Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04062 (GLCM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 184. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucosylceramidase

EC=3.2.1.45
Alternative name(s):
Acid beta-glucosidase
Alglucerase
Beta-glucocerebrosidase
Short name=Beta-GC
D-glucosyl-N-acylsphingosine glucohydrolase
Imiglucerase
Gene names
Name:GBA
Synonyms:GC, GLUC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Interacts with SCARB2. Ref.17 Ref.19

Subcellular location

Lysosome membrane; Peripheral membrane protein; Lumenal side. Note: Interaction with saposin-C promotes membrane association. Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2. Ref.19 Ref.20 Ref.28

Involvement in disease

Gaucher disease (GD) [MIM:230800]: A lysosomal storage disease due to deficient activity of beta-glucocerebrosidase and 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.14 Ref.21 Ref.26 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.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 Ref.72 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77

Gaucher disease 1 (GD1) [MIM:230800]: A form of Gaucher disease characterized by hepatosplenomegaly with consequent anemia and thrombopenia, and bone involvement. The central nervous system is not involved.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.21 Ref.45 Ref.60 Ref.61 Ref.70 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77

Gaucher disease 2 (GD2) [MIM:230900]: The most severe form of Gaucher disease. It manifests soon after birth, with death generally occurring before patients reach two years of age.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.55 Ref.57 Ref.70 Ref.74 Ref.75 Ref.76 Ref.77

Gaucher disease 3 (GD3) [MIM:231000]: A subacute form of neuronopathic Gaucher disease. It has later onset and slower progression compared to the acute form of neuronopathic Gaucher disease 2.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.46 Ref.70 Ref.74 Ref.75 Ref.76 Ref.77

Gaucher disease 3C (GD3C) [MIM:231005]: A variant of subacute neuronopathic Gaucher disease 3 associated with cardiovascular calcifications.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.70 Ref.74 Ref.75 Ref.76 Ref.77

Gaucher disease perinatal lethal (GDPL) [MIM:608013]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.70 Ref.74 Ref.75 Ref.76 Ref.77

Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders. Ref.21 Ref.70 Ref.74 Ref.75 Ref.76 Ref.77

Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Ref.21 Ref.70 Ref.74 Ref.75 Ref.76 Ref.77

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 processLipid metabolism
Sphingolipid metabolism
   Cellular componentLysosome
Membrane
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DiseaseDisease mutation
Gaucher disease
Ichthyosis
Neurodegeneration
Parkinson disease
Parkinsonism
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to tumor necrosis factor

Inferred from mutant phenotype PubMed 19279008. Source: BHF-UCL

ceramide biosynthetic process

Inferred from mutant phenotype PubMed 19279011. Source: BHF-UCL

glucosylceramide catabolic process

Inferred from mutant phenotype PubMed 19279011. Source: BHF-UCL

glycosphingolipid metabolic process

Traceable author statement. Source: Reactome

negative regulation of MAP kinase activity

Inferred from mutant phenotype PubMed 19279008. Source: BHF-UCL

negative regulation of inflammatory response

Inferred by curator PubMed 19279008. Source: BHF-UCL

negative regulation of interleukin-6 production

Inferred from direct assay PubMed 19279008. Source: BHF-UCL

positive regulation of protein dephosphorylation

Inferred from mutant phenotype PubMed 19279008. Source: BHF-UCL

regulation of water loss via skin

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

response to thyroid hormone

Inferred from electronic annotation. Source: Ensembl

skin morphogenesis

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

sphingosine biosynthetic process

Inferred from mutant phenotype PubMed 19279011. Source: BHF-UCL

termination of signal transduction

Inferred from mutant phenotype PubMed 19279008. Source: BHF-UCL

   Cellular_componentlysosomal lumen

Inferred from sequence or structural similarity Ref.19. Source: BHF-UCL

lysosomal membrane

Inferred from direct assay Ref.20. Source: UniProtKB

   Molecular_functionglucosylceramidase activity

Inferred from direct assay PubMed 19279011. Source: BHF-UCL

receptor binding

Inferred from sequence or structural similarity Ref.19. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Scarb2O351141EBI-1564609,EBI-1564519From 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939In isoform Long Ref.12
Signal peptide21 – 3919In isoform Short Ref.12
Chain40 – 536497Glucosylceramidase
PRO_0000012177

Sites

Active site2741Proton donor Ref.16 Ref.25
Active site3791Nucleophile Ref.16 Ref.25

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Ref.24 Ref.27
Glycosylation981N-linked (GlcNAc...) Ref.18 Ref.22 Ref.27
Glycosylation1851N-linked (GlcNAc...) Ref.18 Ref.27
Glycosylation3091N-linked (GlcNAc...) Ref.18 Ref.22
Glycosylation5011N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 55 Ref.24
Disulfide bond57 ↔ 62 Ref.24

Natural variations

Alternative sequence1 – 161161Missing in isoform 3.
VSP_025216
Alternative sequence1 – 2020Missing in isoform Short.
VSP_018800
Alternative sequence422 – 4232LA → PS in isoform 3.
VSP_025217
Alternative sequence425 – 536112Missing in isoform 3.
VSP_025218
Natural variant461K → E in a patient with Parkinson disease. Ref.21
VAR_063066
Natural variant541V → L in GD. Ref.43
VAR_003255
Natural variant551C → S in GD; neuronopathic and perinatal lethal forms; loss of activity. Ref.26 Ref.67 Ref.71
VAR_032394
Natural variant631D → N in GD1; very low activity. Ref.73
VAR_032395
Natural variant761F → V in GD. Ref.48
VAR_003256
Natural variant801E → K in GD2. Ref.57
Corresponds to variant rs1141808 [ dbSNP | Ensembl ].
VAR_009033
Natural variant821T → I in GD.
VAR_003257
Natural variant851G → E in GD. Ref.43 Ref.48
VAR_003258
Natural variant871R → Q in GD; 20% of normal activity. Ref.26
VAR_032197
Natural variant871R → W in GD; mild. Ref.48 Ref.50 Ref.66
Corresponds to variant rs1141814 [ dbSNP | Ensembl ].
VAR_003259
Natural variant921M → T.
Corresponds to variant rs3205619 [ dbSNP | Ensembl ].
VAR_032396
Natural variant1181K → N in GD; mild; 8% of normal activity; increases susceptibility to proteolytic degradation. Ref.26 Ref.66
VAR_003260
Natural variant1291A → T in GD. Ref.66
VAR_032397
Natural variant1461S → L in GD; type 2. Ref.53
VAR_009034
Natural variant1521G → E in GD. Ref.59
VAR_003261
Natural variant1561N → D in GD. Ref.66
VAR_032398
Natural variant1581I → S in GD1; very low activity. Ref.73
VAR_032399
Natural variant1581I → T in GD.
VAR_003262
Natural variant1591R → Q in GD; type 2; 13% of normal activity. Ref.26 Ref.66
VAR_003263
Natural variant1591R → W in GD; severe. Ref.48 Ref.66 Ref.73
VAR_003264
Natural variant1611P → L in GD; 16% of normal activity. Ref.26
VAR_032198
Natural variant1611P → S in GD; mild.
VAR_003265
Natural variant1621M → V in GD; loss of activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032199
Natural variant1661D → V in GD; 9% of normal activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032200
Natural variant1701R → C in GD1 and GD2; also found in a patient with Parkinson disease. Ref.21 Ref.57 Ref.73
VAR_009035
Natural variant1701R → L in GD. Ref.66
VAR_009036
Natural variant1731T → I in GD. Ref.66
VAR_032400
Natural variant1731T → P in GD. Ref.59 Ref.65
VAR_003266
Natural variant1751A → E in GD. Ref.68
VAR_032401
Natural variant1791D → H in GD.
VAR_003267
Natural variant1961K → Q in GD; severe.
VAR_003268
Natural variant1981P → L in GD. Ref.53
VAR_009037
Natural variant1981P → T in GD. Ref.69
VAR_032402
Natural variant2001I → N in GD; 5% of normal activity. Ref.26
VAR_032201
Natural variant2001I → S in GD.
VAR_010059
Natural variant2011H → P in GD. Ref.68
VAR_032403
Natural variant2091R → C in GD. Ref.66
VAR_032404
Natural variant2091R → P in GD. Ref.66
VAR_003269
Natural variant2131L → F in GD; 12% of normal activity. Ref.26
VAR_032202
Natural variant2151A → D in GD. Ref.39
VAR_003270
Natural variant2171P → S in GD; type 2. Ref.41
VAR_003271
Natural variant2211P → L in GD1; very low activity. Ref.73
VAR_032405
Natural variant2211P → T in GD. Ref.39
VAR_003272
Natural variant2231W → R in GD; gene conversion. Ref.5
VAR_003273
Natural variant2241L → F in GD; 4% of normal activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032203
Natural variant2271N → K in GD; gene conversion.
Corresponds to variant rs381418 [ dbSNP | Ensembl ].
VAR_003275
Natural variant2271N → S in GD; type 2. Ref.43 Ref.48 Ref.66
Corresponds to variant rs364897 [ dbSNP | Ensembl ].
VAR_003274
Natural variant2281G → V in GD. Ref.51
VAR_010060
Natural variant2291A → E in GD; type 2.
VAR_009038
Natural variant2291A → T in GD. Ref.66
VAR_032406
Natural variant2301V → E in GD1; very low activity. Ref.73
VAR_032407
Natural variant2301V → G in GD1; gene conversion. Ref.5 Ref.60
Corresponds to variant rs381427 [ dbSNP | Ensembl ].
VAR_003276
Natural variant2321G → E in GD; also found in a patient with Parkinson disease; 7% of normal activity. Ref.21 Ref.26
VAR_032204
Natural variant2341G → E in GD; severe. Ref.50
VAR_003277
Natural variant2341G → W in GD. Ref.65
VAR_009039
Natural variant2351S → P in GD; type 2; gene conversion. Ref.5 Ref.66
Corresponds to variant rs1064644 [ dbSNP | Ensembl ].
VAR_003278
Natural variant2371K → E in GD; severe; loss of activity; increases susceptibility to proteolytic degradation. Ref.26 Ref.68
VAR_032205
Natural variant2411G → E in GD.
VAR_010061
Natural variant2411G → R in GD; type 1 and type 2; gene conversion. Ref.5 Ref.39 Ref.50 Ref.62 Ref.66 Ref.69 Ref.73
VAR_003279
Natural variant2441Y → C in GD. Ref.62
VAR_010062
Natural variant2511Y → H in GD.
VAR_003280
Natural variant2521F → I in GD; type 2; gene conversion. Ref.5 Ref.48 Ref.50 Ref.51 Ref.62 Ref.66
Corresponds to variant rs381737 [ dbSNP | Ensembl ].
VAR_003281
Natural variant2551F → Y in GD; mild. Ref.33
VAR_003282
Natural variant2701T → R in GD. Ref.69
VAR_032408
Natural variant2761S → P in GD.
VAR_003283
Natural variant2901F → L in GD; perinatal lethal form. Ref.68
VAR_032409
Natural variant2941H → Q in GD1; also found in Gaucher disease type 2. Ref.73
VAR_009040
Natural variant2961R → Q in GD; type 2; also found in a patient with Parkinson disease. Ref.21 Ref.39 Ref.66
VAR_003284
Natural variant2981F → L in GD; type 2; 4% of normal activity. Ref.2 Ref.26
VAR_009041
Natural variant3031L → I in GD; 5% of normal activity. Ref.26
VAR_032206
Natural variant3041G → D in GD.
VAR_010063
Natural variant3051P → R in GD; mild.
VAR_003285
Natural variant3101S → G. Ref.5
Corresponds to variant rs1057942 [ dbSNP | Ensembl ].
VAR_032410
Natural variant3101S → N in GD; less than 5% of normal activity. Ref.50
VAR_010064
Natural variant3241R → C in GD; type 1. Ref.39 Ref.66 Ref.73
VAR_003286
Natural variant3241R → H in GD; type 2.
VAR_009042
Natural variant3281P → L in GD; mild.
VAR_003287
Natural variant3421K → I in GD.
VAR_003288
Natural variant3431Y → C in GD; type 2; 16% of normal activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_009043
Natural variant3481A → V in GD.
VAR_003289
Natural variant3501H → R in perinatal lethal GD. Ref.64
VAR_009044
Natural variant3511W → C in GD; mild.
VAR_003290
Natural variant3521Y → H in GD. Ref.44
VAR_003291
Natural variant3541D → H in GD.
VAR_003292
Natural variant3571A → D in GD.
VAR_003293
Natural variant3621T → I in GD; 6% of normal activity. Ref.26
VAR_003294
Natural variant3631L → P in GD.
VAR_003295
Natural variant3641G → R in GD; type 2. Ref.5
VAR_003296
Natural variant3651E → K in GD; mild; 42% of normal activity. Ref.26 Ref.66
Corresponds to variant rs2230288 [ dbSNP | Ensembl ].
VAR_003297
Natural variant3681R → H. Ref.5
Corresponds to variant rs1064648 [ dbSNP | Ensembl ].
VAR_032411
Natural variant3801A → T in GD. Ref.53 Ref.66
VAR_009045
Natural variant3811C → G in GD; type 2; loss of activity. Ref.26
VAR_003298
Natural variant3881E → K in GD; 12% of normal activity. Ref.26
VAR_032207
Natural variant3911V → L in GD. Ref.50
VAR_010065
Natural variant3921R → G in GD. Ref.58
VAR_010066
Natural variant3921R → W in GD; 5% of normal activity. Ref.26
VAR_032208
Natural variant3981R → Q in GD; mild. Ref.44
VAR_003299
Natural variant4001M → I in GD. Ref.69
Corresponds to variant rs149487315 [ dbSNP | Ensembl ].
VAR_032412
Natural variant4021Y → C in GD; 8% of normal activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032209
Natural variant4031S → T in GD; mild.
VAR_003300
Natural variant4051S → G in GD. Ref.51
VAR_010067
Natural variant4051S → N in GD. Ref.53
VAR_009046
Natural variant4081T → M in GD. Ref.66
Corresponds to variant rs2230289 [ dbSNP | Ensembl ].
VAR_003301
Natural variant4091N → S in GD1; common mutation; associated with susceptibility to Parkinson disease; alters interaction with saposin-C and membranes and thereby reduces enzyme activity; mild. Ref.14 Ref.21 Ref.26 Ref.38 Ref.40 Ref.42 Ref.50 Ref.60 Ref.61 Ref.65 Ref.66 Ref.72 Ref.73 Ref.76 Ref.77
Corresponds to variant rs76763715 [ dbSNP | Ensembl ].
VAR_003302
Natural variant4101L → V in GD; 15% of normal activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032210
Natural variant4141V → L in GD; mild. Ref.47
VAR_010068
Natural variant4161G → S in GD; mild. Ref.65 Ref.66
VAR_003303
Natural variant4171W → G in GD. Ref.39
VAR_003304
Natural variant4191D → A in GD; type 2; also found in a patient with Parkinson disease. Ref.21
VAR_003305
Natural variant4191D → H in GD; 4% of normal activity. Ref.26
VAR_032211
Natural variant4191D → N in GD. Ref.39
VAR_003306
Natural variant4211N → K in GD; 22% of normal activity. Ref.26
VAR_032212
Natural variant4261P → L in GD. Ref.42
VAR_010069
Natural variant4281G → E in GD; type 2. Ref.59
VAR_003307
Natural variant4291G → R in GD; 17% of normal activity. Ref.26
VAR_032213
Natural variant4301P → L in GD. Ref.59
VAR_003308
Natural variant4311N → I in GD; type 2. Ref.59
VAR_003309
Natural variant4321W → R in GD. Ref.53
VAR_009047
Natural variant4331V → L in GD; severe; 12% of normal activity. Ref.26 Ref.42 Ref.66
VAR_003310
Natural variant4351N → T in GD1; mild. Ref.45
VAR_003311
Natural variant4361F → S in GD; 6% of normal activity; alters protein stability and increases susceptibility to proteolytic degradation. Ref.26
VAR_032214
Natural variant4371V → F in perinatal lethal GD. Ref.64
VAR_009048
Natural variant4371V → L in GD3. Ref.46
VAR_010070
Natural variant4381D → N in GD; type 1 and type 2; 14% of normal activity; increases susceptibility to proteolytic degradation. Ref.26 Ref.37 Ref.73
VAR_003312
Natural variant4381D → Y in GD. Ref.66
VAR_032413
Natural variant4401P → L in GD1. Ref.61 Ref.73
VAR_010071
Natural variant4411I → F in GD; type 3. Ref.68
VAR_032414
Natural variant4411I → T in GD; mild. Ref.47
VAR_010072
Natural variant4481D → H in GD; type 1 and type neuronopathic; at homozygosity it causes GD3C; also found in a patient with Parkinson disease; gene conversion; very low activity; alters protein stability. Ref.21 Ref.26 Ref.40 Ref.51 Ref.52 Ref.62 Ref.65 Ref.66 Ref.67 Ref.73
Corresponds to variant rs1064651 [ dbSNP | Ensembl ].
VAR_003313
Natural variant4481D → V in GD; severe; very low activity; alters protein stability.
VAR_003314
Natural variant4501F → I in GD.
VAR_010073
Natural variant4511Y → H in GD. Ref.59
VAR_003315
Natural variant4521K → Q in GD. Ref.51
VAR_010074
Natural variant4541P → R in GD; type 2.
VAR_003316
Natural variant4551M → V in GD; loss of activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032215
Natural variant4561F → V in GD.
VAR_003317
Natural variant4571Y → C in GD. Ref.38 Ref.73
VAR_003318
Natural variant4601G → D in GD1; associated with R-490; loss of activity. Ref.73
VAR_032415
Natural variant4641K → E in GD; severe.
VAR_003319
Natural variant4821D → N in a patient with Parkinson disease. Ref.21
Corresponds to variant rs75671029 [ dbSNP | Ensembl ].
VAR_063067
Natural variant4831L → P in GD1 and GD2; common mutation; associated with susceptibility to Parkinson disease; gene conversion; very low activity; alters protein stability. Ref.21 Ref.26 Ref.40 Ref.42 Ref.48 Ref.51 Ref.57 Ref.62 Ref.65 Ref.66 Ref.73 Ref.75 Ref.76 Ref.77
VAR_003321
Natural variant4831L → R in GD; severe.
VAR_003320
Natural variant4851A → P in GD.
VAR_003322
Natural variant4901H → R in GD; type 1; associated with D-460. Ref.69 Ref.73
VAR_032416
Natural variant4951A → P in GD; gene conversion. Ref.21
Corresponds to variant rs368060 [ dbSNP | Ensembl ].
VAR_003323
Natural variant4971V → L. Ref.21
VAR_063068
Natural variant5001L → P in GD; 10% of normal activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032216
Natural variant5011N → K in GD; type 2. Ref.49
VAR_009049
Natural variant5021R → C in GD; 37% of normal activity; also found in patients with Parkinson disease. Ref.21 Ref.40 Ref.66
VAR_003324
Natural variant5021R → P in GD; loss of activity; increases susceptibility to proteolytic degradation. Ref.26
VAR_032217
Natural variant5091L → P.
VAR_003325
Natural variant5131D → Y in GD2. Ref.55
VAR_009050
Natural variant5171G → S in GD.
VAR_003326
Natural variant5301T → I in GD3. Ref.46
VAR_010075
Natural variant5351R → C in GD; mild. Ref.51
VAR_003327
Natural variant5351R → H in GD; mild. Ref.36
VAR_003328

Experimental info

Mutagenesis431C → S: Loss of activity. Ref.26
Mutagenesis571C → S: Loss of activity. Ref.26
Mutagenesis621C → S: Loss of activity. Ref.26
Mutagenesis3791E → G: Decreases activity 1000-fold. Ref.16
Sequence conflict2271N → R in BAA02546. Ref.5
Sequence conflict4701S → I AA sequence Ref.15
Sequence conflict5341R → H in AAA35873. Ref.1

Secondary structure

................................................................................................. 536
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 9, 2004. Version 3.
Checksum: FA1E15684344A0E6

FASTA53659,716
        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 

« Hide

Isoform Short [UniParc].

Checksum: 3905C3D0AA3B1C2B
Show »

FASTA51657,455
Isoform 3 [UniParc].

Checksum: BF20F409A5BB4AD0
Show »

FASTA26329,897

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[12]"Structural 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] [Europe PMC] [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)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 409-462, VARIANT GD1 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-379, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-98; ASN-185 AND ASN-309.
[19]"LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase."
Reczek D., Schwake M., Schroder J., Hughes H., Blanz J., Jin X., Brondyk W., Van Patten S., Edmunds T., Saftig P.
Cell 131:770-783(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SCARB2.
[20]"Integral and associated lysosomal membrane proteins."
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.
Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Placenta.
[21]"Glucocerebrosidase mutations in clinical and pathologically proven Parkinson's disease."
Neumann J., Bras J., Deas E., O'Sullivan S.S., Parkkinen L., Lachmann R.H., Li A., Holton J., Guerreiro R., Paudel R., Segarane B., Singleton A., Lees A., Hardy J., Houlden H., Revesz T., Wood N.W.
Brain 132:1783-1794(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PARKINSON DISEASE, VARIANTS GLU-46; CYS-170; GLU-232; GLN-296; SER-409; ALA-419; HIS-448; ASN-482; PRO-483; PRO-495; LEU-497 AND CYS-502.
[22]"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-98 AND ASN-309.
Tissue: Liver.
[23]"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].
[24]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-536, GLYCOSYLATION AT ASN-58, DISULFIDE BONDS.
[25]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-536 IN COMPLEX WITH SYNTHETIC INHIBITOR, ACTIVE SITE.
[26]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-536, CHARACTERIZATION OF VARIANTS GD 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.
[27]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 40-536, GLYCOSYLATION AT ASN-58; ASN-98 AND ASN-185.
[28]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 40-536 IN COMPLEXES WITH ISOFAGOMINE, SUBCELLULAR LOCATION.
[29]"Mutations causing Gaucher disease."
Horowitz M., Zimran A.
Hum. Mutat. 3:1-11(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON GD VARIANTS.
[30]"Glucocerebrosidase (Gaucher disease)."
Beutler E., Gelbart T.
Hum. Mutat. 8:207-213(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON GD VARIANTS.
[31]"Type 2 Gaucher disease: an expanding phenotype."
Tayebi N., Stone D.L., Sidransky E.
Mol. Genet. Metab. 68:209-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON GD VARIANTS.
[32]"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] [Europe PMC] [Abstract]
Cited for: REVIEW ON GD VARIANTS.
[33]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD TYR-255.
[34]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD.
[35]"Identification of six new Gaucher disease mutations."
Beutler E., Gelbart T., West C.
Genomics 15:203-205(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GD.
[36]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD HIS-535.
[37]"Two new Gaucher disease mutations."
Beutler E., Gelbart T.
Hum. Genet. 93:209-210(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GD ASN-438.
[38]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD SER-409 AND CYS-457.
[39]"Glucocerebrosidase mutations in Gaucher disease."
Beutler E., Demina A., Gelbart T.
Mol. Med. 1:82-92(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GD ASP-215; THR-221; ARG-241; GLN-296; CYS-324; GLY-417 AND ASN-419.
[40]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD SER-409; HIS-448; PRO-483 AND CYS-502.
[41]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD SER-217.
[42]"The molecular characterization of Gaucher disease in South Africa."
Morar B., Lane A.B.
Clin. Genet. 50:78-84(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GD SER-409; LEU-426; LEU-433 AND PRO-483.
[43]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD LEU-54; GLU-85 AND SER-227.
[44]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD HIS-352 AND GLN-398.
[45]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD1 THR-435.
[46]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD3 LEU-437 AND ILE-530.
[47]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD LEU-414 AND THR-441.
[48]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD VAL-76; GLU-85; TRP-87; TRP-159; SER-227; ILE-252 AND PRO-483.
[49]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD LYS-501.
[50]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD TRP-87; GLU-234; ARG-241; ILE-252; ASN-310; LEU-391 AND SER-409.
[51]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD VAL-228; ILE-252; GLY-405; HIS-448; GLN-452; PRO-483 AND CYS-535.
[52]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PSEUDO-GAUCHER HIS-448.
[53]"Six new Gaucher disease mutations."
Demina A., Beutler E.
Acta Haematol. 99:80-82(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GD LEU-146; LEU-198; THR-380; ASN-405 AND ARG-432.
[54]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD.
[55]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD2 TYR-513.
[56]"Hematologically important mutations: Gaucher disease."
Beutler E., Gelbart T.
Blood Cells Mol. Dis. 24:2-8(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GD.
[57]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD2 LYS-80; CYS-170 AND PRO-483.
[58]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD GLY-392.
[59]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD GLU-152; PRO-173; GLU-428; LEU-430; ILE-431 AND HIS-451.
[60]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD1 GLY-230 AND SER-409.
[61]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD1 SER-409 AND LEU-440.
[62]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD ARG-241; CYS-244; ILE-252; HIS-448 AND PRO-483.
[63]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD.
[64]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS PERINATAL LETHAL GD ARG-350 AND PHE-437.
[65]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD PRO-173; TRP-234; SER-409; SER-416; HIS-448 AND PRO-483.
[66]"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] [Europe PMC] [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.
[67]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD SER-55 AND HIS-448.
[68]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD GLU-175; PRO-201; GLU-237; LEU-290 AND PHE-441.
[69]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD THR-198; ARG-241; ARG-270; ILE-400 AND ARG-490.
[70]"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] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
[71]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GD SER-55.
[72]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT GD SER-409.
[73]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GD1 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 GD1 ASN-63; SER-158; LEU-221; GLU-230 AND ASP-460.
[74]"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] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN PARKINSON DISEASE.
[75]"Glucocerebrosidase mutations and risk of Parkinson disease in Chinese patients."
Tan E.K., Tong J., Fook-Chong S., Yih Y., Wong M.C., Pavanni R., Zhao Y.
Arch. Neurol. 64:1056-1058(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF VARIANT GD PRO-483 IN SUSCEPTIBILITY TO PARKINSON DISEASE.
[76]"Glucocerebrosidase gene mutations: a risk factor for Lewy body disorders."
Mata I.F., Samii A., Schneer S.H., Roberts J.W., Griffith A., Leis B.C., Schellenberg G.D., Sidransky E., Bird T.D., Leverenz J.B., Tsuang D., Zabetian C.P.
Arch. Neurol. 65:379-382(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF VARIANTS GD SER-409 AND PRO-483 IN SUSCEPTIBILITY TO PARKINSON DISEASE.
[77]"Multicenter analysis of glucocerebrosidase mutations in Parkinson's disease."
Sidransky E., Nalls M.A., Aasly J.O., Aharon-Peretz J., Annesi G., Barbosa E.R., Bar-Shira A., Berg D., Bras J., Brice A., Chen C.M., Clark L.N., Condroyer C., De Marco E.V., Durr A., Eblan M.J., Fahn S., Farrer M.J. expand/collapse author list , Fung H.C., Gan-Or Z., Gasser T., Gershoni-Baruch R., Giladi N., Griffith A., Gurevich T., Januario C., Kropp P., Lang A.E., Lee-Chen G.J., Lesage S., Marder K., Mata I.F., Mirelman A., Mitsui J., Mizuta I., Nicoletti G., Oliveira C., Ottman R., Orr-Urtreger A., Pereira L.V., Quattrone A., Rogaeva E., Rolfs A., Rosenbaum H., Rozenberg R., Samii A., Samaddar T., Schulte C., Sharma M., Singleton A., Spitz M., Tan E.K., Tayebi N., Toda T., Troiano A.R., Tsuji S., Wittstock M., Wolfsberg T.G., Wu Y.R., Zabetian C.P., Zhao Y., Ziegler S.G.
N. Engl. J. Med. 361:1651-1661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF VARIANTS GD SER-409 AND PRO-483 IN SUSCEPTIBILITY TO PARKINSON DISEASE.
+Additional computationally mapped references.

Web resources

Ceredase

Clinical information on Ceredase

Cerezyme

Clinical information on Cerezyme

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIREUHUGC. A94068.
I52980.
I67792.
RefSeqNP_000148.2. NM_000157.3.
NP_001005741.1. NM_001005741.2.
NP_001005742.1. NM_001005742.2.
UniGeneHs.282997.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OGSX-ray2.00A/B40-536[»]
1Y7VX-ray2.40A/B40-536[»]
2F61X-ray2.50A/B40-536[»]
2J25X-ray2.90A/B40-536[»]
2NSXX-ray2.11A/B/C/D40-536[»]
2NT0X-ray1.79A/B/C/D40-536[»]
2NT1X-ray2.30A/B/C/D40-536[»]
2V3DX-ray1.96A/B40-536[»]
2V3EX-ray2.00A/B40-536[»]
2V3FX-ray1.95A/B40-536[»]
2VT0X-ray2.15A/B40-536[»]
2WCGX-ray2.30A/B40-536[»]
2WKLX-ray2.70A/B40-536[»]
2XWDX-ray2.66A/B40-536[»]
2XWEX-ray2.31A/B40-536[»]
3GXDX-ray2.50A/B/C/D40-536[»]
3GXFX-ray2.40A/B/C/D40-536[»]
3GXIX-ray1.84A/B/C/D40-536[»]
3GXMX-ray2.20A/B/C/D40-536[»]
3KE0X-ray2.70A/B40-536[»]
3KEHX-ray2.80A/B40-536[»]
3RIKX-ray2.48A/B/C/D40-536[»]
3RILX-ray2.40A/B/C/D40-536[»]
ProteinModelPortalP04062.
SMRP04062. Positions 40-536.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108899. 11 interactions.
DIPDIP-38645N.
IntActP04062. 5 interactions.
MINTMINT-3004354.
STRING9606.ENSP00000314508.

Chemistry

BindingDBP04062.
ChEMBLCHEMBL2179.
DrugBankDB00088. Alglucerase.
DB00053. Imiglucerase.

Protein family/group databases

Allergome8244. Hom s Glucocerebrosidase.
CAZyGH30. Glycoside Hydrolase Family 30.

PTM databases

PhosphoSiteP04062.

Polymorphism databases

DMDM55584151.

Proteomic databases

PaxDbP04062.
PRIDEP04062.

Protocols and materials databases

DNASU2629.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327247; ENSP00000314508; ENSG00000177628. [P04062-1]
ENST00000368373; ENSP00000357357; ENSG00000177628. [P04062-1]
GeneID2629.
KEGGhsa:2629.
UCSCuc001fjh.3. human. [P04062-1]

Organism-specific databases

CTD2629.
GeneCardsGC01M155204.
H-InvDBHIX0001123.
HGNCHGNC:4177. GBA.
HPAHPA006667.
MIM168600. phenotype.
230800. phenotype.
230900. phenotype.
231000. phenotype.
231005. phenotype.
606463. gene.
608013. phenotype.
neXtProtNX_P04062.
Orphanet1648. Dementia with Lewy body.
85212. Fetal Gaucher disease.
2072. Gaucher disease - ophthalmoplegia - cardiovascular calcification.
77259. Gaucher disease type 1.
77260. Gaucher disease type 2.
77261. Gaucher disease type 3.
319705. Parkinson disease.
2828. Young adult-onset Parkinsonism.
PharmGKBPA28591.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5520.
HOVERGENHBG002285.
InParanoidP04062.
KOK01201.
OMAAAKYVWG.
OrthoDBEOG76DTRZ.
PhylomeDBP04062.
TreeFamTF314254.

Enzyme and pathway databases

BRENDA3.2.1.45. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP04062.
BgeeP04062.
CleanExHS_GBA.
HS_GC.
GenevestigatorP04062.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR013780. Glyco_hydro_13_b.
IPR001139. Glyco_hydro_30.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR11069. PTHR11069. 1 hit.
PfamPF02055. Glyco_hydro_30. 1 hit.
[Graphical view]
PRINTSPR00843. GLHYDRLASE30.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP04062.
GeneWikiGlucocerebrosidase.
GenomeRNAi2629.
NextBio10357.
PROP04062.
SOURCESearch...

Entry information

Entry nameGLCM_HUMAN
AccessionPrimary (citable) accession number: P04062
Secondary accession number(s): A8K796 expand/collapse secondary AC list , Q16545, Q4VX22, Q6I9R6, Q9UMJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 9, 2004
Last modified: April 16, 2014
This is version 184 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries