InnateDB: Systems Biology of the Innate Immune Response

Homo sapiens Protein: GLB1

Summary

InnateDB Protein

IDBP-230735.6

Last Modified

2014-10-13 [Report errors or provide feedback]

Gene Symbol

GLB1

Protein Name

galactosidase, beta 1

Synonyms

EBP; ELNR1; MPS4B;

Species

Homo sapiens

Ensembl Protein

ENSP00000382333

InnateDB Gene

IDBG-23941 (GLB1)

Protein Structure

UniProt Annotation

Function

Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.Isoform 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.

Subcellular Localization

Isoform 1: Lysosome.Isoform 2: Cytoplasm, perinuclear region. Note=Localized to the perinuclear area of the cytoplasm but not to lysosomes.

Disease Associations

GM1-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:0000269PubMed:10338095, ECO:0000269PubMed:10737981, ECO:0000269PubMed:10839995, ECO:0000269PubMed:1487238, ECO:0000269PubMed:15365997, ECO:0000269PubMed:15714521, ECO:0000269PubMed:15791924, ECO:0000269PubMed:16538002, ECO:0000269PubMed:16941474, ECO:0000269PubMed:17309651, ECO:0000269PubMed:1907800, ECO:0000269PubMed:1909089, ECO:0000269PubMed:1928092, ECO:0000269PubMed:19472408, ECO:0000269PubMed:8213816, ECO:0000269Ref.22, ECO:0000269Ref.25}. Note=The disease is caused by mutations affecting the gene represented in this entry.GM1-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:0000269PubMed:10737981, ECO:0000269PubMed:12644936, ECO:0000269PubMed:15714521, ECO:0000269PubMed:16941474, ECO:0000269PubMed:17309651, ECO:0000269PubMed:1907800, ECO:0000269PubMed:1909089, ECO:0000269PubMed:19472408, ECO:0000269PubMed:8213816}. Note=The disease is caused by mutations affecting the gene represented in this entry.GM1-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:0000269PubMed:11511921, ECO:0000269PubMed:15986423, ECO:0000269PubMed:16941474, ECO:0000269PubMed:17309651, ECO:0000269PubMed:1907800, ECO:0000269PubMed:1909089, ECO:0000269PubMed:19472408, ECO:0000269PubMed:8198123, ECO:0000269Ref.22, ECO:0000269Ref.24}. Note=The disease is caused by mutations affecting the gene represented in this entry.Mucopolysaccharidosis 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:0000269PubMed:11511921, ECO:0000269PubMed:12393180, ECO:0000269PubMed:16538002, ECO:0000269PubMed:16941474, ECO:0000269PubMed:1928092, ECO:0000269PubMed:19472408, ECO:0000269PubMed:7586649}. Note=The disease is caused by mutations affecting the gene represented in this entry.

Tissue Specificity

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 17 experimentally validated interaction(s) in this database.

Experimentally validated
Total	17 [view]
Protein-Protein	17 [view]
Protein-DNA	0
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Gene Ontology

Molecular Function

Accession	GO Term
GO:0004553	hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565	beta-galactosidase activity
GO:0005515	protein binding

Biological Process

GO:0005975	carbohydrate metabolic process
GO:0006027	glycosaminoglycan catabolic process
GO:0006665	sphingolipid metabolic process
GO:0006687	glycosphingolipid metabolic process
GO:0030203	glycosaminoglycan metabolic process
GO:0042339	keratan sulfate metabolic process
GO:0042340	keratan sulfate catabolic process
GO:0044281	small molecule metabolic process

Cellular Component

GO:0005737	cytoplasm
GO:0005794	Golgi apparatus
GO:0009341	beta-galactosidase complex
GO:0043202	lysosomal lumen
GO:0048471	perinuclear region of cytoplasm
GO:0070062	extracellular vesicular exosome

Protein Structure and Domains

PDB ID

InterPro

IPR001944 Glycoside hydrolase, family 35
IPR008979 Galactose-binding domain-like
IPR013529 Glycoside hydrolase, family 42, N-terminal
IPR017853 Glycoside hydrolase, superfamily

PFAM

PF01301
PF02449

PRINTS

PR00742

PIRSF

SMART

TIGRFAMs

Post-translational Modifications

Modification

Cross-References

SwissProt

P16278