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Protein Page:
GBA (human)

Overview
GBA Defects in GBA are the cause of Gaucher disease (GD); also known as glucocerebrosidase deficiency. GD is the most prevalent lysosomal storage disease, 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. Defects in GBA are the cause of Gaucher disease type 1 (GD1); also known as adult non-neuronopathic Gaucher disease. GD1 is characterized by hepatosplenomegaly with consequent anemia and thrombopenia, and bone involvement. The central nervous system is not involved. Defects in GBA are the cause of Gaucher disease type 2 (GD2); also known as acute neuronopathic Gaucher disease. GD2 is the most severe form and is universally progressive and fatal. It manifests soon after birth, with death generally occurring before patients reach two years of age. Defects in GBA are the cause of Gaucher disease type 3 (GD3); also known as subacute neuronopathic Gaucher disease. GD3 has central nervous manifestations. Defects in GBA are the cause of Gaucher disease type 3C (GD3C); also known as pseudo-Gaucher disease or Gaucher-like disease. Defects in GBA are the cause of Gaucher disease perinatal lethal (GDPL). It is a 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. 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. Defects in GBA contribute to susceptibility to Parkinson disease (PARK). 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. Belongs to the glycosyl hydrolase 30 family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Lipid Metabolism - sphingolipid; EC 3.2.1.45; Glycan Metabolism - other glycan degradation; Hydrolase
Cellular Component: lysosomal lumen; lysosomal membrane
Molecular Function: protein binding; glucosylceramidase activity; receptor binding
Biological Process: regulation of water loss via skin; glucosylceramide catabolic process; cell death; negative regulation of MAP kinase activity; sphingolipid metabolic process; skin morphogenesis; response to estrogen stimulus; negative regulation of inflammatory response; carbohydrate metabolic process; response to glucocorticoid stimulus; negative regulation of interleukin-6 production; sphingosine biosynthetic process; ceramide biosynthetic process; glycosphingolipid metabolic process; response to testosterone stimulus; positive regulation of protein amino acid dephosphorylation; response to pH
Reference #:  P04062 (UniProtKB)
Alt. Names/Synonyms: Acid beta-glucosidase; Alglucerase; Beta-glucocerebrosidase; D-glucosyl-N-acylsphingosine glucohydrolase; GBA; GBA1; GC; GCB; GLCM; GLUC; glucosidase, beta, acid; Glucosylceramidase; Imiglucerase; lysosomal glucocerebrosidase
Gene Symbols: GBA
Molecular weight: 59,716 Da
Basal Isoelectric point: 7.29  Predict pI for various phosphorylation states
Select Structure to View Below

GBA

Protein Structure Not Found.


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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T311 GPTLANSTHHNVRLL
0 2 Y451-p DITKDTFyKQPMFYH
  mouse

 
S291-p GPALANSsHDVKLLM
Y430-p DIPKDAFyKQPMFYH
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