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Protein Page:
GBA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Hydrolase; Lipid Metabolism - sphingolipid; Glycan Metabolism - other glycan degradation; EC 3.2.1.45
Chromosomal Location of Human Ortholog: 1q21
Cellular Component: lysosomal lumen; lysosomal membrane
Molecular Function: glucosylceramidase activity; protein binding; receptor binding
Biological Process: carbohydrate metabolic process; cellular response to starvation; ceramide biosynthetic process; glucosylceramide catabolic process; glycosphingolipid metabolic process; negative regulation of inflammatory response; negative regulation of interleukin-6 production; negative regulation of MAP kinase activity; positive regulation of macroautophagy; positive regulation of protein amino acid dephosphorylation; regulation of macroautophagy; regulation of proteasomal ubiquitin-dependent protein catabolic process; regulation of water loss via skin; response to estrogen stimulus; response to glucocorticoid stimulus; response to pH; response to testosterone stimulus; skin morphogenesis; sphingosine biosynthetic process
Disease: Dementia, Lewy Body; Gaucher Disease, Perinatal Lethal; Gaucher Disease, Type I; Gaucher Disease, Type Ii; Gaucher Disease, Type Iii; Gaucher Disease, Type Iiic; Parkinson Disease, Late-onset
Reference #:  P04062 (UniProtKB)
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 Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 S136‑p ALNILALsPPAQNLL
0 1 K233‑ub TNGAVNGkGSLKGQP
0 1 Y244‑p KGQPGDIyHQTWARY
0 1 T311 GPTLANSTHHNVRLL
0 1 T336‑p HWAKVVLtDPEAAKY
0 1 S405‑p RGMQYSHsIITNLLy
0 1 Y412‑p sIITNLLyHVVGWTD
0 1 Y451 DITKDTFYKQPMFYH
0 1 K512‑ub KDVPLTIkDPAVGFL
0 1 S523‑p VGFLETIsPGYSIHT
  mouse

 
S116 ALNILALSPPTQKLL
K213 TNGRVNGKGSLKGQP
F224 KGQPGDIFHQTWANY
S291‑p GPALANSsHDVKLLM
S315 RWAEVVLSDPEAAKY
S384 RGMQYSHSIITNLLY
Y391 SIITNLLYHVTGWTD
Y430‑p DIPKDAFyKQPMFYH
S491 EDVPLTISDPDLGFL
S502 LGFLETVSPGYSIHT
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