Target Name: GBA2
NCBI ID: G57704
Other Name(s): Non-lysosomal glucosylceramidase (isoform 1) | Cholesterol glucosyltransferase GBA2 | Glucosylceramidase 2 | SPG46 | AD035 | non-lysosomal galactosylceramidase | cholesterol glucosyltransferase GBA2 | bile acid beta-glucosidase GBA2 | Non-lysosomal glycosylceramidase | Bile acid beta-glucosidase GBA2 | glucosylceramidase 2 | Beta-glucocerebrosidase 2 | glucosylceramidase beta 2 | Non-lysosomal glucosylceramidase | GBA2 variant 1 | NLGase | glucosidase, beta (bile acid) 2 | Bile acid glucosyl transferase GBA2 | KIAA1605 | Non-lysosomal cholesterol glycosyltransferase | beta-glucocerebrosidase 2 | Non-lysosomal galactosylceramidase | glucocerebrosidase 2 | Glucosylceramidase beta 2, transcript variant 1 | non-lysosomal glycosylceramidase | bile acid glucosyl transferase GBA2 | MGC16895 | Bile acid beta-glucosidase | cholesteryl-beta-glucosidase GBA2 | Cholesteryl-beta-glucosidase GBA2 | Glucosidase, beta, acid 2 (GBA2, bile acid) | DKFZp762K054 | Beta-glucosidase 2 | non-lysosomal cholesterol glycosyltransferase | GBA2_HUMAN

GBA2: A Potential Drug Target and Biomarker for Non-Lysosomal Glucosylceramidase (ISOFORM 1)

Glucosylceramidase (ISOFORM 1) is a hydrolase that removes the N-acetylglucosamine (NAG) from the glucosyl group of a glycyl group in a specific order. It is a key enzyme in the glycosylation pathway, which is a critical post-translational modification that modifies Chemical properties and biological activities of the galactose residues. NAG is a key modification that enables the efficient interaction of various cellular signaling pathways, including the TGF-β pathway.

GBA2, the non-lysosomal glucosylceramidase (ISOFORM 1), is a key enzyme in the glycosylation pathway that is responsible for the removal of NAG from the glucosyl group of N-acetylglucosamine (NAG). GBA2 is a 26 kDa protein that is expressed in various tissues, including liver, spleen, and muscle. It is primarily localized to the endoplasmic reticulum (ER) and is considered as a protein of interest (PoI) due to its unique function in the glycosylation pathway.

GBA2 functions as a critical enzyme in the glycosylation pathway by removing NAG from the glucosyl group of N-acetylglucosamine (NAG). The NAG is a key modification that enables the efficient interaction of various cellular signaling pathways, including the TGF-β pathway. The TGF-β pathway is a well-established signaling pathway that plays a crucial role in cellular growth, development, and regulation of various physiological processes. The NAG is the key modification that enables the TGF-β pathway to function properly.

GBA2 is a PoI due to its unique function in the glycosylation pathway. It is a potential drug target and biomarker that can be targeted by small molecules or antibodies to inhibit its function. The inhibition of GBA2 function has been shown to have therapeutic potential in various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

GBA2 has also been shown to be a potential biomarker for several diseases, including cancer. GBA2 is expressed in various tissues and has been shown to be involved in the development and progression of several types of cancer, including breast, ovarian, and prostate cancer. GBA2 has also been shown to be a potential target for cancer therapies that target the TGF-β pathway, including inhibitors of the TGF-β receptor.

In addition to its potential therapeutic and biomarker applications, GBA2 is also of interest due to its unique structure and function. GBA2 is a 26 kDa protein that consists of a single gene with four exons. It has a unique 26 kDa protein domain that is located at its N-terminus. The 26 kDa protein domain is responsible for the catalytic activity of GBA2 and is the only region of the protein that is known to function in the glycosylation pathway.

GBA2 is also of interest due to its unique distribution in various tissues. GBA2 is primarily localized to the endoplasmic reticulum (ER) and is also found in the cytoplasm of various cells. This unique distribution suggests that GBA2 may have a unique function in the cell signaling pathways and may be involved in the regulation of various cellular processes.

In conclusion, GBA2 is a non-lysosomal glucosylceramidase (ISOFORM 1) that is responsible for the removal of N-acetylglucosamine (NAG) from the glucosyl group of N-acetylglucosamine (NAG). GBA2 is a

Protein Name: Glucosylceramidase Beta 2

Functions: Non-lysosomal glucosylceramidase that catalyzes the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) to free glucose and ceramides (such as N-acylsphing-4-enine) (PubMed:17105727, PubMed:30308956, PubMed:32144204). GlcCers are membrane glycosphingolipids that have a wide intracellular distribution (By similarity). They are the main precursors of more complex glycosphingolipids that play a role in cellular growth, differentiation, adhesion, signaling, cytoskeletal dynamics and membrane properties (By similarity). Involved in the transglucosylation of cholesterol, transfers glucose from GlcCer to cholesterol, thereby modifying its water solubility and biological properties (PubMed:32144204). Under specific conditions, may catalyze the reverse reaction, transferring glucose from cholesteryl-3-beta-D-glucoside to ceramide (such as N-acylsphing-4-enine) (Probable). May play a role in the metabolism of bile acids (PubMed:11489889, PubMed:9111029, PubMed:17080196). Able to hydrolyze bile acid 3-O-glucosides as well as to produce bile acid-glucose conjugates thanks to a bile acid glucosyl transferase activity (PubMed:11489889, PubMed:9111029, PubMed:17080196). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the galactosyl transfer between GalCers and cholesterol in vitro with lower activity compared with their activity against GlcCers (PubMed:32144204)

More Common Targets

GBA3 | GBAP1 | GBE1 | GBF1 | GBGT1 | GBP1 | GBP1P1 | GBP2 | GBP3 | GBP4 | GBP5 | GBP6 | GBP7 | GBX1 | GBX2 | GC | GCA | GCAT | GCC1 | GCC2 | GCC2-AS1 | GCDH | GCFC2 | GCG | GCGR | GCH1 | GCHFR | GCK | GCKR | GCLC | GCLM | GCM1 | GCM2 | GCN1 | GCNA | GCNT1 | GCNT1P3 | GCNT2 | GCNT3 | GCNT4 | GCNT7 | GCOM1 | GCSAM | GCSAML | GCSAML-AS1 | GCSH | GCSHP3 | GCSIR | GDA | GDAP1 | GDAP1L1 | GDAP2 | GDE1 | GDF1 | GDF10 | GDF11 | GDF15 | GDF2 | GDF3 | GDF5 | GDF6 | GDF7 | GDF9 | GDI1 | GDI2 | GDI2P1 | GDNF | GDNF Family Receptor alpha | GDNF-AS1 | GDPD1 | GDPD2 | GDPD3 | GDPD4 | GDPD5 | GDPGP1 | GEM | GEMIN2 | GEMIN4 | GEMIN5 | GEMIN6 | GEMIN7 | GEMIN8 | GEMIN8P1 | GEMIN8P4 | GEN1 | general transcription factor IIF (TFIIF) | General transcription factor IIH | Geranylgeranyl transferase | Geranylgeranyl transferase type-1 | GET1 | GET3 | GET4 | GFAP | GFER | GFI1 | GFI1B | GFM1 | GFM2 | GFOD1 | GFOD2