Reviewed, UniProtKB/Swiss-Prot P04062 (GLCM_HUMAN)

Names and origin

Protein names

Recommended name:
    Glucosylceramidase
    EC=3.2.1.45
Alternative name(s):
    Beta-glucocerebrosidase
    Acid beta-glucosidase
    D-glucosyl-N-acylsphingosine glucohydrolase
    Alglucerase
    Imiglucerase

Gene names

Name:	GBA
Synonyms:	GC, GLUC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	536 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	D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine.
Enzyme regulation	Requires saposin-C and anionic phospholipids for activity.
Subunit structure	Interacts with saposin-C. Ref.17
Subcellular location	Lysosome membrane; Peripheral membrane protein; Lumenal side. Note: Interaction with saposin-C promotes membrane association. Ref.25
Involvement in disease	Defects in GBA are the cause of Gaucher disease (GD) [MIM:230800]; also known as glucocerebrosidase deficiency. GD is the most prevalent lysosomal storage disease, characterized by accumulation of glucosylceramide in the reticulo-endothelial system. Different clinical forms are recognized depending on the presence (neuronopathic forms) or absence of central nervous system involvement, severity and age of onset. Ref.5 Ref.14 Ref.23 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.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Defects in GBA are the cause of Gaucher disease type 1 (GD1) [MIM:230800]; also known as adult non-neuronopathic Gaucher disease. GD1 is characterized by hepatosplenomegaly with consequent anemia and thrombopenia, and bone involvement. The central nervous system is not involved. Ref.67 Ref.71 Defects in GBA are the cause of Gaucher disease type 2 (GD2) [MIM:230900]; also known as acute neuronopathic. GD2 is the most severe form and is universally progressive and fatal. It manifests soon after birth, with death generally occurring before patients reach two years of age. Ref.67 Ref.71 Defects in GBA are the cause of Gaucher disease type 3 (GD3) [MIM:231000]; also known as subacute neuronopathic. GD3 has central nervous manifestations. Ref.67 Ref.71 Defects in GBA are the cause of Gaucher disease type 3C [MIM:231005]; also known as pseudo-Gaucher disease or Gaucher-like disease. Ref.67 Ref.71 Defects in GBA are the cause of perinatal lethal Gaucher disease [MIM:608013]. It is a distinct form of Gaucher disease type 2, characterized by fetal onset. Hydrops fetalis, in utero fetal death and neonatal distress are prominent features. When hydrops is absent, neurologic involvement begins in the first week and leads to death within 3 months. Hepatosplenomegaly is a major sign, and is associated with ichthyosis, arthrogryposis, and facial dysmorphism. Ref.67 Ref.71 Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis [MIM:236750]. Hydrops fetalis is a generalized edema of the fetus with fluid accumulation in the body cavities. Ref.67 Ref.71 Defects in GBA may be a risk factor in the development of Parkinson disease (PD) [MIM:168600]. Simultaneous occurrence of Parkinson disease and Gaucher disease is marked by atypical parkinsonism generally presenting by the fourth through sixth decades of life. The combination progresses inexorably and is refractory to conventional anti-Parkinson therapy. Ref.67 Ref.71
Pharmaceutical use	Available under the names Ceredase and Cerezyme (Genzyme). Used to treat Gaucher's disease.
Sequence similarities	Belongs to the glycosyl hydrolase 30 family.

Ontologies

Keywords
Biological process	Lipid metabolism Sphingolipid metabolism
Cellular component	Lysosome Membrane
Coding sequence diversity	Alternative initiation Alternative splicing Polymorphism
Disease	Disease mutation Gaucher disease Ichthyosis
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro lysosome organization Inferred from electronic annotation. Source: UniProtKB-KW sphingolipid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro glucosylceramidase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Scarb2	O35114	1	EBI-1564609,EBI-1564519	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform Long (identifier: P04062-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Has a 39 residue signal sequence. The upstream initiation site produces two to three times as much protein as does the downstream initiation codon.

Isoform Short (identifier: P04062-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.

Note: Has a 19 residue signal sequence.

Isoform 3 (identifier: P04062-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-161: Missing.
     422-423: LA → PS
     425-536: Missing.

Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 39

39

In isoform Long Ref.12

Signal peptide

21 – 39

19

In isoform Short Ref.12

Chain

40 – 536

497

Glucosylceramidase

PRO_0000012177

Sites

Active site

274

1

Proton donor Ref.16 Ref.22

Active site

379

1

Nucleophile Ref.16 Ref.22

Amino acid modifications

Glycosylation

58

1

N-linked (GlcNAc...) Ref.21 Ref.24

Glycosylation

98

1

N-linked (GlcNAc...) Ref.24 Ref.18

Glycosylation

185

1

N-linked (GlcNAc...) Ref.24 Ref.18

Glycosylation

309

1

N-linked (GlcNAc...) Ref.18

Glycosylation

501

1

N-linked (GlcNAc...) Potential

Disulfide bond

43 ↔ 55

Ref.21

Disulfide bond

57 ↔ 62

Ref.21

Natural variations

Alternative sequence

1 – 161

161

Missing in isoform 3.

VSP_025216

Alternative sequence

1 – 20

20

Missing in isoform Short.

VSP_018800

Alternative sequence

422 – 423

2

LA → PS in isoform 3.

VSP_025217

Alternative sequence

425 – 536

112

Missing in isoform 3.

VSP_025218

Natural variant

54

1

V → L in GD. Ref.40

VAR_003255

Natural variant

55

1

C → S in GD; neuronopathic and perinatal lethal forms; loss of activity. Ref.64 Ref.68

VAR_032394

Natural variant

63

1

D → N in GD; type 1; very low activity. Ref.70

VAR_032395

Natural variant

76

1

F → V in GD. Ref.45

VAR_003256

Natural variant

80

1

E → K in GD; type 2. dbSNP rs1141808. Ref.54

VAR_009033

Natural variant

82

1

T → I in GD.

VAR_003257

Natural variant

85

1

G → E in GD. Ref.40 Ref.45

VAR_003258

Natural variant

87

1

R → Q in GD; 20% of normal activity. Ref.45 Ref.47 Ref.63

VAR_032197

Natural variant

87

1

R → W in GD; mild. dbSNP rs1141814. Ref.45 Ref.47 Ref.63

VAR_003259

Natural variant

92

1

M → T: dbSNP rs3205619.

VAR_032396

Natural variant

118

1

K → N in GD; mild; 8% of normal activity; increases susceptibility to proteolytic degradation. Ref.63

VAR_003260

Natural variant

129

1

A → T in GD. Ref.63

VAR_032397

Natural variant

146

1

S → L in GD; type 2. Ref.50

VAR_009034

Natural variant

152

1

G → E in GD. Ref.56

VAR_003261

Natural variant

156

1

N → D in GD. Ref.63

VAR_032398

Natural variant

158

1

I → S in GD; type 1; very low activity. Ref.70

VAR_032399

Natural variant

158

1

I → T in GD. Ref.70

VAR_003262

Natural variant

159

1

R → Q in GD; type 2; 13% of normal activity. Ref.45 Ref.63 Ref.70

VAR_003263

Natural variant

159

1

R → W in GD; severe. Ref.45 Ref.63 Ref.70

VAR_003264

Natural variant

161

1

P → L in GD; 16% of normal activity.

VAR_032198

Natural variant

161

1

P → S in GD; mild.

VAR_003265

Natural variant

162

1

M → V in GD; loss of activity; increases susceptibility to proteolytic degradation.

VAR_032199

Natural variant

166

1

D → V in GD; 9% of normal activity; increases susceptibility to proteolytic degradation.

VAR_032200

Natural variant

170

1

R → C in GD; type 1 and type 2. Ref.54 Ref.63 Ref.70

VAR_009035

Natural variant

170

1

R → L in GD. Ref.54 Ref.63 Ref.70

VAR_009036

Natural variant

173

1

T → I in GD. Ref.56 Ref.62 Ref.63

VAR_032400

Natural variant

173

1

T → P in GD. Ref.56 Ref.62 Ref.63

VAR_003266

Natural variant

175

1

A → E in GD. Ref.65

VAR_032401

Natural variant

179

1

D → H in GD.

VAR_003267

Natural variant

196

1

K → Q in GD; severe.

VAR_003268

Natural variant

198

1

P → L in GD. Ref.50 Ref.66

VAR_009037

Natural variant

198

1

P → T in GD. Ref.50 Ref.66

VAR_032402

Natural variant

200

1

I → N in GD; 5% of normal activity.

VAR_032201

Natural variant

200

1

I → S in GD.

VAR_010059

Natural variant

201

1

H → P in GD. Ref.65

VAR_032403

Natural variant

209

1

R → C in GD. Ref.63

VAR_032404

Natural variant

209

1

R → P in GD. Ref.63

VAR_003269

Natural variant

213

1

L → F in GD; 12% of normal activity.

VAR_032202

Natural variant

215

1

A → D in GD. Ref.36

VAR_003270

Natural variant

217

1

P → S in GD; type 2. Ref.38

VAR_003271

Natural variant

221

1

P → L in GD; type 1; very low activity. Ref.36 Ref.70

VAR_032405

Natural variant

221

1

P → T in GD. Ref.36 Ref.70

VAR_003272

Natural variant

223

1

W → R in GD; gene conversion. Ref.5

VAR_003273

Natural variant

224

1

L → F in GD; 4% of normal activity; increases susceptibility to proteolytic degradation.

VAR_032203

Natural variant

227

1

N → K in GD; gene conversion. dbSNP rs381418. Ref.40 Ref.45 Ref.63

VAR_003275

Natural variant

227

1

N → S in GD; type 2. dbSNP rs364897. Ref.40 Ref.45 Ref.63

VAR_003274

Natural variant

228

1

G → V in GD. Ref.48

VAR_010060

Natural variant

229

1

A → E in GD; type 2. Ref.63

VAR_009038

Natural variant

229

1

A → T in GD. Ref.63

VAR_032406

Natural variant

230

1

V → E in GD; type 1; very low activity. Ref.5 Ref.57 Ref.70

VAR_032407

Natural variant

230

1

V → G in GD; mild; gene conversion. dbSNP rs381427. Ref.5 Ref.57 Ref.70

VAR_003276

Natural variant

232

1

G → E in GD; 7% of normal activity.

VAR_032204

Natural variant

234

1

G → E in GD; severe. Ref.47 Ref.62

VAR_003277

Natural variant

234

1

G → W in GD. Ref.47 Ref.62

VAR_009039

Natural variant

235

1

S → P in GD; type 2; gene conversion. dbSNP rs1064644. Ref.5 Ref.63

VAR_003278

Natural variant

237

1

K → E in GD; severe; loss of activity; increases susceptibility to proteolytic degradation. Ref.65

VAR_032205

Natural variant

241

1

G → E in GD. Ref.5 Ref.36 Ref.47 Ref.59 Ref.63 Ref.66 Ref.70

VAR_010061

Natural variant

241

1

G → R in GD; type 1 and type 2; gene conversion. Ref.5 Ref.36 Ref.47 Ref.59 Ref.63 Ref.66 Ref.70

VAR_003279

Natural variant

244

1

Y → C in GD. Ref.59

VAR_010062

Natural variant

251

1

Y → H in GD.

VAR_003280

Natural variant

252

1

F → I in GD; type 2; gene conversion. dbSNP rs381737. Ref.5 Ref.45 Ref.47 Ref.48 Ref.59 Ref.63

VAR_003281

Natural variant

255

1

F → Y in GD; mild. Ref.30

VAR_003282

Natural variant

270

1

T → R in GD. Ref.66

VAR_032408

Natural variant

276

1

S → P in GD.

VAR_003283

Natural variant

290

1

F → L in GD; perinatal lethal form. Ref.65

VAR_032409

Natural variant

294

1

H → Q in GD; type 1 and type 2. Ref.70

VAR_009040

Natural variant

296

1

R → Q in GD; type 2. Ref.36 Ref.63

VAR_003284

Natural variant

298

1

F → L in GD; type 2; 4% of normal activity.

VAR_009041

Natural variant

303

1

L → I in GD; 5% of normal activity.

VAR_032206

Natural variant

304

1

G → D in GD.

VAR_010063

Natural variant

305

1

P → R in GD; mild.

VAR_003285

Natural variant

310

1

S → G: dbSNP rs1057942. Ref.5 Ref.47

VAR_032410

Natural variant

310

1

S → N in GD; less than 5% of normal activity. Ref.47

VAR_010064

Natural variant

324

1

R → C in GD; type 1. Ref.36 Ref.63 Ref.70

VAR_003286

Natural variant

324

1

R → H in GD; type 2. Ref.36 Ref.63 Ref.70

VAR_009042

Natural variant

328

1

P → L in GD; mild.

VAR_003287

Natural variant

342

1

K → I in GD.

VAR_003288

Natural variant

343

1

Y → C in GD; type 2; 16% of normal activity; increases susceptibility to proteolytic degradation.

VAR_009043

Natural variant

348

1

A → V in GD.

VAR_003289

Natural variant

350

1

H → R in perinatal lethal GD. Ref.61

VAR_009044

Natural variant

351

1

W → C in GD; mild.

VAR_003290

Natural variant

352

1

Y → H in GD. Ref.41

VAR_003291

Natural variant

354

1

D → H in GD.

VAR_003292

Natural variant

357

1

A → D in GD.

VAR_003293

Natural variant

362

1

T → I in GD; 6% of normal activity.

VAR_003294

Natural variant

363

1

L → P in GD.

VAR_003295

Natural variant

364

1

G → R in GD; type 2. Ref.5

VAR_003296

Natural variant

365

1

E → K in GD; mild; 42% of normal activity. dbSNP rs2230288.

VAR_003297

Natural variant

368

1

R → H: dbSNP rs1064648. Ref.5

VAR_032411

Natural variant

380

1

A → T in GD. Ref.50 Ref.63

VAR_009045

Natural variant

381

1

C → G in GD; type 2; loss of activity.

VAR_003298

Natural variant

388

1

E → K in GD; 12% of normal activity.

VAR_032207

Natural variant

391

1

V → L in GD. Ref.47

VAR_010065

Natural variant

392

1

R → G in GD. Ref.55

VAR_010066

Natural variant

392

1

R → W in GD; 5% of normal activity. Ref.55

VAR_032208

Natural variant

398

1

R → Q in GD; mild. Ref.41

VAR_003299

Natural variant

400

1

M → I in GD. Ref.66

VAR_032412

Natural variant

402

1

Y → C in GD; 8% of normal activity; increases susceptibility to proteolytic degradation.

VAR_032209

Natural variant

403

1

S → T in GD; mild.

VAR_003300

Natural variant

405

1

S → G in GD. Ref.48 Ref.50

VAR_010067

Natural variant

405

1

S → N in GD. Ref.48 Ref.50

VAR_009046

Natural variant

408

1

T → M in GD. dbSNP rs2230289. Ref.63

VAR_003301

Natural variant

409

1

N → S in GD; common mutation; alters interaction with saposin-C and membranes and thereby reduces enzyme activity; mild. Ref.14 Ref.35 Ref.37 Ref.39 Ref.47 Ref.57 Ref.58 Ref.62 Ref.63 Ref.69 Ref.70

VAR_003302

Natural variant

410

1

L → V in GD; 15% of normal activity; increases susceptibility to proteolytic degradation.

VAR_032210

Natural variant

414

1

V → L in GD; mild. Ref.44

VAR_010068

Natural variant

416

1

G → S in GD; mild. Ref.62 Ref.63

VAR_003303

Natural variant

417

1

W → G in GD. Ref.36

VAR_003304

Natural variant

419

1

D → A in GD; type 2. Ref.36

VAR_003305

Natural variant

419

1

D → H in GD; 4% of normal activity. Ref.36

VAR_032211

Natural variant

419

1

D → N in GD. Ref.36

VAR_003306

Natural variant

421

1

N → K in GD; 22% of normal activity.

VAR_032212

Natural variant

426

1

P → L in GD. Ref.39

VAR_010069

Natural variant

428

1

G → E in GD; type 2. Ref.56

VAR_003307

Natural variant

429

1

G → R in GD; 17% of normal activity.

VAR_032213

Natural variant

430

1

P → L in GD. Ref.56

VAR_003308

Natural variant

431

1

N → I in GD; type 2. Ref.56

VAR_003309

Natural variant

432

1

W → R in GD. Ref.50

VAR_009047

Natural variant

433

1

V → L in GD; severe; 12% of normal activity. Ref.39 Ref.63

VAR_003310

Natural variant

435

1

N → T in GD; mild. Ref.42

VAR_003311

Natural variant

436

1

F → S in GD; 6% of normal activity; alters protein stability and increases susceptibility to proteolytic degradation.

VAR_032214

Natural variant

437

1

V → F in perinatal lethal GD. Ref.43 Ref.61

VAR_009048

Natural variant

437

1

V → L in GD; type 3. Ref.43

VAR_010070

Natural variant

438

1

D → N in GD; type 1 and type 2; 14% of normal activity; increases susceptibility to proteolytic degradation. Ref.34 Ref.63 Ref.70

VAR_003312

Natural variant

438

1

D → Y in GD. Ref.34 Ref.63 Ref.70

VAR_032413

Natural variant

440

1

P → L in GD. Ref.58 Ref.70

VAR_010071

Natural variant

441

1

I → F in GD; type 3. Ref.44 Ref.65

VAR_032414

Natural variant

441

1

I → T in GD; mild. Ref.44 Ref.65

VAR_010072

Natural variant

448

1

D → H in GD; type 1 and type neuronopathic; at homozygosity it causes Gaucher disease type 3C; gene conversion; very low activity; alters protein stability. dbSNP rs1064651. Ref.37 Ref.48 Ref.59 Ref.62 Ref.63 Ref.64 Ref.70

VAR_003313

Natural variant

448

1

D → V in GD; severe; very low activity; alters protein stability. Ref.37 Ref.48 Ref.59 Ref.62 Ref.63 Ref.64 Ref.70

VAR_003314

Natural variant

450

1

F → I in GD.

VAR_010073

Natural variant

451

1

Y → H in GD. Ref.56

VAR_003315

Natural variant

452

1

K → Q in GD. Ref.48

VAR_010074

Natural variant

454

1

P → R in GD; type 2.

VAR_003316

Natural variant

455

1

M → V in GD; loss of activity; increases susceptibility to proteolytic degradation.

VAR_032215

Natural variant

456

1

F → V in GD.

VAR_003317

Natural variant

457

1

Y → C in GD. Ref.35 Ref.70

VAR_003318

Natural variant

460

1

G → D in GD; type 1; associated with R-490; loss of activity. Ref.70

VAR_032415

Natural variant

464

1

K → E in GD; severe.

VAR_003319

Natural variant

483

1

L → P in GD; type 1 and type 2; common mutation; gene conversion; very low activity; alters protein stability. Ref.37 Ref.39 Ref.45 Ref.48 Ref.54 Ref.59 Ref.62 Ref.63 Ref.70

VAR_003321

Natural variant

483

1

L → R in GD; severe. Ref.37 Ref.39 Ref.45 Ref.48 Ref.54 Ref.59 Ref.62 Ref.63 Ref.70

VAR_003320

Natural variant

485

1

A → P in GD.

VAR_003322

Natural variant

490

1

H → R in GD; type 1; associated with D-460. Ref.66 Ref.70

VAR_032416

Natural variant

495

1

A → P in GD; gene conversion. dbSNP rs368060.

VAR_003323

Natural variant

500

1

L → P in GD; 10% of normal activity; increases susceptibility to proteolytic degradation.

VAR_032216

Natural variant

501

1

N → K in GD; type 2. Ref.46

VAR_009049

Natural variant

502

1

R → C in GD; 37% of normal activity. Ref.37 Ref.63

VAR_003324

Natural variant

502

1

R → P in GD; loss of activity; increases susceptibility to proteolytic degradation. Ref.37 Ref.63

VAR_032217

Natural variant

509

1

L → P

VAR_003325

Natural variant

513

1

D → Y in GD; type 2. Ref.52

VAR_009050

Natural variant

517

1

G → S in GD.

VAR_003326

Natural variant

530

1

T → I in GD; type 3; severe. Ref.43

VAR_010075

Natural variant

535

1

R → C in GD; mild. Ref.33 Ref.48

VAR_003327

Natural variant

535

1

R → H in GD; mild. Ref.33 Ref.48

VAR_003328

Experimental info

Mutagenesis

43

1

C → S: Loss of activity. Ref.23

Mutagenesis

57

1

C → S: Loss of activity. Ref.23

Mutagenesis

62

1

C → S: Loss of activity. Ref.23

Mutagenesis

379

1

E → G: Decreases activity 1000-fold. Ref.16

Sequence conflict

227

1

N → R in BAA02546. Ref.5

Sequence conflict

470

1

S → I AA sequence Ref.15

Sequence conflict

534

1

R → H in AAA35873. Ref.1

Secondary structure

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536

Helix Strand Turn

Details...

Beta strand

49 – 52

4

Beta strand

54 – 60

7

Beta strand

75 – 82

8

Beta strand

88 – 94

7

Beta strand

96 – 98

3

Beta strand

103 – 116

14

Beta strand

119 – 123

5

Helix

126 – 132

7

Helix

137 – 148

12

Turn

150 – 153

4

Beta strand

157 – 163

7

Beta strand

166 – 170

5

Beta strand

177 – 179

3

Helix

190 – 193

4

Helix

196 – 206

11

Beta strand

212 – 218

7

Helix

222 – 224

3

Beta strand

229 – 233

5

Beta strand

235 – 238

4

Helix

243 – 261

19

Beta strand

267 – 271

5

Helix

277 – 279

3

Helix

292 – 301

10

Helix

303 – 308

6

Turn

311 – 314

4

Beta strand

315 – 323

9

Helix

324 – 326

3

Helix

329 – 335

7

Helix

338 – 341

4

Beta strand

346 – 352

7

Helix

359 – 369

11

Beta strand

373 – 381

9

Helix

396 – 411

16

Beta strand

414 – 422

9

Beta strand

440 – 444

5

Helix

445 – 447

3

Beta strand

449 – 452

4

Helix

454 – 463

10

Beta strand

471 – 479

9

Beta strand

482 – 489

8

Beta strand

495 – 501

7

Beta strand

503 – 505

3

Beta strand

507 – 513

7

Turn

514 – 516

3

Beta strand

517 – 523

7

Beta strand

527 – 533

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified November 9, 2004. Version 3. Checksum: FA1E15684344A0E6	FASTA	536	59,716
	10 20 30 40 50 60 MEFSSPSREE CPKPLSRVSI MAGSLTGLLL LQAVSWASGA RPCIPKSFGY SSVVCVCNAT 70 80 90 100 110 120 YCDSFDPPTF PALGTFSRYE STRSGRRMEL SMGPIQANHT GTGLLLTLQP EQKFQKVKGF 130 140 150 160 170 180 GGAMTDAAAL NILALSPPAQ NLLLKSYFSE EGIGYNIIRV PMASCDFSIR TYTYADTPDD 190 200 210 220 230 240 FQLHNFSLPE EDTKLKIPLI HRALQLAQRP VSLLASPWTS PTWLKTNGAV NGKGSLKGQP 250 260 270 280 290 300 GDIYHQTWAR YFVKFLDAYA EHKLQFWAVT AENEPSAGLL SGYPFQCLGF TPEHQRDFIA 310 320 330 340 350 360 RDLGPTLANS THHNVRLLML DDQRLLLPHW AKVVLTDPEA AKYVHGIAVH WYLDFLAPAK 370 380 390 400 410 420 ATLGETHRLF PNTMLFASEA CVGSKFWEQS VRLGSWDRGM QYSHSIITNL LYHVVGWTDW 430 440 450 460 470 480 NLALNPEGGP NWVRNFVDSP IIVDITKDTF YKQPMFYHLG HFSKFIPEGS QRVGLVASQK 490 500 510 520 530 NDLDAVALMH PDGSAVVVVL NRSSKDVPLT IKDPAVGFLE TISPGYSIHT YLWRRQ
	Isoform Short. Checksum: 3905C3D0AA3B1C2B	FASTA	516	57,455
	10 20 30 40 50 60 MAGSLTGLLL LQAVSWASGA RPCIPKSFGY SSVVCVCNAT YCDSFDPPTF PALGTFSRYE 70 80 90 100 110 120 STRSGRRMEL SMGPIQANHT GTGLLLTLQP EQKFQKVKGF GGAMTDAAAL NILALSPPAQ 130 140 150 160 170 180 NLLLKSYFSE EGIGYNIIRV PMASCDFSIR TYTYADTPDD FQLHNFSLPE EDTKLKIPLI 190 200 210 220 230 240 HRALQLAQRP VSLLASPWTS PTWLKTNGAV NGKGSLKGQP GDIYHQTWAR YFVKFLDAYA 250 260 270 280 290 300 EHKLQFWAVT AENEPSAGLL SGYPFQCLGF TPEHQRDFIA RDLGPTLANS THHNVRLLML 310 320 330 340 350 360 DDQRLLLPHW AKVVLTDPEA AKYVHGIAVH WYLDFLAPAK ATLGETHRLF PNTMLFASEA 370 380 390 400 410 420 CVGSKFWEQS VRLGSWDRGM QYSHSIITNL LYHVVGWTDW NLALNPEGGP NWVRNFVDSP 430 440 450 460 470 480 IIVDITKDTF YKQPMFYHLG HFSKFIPEGS QRVGLVASQK NDLDAVALMH PDGSAVVVVL 490 500 510 NRSSKDVPLT IKDPAVGFLE TISPGYSIHT YLWRRQ
	Isoform 3. Checksum: BF20F409A5BB4AD0	FASTA	263	29,897
	10 20 30 40 50 60 MASCDFSIRT YTYADTPDDF QLHNFSLPEE DTKLKIPLIH RALQLAQRPV SLLASPWTSP 70 80 90 100 110 120 TWLKTNGAVN GKGSLKGQPG DIYHQTWARY FVKFLDAYAE HKLQFWAVTA ENEPSAGLLS 130 140 150 160 170 180 GYPFQCLGFT PEHQRDFIAR DLGPTLANST HHNVRLLMLD DQRLLLPHWA KVVLTDPEAA 190 200 210 220 230 240 KYVHGIAVHW YLDFLAPAKA TLGETHRLFP NTMLFASEAC VGSKFWEQSV RLGSWDRGMQ 250 260 YSHSIITNLL YHVVGWTDWN PSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of human glucocerebrosidase cDNA." Sorge J., West C., Westwood B., Beutler E. Proc. Natl. Acad. Sci. U.S.A. 82:7289-7293(1985) [PubMed: 3864160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). Tissue: Placenta.
[2]	"Nucleotide sequence of cDNA containing the complete coding sequence for human lysosomal glucocerebrosidase." Tsuji S., Choudary P.V., Martin B.M., Winfield S., Barranger J.A., Ginns E.I. J. Biol. Chem. 261:50-53(1986) [PubMed: 3001061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANT LEU-298. Tissue: Hepatoma.
[3]	"The human glucocerebrosidase gene and pseudogene: structure and evolution." Horowitz M., Wilder S., Horowitz Z., Reiner O., Gelbart T., Beutler E. Genomics 4:87-96(1989) [PubMed: 2914709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[4]	"Polymorphisms in the human glucocerebrosidase gene." Beutler E., West C., Gelbart T. Genomics 12:795-800(1992) [PubMed: 1572652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[5]	"A novel transcript from a pseudogene for human glucocerebrosidase in non-Gaucher disease cells." Imai K., Nakamura M., Yamada M., Asano A., Yokoyama S., Tsuji S., Ginns E.I. Gene 136:365-368(1993) [PubMed: 8294033] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND 3), VARIANTS GD ARG-223; GLY-230; PRO-235; ARG-241; ILE-252 AND ARG-364, VARIANTS GLY-310 AND HIS-368.
[6]	"Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease." Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E. Genome Res. 7:1020-1026(1997) [PubMed: 9331372] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[8]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORM LONG). Tissue: Placenta.
[10]	"Structural analysis of the human glucocerebrosidase genes." Reiner O., Wigderson M., Horowitz M. DNA 7:107-116(1988) [PubMed: 3359914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-11.
[11]	"The human glucocerebrosidase gene has two functional ATG initiator codons." Sorge J.A., West C., Kuhl W., Treger L., Beutler E. Am. J. Hum. Genet. 41:1016-1024(1987) [PubMed: 3687939] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[12]	"Sturctural studies of human placental glucocerebrosidase." Martin B.M., Murray G.J., Coligan J.E., Raum M., Brady R.O., Barranger J.A. Fed. Proc. 43:1869-1869(1984) Cited for: PROTEIN SEQUENCE OF 40-44. Tissue: Placenta.
[13]	"Isolation of cDNA clones for human beta-glucocerebrosidase using the lambda gt11 expression system." Ginns E.I., Choudary P.V., Martin B.M., Winfield S., Stubblefield B., Mayor J., Merkle-Lehman D., Murray G.J., Bowers L.A., Barranger J.A. Biochem. Biophys. Res. Commun. 123:574-580(1984) [PubMed: 6091633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 403-416.
[14]	"Genetic heterogeneity in type 1 Gaucher disease: multiple genotypes in Ashkenazic and non-Ashkenazic individuals." Tsuji S., Martin B.M., Barranger J.A., Stubblefield B.K., LaMarca M.E., Ginns E.I. Proc. Natl. Acad. Sci. U.S.A. 85:2349-2352(1988) [PubMed: 3353383] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-462, VARIANT GD SER-409. Tissue: Skin.
[15]	"Human acid beta-glucosidase: isolation and amino acid sequence of a peptide containing the catalytic site." Dinur T., Osiecki K.M., Legler G., Gatt S., Desnick R.J., Grabowski G.A. Proc. Natl. Acad. Sci. U.S.A. 83:1660-1664(1986) [PubMed: 3456607] [Abstract] Cited for: PROTEIN SEQUENCE OF 469-520. Tissue: Placenta.
[16]	"Identification of Glu340 as the active-site nucleophile in human glucocerebrosidase by use of electrospray tandem mass spectrometry." Miao S., McCarter J.D., Grace M.E., Grabowski G.A., Aebersold R., Withers S.G. J. Biol. Chem. 269:10975-10978(1994) [PubMed: 7908905] [Abstract] Cited for: MASS SPECTROMETRY, MUTAGENESIS OF GLU-379, ACTIVE SITE.
[17]	"Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids." Salvioli R., Tatti M., Ciaffoni F., Vaccaro A.M. FEBS Lett. 472:17-21(2000) [PubMed: 10781797] [Abstract] Cited for: INTERACTION WITH SAPOSIN-C AND MEMBRANES CONTAINING ANIONIC PHOSPHOLIPIDS.
[18]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-98; ASN-185 AND ASN-309.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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-98 AND ASN-309, MASS SPECTROMETRY. Tissue: Liver.
[21]	"X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease." Dvir H., Harel M., McCarthy A.A., Toker L., Silman I., Futerman A.H., Sussman J.L. EMBO Rep. 4:704-709(2003) [PubMed: 12792654] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-536, GLYCOSYLATION AT ASN-58, DISULFIDE BONDS.
[22]	"X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease." Premkumar L., Sawkar A.R., Boldin-Adamsky S., Toker L., Silman I., Kelly J.W., Futerman A.H., Sussman J.L. J. Biol. Chem. 280:23815-23819(2005) [PubMed: 15817452] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-536 IN COMPLEX WITH SYNTHETIC INHIBITOR, ACTIVE SITE.
[23]	"Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations." Liou B., Kazimierczuk A., Zhang M., Scott C.R., Hegde R.S., Grabowski G.A. J. Biol. Chem. 281:4242-4253(2006) [PubMed: 16293621] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-536, CHARACTERIZATION OF GD VARIANTS SER-55; GLN-87; ASN-118; GLN-159; LEU-161; VAL-162; VAL-166; ASN-200; PHE-213; PHE-224; GLU-232; GLU-237; LEU-298; ILE-303; CYS-343; ILE-362; LYS-365; GLY-381; LYS-388; TRP-392; CYS-402; SER-409; VAL-410; HIS-419; LYS-421; ARG-429; LEU-433; SER-436; ASN-438; HIS-448; VAL-455; PRO-483; PRO-500 AND PRO-502, MUTAGENESIS OF CYS-43; CYS-57 AND CYS-62.
[24]	"Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease." Brumshtein B., Wormald M.R., Silman I., Futerman A.H., Sussman J.L. Acta Crystallogr. D 62:1458-1465(2006) [PubMed: 17139081] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 40-536, GLYCOSYLATION AT ASN-58; ASN-98 AND ASN-185.
[25]	"Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease." Lieberman R.L., Wustman B.A., Huertas P., Powe A.C. Jr., Pine C.W., Khanna R., Schlossmacher M.G., Ringe D., Petsko G.A. Nat. Chem. Biol. 3:101-107(2007) [PubMed: 17187079] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 40-536 IN COMPLEXES WITH ISOFAGOMINE, SUBCELLULAR LOCATION.
[26]	"Mutations causing Gaucher disease." Horowitz M., Zimran A. Hum. Mutat. 3:1-11(1994) [PubMed: 8118460] [Abstract] Cited for: REVIEW ON GD VARIANTS.
[27]	"Glucocerebrosidase (Gaucher disease)." Beutler E., Gelbart T. Hum. Mutat. 8:207-213(1996) [PubMed: 8889578] [Abstract] Cited for: REVIEW ON GD VARIANTS.
[28]	"Type 2 gaucher disease: an expanding phenotype." Tayebi N., Stone D.L., Sidransky E. Mol. Genet. Metab. 68:209-219(1999) [PubMed: 10527671] [Abstract] Cited for: REVIEW ON GD VARIANTS.
[29]	"Glucocerebrosidase gene mutations in patients with type 2 Gaucher disease." Stone D.L., Tayebi N., Orvisky E., Stubblefield B., Madike V., Sidransky E. Hum. Mutat. 15:181-188(2000) [PubMed: 10649495] [Abstract] Cited for: REVIEW ON GD VARIANTS.
[30]	"Gaucher disease associated with a unique KpnI restriction site: identification of the amino-acid substitution." Beutler E., Gelbart T. Ann. Hum. Genet. 54:149-153(1990) [PubMed: 1974409] [Abstract] Cited for: VARIANT GD TYR-255.
[31]	"Sequence of two alleles responsible for Gaucher disease." Hong C.M., Ohashi T., Yu X.J., Weiler S., Barranger J.A. DNA Cell Biol. 9:233-241(1990) [PubMed: 1972019] [Abstract] Cited for: VARIANTS GD.
[32]	"Identification of six new Gaucher disease mutations." Beutler E., Gelbart T., West C. Genomics 15:203-205(1993) [PubMed: 8432537] [Abstract] Cited for: VARIANTS GD.
[33]	"DNA analysis of an uncommon missense mutation in a Gaucher disease patient of Jewish-Polish-Russian descent." Choy F.Y.M., Wei C., Applegarth D.A., McGillivray B.C. Am. J. Med. Genet. 51:156-160(1994) [PubMed: 7916532] [Abstract] Cited for: VARIANT GD HIS-535.
[34]	"Two new Gaucher disease mutations." Beutler E., Gelbart T. Hum. Genet. 93:209-210(1994) [PubMed: 8112750] [Abstract] Cited for: VARIANT GD ASN-438.
[35]	"Y418C: a novel mutation in exon 9 of the glucocerebrosidase gene of a patient with Gaucher disease creates a new Bgl I site." Tuteja R., Tuteja N., Lilliu F., Bembi B., Galanello R., Cao A., Baralle F.E. Hum. Genet. 94:314-315(1994) [PubMed: 8076951] [Abstract] Cited for: VARIANTS GD SER-409 AND CYS-457.
[36]	"Glucocerebrosidase mutations in Gaucher disease." Beutler E., Demina A., Gelbart T. Mol. Med. 1:82-92(1994) [PubMed: 8790604] [Abstract] Cited for: VARIANTS GD ASP-215; THR-221; ARG-241; GLN-296; CYS-324; GLY-417 AND ASN-419.
[37]	"Gaucher disease in Spanish patients: analysis of eight mutations." Cormand B., Vilageliu L., Burguera J.M., Balcells S., Gonzalez-Duarte R., Grinberg D., Chabas A. Hum. Mutat. 5:303-309(1995) [PubMed: 7627184] [Abstract] Cited for: VARIANTS GD SER-409; HIS-448; PRO-483 AND CYS-502.
[38]	"Identification of a new mutation (P178S) in an African-American patient with type 2 Gaucher disease." Choy F.Y.M., Wei C. Hum. Mutat. 5:345-347(1995) [PubMed: 7627192] [Abstract] Cited for: VARIANT GD SER-217.
[39]	"The molecular characterization of Gaucher disease in South Africa." Morar B., Lane A.B. Clin. Genet. 50:78-84(1996) [PubMed: 8937765] [Abstract] Cited for: VARIANTS GD SER-409; LEU-426; LEU-433 AND PRO-483.
[40]	"Gaucher disease: identification of three new mutations in the Korean and Chinese (Taiwanese) populations." Kim J.-W., Liou B.B., Lai M.-Y., Ponce E., Grabowski G.A. Hum. Mutat. 7:214-218(1996) [PubMed: 8829654] [Abstract] Cited for: VARIANTS GD LEU-54; GLU-85 AND SER-227.
[41]	"Two novel (1098insA and Y313H) and one rare (R359Q) mutations detected in exon 8 of the beta-glucocerebrosidase gene in Gaucher's disease patients." Cormand B., Vilageliu L., Balcells S., Gonzalez-Duatre R., Chabas A., Grinberg D. Hum. Mutat. 7:272-274(1996) [PubMed: 8829663] [Abstract] Cited for: VARIANTS GD HIS-352 AND GLN-398.
[42]	"Type 1 Gaucher disease: identification of N396T and prevalence of glucocerebrosidase mutations in the Portuguese." Amaral O., Pinto E., Fortuna M., Lacerda L., Sa Miranda M.C. Hum. Mutat. 8:280-281(1996) [PubMed: 8889591] [Abstract] Cited for: VARIANT GD THR-435.
[43]	"Two new missense mutations in a non-Jewish Caucasian family with type 3 Gaucher disease." Seeman P.J.V., Finckh U., Hoeppner J., Lakner V., Liebisch I., Grau G., Rolfs A. Neurology 46:1102-1107(1996) [PubMed: 8780099] [Abstract] Cited for: VARIANTS GD LEU-437 AND ILE-530.
[44]	"Two new mild homozygous mutations in Gaucher disease patients: clinical signs and biochemical analyses." Cormand B., Grinberg D., Gort L., Fiumara A., Barone R., Vilageliu L., Chabas A. Am. J. Med. Genet. 70:437-443(1997) [PubMed: 9182788] [Abstract] Cited for: VARIANTS GD LEU-414 AND THR-441.
[45]	"Identification of two novel and four uncommon missense mutations among Chinese Gaucher disease patients." Choy F.Y.M., Humphries M.L., Shi H. Am. J. Med. Genet. 71:172-178(1997) [PubMed: 9217217] [Abstract] Cited for: VARIANTS GD VAL-76; GLU-85; TRP-87; TRP-159; SER-227; ILE-252 AND PRO-483.
[46]	"Mutation analysis in 46 British and Irish patients with Gaucher's disease." Hatton C.E., Cooper A., Whitehouse C., Wraith J.E. Arch. Dis. Child. 77:17-22(1997) [PubMed: 9279145] [Abstract] Cited for: VARIANT GD LYS-501.
[47]	"Identification and expression of acid beta-glucosidase mutations causing severe type 1 and neurologic type 2 Gaucher disease in non-Jewish patients." Grace M.E., Desnick R.J., Pastores G.M. J. Clin. Invest. 99:2530-2537(1997) [PubMed: 9153297] [Abstract] Cited for: VARIANTS GD TRP-87; GLU-234; ARG-241; ILE-252; ASN-310; LEU-391 AND SER-409.
[48]	"Mutation prevalence among 47 unrelated Japanese patients with Gaucher disease: identification of four novel mutations." Ida H., Rennert O.M., Kawame H., Maekawa K., Eto Y. J. Inherit. Metab. Dis. 20:67-73(1997) [PubMed: 9061570] [Abstract] Cited for: VARIANTS GD VAL-228; ILE-252; GLY-405; HIS-448; GLN-452; PRO-483 AND CYS-535.
[49]	"D409H/D409H genotype in Gaucher-like disease." Uyama E., Uchino M., Ida H., Eto Y., Owada M. J. Med. Genet. 34:175-175(1997) [PubMed: 9040001] [Abstract] Cited for: VARIANT PSEUDO-GAUCHER HIS-448.
[50]	"Six new Gaucher disease mutations." Demina A., Beutler E. Acta Haematol. 99:80-82(1998) [PubMed: 9554454] [Abstract] Cited for: VARIANTS GD LEU-146; LEU-198; THR-380; ASN-405 AND ARG-432.
[51]	"Exhaustive screening of the acid beta-glucosidase gene, by fluorescence-assisted mismatch analysis using universal primers: mutation profile and genotype/phenotype correlations in Gaucher disease." Germain D.P., Puech J.-P., Caillaud C., Kahn A., Poenaru L. Am. J. Hum. Genet. 63:415-427(1998) [PubMed: 9683600] [Abstract] Cited for: VARIANTS GD.
[52]	"Gaucher type 2 disease: identification of a novel transversion mutation in a French-Irish patient." Choy F.Y.M., Humphries M.L., Ben-Yoseph Y. Am. J. Med. Genet. 78:92-93(1998) [PubMed: 9637431] [Abstract] Cited for: VARIANT GD TYR-513.
[53]	"Hematologically important mutations: Gaucher disease." Beutler E., Gelbart T. Blood Cells Mol. Dis. 24:2-8(1998) [PubMed: 9516376] [Abstract] Cited for: VARIANTS GD.
[54]	"A novel complex allele and two new point mutations in type 2 (acute neuronopathic) Gaucher disease." Sinclair G., Choy F.Y.M., Humphries L. Blood Cells Mol. Dis. 24:420-427(1998) [PubMed: 9851895] [Abstract] Cited for: VARIANTS GD LYS-80; CYS-170 AND PRO-483.
[55]	"A novel mutation of the beta-glucocerebrosidase gene associated with neurologic manifestations in three sibs." Parenti G., Filocamo M., Titomanlio L., Rizzolo G., Silvestro E., Perretti A., Gatti R., Andria G. Clin. Genet. 53:281-285(1998) [PubMed: 9650766] [Abstract] Cited for: VARIANT GD GLY-392.
[56]	"Molecular analysis and clinical findings in the Spanish Gaucher disease population: putative haplotype of the N370S ancestral chromosome." Cormand B., Grinberg D., Gort L., Chabas A., Vilageliu L. Hum. Mutat. 11:295-305(1998) [PubMed: 9554746] [Abstract] Cited for: VARIANTS GD GLU-152; PRO-173; GLU-428; LEU-430; ILE-431 AND HIS-451.
[57]	"A novel mutation (V191G) in a German-British type 1 Gaucher disease patient." Choy F.Y.M., Humphries M.L., Ben-Yoseph Y. Hum. Mutat. 11:411-412(1998) [PubMed: 10206680] [Abstract] Cited for: VARIANTS GD GLY-230 AND SER-409.
[58]	"Type 1 Gaucher disease presenting with extensive mandibular lytic lesions: identification and expression of a novel acid beta-glucosidase mutation." Wasserstein M.P., Martignetti J.A., Zeitlin R., Lumerman H., Solomon M., Grace M.E., Desnick R.J. Am. J. Med. Genet. 84:334-339(1999) [PubMed: 10340647] [Abstract] Cited for: VARIANTS GD SER-409 AND LEU-440.
[59]	"Glucocerebrosidase mutations among Chinese neuronopathic and non-neuronopathic Gaucher disease patients." Choy F.Y.M., Wong K., Shi H.P. Am. J. Med. Genet. 84:484-486(1999) [PubMed: 10360404] [Abstract] Cited for: VARIANTS GD ARG-241; CYS-244; ILE-252; HIS-448 AND PRO-483.
[60]	"Analysis of the beta-glucocerebrosidase gene in Czech and Slovak Gaucher patients: mutation profile and description of six novel mutant alleles." Hodanov K., Hrebicek M., Cervenkov M., Mrzov L., Veprekov L., Zemen J. Blood Cells Mol. Dis. 25:287-298(1999) [PubMed: 10744424] [Abstract] Cited for: VARIANTS GD.
[61]	"Is the perinatal lethal form of Gaucher disease more common than classic type 2 Gaucher disease?" Stone D.L., van Diggelen O.P., de Klerk J.B.C., Gaillard J.L.J., Niermeijer M.F., Willemsen R., Tayebi N., Sidransky E. Eur. J. Hum. Genet. 7:505-509(1999) [PubMed: 10352942] [Abstract] Cited for: VARIANTS PERINATAL LETHAL GD ARG-350 AND PHE-437.
[62]	"Detection of three rare (G377S, T134P and 1451delAC), and two novel mutations (G195W and Rec[1263del55;1342G>C]] in Spanish Gaucher disease patients." Sarria A.J., Giraldo P., Perez-Calvo J.I., Pocovi M. Hum. Mutat. 14:88-88(1999) [PubMed: 10447266] [Abstract] Cited for: VARIANTS GD PRO-173; TRP-234; SER-409; SER-416; HIS-448 AND PRO-483.
[63]	"Analysis and classification of 304 mutant alleles in patients with type 1 and type 3 Gaucher disease." Koprivica V., Stone D.L., Park J.K., Callahan M., Frisch A., Cohen I.J., Tayebi N., Sidransky E. Am. J. Hum. Genet. 66:1777-1786(2000) [PubMed: 10796875] [Abstract] Cited for: VARIANTS GD TRP-87; ASN-118; THR-129; ASP-156; GLN-159; TRP-159; LEU-170; ILE-173; CYS-209; PRO-209; SER-227; THR-229; PRO-235; ARG-241; ILE-252; GLN-296; CYS-324; THR-380; MET-408; SER-409; SER-416; LEU-433; TYR-438; HIS-448; PRO-483 AND CYS-502, VARIANT LYS-365.
[64]	"Variant Gaucher disease characterized by dysmorphic features, absence of cardiovascular involvement, laryngospasm, and compound heterozygosity for a novel mutation (D409H/C16S)." Bodamer O.A.F., Church H.J., Cooper A., Wraith J.E., Scott C.R., Scaglia F. Am. J. Med. Genet. 109:328-331(2002) [PubMed: 11992489] [Abstract] Cited for: VARIANTS GD SER-55 AND HIS-448.
[65]	"The identification of eight novel glucocerebrosidase (GBA) mutations in patients with Gaucher disease." Orvisky E., Park J.K., Parker A., Walker J.M., Martin B.M., Stubblefield B.K., Uyama E., Tayebi N., Sidransky E. Hum. Mutat. 19:458-459(2002) [PubMed: 11933202] [Abstract] Cited for: VARIANTS GD GLU-175; PRO-201; GLU-237; LEU-290 AND PHE-441.
[66]	"Analysis of the glucocerebrosidase gene and mutation profile in 144 Italian gaucher patients." Filocamo M., Mazzotti R., Stroppiano M., Seri M., Giona F., Parenti G., Regis S., Corsolini F., Zoboli S., Gatti R. Hum. Mutat. 20:234-235(2002) [PubMed: 12204005] [Abstract] Cited for: VARIANTS GD THR-198; ARG-241; ARG-270; ILE-400 AND ARG-490.
[67]	"Gaucher's disease with Parkinson's disease: clinical and pathological aspects." Bembi B., Zambito Marsala S., Sidransky E., Ciana G., Carrozzi M., Zorzon M., Martini C., Gioulis M., Pittis M.G., Capus L. Neurology 61:99-101(2003) [PubMed: 12847165] [Abstract] Cited for: POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
[68]	"Homozygous loss of a cysteine residue in the glucocerebrosidase gene results in Gaucher's disease with a hydropic phenotype." Church H.J., Cooper A., Stewart F., Thornton C.M., Wraith J.E. Eur. J. Hum. Genet. 12:975-978(2004) [PubMed: 15292921] [Abstract] Cited for: VARIANT GD SER-55.
[69]	"The N370S (Asn370->Ser) mutation affects the capacity of glucosylceramidase to interact with anionic phospholipid-containing membranes and saposin C." Salvioli R., Tatti M., Scarpa S., Moavero S.M., Ciaffoni F., Felicetti F., Kaneski C.R., Brady R.O., Vaccaro A.M. Biochem. J. 390:95-103(2005) [PubMed: 15826241] [Abstract] Cited for: CHARACTERIZATION OF VARIANT GD SER-409.
[70]	"Identification and functional characterization of five novel mutant alleles in 58 Italian patients with Gaucher disease type 1." Miocic S., Filocamo M., Dominissini S., Montalvo A.L., Vlahovicek K., Deganuto M., Mazzotti R., Cariati R., Bembi B., Pittis M.G. Hum. Mutat. 25:100-100(2005) [PubMed: 15605411] [Abstract] Cited for: VARIANTS GD ASN-63; SER-158; TRP-159; CYS-170; LEU-221; GLU-230; ARG-241; GLN-294; CYS-324; SER-409; ASN-438; LEU-440; HIS-448; CYS-457; ASP-460; PRO-483 AND ARG-490, CHARACTERIZATION OF VARIANTS GD ASN-63; SER-158; LEU-221; GLU-230 AND ASP-460.
[71]	"Mutations in the glucocerebrosidase gene and Parkinson disease: phenotype-genotype correlation." Aharon-Peretz J., Badarny S., Rosenbaum H., Gershoni-Baruch R. Neurology 65:1460-1461(2005) [PubMed: 16148263] [Abstract] Cited for: POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
+	Additional computationally mapped references.

Web resources

Ceredase

Clinical information on Ceredase

Cerezyme

Clinical information on Cerezyme

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

M16328 mRNA. Translation: AAA35873.1.
K02920 mRNA. Translation: AAA35877.1.
J03059 Genomic DNA. Translation: AAC63056.1.
D13286 mRNA. Translation: BAA02545.1.
D13287 mRNA. Translation: BAA02546.1.
AF023268 Genomic DNA. Translation: AAC51820.1.
AK291911 mRNA. Translation: BAF84600.1.
AL713999 Genomic DNA. Translation: CAI95090.1.
BC003356 mRNA. Translation: AAH03356.1.
M19285 mRNA. Translation: AAA35880.1.
M18916 Genomic DNA. Translation: AAA35878.1. Sequence problems.
M18917 Genomic DNA. Translation: AAA35879.1. Sequence problems.
M20248 Genomic DNA. Translation: AAA35874.1.
M20282 Genomic DNA. Translation: AAA35876.1.

IPI

IPI00021807.
IPI00759616.
IPI00845473.

PIR

EUHUGC. A94068.
I52980.
I67792.

RefSeq

NP_000148.2.
NP_001005741.1.
NP_001005742.1.
NP_001005749.1.
NP_001005750.1.

UniGene

Hs.282997

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OGS	X-ray	2.00	A/B	40-536	[»]
1Y7V	X-ray	2.40	A/B	40-536	[»]
2F61	X-ray	2.50	A/B	40-536	[»]
2J25	X-ray	2.90	A/B	40-536	[»]
2NSX	X-ray	2.11	A/B/C/D	40-536	[»]
2NT0	X-ray	1.79	A/B/C/D	40-536	[»]
2NT1	X-ray	2.30	A/B/C/D	40-536	[»]
2V3D	X-ray	1.96	A/B	40-536	[»]
2V3E	X-ray	2.00	A/B	40-536	[»]
2V3F	X-ray	1.95	A/B	40-536	[»]
3GXD	X-ray	2.50	A/B/C/D	40-536	[»]
3GXF	X-ray	2.40	A/B/C/D	40-536	[»]
3GXI	X-ray	1.84	A/B/C/D	40-536	[»]
3GXM	X-ray	2.20	A/B/C/D	40-536	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P04062. 1 interaction.

Protein family/group databases

CAZy

GH30. Glycoside Hydrolase Family 30.

PTM databases

PhosphoSite

P04062.

Proteomic databases

PRIDE

P04062.

Genome annotation databases

Ensembl

ENSG00000177628. Homo sapiens. [Contig view]

GeneID

2629.

KEGG

hsa:2629.

NMPDR

fig|9606.3.peg.2212.

Organism-specific databases

GeneCards

GC01M153470.

H-InvDB

HIX0001115.

HGNC

HGNC:4177. GBA.

HPA

HPA006667.

MIM

168600. phenotype.
230800. phenotype.
230900. phenotype.
231000. phenotype.
231005. phenotype.
236750. phenotype.
606463. gene.
608013. phenotype.

Orphanet

355. Gaucher disease.
2072. Gaucher disease - ophthalmoplegia - cardiovascular calcification.
77259. Gaucher disease, type 1.
77260. Gaucher disease, type 2.
77261. Gaucher disease, type 3.
85212. Perinatal-lethal Gaucher disease.

PharmGKB

PA28591.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P04062.

HOVERGEN

P04062.

OMA

P04062. QNEPMAV.

Enzyme and pathway databases

BRENDA

3.2.1.45. 247.

Gene expression databases

CleanEx

HS_GBA.
HS_GC.

GermOnline

ENSG00000177628. Homo sapiens.

Family and domain databases

InterPro

IPR001139. Glyco_hydro_30.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PANTHER

PTHR11069. Glyco_hydro_30. 1 hit.

Pfam

PF02055. Glyco_hydro_30. 1 hit.
[Graphical view]

PRINTS

PR00843. GLHYDRLASE30.

ProtoNet

Search...

Other Resources

DrugBank

DB00088. Alglucerase.
DB00053. Imiglucerase.

NextBio

10357.

SOURCE

Search...

Entry information

Entry name

GLCM_HUMAN

Accession

Primary (citable) accession number: P04062
Secondary accession number(s): A8K796 , Q16545, Q4VX22, Q6I9R6, Q9UMJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 9, 2004
Last modified:	June 16, 2009
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)