ref.46 Ref.51

VAR_000447

Natural variant

112

1

R → H in FD; mild. Ref.44 Ref.51

VAR_000448

Natural variant

112

1

R → S in FD. Ref.51

VAR_062555

Natural variant

113

1

F → L in FD; mild. Ref.34

VAR_012384

Natural variant

113

1

F → S in FD. Ref.46

VAR_012385

Natural variant

120 – 121

2

LA → PT in FD.

VAR_000449

Natural variant

120

1

L → V in FD; has 42% of wild-type activity. Ref.53

VAR_062556

Natural variant

128

1

G → E in FD. Ref.31

VAR_000450

Natural variant

131

1

L → P in FD.

VAR_000451

Natural variant

134

1

Y → S in FD. Ref.34 Ref.51

VAR_012386

Natural variant

135

1

A → V in FD. Ref.51

VAR_062557

Natural variant

138

1

G → R in FD. Ref.34

VAR_012387

Natural variant

142

1

C → R in FD. Ref.42

VAR_012388

Natural variant

142

1

C → Y in FD. Ref.24 Ref.33

VAR_000452

Natural variant

143

1

A → P in FD. Ref.47

VAR_000453

Natural variant

143

1

A → T in FD. Ref.34 Ref.46 Ref.52

VAR_012389

Natural variant

144

1

G → V in FD.

VAR_000454

Natural variant

146

1

P → S in FD; mild.
Corresponds to variant rs28935194 [ dbSNP | Ensembl ].

VAR_000455

Natural variant

148

1

S → N in FD. Ref.44

VAR_012390

Natural variant

148

1

S → R in FD. Ref.34 Ref.42

VAR_012391

Natural variant

156

1

A → T in FD. Ref.25
Corresponds to variant rs28935195 [ dbSNP | Ensembl ].

VAR_000456

Natural variant

156

1

A → V in FD. Ref.23 Ref.24 Ref.33

VAR_000457

Natural variant

162

1

W → C in FD. Ref.30

VAR_012392

Natural variant

162

1

W → R in FD. Ref.19
Corresponds to variant rs28935196 [ dbSNP | Ensembl ].

VAR_000458

Natural variant

163

1

G → V in FD. Ref.34

VAR_012393

Natural variant

165

1

D → V in FD. Ref.21 Ref.42

VAR_000459

Natural variant

166

1

L → V in FD. Ref.23 Ref.24 Ref.33

VAR_000460

Natural variant

170

1

D → V in FD. Ref.34

VAR_012394

Natural variant

171

1

G → D in FD. Ref.51

VAR_062558

Natural variant

172

1

C → R in FD. Ref.44

VAR_012395

Natural variant

172

1

C → Y in FD.

VAR_000461

Natural variant

183

1

G → D in FD. Ref.42

VAR_012396

Natural variant

187

1

M → V in FD. Ref.44

VAR_012397

Natural variant

201

1

S → F in FD. Ref.51

VAR_062559

Natural variant

202

1

C → W in FD. Ref.39
Corresponds to variant rs28936082 [ dbSNP | Ensembl ].

VAR_000462

Natural variant

202

1

C → Y in FD. Ref.34

VAR_012398

Natural variant

205 – 207

3

Missing in FD.

VAR_012399

Natural variant

205

1

P → T in FD. Ref.28 Ref.31

VAR_000463

Natural variant

215

1

N → S in FD; mild. Ref.20 Ref.38 Ref.42 Ref.46 Ref.51
Corresponds to variant rs28935197 [ dbSNP | Ensembl ].

VAR_000464

Natural variant

216

1

Y → D in FD. Ref.34

VAR_012400

Natural variant

219

1

I → N in FD.

VAR_000465

Natural variant

219

1

I → T in FD; has 46% of wild-type activity. Ref.53

VAR_062560

Natural variant

223

1

C → G in FD. Ref.39

VAR_012401

Natural variant

224

1

N → D in FD. Ref.38 Ref.39

VAR_000466

Natural variant

224

1

N → S in FD. Ref.44

VAR_012402

Natural variant

226

1

W → R in FD. Ref.44

VAR_012403

Natural variant

227

1

R → Q in FD. Ref.19 Ref.44
Corresponds to variant rs28935198 [ dbSNP | Ensembl ].

VAR_000467

Natural variant

230

1

A → T in FD. Ref.44

VAR_012404

Natural variant

231

1

D → N in FD. Ref.32

VAR_000468

Natural variant

234

1

D → E in FD. Ref.51

VAR_062561

Natural variant

235

1

S → C in FD. Ref.42

VAR_012405

Natural variant

236

1

W → C in FD. Ref.28

VAR_012406

Natural variant

236

1

W → L in FD. Ref.42

VAR_012407

Natural variant

242

1

I → N in FD. Ref.33

VAR_012408

Natural variant

244

1

D → H in FD. Ref.42

VAR_012409

Natural variant

244

1

D → N in FD.

VAR_000469

Natural variant

247

1

S → SWTS in FD.

VAR_000470

Natural variant

258

1

G → R in FD. Ref.46

VAR_012410

Natural variant

259

1

P → L in FD. Ref.42

VAR_012411

Natural variant

259

1

P → R in FD. Ref.46

VAR_012412

Natural variant

260

1

G → A in FD. Ref.23 Ref.33

VAR_012413

Natural variant

261

1

G → D in FD. Ref.33 Ref.51

VAR_012414

Natural variant

263

1

N → S in FD. Ref.34

VAR_012415

Natural variant

264

1

D → V in FD. Ref.19 Ref.51
Corresponds to variant rs28935486 [ dbSNP | Ensembl ].

VAR_000471

Natural variant

264

1

D → Y in FD. Ref.51

VAR_062562

Natural variant

265

1

P → R in FD. Ref.30

VAR_012416

Natural variant

266

1

D → H in FD. Ref.44

VAR_032291

Natural variant

266

1

D → N in FD. Ref.43

VAR_012418

Natural variant

266

1

D → V in FD. Ref.19
Corresponds to variant rs28935487 [ dbSNP | Ensembl ].

VAR_000472

Natural variant

267

1

M → I in FD. Ref.42 Ref.46

VAR_012419

Natural variant

269

1

V → A in FD. Ref.20
Corresponds to variant rs28935488 [ dbSNP | Ensembl ].

VAR_000473

Natural variant

272

1

N → K in FD.

VAR_000474

Natural variant

272

1

N → S in FD. Ref.50
Corresponds to variant rs28935495 [ dbSNP | Ensembl ].

VAR_032292

Natural variant

276

1

S → G in FD. Ref.51

VAR_062563

Natural variant

279

1

Q → E in FD; mild; does not significantly affect the enzyme activity but the mutant protein levels are decreased presumably in the ER of the cells. Ref.18 Ref.23 Ref.33 Ref.41
Corresponds to variant rs28935485 [ dbSNP | Ensembl ].

VAR_000475

Natural variant

279

1

Q → H in FD. Ref.46

VAR_012420

Natural variant

280

1

Q → H in FD. Ref.46

VAR_012421

Natural variant

284

1

M → T in FD. Ref.31

VAR_000476

Natural variant

285

1

A → P in FD. Ref.51

VAR_062564

Natural variant

287

1

W → C in FD. Ref.34

VAR_012422

Natural variant

287

1

W → G in FD. Ref.28

VAR_012423

Natural variant

288

1

A → D in FD.

VAR_000477

Natural variant

289

1

I → F in FD. Ref.42

VAR_012424

Natural variant

296

1

M → I in FD; atypical. Ref.23 Ref.26 Ref.33

VAR_012425

Natural variant

296

1

M → V in FD; mild. Ref.15

VAR_000478

Natural variant

297

1

S → F in FD. Ref.19
Corresponds to variant rs28935489 [ dbSNP | Ensembl ].

VAR_000479

Natural variant

298

1

N → H in FD. Ref.28 Ref.46

VAR_012426

Natural variant

298

1

N → K in FD. Ref.31

VAR_000480

Natural variant

298

1

N → S in FD. Ref.34

VAR_012427

Natural variant

300

1

L → F in FD. Ref.51

VAR_062565

Natural variant

301

1

R → Q in FD; mild; does not significantly affect the enzyme activity but the mutant protein levels are decreased presumably in the ER of the cells. Ref.16 Ref.18 Ref.23 Ref.25 Ref.27 Ref.33 Ref.39 Ref.41 Ref.44

VAR_000481

Natural variant

313

1

D → Y in FD. Ref.19 Ref.38 Ref.46
Corresponds to variant rs28935490 [ dbSNP | Ensembl ].

VAR_000482

Natural variant

316 – 322

7

Missing in FD.

VAR_012429

Natural variant

316

1

V → E in FD. Ref.21

VAR_000483

Natural variant

320

1

N → K in FD. Ref.23 Ref.33

VAR_012430

Natural variant

320

1

N → Y in FD. Ref.44

VAR_012431

Natural variant

321

1

Q → E in FD. Ref.42

VAR_012432

Natural variant

327

1

Q → K in FD. Ref.20 Ref.39
Corresponds to variant rs28935491 [ dbSNP | Ensembl ].

VAR_000484

Natural variant

328

1

G → A in FD. Ref.19 Ref.51
Corresponds to variant rs28935492 [ dbSNP | Ensembl ].

VAR_000486

Natural variant

328

1

G → R in FD. Ref.18 Ref.23 Ref.33

VAR_000485

Natural variant

328

1

G → V in FD. Ref.51

VAR_062566

Natural variant

338

1

E → K in FD. Ref.51

VAR_062567

Natural variant

340

1

W → R in FD. Ref.28

VAR_012433

Natural variant

341

1

E → K in FD. Ref.40

VAR_012434

Natural variant

342

1

R → Q in FD; severe.
Corresponds to variant rs28935493 [ dbSNP | Ensembl ].

VAR_000487

Natural variant

356

1

R → Q in FD; has 15% of wild-type activity. Ref.53

VAR_062568

Natural variant

356

1

R → W in FD; severe. Ref.17

VAR_000488

Natural variant

358

1

E → A in FD. Ref.51

VAR_062569

Natural variant

358

1

E → K in FD. Ref.36

VAR_000489

Natural variant

358

1

Missing in FD. Ref.31 Ref.33 Ref.42 Ref.51

VAR_000490

Natural variant

360

1

G → C in FD; has 6% of wild-type activity. Ref.53

VAR_062570

Natural variant

361

1

G → R in FD; severe. Ref.20
Corresponds to variant rs28935494 [ dbSNP | Ensembl ].

VAR_000491

Natural variant

363

1

R → H in FD. Ref.46

VAR_012435

Natural variant

373

1

G → D in FD. Ref.45

VAR_012436

Natural variant

373

1

G → S in FD. Ref.23 Ref.33

VAR_012437

Natural variant

377

1

A → D in FD. Ref.46

VAR_012438

Natural variant

378

1

C → Y in FD. Ref.42

VAR_012439

Natural variant

383

1

Missing in FD; severe; with facial telangiectasias. Ref.29

VAR_000492

Natural variant

396

1

F → Y in RNA edited version.

VAR_000493

Natural variant

404

1

Missing in FD; mild. Ref.19 Ref.34 Ref.51

VAR_000494

Natural variant

409

1

P → A in FD. Ref.46

VAR_012440

Natural variant

409

1

P → T in FD. Ref.46

VAR_012441

Natural variant

410

1

T → A in FD; mild. Ref.48

VAR_032293

Natural variant

414

1

L → S in FD. Ref.51

VAR_062571

Secondary structure

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429

Helix Strand Turn

Details...

Beta strand

42 – 46

5

Helix

47 – 50

4

Turn

56 – 58

3

Turn

60 – 62

3

Beta strand

63 – 65

3

Helix

66 – 78

13

Helix

81 – 84

4

Beta strand

88 – 90

3

Beta strand

102 – 104

3

Turn

110 – 112

3

Beta strand

113 – 115

3

Helix

116 – 126

11

Beta strand

130 – 140

11

Beta strand

144 – 146

3

Turn

149 – 151

3

Helix

152 – 162

11

Beta strand

166 – 170

5

Helix

177 – 193

17

Beta strand

199 – 202

4

Helix

205 – 208

4

Turn

209 – 211

3

Helix

216 – 222

7

Beta strand

224 – 227

4

Helix

236 – 248

13

Helix

250 – 253

4

Turn

254 – 256

3

Beta strand

261 – 264

4

Beta strand

272 – 274

3

Helix

277 – 289

13

Beta strand

294 – 296

3

Helix

305 – 311

7

Helix

314 – 320

7

Beta strand

329 – 334

6

Beta strand

337 – 343

7

Helix

345 – 347

3

Beta strand

349 – 355

7

Beta strand

359 – 361

3

Beta strand

363 – 368

6

Helix

369 – 371

3

Helix

373 – 375

3

Turn

376 – 378

3

Beta strand

379 – 390

12

Beta strand

392 – 398

7

Beta strand

402 – 407

6

Beta strand

412 – 419

8

Helix

420 – 424

5

Sequences

	Sequence		Length	Mass (Da)
	P06280 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 613F8BF21B107D7B	FASTA	429	48,767
	10 20 30 40 50 60 MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF MCNLDCQEEP 70 80 90 100 110 120 DSCISEKLFM EMAELMVSEG WKDAGYEYLC IDDCWMAPQR DSEGRLQADP QRFPHGIRQL 130 140 150 160 170 180 ANYVHSKGLK LGIYADVGNK TCAGFPGSFG YYDIDAQTFA DWGVDLLKFD GCYCDSLENL 190 200 210 220 230 240 ADGYKHMSLA LNRTGRSIVY SCEWPLYMWP FQKPNYTEIR QYCNHWRNFA DIDDSWKSIK 250 260 270 280 290 300 SILDWTSFNQ ERIVDVAGPG GWNDPDMLVI GNFGLSWNQQ VTQMALWAIM AAPLFMSNDL 310 320 330 340 350 360 RHISPQAKAL LQDKDVIAIN QDPLGKQGYQ LRQGDNFEVW ERPLSGLAWA VAMINRQEIG 370 380 390 400 410 420 GPRSYTIAVA SLGKGVACNP ACFITQLLPV KRKLGFYEWT SRLRSHINPT GTVLLQLENT MQMSLKDLL

References

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[1]	"Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A." Tsuji S., Martin B.M., Kaslow D.C., Migeon B.R., Choudary P.V., Stubblefield B.K., Mayor J.A., Murray G.J., Barranger J.A., Ginns E.I. Eur. J. Biochem. 165:275-280(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[2]	"Nucleotide sequence of the human alpha-galactosidase A gene." Kornreich R., Desnick R.J., Bishop D.F. Nucleic Acids Res. 17:3301-3302(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lymphoblast.
[3]	"Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci." Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., Gibbs R.A. Mamm. Genome 6:334-338(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Tissue: Uterus.
[6]	"Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme." Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M., Desnick R.J. Proc. Natl. Acad. Sci. U.S.A. 83:4859-4863(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-429, PARTIAL PROTEIN SEQUENCE. Tissue: Lung.
[7]	"A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A." Quinn M., Hantzopoulos P., Fidanza V., Calhoun D.H. Gene 58:177-188(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[8]	"Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region." Bishop D.F., Kornreich R., Desnick R.J. Proc. Natl. Acad. Sci. U.S.A. 85:3903-3907(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[9]	"Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion." Novo F.J., Kruszewski A., McDermot K.D., Goldspink G., Gorecki D.C. Nucleic Acids Res. 23:2636-2640(1995) [PubMed] [Europe PMC] [Abstract] Cited for: RNA EDITING OF POSITION 396.
[10]	"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-215, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"The molecular defect leading to Fabry disease: structure of human alpha-galactosidase." Garman S.C., Garboczi D.N. J. Mol. Biol. 337:319-335(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH PRODUCT, HOMODIMERIZATION, GLYCOSYLATION AT ASN-139; ASN-192 AND ASN-215.
[13]	"Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene." Eng C.M., Desnick R.J. Hum. Mutat. 3:103-111(1994) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FD VARIANTS.
[14]	"A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser." Koide T., Ishiura M., Iwai K., Inoue M., Kaneda Y., Okada Y., Uchida T. FEBS Lett. 259:353-356(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD SER-40.
[15]	"An atypical variant of Fabry's disease with manifestations confined to the myocardium." von Scheidt W., Eng C.M., Fitzmaurice T.F., Erdmann E., Hubner G., Olsen E.G.J., Christomanou H., Kandolf R., Bishop D.F., Desnick R.J. N. Engl. J. Med. 324:395-399(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD VAL-296.
[16]	"Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease." Sakuraba H., Oshima A., Fukuhara Y., Shimmoto M., Nagao Y., Bishop D.F., Desnick R.J., Suzuki Y. Am. J. Hum. Genet. 47:784-789(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD GLN-301.
[17]	"Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene." Bernstein H.S., Bishop D.F., Astrin K.H., Kornreich R., Eng C.M., Sakuraba H., Desnick R.J. J. Clin. Invest. 83:1390-1399(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD TRP-356.
[18]	"Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease." Ishii S., Sakuraba H., Suzuki Y. Hum. Genet. 89:29-32(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD GLN-66; CYS-112; GLU-279; GLN-301 AND ARG-328.
[19]	"Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease." Eng C.M., Resnick-Silverman L.A., Niehaus D.J., Astrin K.H., Desnick R.J. Am. J. Hum. Genet. 53:1186-1197(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD SER-34; GLY-56; ARG-162; GLN-227; VAL-264; VAL-266; PHE-297; TYR-313; ALA-328 AND ARG-404 DEL.
[20]	"Mutation analysis in patients with the typical form of Anderson-Fabry disease." Davies J.P., Winchester B.G., Malcolm S. Hum. Mol. Genet. 2:1051-1053(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD SER-34; SER-215; ALA-269; LYS-327 AND ARG-361.
[21]	"Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease." Davies J.P., Christomanou H., Winchester B.G., Malcolm S. Hum. Mol. Genet. 3:667-669(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD ARG-35; LEU-49; VAL-165 AND GLU-316.
[22]	"Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene." Eng C.M., Niehaus D.J., Enriquez A.L., Burgert T.S., Ludman M.D., Desnick R.J. Hum. Mol. Genet. 3:1795-1799(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD.
[23]	"Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease." Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H., Suzuki Y. Biochem. Biophys. Res. Commun. 214:1219-1224(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD GLN-66; CYS-112; VAL-156; VAL-166; ALA-260; GLU-279; ILE-296; GLN-301; LYS-320; ARG-328 AND SER-373.
[24]	"Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins." Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y. Hum. Genet. 95:557-561(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD TYR-142; VAL-156 AND VAL-166.
[25]	"Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease." Madsen K.M., Hasholt L., Soerensen S.A., Lagerstroem Fermer M., Dahl N. Hum. Mutat. 5:277-278(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD PRO-32; SER-34; ASP-85; THR-156 AND GLN-301.
[26]	"An atypical variant of Fabry's disease in men with left ventricular hypertrophy." Nakao S., Takenaka T., Maeda M., Kodama C., Tanaka A., Tahara M., Yoshida A., Kuriyama M., Hayashibe H., Sakuraba H., Tanaka H. N. Engl. J. Med. 333:288-293(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD PRO-20 AND ILE-296.
[27]	"Point mutation in the alpha-galactosidase A gene of atypical Fabry disease with only nephropathy." Sawada K., Mizoguchi K., Hishida A., Kaneko E., Koide Y., Nishimura K., Kimura M. Clin. Nephrol. 45:289-294(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD GLN-301.
[28]	"Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries." Davies J.P., Eng C.M., Hill J.A., Malcolm S., MacDermot K., Winchester B.G., Desnick R.J. Eur. J. Hum. Genet. 4:219-224(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD VAL-42; SER-49; TYR-56; HIS-92; GLY-93; THR-205; CYS-236; GLY-287; HIS-298 AND ARG-340.
[29]	"Novel trinucleotide deletion in Fabry's disease." Cariolou M.A., Christodoulides M., Manoli P., Kokkofitou A., Tsambaos D. Hum. Genet. 97:468-470(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD PHE-383 DEL.
[30]	"Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease." Germain D.P., Biasotto M., Tosi M., Meo T., Kahn A., Poenaru L. Hum. Genet. 98:719-726(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD ARG-52; CYS-162; ARG-265 AND 316-VAL--ASP-322 DEL.
[31]	"A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene." Blanch L.C., Meaney C., Morris C.P. Hum. Mutat. 8:38-43(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD ARG-52; GLU-128; THR-205; THR-284; LYS-298 AND GLU-358 DEL.
[32]	"Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene." Redonnet-Vernhet I., Ploos van Amstel J.K., Jansen R.P.M., Wevers R.A., Salvayre R., Levade T. J. Med. Genet. 33:682-688(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD ASN-231.
[33]	"Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis." Takata T., Okumiya T., Hayashibe H., Shimmoto M., Kase R., Itoh K., Utsumi K., Kamei S., Sakuraba H. Brain Dev. 19:111-116(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD PRO-20; SER-40; GLN-66; VAL-72; CYS-112; TYR-142; VAL-156; VAL-166; ASN-242; ALA-260; ASP-261; GLU-279; ILE-296; GLN-301; LYS-320; ARG-328; GLU-358 DEL AND SER-373.
[34]	"Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes." Eng C.M., Ashley G.A., Burgert T.S., Enriquez A.L., D'Souza M., Desnick R.J. Mol. Med. 3:174-182(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD VAL-31; 45-ARG-SER-46; ARG-46; CYS-86; PRO-89; THR-91; TYR-92; TYR-94; VAL-97; THR-100; LEU-113; SER-134; ARG-138; THR-143; ARG-148; VAL-163; VAL-170; TYR-202; 205-PRO--TYR-207 DEL; ASP-216; SER-263; CYS-287; SER-298 AND ARG-404 DEL.
[35]	"Identification of a novel point mutation (S65T) in alpha-galactosidase A gene in Chinese patients with Fabry disease." Chen C.-H., Shyu P.-W., Wu S.-J., Sheu S.-S., Desnick R.J., Hsiao K.-J. Hum. Mutat. 11:328-330(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD THR-65.
[36]	"A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease." Miyazaki T., Kajita M., Ohmori S., Mizutani N., Niwa T., Murata Y., Seo H. Hum. Mutat. Suppl. 1:S139-S140(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD LYS-358.
[37]	"Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote." Okumiya T., Kawamura O., Itoh K., Kase R., Ishii S., Kamei S., Sakuraba H. Hum. Mutat. Suppl. 1:S213-S216(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD VAL-72.
[38]	"Mutation analysis in 11 French patients with Fabry disease." Guffon N., Froissart R., Chevalier-Porst F., Maire I. Hum. Mutat. Suppl. 1:S288-S290(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD SER-40; SER-215; ASP-224; TYR-313 AND TRP-THR-SER-247 INS.
[39]	"Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches." Germain D.P., Poenaru L. Biochem. Biophys. Res. Commun. 257:708-713(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD TRP-202; GLY-223; ASP-224; GLN-301 AND LYS-327.
[40]	"The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A." Beyer E.M., Karpova E.A., Udalova O.V., Ploos van Amstel J.K., van Diggelen O.P., Tsvetkova I.V. Clin. Chim. Acta 280:81-89(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD LYS-341.
[41]	"Characterization of two alpha-galactosidase mutants (Q279E and R301Q) found in an atypical variant of Fabry disease." Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoh K., Sandhoff K., Sakuraba H. Biochim. Biophys. Acta 1501:227-235(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS FD GLU-279 AND GLN-301.
[42]	"Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease." Topaloglu A.K., Ashley G.A., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J. Mol. Med. 5:806-811(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD VAL-42; CYS-112; ARG-142; ARG-148; VAL-165; ASP-183; SER-215; CYS-235; LEU-236; HIS-244; LEU-259; ILE-267; PHE-289; GLU-321; GLU-358 DEL AND TYR-378.
[43]	"Identification of four novel mutations in five unrelated Korean families with Fabry disease." Lee J.-K., Kim G.-H., Kim J.-S., Kim K.-K., Lee M.-C., Yoo H.-W. Clin. Genet. 58:228-233(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD ASN-266.
[44]	"Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes." Ashton-Prolla P., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J. J. Invest. Med. 48:227-235(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD LEU-40; SER-95; CYS-112; HIS-112; ASN-148; ARG-172; VAL-187; SER-224; ARG-226; GLN-227; THR-230; HIS-266; GLN-301 AND TYR-320.
[45]	"Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease." Germain D.P., Salard D., Fellmann F., Azibi K., Caillaud C., Bernard M.-C., Poenaru L. Hum. Mutat. 17:353-353(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD ASP-373.
[46]	"Fabry disease: 20 novel GLA mutations in 35 families." Blaydon D., Hill J.A., Winchester B.G. Hum. Mutat. 18:459-459(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD TYR-46; GLY-47; PRO-49; SER-94; SER-95; CYS-112; SER-113; THR-143; SER-215; ARG-258; ARG-259; ILE-267; HIS-279; HIS-280; HIS-298; TYR-313; HIS-363; ASP-377; ALA-409 AND THR-409.
[47]	"Natural history of Fabry renal disease: influence of alpha-galactosidase A activity and genetic mutations on clinical course." Branton M.H., Schiffmann R., Sabnis S.G., Murray G.J., Quirk J.M., Altarescu G., Goldfarb L., Brady R.O., Balow J.E., Austin H.A. III, Kopp J.B. Medicine (Baltimore) 81:122-138(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD PRO-143.
[48]	"Two novel mutations in the alpha-galactosidase A gene in Chinese patients with Fabry disease." Yang C.-C., Lai L.-W., Whitehair O., Hwu W.-L., Chiang S.-C., Lien Y.-H.H. Clin. Genet. 63:205-209(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD ALA-410.
[49]	"Analysis of splice-site mutations of the alpha-galactosidase A gene in Fabry disease." Lai L.-W., Whitehair O., Wu M.-J., O'Meara M., Lien Y.-H.H. Clin. Genet. 63:476-482(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT FD THR-65.
[50]	"Remarkable variability in renal disease in a large Slovenian family with Fabry disease." Verovnik F., Benko D., Vujkovac B., Linthorst G.E. Eur. J. Hum. Genet. 12:678-681(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD SER-272.
[51]	"Detection of alpha-galactosidase a mutations causing Fabry disease by denaturing high performance liquid chromatography." Shabbeer J., Robinson M., Desnick R.J. Hum. Mutat. 25:299-305(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD VAL-31; LEU-42; ARG-43; ASN-93; CYS-112; HIS-112; SER-112; SER-134; VAL-135; ASP-171; PHE-201; SER-215; GLU-234; ASP-261; TYR-264; VAL-264; GLY-276; PRO-285; PHE-300; ALA-328; VAL-328; LYS-338; ALA-358; GLU-358 DEL; ARG-404 DEL AND SER-414.
[52]	"Later-onset Fabry disease: an adult variant presenting with the cramp-fasciculation syndrome." Nance C.S., Klein C.J., Banikazemi M., Dikman S.H., Phelps R.G., McArthur J.C., Rodriguez M., Desnick R.J. Arch. Neurol. 63:453-457(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FD THR-143.
[53]	"Newborn screening for Fabry disease in Taiwan reveals a high incidence of the later-onset GLA mutation c.936+919G>A (IVS4+919G>A)." Hwu W.L., Chien Y.H., Lee N.C., Chiang S.C., Dobrovolny R., Huang A.C., Yeh H.Y., Chao M.C., Lin S.J., Kitagawa T., Desnick R.J., Hsu L.W. Hum. Mutat. 30:1397-1405(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FD 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219; GLN-356 AND CYS-360, CHARACTERIZATION OF VARIANTS FD 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219; GLN-356 AND CYS-360.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05790 mRNA. Translation: CAA29232.1.
X14448 Genomic DNA. Translation: CAA32617.1.
U78027 Genomic DNA. Translation: AAB64203.1.
AL035422 Genomic DNA. Translation: CAB55878.1.
BC002689 mRNA. Translation: AAH02689.1.
M13571 Genomic DNA. Translation: AAA51676.1.
D00039 mRNA. No translation available.
M18242 Genomic DNA. Translation: AAA52514.1.
X16889 mRNA. No translation available.
M20317 Genomic DNA. Translation: AAA52559.1. Sequence problems.

IPI

IPI00025869.

PIR

GBHUA. S04081.

RefSeq

NP_000160.1. NM_000169.2.

UniGene

Hs.69089.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R46	X-ray	3.25	A/B	32-429	[»]
1R47	X-ray	3.45	A/B	32-429	[»]
3GXN	X-ray	3.01	A/B	32-429	[»]
3GXP	X-ray	2.20	A/B	32-429	[»]
3GXT	X-ray	2.70	A/B	32-429	[»]
3HG2	X-ray	2.30	A/B	32-429	[»]
3HG3	X-ray	1.90	A/B	32-429	[»]
3HG4	X-ray	2.30	A/B	32-429	[»]
3HG5	X-ray	2.30	A/B	32-429	[»]
3LX9	X-ray	2.04	A/B	32-429	[»]
3LXA	X-ray	3.04	A/B	32-429	[»]
3LXB	X-ray	2.85	A/B	32-429	[»]
3LXC	X-ray	2.35	A/B	32-429	[»]
3S5Y	X-ray	2.10	A/B	32-429	[»]
3S5Z	X-ray	2.00	A/B	32-429	[»]
3TV8	X-ray	2.64	A/B	32-429	[»]

ProteinModelPortal

P06280.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06280. 2 interactions.

STRING

9606.ENSP00000218516.

Protein family/group databases

Allergome

9621. Hom s alpha-Galactosidase.

CAZy

GH27. Glycoside Hydrolase Family 27.

PTM databases

PhosphoSite

P06280.

Polymorphism databases

DMDM

113499.

Proteomic databases

PaxDb

P06280.

PeptideAtlas

P06280.

PRIDE

P06280.

Protocols and materials databases

DNASU

2717.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000218516; ENSP00000218516; ENSG00000102393.
ENST00000598114; ENSP00000471787; ENSG00000268815.

GeneID

2717.

KEGG

hsa:2717.

UCSC

uc004ehl.1. human.

Organism-specific databases

CTD

2717.

GeneCards

GC0XM100652.

HGNC

HGNC:4296. GLA.

HPA

HPA000237.
HPA000966.

MIM

300644. gene.
301500. phenotype.

neXtProt

NX_P06280.

Orphanet

324. Fabry disease.

PharmGKB

PA28707.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG68897.

HOGENOM

HOG000161224.

HOVERGEN

HBG001989.

InParanoid

P06280.

KO

K01189.

OMA

GYKHMSL.

OrthoDB

EOG4933J0.

PhylomeDB

P06280.

Enzyme and pathway databases

BioCyc

MetaCyc:HS02389-MONOMER.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P06280.

Bgee

P06280.

CleanEx

HS_GLA.

Genevestigator

P06280.

GermOnline

ENSG00000102393. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF02065. Melibiase. 1 hit.
[Graphical view]

PRINTS

PR00740. GLHYDRLASE27.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06280.

ChEMBL

CHEMBL2524.

DrugBank

DB00103. Agalsidase beta.

EvolutionaryTrace

P06280.

GenomeRNAi

2717.

NextBio

10728.

SOURCE

Search...

Entry information

Entry name

AGAL_HUMAN

Accession

Primary (citable) accession number: P06280

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 156 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.