MGP Database

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MGP001221

UniProt Annotations

Entry Information
Gene Namegalactosidase, beta 1
Protein EntryBGAL_HUMAN
UniProt IDP16278
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; IsoId=P16278-1; Sequence=Displayed; Name=2; Synonyms=Beta-galactosidase-related protein, Beta-galactosidase-like protein, S-Gal, Elastin-binding protein, EBP; IsoId=P16278-2, P16279-1; Sequence=VSP_031241; Name=3; IsoId=P16278-3; Sequence=VSP_039974; Note=No experimental confirmation available.;
Catalytic ActivityHydrolysis of terminal non-reducing beta-D- galactose residues in beta-D-galactosides.
DiseaseGM1-gangliosidosis 1 (GM1G1) [MIM:230500]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM1 gangliosides, glycoproteins and keratan sulfate primarily in neurons of the central nervous system. GM1-gangliosidosis type 1 is characterized by onset within the first three months of life, central nervous system degeneration, coarse facial features, hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler syndrome, and rapidly progressive psychomotor deterioration. Urinary oligosaccharide levels are high. It leads to death usually between the first and second year of life. {ECO:0000269|PubMed:10338095, ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:10839995, ECO:0000269|PubMed:1487238, ECO:0000269|PubMed:15365997, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:15791924, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:8213816, ECO:0000269|Ref.22, ECO:0000269|Ref.25}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseGM1-gangliosidosis 2 (GM1G2) [MIM:230600]: A gangliosidosis characterized by onset between ages 1 and 5. The main symptom is locomotor ataxia, ultimately leading to a state of decerebration with epileptic seizures. Patients do not display the skeletal changes associated with the infantile form, but they nonetheless excrete elevated amounts of beta-linked galactose- terminal oligosaccharides. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:12644936, ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:8213816}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseGM1-gangliosidosis 3 (GM1G3) [MIM:230650]: A gangliosidosis with a variable phenotype. Patients show mild skeletal abnormalities, dysarthria, gait disturbance, dystonia and visual impairment. Visceromegaly is absent. Intellectual deficit can initially be mild or absent but progresses over time. Inheritance is autosomal recessive. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:15986423, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:8198123, ECO:0000269|Ref.22, ECO:0000269|Ref.24}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseMucopolysaccharidosis 4B (MPS4B) [MIM:253010]: A form of mucopolysaccharidosis type 4, an autosomal recessive lysosomal storage disease characterized by intracellular accumulation of keratan sulfate and chondroitin-6-sulfate. Key clinical features include short stature, skeletal dysplasia, dental anomalies, and corneal clouding. Intelligence is normal and there is no direct central nervous system involvement, although the skeletal changes may result in neurologic complications. There is variable severity, but patients with the severe phenotype usually do not survive past the second or third decade of life. {ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:12393180, ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:1928092, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:7586649}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionCleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
FunctionIsoform 2 has no beta-galactosidase catalytic activity, but plays functional roles in the formation of extracellular elastic fibers (elastogenesis) and in the development of connective tissue. Seems to be identical to the elastin-binding protein (EBP), a major component of the non-integrin cell surface receptor expressed on fibroblasts, smooth muscle cells, chondroblasts, leukocytes, and certain cancer cell types. In elastin producing cells, associates with tropoelastin intracellularly and functions as a recycling molecular chaperone which facilitates the secretions of tropoelastin and its assembly into elastic fibers.
InteractionQ9NSA3:CTNNBIP1; NbExp=1; IntAct=EBI-989638, EBI-747082; Q99519:NEU1; NbExp=1; IntAct=EBI-989638, EBI-721517;
SimilarityBelongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
Subcellular LocationIsoform 1: Lysosome.
Subcellular LocationIsoform 2: Cytoplasm, perinuclear region. Note=Localized to the perinuclear area of the cytoplasm but not to lysosomes.
Web ResourceName=Wikipedia; Note=Beta-galactosidase entry; URL="http://en.wikipedia.org/wiki/Beta-galactosidase";
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