HUMAN:AGAL

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	GLA
Protein Name(s)	Alpha-galactosidase A Alpha-D-galactosidase A Alpha-D-galactoside galactohydrolase Melibiase
External Links
UniProt	P06280
EMBL	X05790 X14448 U78027 AL035422 BC002689 M13571 D00039 M18242 X16889 M20317
CCDS	CCDS14484.1
PIR	S04081
RefSeq	NP_000160.1
UniGene	Hs.69089
PDB	1R46 1R47 3GXN 3GXP 3GXT 3HG2 3HG3 3HG4 3HG5 3LX9 3LXA 3LXB 3LXC 3S5Y 3S5Z 3TV8 4NXS
PDBsum	1R46 1R47 3GXN 3GXP 3GXT 3HG2 3HG3 3HG4 3HG5 3LX9 3LXA 3LXB 3LXC 3S5Y 3S5Z 3TV8 4NXS
ProteinModelPortal	P06280
SMR	P06280
BioGrid	108981
IntAct	P06280
STRING	9606.ENSP00000218516
BindingDB	P06280
ChEMBL	CHEMBL2524
Allergome	9621
CAZy	GH27
PhosphoSite	P06280
MaxQB	P06280
PaxDb	P06280
PeptideAtlas	P06280
PRIDE	P06280
DNASU	2717
Ensembl	ENST00000218516
GeneID	2717
KEGG	hsa:2717
UCSC	uc004ehl.1
CTD	2717
GeneCards	GC0XM100652
GeneReviews	GLA
HGNC	HGNC:4296
HPA	HPA000237 HPA000966
MIM	300644 301500
neXtProt	NX_P06280
Orphanet	324
PharmGKB	PA28707
eggNOG	NOG68897
HOGENOM	HOG000161224
HOVERGEN	HBG001989
InParanoid	P06280
KO	K01189
OMA	LADGYKH
OrthoDB	EOG7F24SV
PhylomeDB	P06280
TreeFam	TF312909
BioCyc	MetaCyc:HS02389-MONOMER
Reactome	REACT_116105
SABIO-RK	P06280
EvolutionaryTrace	P06280
GeneWiki	Alpha-galactosidase
GenomeRNAi	2717
NextBio	10728
PRO	PR:P06280
Proteomes	UP000005640
Bgee	P06280
CleanEx	HS_GLA
ExpressionAtlas	P06280
Genevestigator	P06280
GO	GO:0005737 GO:0005576 GO:0070062 GO:0005794 GO:0043202 GO:0005764 GO:0004557 GO:0003824 GO:0016936 GO:0016787 GO:0042803 GO:0052692 GO:0005102 GO:0016139 GO:0046479 GO:0006687 GO:0046477 GO:0045019 GO:0051001 GO:0009311 GO:0044281 GO:0006665
Gene3D	2.60.40.1180 3.20.20.70
InterPro	IPR013785 IPR013780 IPR002241 IPR000111 IPR017853
Pfam	PF02065
PRINTS	PR00740
SUPFAM	SSF51445
PROSITE	PS00512

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0005773	vacuole	PMID:1332979^[1]	ECO:0000314			C	Fig 1A	complete
	GO:0005802	trans-Golgi network	PMID:1332979^[1]	ECO:0000314			C	Fig 1B	complete
enables	GO:0004557	alpha-galactosidase activity	PMID:27211852^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0051001	negative regulation of nitric-oxide synthase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51569	P	Seeded From UniProt	complete
involved_in	GO:0046477	glycosylceramide catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51569	P	Seeded From UniProt	complete
involved_in	GO:0045019	negative regulation of nitric oxide biosynthetic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51569	P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:6256390^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009311	oligosaccharide metabolic process	PMID:39940^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:1332979^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:1332979^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:1332979^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:1332979^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:3029062^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:1332979^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004557	alpha-galactosidase activity	PMID:16372133^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004557	alpha-galactosidase activity	PMID:39940^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	PMID:39940^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0046477	glycosylceramide catabolic process	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1347344 PANTHER:PTN000155295	P	Seeded From UniProt	complete
involved_in	GO:0016139	glycoside catabolic process	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000155295 WB:WBGene00011095	P	Seeded From UniProt	complete
involved_in	GO:0009311	oligosaccharide metabolic process	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000155295 UniProtKB:P06280	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000155295 UniProtKB:P06280 WB:WBGene00011095	C	Seeded From UniProt	complete
enables	GO:0004557	alpha-galactosidase activity	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1347344 PANTHER:PTN000155295 PomBase:SPAC869.07c RGD:1589721 UniProtKB:P06280 UniProtKB:Q5AX28	F	Seeded From UniProt	complete
enables	GO:0016936	galactoside binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D3ZJF9 ensembl:ENSRNOP00000015494	F	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D3ZJF9 ensembl:ENSRNOP00000015494	C	Seeded From UniProt	complete
enables	GO:0004557	alpha-galactosidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D3ZJF9 ensembl:ENSRNOP00000015494	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013785	F	Seeded From UniProt	complete
enables	GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000111 InterPro:IPR002241	F	Seeded From UniProt	complete
involved_in	GO:0005975	carbohydrate metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000111 InterPro:IPR002241	P	Seeded From UniProt	complete
enables	GO:0004557	alpha-galactosidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.22	F	Seeded From UniProt	complete
enables	GO:0052692	raffinose alpha-galactosidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.1.22	F	Seeded From UniProt	complete
involved_in	GO:0046479	glycosphingolipid catabolic process	PMID:2160973^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	PMID:7911050^[10]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:3029062^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0043202	lysosomal lumen	Reactome:R-HSA-1605736	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0035578	azurophil granule lumen	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006687	glycosphingolipid metabolic process	Reactome:R-HSA-1660662	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	P	Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0458 UniProtKB-SubCell:SL-0158	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Ioannou, YA et al. (1992) Overexpression of human alpha-galactosidase A results in its intracellular aggregation, crystallization in lysosomes, and selective secretion. J. Cell Biol. 119 1137-50 PubMed GONUTS page
↑ Ge, W et al. (2017) A novel mutation of α-galactosidase A gene causes Fabry disease mimicking primary erythromelalgia in a Chinese family. Int. J. Neurosci. 127 448-453 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Bishop, DF & Desnick, RJ (1981) Affinity purification of alpha-galactosidase A from human spleen, placenta, and plasma with elimination of pyrogen contamination. Properties of the purified splenic enzyme compared to other forms. J. Biol. Chem. 256 1307-16 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Dean, KJ & Sweeley, CC (1979) Studies on human liver alpha-galactosidases. I. Purification of alpha-galactosidase A and its enzymatic properties with glycolipid and oligosaccharide substrates. J. Biol. Chem. 254 9994-10000 PubMed GONUTS page
↑ ^6.0 ^6.1 Lemansky, P et al. (1987) Synthesis and processing of alpha-galactosidase A in human fibroblasts. Evidence for different mutations in Fabry disease. J. Biol. Chem. 262 2062-5 PubMed GONUTS page
↑ Sakuraba, H et al. (2006) Comparison of the effects of agalsidase alfa and agalsidase beta on cultured human Fabry fibroblasts and Fabry mice. J. Hum. Genet. 51 180-8 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Kornreich, R et al. (1990) Alpha-galactosidase A gene rearrangements causing Fabry disease. Identification of short direct repeats at breakpoints in an Alu-rich gene. J. Biol. Chem. 265 9319-26 PubMed GONUTS page
↑ Eng, CM & Desnick, RJ (1994) Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum. Mutat. 3 103-11 PubMed GONUTS page

[PMID:1332979-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Ioannou, YA et al. (1992) Overexpression of human alpha-galactosidase A results in its intracellular aggregation, crystallization in lysosomes, and selective secretion. J. Cell Biol. 119 1137-50 PubMed GONUTS page

[PMID:27211852-2] Ge, W et al. (2017) A novel mutation of α-galactosidase A gene causes Fabry disease mimicking primary erythromelalgia in a Chinese family. Int. J. Neurosci. 127 448-453 PubMed GONUTS page

[PMID:23533145-3] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:6256390-4] Bishop, DF & Desnick, RJ (1981) Affinity purification of alpha-galactosidase A from human spleen, placenta, and plasma with elimination of pyrogen contamination. Properties of the purified splenic enzyme compared to other forms. J. Biol. Chem. 256 1307-16 PubMed GONUTS page

[PMID:39940-5] 5.0 ^5.1 ^5.2 Dean, KJ & Sweeley, CC (1979) Studies on human liver alpha-galactosidases. I. Purification of alpha-galactosidase A and its enzymatic properties with glycolipid and oligosaccharide substrates. J. Biol. Chem. 254 9994-10000 PubMed GONUTS page

[PMID:3029062-6] 6.0 ^6.1 Lemansky, P et al. (1987) Synthesis and processing of alpha-galactosidase A in human fibroblasts. Evidence for different mutations in Fabry disease. J. Biol. Chem. 262 2062-5 PubMed GONUTS page

[PMID:16372133-7] Sakuraba, H et al. (2006) Comparison of the effects of agalsidase alfa and agalsidase beta on cultured human Fabry fibroblasts and Fabry mice. J. Hum. Genet. 51 180-8 PubMed GONUTS page

[PMID:21873635-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:2160973-9] Kornreich, R et al. (1990) Alpha-galactosidase A gene rearrangements causing Fabry disease. Identification of short direct repeats at breakpoints in an Alu-rich gene. J. Biol. Chem. 265 9319-26 PubMed GONUTS page

[PMID:7911050-10] Eng, CM & Desnick, RJ (1994) Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. Hum. Mutat. 3 103-11 PubMed GONUTS page

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HUMAN:AGAL

Contents

Annotations

Notes

References

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