Search results for CTSA

Showing 15 results out of 15

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Protein (7 results from a total of 7)

Identifier: R-HSA-1181230
Species: Homo sapiens
Compartment: lysosomal lumen
Primary external reference: UniProt: CTSA: P10619
Identifier: R-HSA-6799120
Species: Homo sapiens
Compartment: azurophil granule lumen
Primary external reference: UniProt: CTSA: P10619
Identifier: R-HSA-1605642
Species: Homo sapiens
Compartment: lysosomal lumen
Primary external reference: UniProt: CTSA: P10619
Identifier: R-HSA-6799135
Species: Homo sapiens
Compartment: azurophil granule lumen
Primary external reference: UniProt: P10619
Identifier: R-HSA-6806187
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: P10619
Identifier: R-HSA-1605735
Species: Homo sapiens
Compartment: lysosomal lumen
Primary external reference: UniProt: P10619
Identifier: R-HSA-6806233
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: P10619

Complex (4 results from a total of 4)

Identifier: R-HSA-1605630
Species: Homo sapiens
Compartment: lysosomal lumen
Identifier: R-HSA-9638117
Species: Homo sapiens
Compartment: lysosomal lumen
Identifier: R-HSA-1605684
Species: Homo sapiens
Compartment: lysosomal lumen
Identifier: R-HSA-4088186
Species: Homo sapiens
Compartment: lysosomal lumen

Reaction (4 results from a total of 4)

Identifier: R-HSA-1605724
Species: Homo sapiens
Compartment: lysosomal lumen
Sialidases (NEU, neuraminidases) hydrolyze sialic acids (N-acetylneuramic acid, Neu5Ac, NANA) to produce asialo compounds, a step in the degradation process of glycoproteins and gangliosides. NEU1 and NEU4 hydrolyse NANA in the lysosomal lumen. NEU1 is active in a multienzyme complex comprising cathepsin A protective protein (CTSA) and beta-galactosidase (Bonten et al. 1996, Rudenko et al. 1995). Defects in NEU1 are the cause of Sialidosis (MIM:256550) (Bonten et al. 1996). CTSA is thought to exert a protective function necessary for stability and activity of these enzymes (Galjart et al. 1988). Defects in CTSA are the cause of galactosialidosis (GSL, MIM:256540) (Zhou et al. 1991). NEU4 is also a lysosomal sialidase which, unlike NEU1, doesn't require association with other proteins for enzymatic activity. Isoform 2 is thought to be the lysosomal sialidase (Seyrantepe et al. 2004).
Identifier: R-HSA-4084999
Species: Homo sapiens
Compartment: lysosomal lumen
Sialidases 1-4 (NEU1-4, neuraminidases, receptor-destroying enzymes, RDEs) hydrolyse sialic acids (N-acetylneuraminic acid, Neu5Ac) to produce asialo compounds, a step in the degradation process of glycoproteins and gangliosides and are expressed in a variety of cellular locations. NEU4 is an extrinsic membrane protein associated with lysosomes, mitochondria and endoplasmic reticulum. It has broad sialidase activity against glycoconjugates with alpha2,3-, alpha2,6- or alpha2,8-linkages (Bigi et al. 2010, Monti et al. 2004, Seyrantepe et al. 2004). NEU1 (lysosomal sialidase) hydrolyses Neu5Ac from glycoconjugates with alpha2,3-, alpha2,6- or alpha2,8-linked terminal sialated residues in the lysosomal lumen. NEU1 is active in a multienzyme complex comprising cathepsin A protective protein (CTSA) and beta-galactosidase (Bonten et al. 1996, Rudenko et al. 1995). Defects in NEU1 cause Sialidosis (MIM:256550), a lysosomal storage disorder manifesting as type I (late-onset) or type II (earlier-onset) (Bonten et al. 1996). CTSA is thought to exert a protective function necessary for stability and activity of these enzymes (Galjart et al. 1988). Defects in CTSA are the cause of galactosialidosis (GSL; MIM:256540) (Zhou et al. 1991).
Identifier: R-HSA-9638120
Species: Homo sapiens
Compartment: lysosomal lumen
Sialidases 1-4 (NEU1-4, neuraminidases, receptor-destroying enzymes, RDEs) hydrolyse sialic acids (N-acetylneuraminic acid, Neu5Ac) to produce asialo compounds, a step in the degradation process of glycoproteins and gangliosides and are expressed in a variety of cellular locations. NEU4 is an extrinsic membrane protein associated with lysosomes, mitochondria and endoplasmic reticulum. It has broad sialidase activity against glycoconjugates with alpha2,3-, alpha2,6- or alpha2,8-linkages (Bigi et al. 2010, Monti et al. 2004, Seyrantepe et al. 2004). NEU1 (lysosomal sialidase) hydrolyses Neu5Ac from glycoconjugates with alpha2,3-, alpha2,6- or alpha2,8-linked terminal sialated residues in the lysosomal lumen. NEU1 is active in a multienzyme complex comprising cathepsin A protective protein (CTSA) and beta-galactosidase (Bonten et al. 1996, Rudenko et al. 1995). Defects in NEU1 cause Sialidosis (MIM:256550), a lysosomal storage disorder manifesting as type I (late-onset) or type II (earlier-onset) (Bonten et al. 1996). CTSA is thought to exert a protective function necessary for stability and activity of these enzymes (Galjart et al. 1988). Defects in CTSA are the cause of galactosialidosis (GSL; MIM:256540) (Zhou et al. 1991).
Identifier: R-HSA-4341669
Species: Homo sapiens
Compartment: lysosomal lumen
NEU1 Sialidase 1 (NEU1, neuraminidase, receptor-destroying enzyme, RDE) normally hydrolyses N-acetylneuraminic acid (Neu5Ac) from glycoconjugates with alpha2,3-, alpha2,6- or alpha2,8-linked terminal sialated residues in the lysosomal lumen, a step in the degradation process of glycoproteins and gangliosides. NEU1 is active in a multienzyme complex comprising cathepsin A protective protein (CTSA) and beta-galactosidase (Bonten et al. 1996, Rudenko et al. 1995). Defects in NEU1 cause Sialidosis (MIM:256550), a lysosomal storage disorder manifesting as type I (late-onset) or type II (earlier-onset) (Bonten et al. 1996). Generally, patients with the more severe type II disease have catalytically inactive enzymes whereas patients with the milder type I disease have some residual activity. Mutations causing the severest type II disease include E377*, L303P, W29*, R225P and W23* (Bonten et al. 1996, Pshezhetsky et al. 1997, Sergi et al. 2001, Pattison et al. 2004).
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