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P06280 (AGAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-galactosidase A

EC=3.2.1.22
Alternative name(s):
Alpha-D-galactosidase A
Alpha-D-galactoside galactohydrolase
Melibiase
INN=Agalsidase
Gene names
Name:GLA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.

Subunit structure

Homodimer. Ref.12

Subcellular location

Lysosome.

Involvement in disease

Fabry disease (FD) [MIM:301500]: Rare X-linked sphingolipidosis disease where glycolipid accumulates in many tissues. The disease consists of an inborn error of glycosphingolipid catabolism. FD patients show systemic accumulation of globotriaosylceramide (Gb3) and related glycosphingolipids in the plasma and cellular lysosomes throughout the body. Clinical recognition in males results from characteristic skin lesions (angiokeratomas) over the lower trunk. Patients may show ocular deposits, febrile episodes, and burning pain in the extremities. Death results from renal failure, cardiac or cerebral complications of hypertension or other vascular disease. Heterozygous females may exhibit the disorder in an attenuated form, they are more likely to show corneal opacities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53

Pharmaceutical use

Available under the names Replagal (from Shire) and Fabrazyme (from Genzyme). Used as a long-term enzyme replacement therapy in patients with a confirmed diagnosis of Fabry disease. The differences between Replagal (also known as agalsidase alpha) and Fabrazyme (also known as agalsidase beta) lies in the glycosylation patterns. Agalsidase beta is produced in the hamster CHO cell line while agalsidase alpha is produced in human cell lines.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

RNA editing

Edited at position 396.
Partially edited. Ref.9

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityRNA editing
   DiseaseDisease mutation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processglycoside catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

glycosphingolipid catabolic process

Traceable author statement PubMed 2160973. Source: UniProtKB

glycosphingolipid metabolic process

Traceable author statement. Source: Reactome

glycosylceramide catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of nitric-oxide synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

oligosaccharide metabolic process

Inferred from direct assay PubMed 39940. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

sphingolipid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from mutant phenotype PubMed 1332979. Source: UniProtKB

cytoplasm

Inferred from mutant phenotype PubMed 1332979. Source: UniProtKB

extracellular region

Inferred from direct assay PubMed 3029062. Source: UniProtKB

lysosomal lumen

Traceable author statement. Source: Reactome

lysosome

Inferred from mutant phenotype PubMed 1332979. Source: UniProtKB

   Molecular_functionalpha-galactosidase activity

Inferred from direct assay PubMed 39940. Source: UniProtKB

catalytic activity

Inferred from direct assay PubMed 39940. Source: UniProtKB

galactoside binding

Inferred from electronic annotation. Source: Ensembl

hydrolase activity

Traceable author statement Ref.13. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 6256390. Source: UniProtKB

raffinose alpha-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

receptor binding

Inferred from direct assay PubMed 1332979. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 429398Alpha-galactosidase A
PRO_0000001004

Regions

Region203 – 2075Substrate binding

Sites

Active site1701Nucleophile By similarity
Active site2311Proton donor By similarity

Amino acid modifications

Glycosylation1391N-linked (GlcNAc...) Ref.12
Glycosylation1921N-linked (GlcNAc...) Ref.12
Glycosylation2151N-linked (GlcNAc...) Ref.10 Ref.12
Glycosylation4081N-linked (GlcNAc...) Potential
Disulfide bond52 ↔ 94
Disulfide bond56 ↔ 63
Disulfide bond142 ↔ 172
Disulfide bond202 ↔ 223
Disulfide bond378 ↔ 382

Natural variations

Natural variant12 – 143Missing in FD; has 4% of wild-type activity.
VAR_062550
Natural variant201A → P in FD; atypical. Ref.26 Ref.33
VAR_012362
Natural variant311A → V in FD. Ref.34 Ref.51
VAR_012363
Natural variant321L → P in FD. Ref.25
VAR_000431
Natural variant341N → S in FD. Ref.19 Ref.20 Ref.25
Corresponds to variant rs28935192 [ dbSNP | Ensembl ].
VAR_000432
Natural variant351G → R in FD. Ref.21
VAR_000433
Natural variant401P → L in FD. Ref.44
VAR_012364
Natural variant401P → S in FD. Ref.14 Ref.33 Ref.38
VAR_000434
Natural variant421M → L in FD. Ref.51
VAR_062551
Natural variant421M → V in FD. Ref.28 Ref.42
VAR_012365
Natural variant431G → R in FD. Ref.51
VAR_062552
Natural variant45 – 462LH → RS in FD.
VAR_012366
Natural variant461H → P in FD; has 36% of wild-type activity. Ref.53
VAR_062553
Natural variant461H → R in FD. Ref.34
VAR_012367
Natural variant461H → Y in FD. Ref.46
VAR_012368
Natural variant471W → G in FD. Ref.46
VAR_012369
Natural variant491R → L in FD. Ref.21
VAR_000435
Natural variant491R → P in FD. Ref.46
VAR_012370
Natural variant491R → S in FD. Ref.28
VAR_012371
Natural variant521C → R in FD. Ref.30 Ref.31
VAR_000436
Natural variant521C → S in FD.
VAR_000437
Natural variant561C → F in FD.
VAR_000438
Natural variant561C → G in FD. Ref.19
Corresponds to variant rs28935193 [ dbSNP | Ensembl ].
VAR_000439
Natural variant561C → Y in FD. Ref.28
VAR_012372
Natural variant591E → K in FD.
VAR_000440
Natural variant651S → T in FD; does not affect enzyme function. Ref.35 Ref.49
VAR_032290
Natural variant661E → Q in FD; has 52% of wild-type activity. Ref.18 Ref.23 Ref.33 Ref.53
Corresponds to variant rs28935191 [ dbSNP | Ensembl ].
VAR_000441
Natural variant721M → V in FD; atypical. Ref.33 Ref.37
VAR_000442
Natural variant851G → D in FD. Ref.25
VAR_000443
Natural variant861Y → C in FD. Ref.34
VAR_012373
Natural variant891L → P in FD. Ref.34
VAR_012374
Natural variant891L → R in FD.
VAR_000444
Natural variant911I → T in FD; mild. Ref.34
VAR_012375
Natural variant921D → H in FD. Ref.28
VAR_012376
Natural variant921D → Y in FD. Ref.34
VAR_012377
Natural variant931D → G in FD. Ref.28
VAR_012378
Natural variant931D → N in FD; has no enzyme activity. Ref.51 Ref.53
VAR_062554
Natural variant941C → S in FD. Ref.46
VAR_012379
Natural variant941C → Y in FD. Ref.34
VAR_012380
Natural variant951W → S in FD. Ref.44 Ref.46
VAR_012381
Natural variant971A → V in FD. Ref.34
VAR_012382
Natural variant1001R → K in FD.
VAR_000445
Natural variant1001R → T in FD. Ref.34
VAR_012383
Natural variant112 – 1176Missing in FD.
VAR_000446
Natural variant1121R → C in FD. Ref.18 Ref.23 Ref.33 Ref.42 Ref.44 Ref.46 Ref.51
VAR_000447
Natural variant1121R → H in FD; mild. Ref.44 Ref.51
VAR_000448
Natural variant1121R → S in FD. Ref.51
VAR_062555
Natural variant1131F → L in FD; mild. Ref.34
VAR_012384
Natural variant1131F → S in FD. Ref.46
VAR_012385
Natural variant120 – 1212LA → PT in FD.
VAR_000449
Natural variant1201L → V in FD; has 42% of wild-type activity. Ref.53
VAR_062556
Natural variant1281G → E in FD. Ref.31
VAR_000450
Natural variant1311L → P in FD.
VAR_000451
Natural variant1341Y → S in FD. Ref.34 Ref.51
VAR_012386
Natural variant1351A → V in FD. Ref.51
VAR_062557
Natural variant1381G → R in FD. Ref.34
VAR_012387
Natural variant1421C → R in FD. Ref.42
VAR_012388
Natural variant1421C → Y in FD. Ref.24 Ref.33
VAR_000452
Natural variant1431A → P in FD. Ref.47
VAR_000453
Natural variant1431A → T in FD. Ref.34 Ref.46 Ref.52
VAR_012389
Natural variant1441G → V in FD.
VAR_000454
Natural variant1461P → S in FD; mild.
Corresponds to variant rs28935194 [ dbSNP | Ensembl ].
VAR_000455
Natural variant1481S → N in FD. Ref.44
VAR_012390
Natural variant1481S → R in FD. Ref.34 Ref.42
VAR_012391
Natural variant1561A → T in FD. Ref.25
Corresponds to variant rs28935195 [ dbSNP | Ensembl ].
VAR_000456
Natural variant1561A → V in FD. Ref.23 Ref.24 Ref.33
VAR_000457
Natural variant1621W → C in FD. Ref.30
VAR_012392
Natural variant1621W → R in FD. Ref.19
Corresponds to variant rs28935196 [ dbSNP | Ensembl ].
VAR_000458
Natural variant1631G → V in FD. Ref.34
VAR_012393
Natural variant1651D → V in FD. Ref.21 Ref.42
VAR_000459
Natural variant1661L → V in FD. Ref.23 Ref.24 Ref.33
VAR_000460
Natural variant1701D → V in FD. Ref.34
VAR_012394
Natural variant1711G → D in FD. Ref.51
VAR_062558
Natural variant1721C → R in FD. Ref.44
VAR_012395
Natural variant1721C → Y in FD.
VAR_000461
Natural variant1831G → D in FD. Ref.42
VAR_012396
Natural variant1871M → V in FD. Ref.44
VAR_012397
Natural variant2011S → F in FD. Ref.51
VAR_062559
Natural variant2021C → W in FD. Ref.39
Corresponds to variant rs28936082 [ dbSNP | Ensembl ].
VAR_000462
Natural variant2021C → Y in FD. Ref.34
VAR_012398
Natural variant205 – 2073Missing in FD.
VAR_012399
Natural variant2051P → T in FD. Ref.28 Ref.31
VAR_000463
Natural variant2151N → S in FD; mild. Ref.20 Ref.38 Ref.42 Ref.46 Ref.51
Corresponds to variant rs28935197 [ dbSNP | Ensembl ].
VAR_000464
Natural variant2161Y → D in FD. Ref.34
VAR_012400
Natural variant2191I → N in FD.
VAR_000465
Natural variant2191I → T in FD; has 46% of wild-type activity. Ref.53
VAR_062560
Natural variant2231C → G in FD. Ref.39
VAR_012401
Natural variant2241N → D in FD. Ref.38 Ref.39
VAR_000466
Natural variant2241N → S in FD. Ref.44
VAR_012402
Natural variant2261W → R in FD. Ref.44
VAR_012403
Natural variant2271R → Q in FD. Ref.19 Ref.44
Corresponds to variant rs28935198 [ dbSNP | Ensembl ].
VAR_000467
Natural variant2301A → T in FD. Ref.44
VAR_012404
Natural variant2311D → N in FD. Ref.32
VAR_000468
Natural variant2341D → E in FD. Ref.51
VAR_062561
Natural variant2351S → C in FD. Ref.42
VAR_012405
Natural variant2361W → C in FD. Ref.28
VAR_012406
Natural variant2361W → L in FD. Ref.42
VAR_012407
Natural variant2421I → N in FD. Ref.33
VAR_012408
Natural variant2441D → H in FD. Ref.42
VAR_012409
Natural variant2441D → N in FD.
VAR_000469
Natural variant2471S → SWTS in FD.
VAR_000470
Natural variant2581G → R in FD. Ref.46
VAR_012410
Natural variant2591P → L in FD. Ref.42
VAR_012411
Natural variant2591P → R in FD. Ref.46
VAR_012412
Natural variant2601G → A in FD. Ref.23 Ref.33
VAR_012413
Natural variant2611G → D in FD. Ref.33 Ref.51
VAR_012414
Natural variant2631N → S in FD. Ref.34
VAR_012415
Natural variant2641D → V in FD. Ref.19 Ref.51
Corresponds to variant rs28935486 [ dbSNP | Ensembl ].
VAR_000471
Natural variant2641D → Y in FD. Ref.51
VAR_062562
Natural variant2651P → R in FD. Ref.30
VAR_012416
Natural variant2661D → H in FD. Ref.44
VAR_032291
Natural variant2661D → N in FD. Ref.43
VAR_012418
Natural variant2661D → V in FD. Ref.19
Corresponds to variant rs28935487 [ dbSNP | Ensembl ].
VAR_000472
Natural variant2671M → I in FD. Ref.42 Ref.46
VAR_012419
Natural variant2691V → A in FD. Ref.20
Corresponds to variant rs28935488 [ dbSNP | Ensembl ].
VAR_000473
Natural variant2721N → K in FD.
VAR_000474
Natural variant2721N → S in FD. Ref.50
Corresponds to variant rs28935495 [ dbSNP | Ensembl ].
VAR_032292
Natural variant2761S → G in FD. Ref.51
VAR_062563
Natural variant2791Q → E in FD; mild; does not significantly affect the enzyme activity but the mutant protein levels are decreased presumably in the ER of the cells. Ref.18 Ref.23 Ref.33 Ref.41
Corresponds to variant rs28935485 [ dbSNP | Ensembl ].
VAR_000475
Natural variant2791Q → H in FD. Ref.46
VAR_012420
Natural variant2801Q → H in FD. Ref.46
VAR_012421
Natural variant2841M → T in FD. Ref.31
VAR_000476
Natural variant2851A → P in FD. Ref.51
VAR_062564
Natural variant2871W → C in FD. Ref.34
VAR_012422
Natural variant2871W → G in FD. Ref.28
VAR_012423
Natural variant2881A → D in FD.
VAR_000477
Natural variant2891I → F in FD. Ref.42
VAR_012424
Natural variant2961M → I in FD; atypical. Ref.23 Ref.26 Ref.33
VAR_012425
Natural variant2961M → V in FD; mild. Ref.15
VAR_000478
Natural variant2971S → F in FD. Ref.19
Corresponds to variant rs28935489 [ dbSNP | Ensembl ].
VAR_000479
Natural variant2981N → H in FD. Ref.28 Ref.46
VAR_012426
Natural variant2981N → K in FD. Ref.31
VAR_000480
Natural variant2981N → S in FD. Ref.34
VAR_012427
Natural variant3001L → F in FD. Ref.51
VAR_062565
Natural variant3011R → Q in FD; mild; does not significantly affect the enzyme activity but the mutant protein levels are decreased presumably in the ER of the cells. Ref.16 Ref.18 Ref.23 Ref.25 Ref.27 Ref.33 Ref.39 Ref.41 Ref.44
VAR_000481
Natural variant3131D → Y in FD. Ref.19 Ref.38 Ref.46
Corresponds to variant rs28935490 [ dbSNP | Ensembl ].
VAR_000482
Natural variant316 – 3227Missing in FD.
VAR_012429
Natural variant3161V → E in FD. Ref.21
VAR_000483
Natural variant3201N → K in FD. Ref.23 Ref.33
VAR_012430
Natural variant3201N → Y in FD. Ref.44
VAR_012431
Natural variant3211Q → E in FD. Ref.42
VAR_012432
Natural variant3271Q → K in FD. Ref.20 Ref.39
Corresponds to variant rs28935491 [ dbSNP | Ensembl ].
VAR_000484
Natural variant3281G → A in FD. Ref.19 Ref.51
Corresponds to variant rs28935492 [ dbSNP | Ensembl ].
VAR_000486
Natural variant3281G → R in FD. Ref.18 Ref.23 Ref.33
VAR_000485
Natural variant3281G → V in FD. Ref.51
VAR_062566
Natural variant3381E → K in FD. Ref.51
VAR_062567
Natural variant3401W → R in FD. Ref.28
VAR_012433
Natural variant3411E → K in FD. Ref.40
VAR_012434
Natural variant3421R → Q in FD; severe.
Corresponds to variant rs28935493 [ dbSNP | Ensembl ].
VAR_000487
Natural variant3561R → Q in FD; has 15% of wild-type activity. Ref.53
VAR_062568
Natural variant3561R → W in FD; severe. Ref.17
VAR_000488
Natural variant3581E → A in FD. Ref.51
VAR_062569
Natural variant3581E → K in FD. Ref.36
VAR_000489
Natural variant3581Missing in FD. Ref.31 Ref.33 Ref.42 Ref.51
VAR_000490
Natural variant3601G → C in FD; has 6% of wild-type activity. Ref.53
VAR_062570
Natural variant3611G → R in FD; severe. Ref.20
Corresponds to variant rs28935494 [ dbSNP | Ensembl ].
VAR_000491
Natural variant3631R → H in FD. Ref.46
VAR_012435
Natural variant3731G → D in FD. Ref.45
VAR_012436
Natural variant3731G → S in FD. Ref.23 Ref.33
VAR_012437
Natural variant3771A → D in FD. Ref.46
VAR_012438
Natural variant3781C → Y in FD. Ref.42
VAR_012439
Natural variant3831Missing in FD; severe; with facial telangiectasias. Ref.29
VAR_000492
Natural variant3961F → Y in RNA edited version.
VAR_000493
Natural variant4041Missing in FD; mild. Ref.19 Ref.34 Ref.51
VAR_000494
Natural variant4091P → A in FD. Ref.46
VAR_012440
Natural variant4091P → T in FD. Ref.46
VAR_012441
Natural variant4101T → A in FD; mild. Ref.48
VAR_032293
Natural variant4141L → S in FD. Ref.51
VAR_062571

Secondary structure

................................................................................. 429
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06280 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 613F8BF21B107D7B

FASTA42948,767
        10         20         30         40         50         60 
MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF MCNLDCQEEP 

        70         80         90        100        110        120 
DSCISEKLFM EMAELMVSEG WKDAGYEYLC IDDCWMAPQR DSEGRLQADP QRFPHGIRQL 

       130        140        150        160        170        180 
ANYVHSKGLK LGIYADVGNK TCAGFPGSFG YYDIDAQTFA DWGVDLLKFD GCYCDSLENL 

       190        200        210        220        230        240 
ADGYKHMSLA LNRTGRSIVY SCEWPLYMWP FQKPNYTEIR QYCNHWRNFA DIDDSWKSIK 

       250        260        270        280        290        300 
SILDWTSFNQ ERIVDVAGPG GWNDPDMLVI GNFGLSWNQQ VTQMALWAIM AAPLFMSNDL 

       310        320        330        340        350        360 
RHISPQAKAL LQDKDVIAIN QDPLGKQGYQ LRQGDNFEVW ERPLSGLAWA VAMINRQEIG 

       370        380        390        400        410        420 
GPRSYTIAVA SLGKGVACNP ACFITQLLPV KRKLGFYEWT SRLRSHINPT GTVLLQLENT 


MQMSLKDLL 

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References

« Hide 'large scale' references
[1]"Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A."
Tsuji S., Martin B.M., Kaslow D.C., Migeon B.R., Choudary P.V., Stubblefield B.K., Mayor J.A., Murray G.J., Barranger J.A., Ginns E.I.
Eur. J. Biochem. 165:275-280(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]"Nucleotide sequence of the human alpha-galactosidase A gene."
Kornreich R., Desnick R.J., Bishop D.F.
Nucleic Acids Res. 17:3301-3302(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lymphoblast.
[3]"Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci."
Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., Gibbs R.A.
Mamm. Genome 6:334-338(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[6]"Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme."
Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M., Desnick R.J.
Proc. Natl. Acad. Sci. U.S.A. 83:4859-4863(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-429, PARTIAL PROTEIN SEQUENCE.
Tissue: Lung.
[7]"A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A."
Quinn M., Hantzopoulos P., Fidanza V., Calhoun D.H.
Gene 58:177-188(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[8]"Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region."
Bishop D.F., Kornreich R., Desnick R.J.
Proc. Natl. Acad. Sci. U.S.A. 85:3903-3907(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
[9]"Editing of human alpha-galactosidase RNA resulting in a pyrimidine to purine conversion."
Novo F.J., Kruszewski A., McDermot K.D., Goldspink G., Gorecki D.C.
Nucleic Acids Res. 23:2636-2640(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA EDITING OF POSITION 396.
[10]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-215.
Tissue: Liver.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The molecular defect leading to Fabry disease: structure of human alpha-galactosidase."
Garman S.C., Garboczi D.N.
J. Mol. Biol. 337:319-335(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH PRODUCT, HOMODIMERIZATION, GLYCOSYLATION AT ASN-139; ASN-192 AND ASN-215.
[13]"Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene."
Eng C.M., Desnick R.J.
Hum. Mutat. 3:103-111(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FD VARIANTS.
[14]"A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser."
Koide T., Ishiura M., Iwai K., Inoue M., Kaneda Y., Okada Y., Uchida T.
FEBS Lett. 259:353-356(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD SER-40.
[15]"An atypical variant of Fabry's disease with manifestations confined to the myocardium."
von Scheidt W., Eng C.M., Fitzmaurice T.F., Erdmann E., Hubner G., Olsen E.G.J., Christomanou H., Kandolf R., Bishop D.F., Desnick R.J.
N. Engl. J. Med. 324:395-399(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD VAL-296.
[16]"Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease."
Sakuraba H., Oshima A., Fukuhara Y., Shimmoto M., Nagao Y., Bishop D.F., Desnick R.J., Suzuki Y.
Am. J. Hum. Genet. 47:784-789(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD GLN-301.
[17]"Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene."
Bernstein H.S., Bishop D.F., Astrin K.H., Kornreich R., Eng C.M., Sakuraba H., Desnick R.J.
J. Clin. Invest. 83:1390-1399(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD TRP-356.
[18]"Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease."
Ishii S., Sakuraba H., Suzuki Y.
Hum. Genet. 89:29-32(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD GLN-66; CYS-112; GLU-279; GLN-301 AND ARG-328.
[19]"Nature and frequency of mutations in the alpha-galactosidase A gene that cause Fabry disease."
Eng C.M., Resnick-Silverman L.A., Niehaus D.J., Astrin K.H., Desnick R.J.
Am. J. Hum. Genet. 53:1186-1197(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD SER-34; GLY-56; ARG-162; GLN-227; VAL-264; VAL-266; PHE-297; TYR-313; ALA-328 AND ARG-404 DEL.
[20]"Mutation analysis in patients with the typical form of Anderson-Fabry disease."
Davies J.P., Winchester B.G., Malcolm S.
Hum. Mol. Genet. 2:1051-1053(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD SER-34; SER-215; ALA-269; LYS-327 AND ARG-361.
[21]"Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry disease."
Davies J.P., Christomanou H., Winchester B.G., Malcolm S.
Hum. Mol. Genet. 3:667-669(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD ARG-35; LEU-49; VAL-165 AND GLU-316.
[22]"Fabry disease: twenty-three mutations including sense and antisense CpG alterations and identification of a deletional hot-spot in the alpha-galactosidase A gene."
Eng C.M., Niehaus D.J., Enriquez A.L., Burgert T.S., Ludman M.D., Desnick R.J.
Hum. Mol. Genet. 3:1795-1799(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD.
[23]"Galactose stabilizes various missense mutants of alpha-galactosidase in Fabry disease."
Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H., Suzuki Y.
Biochem. Biophys. Res. Commun. 214:1219-1224(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD GLN-66; CYS-112; VAL-156; VAL-166; ALA-260; GLU-279; ILE-296; GLN-301; LYS-320; ARG-328 AND SER-373.
[24]"Alpha-galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins."
Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y.
Hum. Genet. 95:557-561(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD TYR-142; VAL-156 AND VAL-166.
[25]"Two novel mutations (L32P) and (G85N) among five different missense mutations in six Danish families with Fabry's disease."
Madsen K.M., Hasholt L., Soerensen S.A., Lagerstroem Fermer M., Dahl N.
Hum. Mutat. 5:277-278(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD PRO-32; SER-34; ASP-85; THR-156 AND GLN-301.
[26]"An atypical variant of Fabry's disease in men with left ventricular hypertrophy."
Nakao S., Takenaka T., Maeda M., Kodama C., Tanaka A., Tahara M., Yoshida A., Kuriyama M., Hayashibe H., Sakuraba H., Tanaka H.
N. Engl. J. Med. 333:288-293(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD PRO-20 AND ILE-296.
[27]"Point mutation in the alpha-galactosidase A gene of atypical Fabry disease with only nephropathy."
Sawada K., Mizoguchi K., Hishida A., Kaneko E., Koide Y., Nishimura K., Kimura M.
Clin. Nephrol. 45:289-294(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD GLN-301.
[28]"Fabry disease: fourteen alpha-galactosidase A mutations in unrelated families from the United Kingdom and other European countries."
Davies J.P., Eng C.M., Hill J.A., Malcolm S., MacDermot K., Winchester B.G., Desnick R.J.
Eur. J. Hum. Genet. 4:219-224(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD VAL-42; SER-49; TYR-56; HIS-92; GLY-93; THR-205; CYS-236; GLY-287; HIS-298 AND ARG-340.
[29]"Novel trinucleotide deletion in Fabry's disease."
Cariolou M.A., Christodoulides M., Manoli P., Kokkofitou A., Tsambaos D.
Hum. Genet. 97:468-470(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD PHE-383 DEL.
[30]"Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of the alpha-galactosidase A gene and detection of carriers in Fabry disease."
Germain D.P., Biasotto M., Tosi M., Meo T., Kahn A., Poenaru L.
Hum. Genet. 98:719-726(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD ARG-52; CYS-162; ARG-265 AND 316-VAL--ASP-322 DEL.
[31]"A sensitive mutation screening strategy for Fabry disease: detection of nine mutations in the alpha-galactosidase A gene."
Blanch L.C., Meaney C., Morris C.P.
Hum. Mutat. 8:38-43(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD ARG-52; GLU-128; THR-205; THR-284; LYS-298 AND GLU-358 DEL.
[32]"Uneven X inactivation in a female monozygotic twin pair with Fabry disease and discordant expression of a novel mutation in the alpha-galactosidase A gene."
Redonnet-Vernhet I., Ploos van Amstel J.K., Jansen R.P.M., Wevers R.A., Salvayre R., Levade T.
J. Med. Genet. 33:682-688(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD ASN-231.
[33]"Screening and detection of gene mutations in Japanese patients with Fabry disease by non-radioactive single-stranded conformation polymorphism analysis."
Takata T., Okumiya T., Hayashibe H., Shimmoto M., Kase R., Itoh K., Utsumi K., Kamei S., Sakuraba H.
Brain Dev. 19:111-116(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD PRO-20; SER-40; GLN-66; VAL-72; CYS-112; TYR-142; VAL-156; VAL-166; ASN-242; ALA-260; ASP-261; GLU-279; ILE-296; GLN-301; LYS-320; ARG-328; GLU-358 DEL AND SER-373.
[34]"Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in patients with classic and variant phenotypes."
Eng C.M., Ashley G.A., Burgert T.S., Enriquez A.L., D'Souza M., Desnick R.J.
Mol. Med. 3:174-182(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD VAL-31; 45-ARG-SER-46; ARG-46; CYS-86; PRO-89; THR-91; TYR-92; TYR-94; VAL-97; THR-100; LEU-113; SER-134; ARG-138; THR-143; ARG-148; VAL-163; VAL-170; TYR-202; 205-PRO--TYR-207 DEL; ASP-216; SER-263; CYS-287; SER-298 AND ARG-404 DEL.
[35]"Identification of a novel point mutation (S65T) in alpha-galactosidase A gene in Chinese patients with Fabry disease."
Chen C.-H., Shyu P.-W., Wu S.-J., Sheu S.-S., Desnick R.J., Hsiao K.-J.
Hum. Mutat. 11:328-330(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD THR-65.
[36]"A novel mutation (E358K) in the alpha-galactosidase A gene detected in a Japanese family with Fabry disease."
Miyazaki T., Kajita M., Ohmori S., Mizutani N., Niwa T., Murata Y., Seo H.
Hum. Mutat. Suppl. 1:S139-S140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD LYS-358.
[37]"Novel missense mutation (M72V) of alpha-galactosidase gene and its expression product in an atypical Fabry hemizygote."
Okumiya T., Kawamura O., Itoh K., Kase R., Ishii S., Kamei S., Sakuraba H.
Hum. Mutat. Suppl. 1:S213-S216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD VAL-72.
[38]"Mutation analysis in 11 French patients with Fabry disease."
Guffon N., Froissart R., Chevalier-Porst F., Maire I.
Hum. Mutat. Suppl. 1:S288-S290(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD SER-40; SER-215; ASP-224; TYR-313 AND TRP-THR-SER-247 INS.
[39]"Fabry disease: identification of novel alpha-galactosidase A mutations and molecular carrier detection by use of fluorescent chemical cleavage of mismatches."
Germain D.P., Poenaru L.
Biochem. Biophys. Res. Commun. 257:708-713(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD TRP-202; GLY-223; ASP-224; GLN-301 AND LYS-327.
[40]"The multiple cases of Fabry disease in a Russian family caused by an E341K amino acid substitution in the alpha-galactosidase A."
Beyer E.M., Karpova E.A., Udalova O.V., Ploos van Amstel J.K., van Diggelen O.P., Tsvetkova I.V.
Clin. Chim. Acta 280:81-89(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD LYS-341.
[41]"Characterization of two alpha-galactosidase mutants (Q279E and R301Q) found in an atypical variant of Fabry disease."
Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoh K., Sandhoff K., Sakuraba H.
Biochim. Biophys. Acta 1501:227-235(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS FD GLU-279 AND GLN-301.
[42]"Twenty novel mutations in the alpha-galactosidase A gene causing Fabry disease."
Topaloglu A.K., Ashley G.A., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J.
Mol. Med. 5:806-811(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD VAL-42; CYS-112; ARG-142; ARG-148; VAL-165; ASP-183; SER-215; CYS-235; LEU-236; HIS-244; LEU-259; ILE-267; PHE-289; GLU-321; GLU-358 DEL AND TYR-378.
[43]"Identification of four novel mutations in five unrelated Korean families with Fabry disease."
Lee J.-K., Kim G.-H., Kim J.-S., Kim K.-K., Lee M.-C., Yoo H.-W.
Clin. Genet. 58:228-233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD ASN-266.
[44]"Fabry disease: twenty-two novel mutations in the alpha-galactosidase A gene and genotype/phenotype correlations in severely and mildly affected hemizygotes and heterozygotes."
Ashton-Prolla P., Tong B., Shabbeer J., Astrin K.H., Eng C.M., Desnick R.J.
J. Invest. Med. 48:227-235(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD LEU-40; SER-95; CYS-112; HIS-112; ASN-148; ARG-172; VAL-187; SER-224; ARG-226; GLN-227; THR-230; HIS-266; GLN-301 AND TYR-320.
[45]"Identification of a novel de novo mutation (G373D) in the alpha-galactosidase A gene (GLA) in a patient affected with Fabry disease."
Germain D.P., Salard D., Fellmann F., Azibi K., Caillaud C., Bernard M.-C., Poenaru L.
Hum. Mutat. 17:353-353(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD ASP-373.
[46]"Fabry disease: 20 novel GLA mutations in 35 families."
Blaydon D., Hill J.A., Winchester B.G.
Hum. Mutat. 18:459-459(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD TYR-46; GLY-47; PRO-49; SER-94; SER-95; CYS-112; SER-113; THR-143; SER-215; ARG-258; ARG-259; ILE-267; HIS-279; HIS-280; HIS-298; TYR-313; HIS-363; ASP-377; ALA-409 AND THR-409.
[47]"Natural history of Fabry renal disease: influence of alpha-galactosidase A activity and genetic mutations on clinical course."
Branton M.H., Schiffmann R., Sabnis S.G., Murray G.J., Quirk J.M., Altarescu G., Goldfarb L., Brady R.O., Balow J.E., Austin H.A. III, Kopp J.B.
Medicine (Baltimore) 81:122-138(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD PRO-143.
[48]"Two novel mutations in the alpha-galactosidase A gene in Chinese patients with Fabry disease."
Yang C.-C., Lai L.-W., Whitehair O., Hwu W.-L., Chiang S.-C., Lien Y.-H.H.
Clin. Genet. 63:205-209(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD ALA-410.
[49]"Analysis of splice-site mutations of the alpha-galactosidase A gene in Fabry disease."
Lai L.-W., Whitehair O., Wu M.-J., O'Meara M., Lien Y.-H.H.
Clin. Genet. 63:476-482(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT FD THR-65.
[50]"Remarkable variability in renal disease in a large Slovenian family with Fabry disease."
Verovnik F., Benko D., Vujkovac B., Linthorst G.E.
Eur. J. Hum. Genet. 12:678-681(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD SER-272.
[51]"Detection of alpha-galactosidase a mutations causing Fabry disease by denaturing high performance liquid chromatography."
Shabbeer J., Robinson M., Desnick R.J.
Hum. Mutat. 25:299-305(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD VAL-31; LEU-42; ARG-43; ASN-93; CYS-112; HIS-112; SER-112; SER-134; VAL-135; ASP-171; PHE-201; SER-215; GLU-234; ASP-261; TYR-264; VAL-264; GLY-276; PRO-285; PHE-300; ALA-328; VAL-328; LYS-338; ALA-358; GLU-358 DEL; ARG-404 DEL AND SER-414.
[52]"Later-onset Fabry disease: an adult variant presenting with the cramp-fasciculation syndrome."
Nance C.S., Klein C.J., Banikazemi M., Dikman S.H., Phelps R.G., McArthur J.C., Rodriguez M., Desnick R.J.
Arch. Neurol. 63:453-457(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FD THR-143.
[53]"Newborn screening for Fabry disease in Taiwan reveals a high incidence of the later-onset GLA mutation c.936+919G>A (IVS4+919G>A)."
Hwu W.L., Chien Y.H., Lee N.C., Chiang S.C., Dobrovolny R., Huang A.C., Yeh H.Y., Chao M.C., Lin S.J., Kitagawa T., Desnick R.J., Hsu L.W.
Hum. Mutat. 30:1397-1405(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FD 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219; GLN-356 AND CYS-360, CHARACTERIZATION OF VARIANTS FD 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219; GLN-356 AND CYS-360.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05790 mRNA. Translation: CAA29232.1.
X14448 Genomic DNA. Translation: CAA32617.1.
U78027 Genomic DNA. Translation: AAB64203.1.
AL035422 Genomic DNA. Translation: CAB55878.1.
BC002689 mRNA. Translation: AAH02689.1.
M13571 Genomic DNA. Translation: AAA51676.1.
D00039 mRNA. Translation: BAA34059.1.
M18242 Genomic DNA. Translation: AAA52514.1.
X16889 mRNA. No translation available.
M20317 Genomic DNA. Translation: AAA52559.1. Sequence problems.
PIRGBHUA. S04081.
RefSeqNP_000160.1. NM_000169.2.
UniGeneHs.69089.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R46X-ray3.25A/B32-429[»]
1R47X-ray3.45A/B32-429[»]
3GXNX-ray3.01A/B32-429[»]
3GXPX-ray2.20A/B32-429[»]
3GXTX-ray2.70A/B32-429[»]
3HG2X-ray2.30A/B32-429[»]
3HG3X-ray1.90A/B32-429[»]
3HG4X-ray2.30A/B32-429[»]
3HG5X-ray2.30A/B32-429[»]
3LX9X-ray2.04A/B32-429[»]
3LXAX-ray3.04A/B32-429[»]
3LXBX-ray2.85A/B32-429[»]
3LXCX-ray2.35A/B32-429[»]
3S5YX-ray2.10A/B32-429[»]
3S5ZX-ray2.00A/B32-429[»]
3TV8X-ray2.64A/B32-429[»]
ProteinModelPortalP06280.
SMRP06280. Positions 32-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108981. 15 interactions.
IntActP06280. 4 interactions.
STRING9606.ENSP00000218516.

Chemistry

BindingDBP06280.
ChEMBLCHEMBL2524.
DrugBankDB00103. Agalsidase beta.

Protein family/group databases

Allergome9621. Hom s alpha-Galactosidase.
CAZyGH27. Glycoside Hydrolase Family 27.

PTM databases

PhosphoSiteP06280.

Proteomic databases

PaxDbP06280.
PeptideAtlasP06280.
PRIDEP06280.

Protocols and materials databases

DNASU2717.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218516; ENSP00000218516; ENSG00000102393.
ENST00000598114; ENSP00000471787; ENSG00000268815.
GeneID2717.
KEGGhsa:2717.
UCSCuc004ehl.1. human.

Organism-specific databases

CTD2717.
GeneCardsGC0XM100652.
HGNCHGNC:4296. GLA.
HPAHPA000237.
HPA000966.
MIM300644. gene.
301500. phenotype.
neXtProtNX_P06280.
Orphanet324. Fabry disease.
PharmGKBPA28707.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68897.
HOGENOMHOG000161224.
HOVERGENHBG001989.
InParanoidP06280.
KOK01189.
OMAGYKHMSL.
OrthoDBEOG7F24SV.
PhylomeDBP06280.
TreeFamTF312909.

Enzyme and pathway databases

BioCycMetaCyc:HS02389-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP06280.

Gene expression databases

ArrayExpressP06280.
BgeeP06280.
CleanExHS_GLA.
GenevestigatorP06280.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSPR00740. GLHYDRLASE27.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06280.
GeneWikiAlpha-galactosidase.
GenomeRNAi2717.
NextBio10728.
PROP06280.
SOURCESearch...

Entry information

Entry nameAGAL_HUMAN
AccessionPrimary (citable) accession number: P06280
Secondary accession number(s): Q6LER7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 166 of the entry and version 1 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 X

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries