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2-aminobenzoyl-Ala-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ala-Arg + 4-nitrophenylalanine
kcat/Km is 20/mM * s
-
-
?
2-aminobenzoyl-Arg-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Arg-Arg + 4-nitrophenylalanine
kcat/Km is 5.2/mM * s
-
-
?
2-aminobenzoyl-Asn-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Asn-Arg + 4-nitrophenylalanine
kcat/Km is 17/mM * s
-
-
?
2-aminobenzoyl-Asp-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Asp-Arg + 4-nitrophenylalanine
kcat/Km is 16/mM * s
-
-
?
2-aminobenzoyl-Cys-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Cys-Arg + 4-nitrophenylalanine
kcat/Km is 11/mM * s
-
-
?
2-aminobenzoyl-Gln-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Gln-Arg + 4-nitrophenylalanine
kcat/Km is 43/mM * s
-
-
?
2-aminobenzoyl-Glu-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Glu-Arg + 4-nitrophenylalanine
kcat/Km is 27/mM * s
-
-
?
2-aminobenzoyl-Gly-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Gly-Arg + 4-nitrophenylalanine
kcat/Km is 4.4/mM * s
-
-
?
2-aminobenzoyl-His-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-His-Arg + 4-nitrophenylalanine
kcat/Km is 4.7/mM * s
-
-
?
2-aminobenzoyl-Ile-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ile-Arg + 4-nitrophenylalanine
kcat/Km is 2.7/mM * s
-
-
?
2-aminobenzoyl-Leu-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Leu-Arg + 4-nitrophenylalanine
kcat/Km is 153/mM * s
-
-
?
2-aminobenzoyl-Lys-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Lys-Arg + 4-nitrophenylalanine
kcat/Km is 5.7/mM * s
-
-
?
2-aminobenzoyl-Met-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Met-Arg + 4-nitrophenylalanine
kcat/Km is 28/mM * s
-
-
?
2-aminobenzoyl-Phe-Ala-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ala + 4-nitrophenylalanine
kcat/Km is 51/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Arg + 4-nitrophenylalanine
kcat/Km is 100/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ala + H2O
2-aminobenzoyl-Phe-Arg + Ala
kcat/Km is 10/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Arg + H2O
2-aminobenzoyl-Phe-Arg + Arg
kcat/Km is 1.7/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Asn + H2O
2-aminobenzoyl-Phe-Arg + Asn
kcat/Km is 5.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Asp + H2O
2-aminobenzoyl-Phe-Arg + Asp
kcat/Km is 8.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Cys + H2O
2-aminobenzoyl-Phe-Arg + Cys
kcat/Km is 73/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Gln + H2O
2-aminobenzoyl-Phe-Arg + Gln
kcat/Km is 4.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Glu + H2O
2-aminobenzoyl-Phe-Arg + Glu
kcat/Km is 7.7/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Gly + H2O
2-aminobenzoyl-Phe-Arg + Gly
kcat/Km is 14/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-His + H2O
2-aminobenzoyl-Phe-Arg + His
kcat/Km is 5.4/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ile + H2O
2-aminobenzoyl-Phe-Arg + Ile
kcat/Km is 3.4/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Leu + H2O
2-aminobenzoyl-Phe-Arg + Leu
kcat/Km is 7.1/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Lys + H2O
2-aminobenzoyl-Phe-Arg + Lys
kcat/Km is 5.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Met + H2O
2-aminobenzoyl-Phe-Arg + Met
kcat/Km is 9.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Phe + H2O
2-aminobenzoyl-Phe-Arg + Phe
kcat/Km is 15/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Ser + H2O
2-aminobenzoyl-Phe-Arg + Ser
kcat/Km is 48/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Thr + H2O
2-aminobenzoyl-Phe-Arg + Thr
kcat/Km is 5.8/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Trp + H2O
2-aminobenzoyl-Phe-Arg + Trp
kcat/Km is 8.6/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Tyr + H2O
2-aminobenzoyl-Phe-Arg + Tyr
kcat/Km is 8.8/mM * s
-
-
?
2-aminobenzoyl-Phe-Arg-Val + H2O
2-aminobenzoyl-Phe-Arg + Val
kcat/Km is 5.9/mM * s
-
-
?
2-aminobenzoyl-Phe-Asn-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asn + 4-nitrophenylalanine
kcat/Km is 13/mM * s
-
-
?
2-aminobenzoyl-Phe-Asp-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Asp + 4-nitrophenylalanine
kcat/Km is 12/mM * s
-
-
?
2-aminobenzoyl-Phe-Cys-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Cys + 4-nitrophenylalanine
kcat/Km is 17/mM * s
-
-
?
2-aminobenzoyl-Phe-Gln-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Gln + 4-nitrophenylalanine
kcat/Km is 73/mM * s
-
-
?
2-aminobenzoyl-Phe-Glu-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Glu + 4-nitrophenylalanine
kcat/Km is 62/mM * s
-
-
?
2-aminobenzoyl-Phe-Gly-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Gly + 4-nitrophenylalanine
kcat/Km is 45/mM * s
-
-
?
2-aminobenzoyl-Phe-His-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-His + 4-nitrophenylalanine
kcat/Km is 3.5/mM * s
-
-
?
2-aminobenzoyl-Phe-Ile-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ile + 4-nitrophenylalanine
kcat/Km is 4.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Leu-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Leu + 4-nitrophenylalanine
kcat/Km is 2.0/mM * s
-
-
?
2-aminobenzoyl-Phe-Lys-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Lys + 4-nitrophenylalanine
kcat/Km is 79/mM * s
-
-
?
2-aminobenzoyl-Phe-Met-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Met + 4-nitrophenylalanine
kcat/Km is 181/mM * s
-
-
?
2-aminobenzoyl-Phe-Phe-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Phe + 4-nitrophenylalanine
kcat/Km is 108/mM * s
-
-
?
2-aminobenzoyl-Phe-Ser-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Ser + 4-nitrophenylalanine
kcat/Km is 32/mM * s
-
-
?
2-aminobenzoyl-Phe-Thr-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Thr + 4-nitrophenylalanine
kcat/Km is 68/mM * s
-
-
?
2-aminobenzoyl-Phe-Trp-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Trp + 4-nitrophenylalanine
kcat/Km is 1.3/mM * s
-
-
?
2-aminobenzoyl-Phe-Tyr-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Tyr + 4-nitrophenylalanine
kcat/Km is 58/mM * s
-
-
?
2-aminobenzoyl-Phe-Val-4-nitrophenylalanine + H2O
2-aminobenzoyl-Phe-Val + 4-nitrophenylalanine
kcat/Km is 4.8/mM * s
-
-
?
2-aminobenzoyl-Pro-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Pro-Arg + 4-nitrophenylalanine
kcat/Km is 0.2/mM * s
-
-
?
2-aminobenzoyl-Ser-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Ser-Arg + 4-nitrophenylalanine
kcat/Km is 8.2/mM * s
-
-
?
2-aminobenzoyl-Thr-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Thr-Arg + 4-nitrophenylalanine
kcat/Km is 8.7/mM * s
-
-
?
2-aminobenzoyl-Trp-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Trp-Arg + 4-nitrophenylalanine
kcat/Km is 12/mM * s
-
-
?
2-aminobenzoyl-Tyr-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Tyr-Arg + 4-nitrophenylalanine
kcat/Km is 400/mM * s
-
-
?
2-aminobenzoyl-Val-Arg-4-nitrophenylalanine + H2O
2-aminobenzoyl-Val-Arg + 4-nitrophenylalanine
kcat/Km is 31/mM * s
-
-
?
7-methoxycoumarin-4-ylacetyl-RPPGFSAFK-N-epsilon-2,4-dinitrophenol + H2O
?
fluorescence cathepsin X/A-selective substrate
-
-
?
profilin + H2O
L-tyrosine + ?
cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
profilin 1 + H2O
?
the molecular target of cathepsin X in tumor cells is profilin 1, a known tumor suppressor and regulator of actin cytoskeleton dynamics. Cathepsin X cleaves off the C-terminal Tyr139 of profilin 1, affecting binding of poly-L-proline ligands and, consequently, tumor cell migration and invasion. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
(2,4-dinitrophenyl)-GFFGW + H2O
(2,4-dinitrophenyl)-GFFG + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFFRW + H2O
(2,4-dinitrophenyl)-GFFR + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFFW + H2O
(2,4-dinitrophenyl)-GFF + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFRFW + H2O
(2,4-dinitrophenyl)-GFR + L-Phe-L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GFRW + H2O
(2,4-dinitrophenyl)-GFR + L-Trp
-
-
-
?
(2,4-dinitrophenyl)-GRFFW + H2O
(2,4-dinitrophenyl)-GRFF + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFF + H2O
(2-aminobenzoyl)-FF + L-Phe
-
-
-
?
(2-aminobenzoyl)-FFFA + H2O
(2-aminobenzoyl)-FFF + L-Ala
-
-
-
?
(2-aminobenzoyl)-FFFP + H2O
(2-aminobenzoyl)-FFF + Pro
-
-
-
?
(2-aminobenzoyl)-FFFR + H2O
(2-aminobenzoyl)-FFF + L-Arg
-
-
-
?
(2-aminobenzoyl)-FFFR-NH2 + H2O
(2-aminobenzoyl)-FFF + Arg-amide
-
-
-
?
(2-aminobenzoyl)-FFFW + H2O
(2-aminobenzoyl)-FFF + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFGW + H2O
(2-aminobenzoyl)-FFG + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFRW + H2O
(2-aminobenzoyl)-FFR + L-Trp
-
-
-
?
(2-aminobenzoyl)-FFRW-NH2 + H2O
(2-aminobenzoyl)-FFR + L-Trp-amide
-
-
-
?
(2-aminobenzoyl)-FRFW-NH2 + H2O
(2-aminobenzoyl)-FR + Phe-Trp-amide
-
-
-
?
2-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
2-aminobenzoyl-Leu-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
2-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
3-aminobenzoyl-FR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-FR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
-
-
-
?
3-aminobenzoyl-LR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-LR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
-
-
-
?
3-aminobenzoyl-RR-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P + H2O
3-aminobenzoyl-RR + (2,3-diaminopropionyl)-(2,4-dinitrophenyl)-P
-
-
-
?
Abz-Phe-Glu-Lys(Dnp)-OH + H2O
?
-
-
-
-
?
AKYNQLMRIEEELGEEARFAGHNFRNPSVL + H2O
?
-
a model peptide derived from rat gamma-enolase carboxyl terminal, overview
-
-
?
benzyloxycarbonyl-FR-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-FR + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-RR-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-RR + 7-amino-4-methylcoumarin
-
-
-
?
bradykinin + H2O
?
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, a mainly B2 receptor
an exclusive B1 receptor
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
hippuryl-L-glutamic acid + H2O
hippuric acid + L-Glu
-
-
-
-
?
KAKFAGRNPRNPLAK + H2O
?
-
a model peptide derived from human alpha-enolase carboxyl terminal, overview
-
-
?
kallidin + H2O
?
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
kallidin + H2O
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
i.e. Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, a mainly B2 receptor
an exclusive B1 receptor
-
?
lymphocyte function associated antigen-1 + H2O
?
ortho-aminobenzoyl-Arg-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
ortho-aminobenzoyl-Lys-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
ortho-aminobenzoyl-Phe-Arg-(2,3-diaminopropionyl)-(2,4-dinitrophenyl)-Pro + H2O
?
-
-
-
-
?
additional information
?
-
CXCL-12 + H2O
?
CXCL-12 is a physiological substrate for secreted cathepsin X
-
-
?
CXCL-12 + H2O
?
chemokine CXCL-12 is a highly potent chemoattractant for HSC secreted by osteoblasts. The exo-peptidase cathepsin X gradually cleaves fifteen amino acids until proline P74 is present at the P2 position
-
-
?
alpha-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
alpha-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide
-
-
?
gamma-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
gamma-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide
-
-
?
lymphocyte function associated antigen-1 + H2O
?
-
cathepsin X cleaves the beta2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and alpha-actinin-1 binding. Cleavage by cathepsin X of the amino acid residues S769, E768 and A767 from the C-terminal of the b2 cytoplasmic tail of LFA-1 promotes binding of the actin-binding protein a-actinin-1
-
-
?
lymphocyte function associated antigen-1 + H2O
?
-
cathepsin X cleaves the amino acid residues S769, E768 and A767 from the C-terminal of LFA-1
-
-
?
additional information
?
-
cathepsin X binds to the membrane lectin endoplasmic reticulum Golgi intermediate compartment protein-53, ERGIC-53, involving the soluble luminal interaction partner multiple coagulation factor deficiency protein 2, MCFD2, which form a cargo receptor complex in the early secretory pathway, but is dispensable for enzyme binding, overview
-
-
?
additional information
?
-
luminal protein-protein interactions between components of the cargo system in the endoplasmic reticulum for secretion of cargo proteins, e.g. cathepsin C or cathepsin Z, involve the cargo transport receptor ERGIC-53, i.e. endoplasmic reticulum-Golgi intermediate compartment protein of 53 kDa, with its luminal interaction partner MCFD2, i.e. multiple coagulation factor deficiency protein 2, MCFD2 is not required for the binding of cathepsin Z and cathepsin C to ERGIC-53 in vivo, overview
-
-
?
additional information
?
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
cathepsin X interacts with the membrane lectin endoplasmic reticulum Golgi intermediate compartment protein-53, ERGIC-53
-
-
?
additional information
?
-
direct interaction between the enzyme and integrin alphavbeta3, overview
-
-
?
additional information
?
-
-
direct interaction between the enzyme and integrin alphavbeta3, overview
-
-
?
additional information
?
-
luminal protein-protein interactions between components of the cargo system in the endoplasmic reticulum for secretion of cargo proteins, e.g. cathepsin C or cathepsin Z, involve the cargo transport receptor ERGIC-53, i.e. endoplasmic reticulum-Golgi intermediate compartment protein of 53 kDa, with its luminal interaction partner MCFD2, i.e. multiple coagulation factor deficiency protein 2, inactivation of ERGIC-53s lectin domain by the N156A point mutation selectively decreases the interaction of ERGIC-53 with its cargo proteins cathepsin Z and cathepsin C, whereas the N156A mutation does not affect ERGIC-53 oligomerization or its interaction with MCFD2, overview
-
-
?
additional information
?
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
cathepsin X is an important regulator of LFA-1 activity, and cathepsin X-upregulated Jurkat T cells exhibit increased homotypic aggregation, cathepsin X induces polarized migration-associated morphology in Jurkat T cells, overview
-
-
?
additional information
?
-
-
the enzyme normally acts as a carboxymonopeptidase. The preference for Arg in the P1 position is so strong that cathepsin X cleaves substrates with Arg in antepenultimate position, acting also as a carboxypeptidase. A large hydrophobic residue such as Trp is preferred in the P1' position, although the enzyme cleaves all P1' residues investigated (Trp, Phe, Ala, Arg, Pro). The enzyme also cleaves the substrates with amide-blocked C-terminal carboxyl group with rates similar to that of the unblocked substrates
-
?
additional information
?
-
-
active cathepsin X mediates the function of beta2 integrin receptors during cell adhesion. It could also be involved in other processes associated with beta2 integrin receptors such as phagocytosis and T cell activation
-
-
?
additional information
?
-
-
cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer
-
-
?
additional information
?
-
-
cathespin X is involved in phagocytosis and regulation of immune response, not involved in degradation of extracellular matrix, a proteolytic event leading to tumor cell invasion and metastasis
-
-
?
additional information
?
-
-
the enzyme is associated with plaques in Alzheimer patients, overview
-
-
?
additional information
?
-
-
the enzyme stimulates macrophage antigen-1 receptor-dependent adhesion and phagocytosis via interaction with integrin beta2 subunit. It plays a role in regulating lymphocyte proliferation via Mac-1 and the other b2 integrin receptor, lymphocyte function-associated antigen-1. Cathepsin X has been shown to suppress proliferation of peripheral blood mononuclear cells, by activation of Mac-1, known as a suppressive factor for lymphocyte proliferation, co-localization of cathepsin X and LFA-1 enhances lymphocyte proliferation, overview
-
-
?
additional information
?
-
-
co-localization of alpha or gamma enolase and cathepsin X. Cathepsin X impairs survival and neuritogenesis of neuronal cells, e.g. it reduces PC12 cell survival and neuritogenesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CXCL-12 + H2O
?
CXCL-12 is a physiological substrate for secreted cathepsin X
-
-
?
profilin + H2O
L-tyrosine + ?
cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
profilin 1 + H2O
?
the molecular target of cathepsin X in tumor cells is profilin 1, a known tumor suppressor and regulator of actin cytoskeleton dynamics. Cathepsin X cleaves off the C-terminal Tyr139 of profilin 1, affecting binding of poly-L-proline ligands and, consequently, tumor cell migration and invasion. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis
-
-
?
alpha-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
-
-
?
bradykinin + H2O
?
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
gamma-enolase + H2O
?
-
cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
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-
?
kallidin + H2O
?
-
the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
-
-
?
lymphocyte function associated antigen-1 + H2O
?
-
cathepsin X cleaves the beta2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and alpha-actinin-1 binding. Cleavage by cathepsin X of the amino acid residues S769, E768 and A767 from the C-terminal of the b2 cytoplasmic tail of LFA-1 promotes binding of the actin-binding protein a-actinin-1
-
-
?
additional information
?
-
additional information
?
-
cathepsin X binds to the membrane lectin endoplasmic reticulum Golgi intermediate compartment protein-53, ERGIC-53, involving the soluble luminal interaction partner multiple coagulation factor deficiency protein 2, MCFD2, which form a cargo receptor complex in the early secretory pathway, but is dispensable for enzyme binding, overview
-
-
?
additional information
?
-
luminal protein-protein interactions between components of the cargo system in the endoplasmic reticulum for secretion of cargo proteins, e.g. cathepsin C or cathepsin Z, involve the cargo transport receptor ERGIC-53, i.e. endoplasmic reticulum-Golgi intermediate compartment protein of 53 kDa, with its luminal interaction partner MCFD2, i.e. multiple coagulation factor deficiency protein 2, MCFD2 is not required for the binding of cathepsin Z and cathepsin C to ERGIC-53 in vivo, overview
-
-
?
additional information
?
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
-
procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
-
-
?
additional information
?
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
-
the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
-
-
?
additional information
?
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
-
cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
-
-
?
additional information
?
-
cathepsin X is an important regulator of LFA-1 activity, and cathepsin X-upregulated Jurkat T cells exhibit increased homotypic aggregation, cathepsin X induces polarized migration-associated morphology in Jurkat T cells, overview
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-
?
additional information
?
-
-
active cathepsin X mediates the function of beta2 integrin receptors during cell adhesion. It could also be involved in other processes associated with beta2 integrin receptors such as phagocytosis and T cell activation
-
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?
additional information
?
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-
cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer
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-
?
additional information
?
-
-
cathespin X is involved in phagocytosis and regulation of immune response, not involved in degradation of extracellular matrix, a proteolytic event leading to tumor cell invasion and metastasis
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-
?
additional information
?
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-
the enzyme is associated with plaques in Alzheimer patients, overview
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?
additional information
?
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-
the enzyme stimulates macrophage antigen-1 receptor-dependent adhesion and phagocytosis via interaction with integrin beta2 subunit. It plays a role in regulating lymphocyte proliferation via Mac-1 and the other b2 integrin receptor, lymphocyte function-associated antigen-1. Cathepsin X has been shown to suppress proliferation of peripheral blood mononuclear cells, by activation of Mac-1, known as a suppressive factor for lymphocyte proliferation, co-localization of cathepsin X and LFA-1 enhances lymphocyte proliferation, overview
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?
additional information
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co-localization of alpha or gamma enolase and cathepsin X. Cathepsin X impairs survival and neuritogenesis of neuronal cells, e.g. it reduces PC12 cell survival and neuritogenesis
-
-
?
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Acquired Immunodeficiency Syndrome
The function of cathepsins B, D, and X in atherosclerosis.
Adenocarcinoma
Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia.
Alagille Syndrome
Increased expression and altered localization of cathepsin Z are associated with progression to jaundice stage in primary biliary cholangitis.
Alzheimer Disease
Diverse Protein Profiles in CNS Myeloid Cells and CNS Tissue From Lipopolysaccharide- and Vehicle-Injected APPSWE/PS1?E9 Transgenic Mice Implicate Cathepsin Z in Alzheimer's Disease.
Alzheimer Disease
Neuroprotective role of ?-enolase in microglia in a mouse model of Alzheimer's disease is regulated by cathepsin X.
Bone Diseases, Metabolic
Cathepsin Z as a novel potential biomarker for osteoporosis.
Breast Neoplasms
Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice.
Carcinogenesis
Cathepsin proteases promote angiogenic sprouting and laser-induced choroidal neovascularisation in mice.
Carcinogenesis
IGF-I receptor phosphorylation is impaired in cathepsin X-deficient prostate cancer cells.
Carcinogenesis
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer.
Carcinogenesis
Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia.
Carcinoma
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer.
Carcinoma
Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia.
Carcinoma, Hepatocellular
Overexpression of cathepsin Z contributes to tumor metastasis by inducing epithelial-mesenchymal transition in hepatocellular carcinoma.
Cardiovascular Diseases
Deciphering the Plasma Proteome of Type 2 Diabetes.
cathepsin x deficiency
Acid carboxypeptidase deficiency in galactosialidosis.
cathepsin x deficiency
Cellular senescence induced by cathepsin X downregulation.
cathepsin x deficiency
IGF-I receptor phosphorylation is impaired in cathepsin X-deficient prostate cancer cells.
cathepsin x deficiency
Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice.
Cholangitis
Increased expression and altered localization of cathepsin Z are associated with progression to jaundice stage in primary biliary cholangitis.
Colorectal Neoplasms
Cathepsin X in serum from patients with colorectal cancer: relation to prognosis.
Colorectal Neoplasms
Characterization of cathepsin X in colorectal cancer development and progression.
Colorectal Neoplasms
KMT2A histone methyltransferase contributes to colorectal cancer development by promoting cathepsin Z transcriptional activation.
Colorectal Neoplasms
Prognostic and predictive value of cathepsin X in serum from colorectal cancer patients.
Diabetes Mellitus, Type 2
Deciphering the Plasma Proteome of Type 2 Diabetes.
Encephalitis
Development of Activity-Based Probes for Cathepsin X.
Encephalomyelitis
A role for cathepsin Z in neuroinflammation provides mechanistic support for an epigenetic risk factor in multiple sclerosis.
Encephalomyelitis, Autoimmune, Experimental
A role for cathepsin Z in neuroinflammation provides mechanistic support for an epigenetic risk factor in multiple sclerosis.
Gallbladder Neoplasms
Identification of prosaposin and transgelin as potential biomarkers for gallbladder cancer using quantitative proteomics.
Gastritis
Cathepsin X prevents an effective immune response against Helicobacter pylori infection.
Gastritis
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer.
Glioma
Localization patterns of cathepsins K and X and their predictive value in glioblastoma.
Hepatitis
Effect on vitamin A on the development of galactosamine-induced hepatitis in rats.
Hepatitis
[Distribution and activity of lysosomal protein catabolic-enzymes of rat liver in galactosamine hepatitis: catepsin D, cathepsin A and acid carboxypeptidase]
Infections
Cathepsin X prevents an effective immune response against Helicobacter pylori infection.
Infections
Cathepsin X-deficient gastric epithelial cells in co-culture with macrophages: characterization of cytokine response and migration capability after helicobacter pylori infection.
Infections
Cathepsins K, L, B, X and W are differentially expressed in normal and chronically inflamed gastric mucosa.
Infections
Generation of a single-chain variable fragment phage display antibody library from naïve mice panned against Fasciola hepatica antigens.
Infections
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer.
Infections
Vaccination of mice with recombinant novel aminopeptidase P and cathepsin X alone or in combination induces protective immunity against Trichinella spiralis infection.
Infections
Vaccine potential of recombinant cathepsin B against Fasciola gigantica.
Inflammatory Breast Neoplasms
Cathepsin B, cathepsin H, cathepsin X and cystatin C in sera of patients with early-stage and inflammatory breast cancer.
Intestinal Volvulus
The Caenorhabditis elegans cathepsin Z-like cysteine protease, Ce-CPZ-1, has a multifunctional role during the worms' development.
Liver Cirrhosis, Biliary
Increased expression and altered localization of cathepsin Z are associated with progression to jaundice stage in primary biliary cholangitis.
Liver Diseases
Increased expression and altered localization of cathepsin Z are associated with progression to jaundice stage in primary biliary cholangitis.
Lung Neoplasms
Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues.
Multiple Sclerosis
A role for cathepsin Z in neuroinflammation provides mechanistic support for an epigenetic risk factor in multiple sclerosis.
Neoplasm Metastasis
Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues.
Neoplasm Metastasis
Overexpression of cathepsin Z contributes to tumor metastasis by inducing epithelial-mesenchymal transition in hepatocellular carcinoma.
Neoplasm Metastasis
Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice.
Neoplasms
Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues.
Neoplasms
Cathepsin proteases promote angiogenic sprouting and laser-induced choroidal neovascularisation in mice.
Neoplasms
Cathepsin X Cleaves Profilin 1 C-Terminal Tyr139 and Influences Clathrin-Mediated Endocytosis.
Neoplasms
Cathepsin X in serum from patients with colorectal cancer: relation to prognosis.
Neoplasms
Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location.
Neoplasms
Cellular senescence induced by cathepsin X downregulation.
Neoplasms
Characterization of cathepsin X in colorectal cancer development and progression.
Neoplasms
Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas.
Neoplasms
Decreased levels of cathepsin Z mRNA expressed by immune blood cells: diagnostic and prognostic implications in prostate cancer.
Neoplasms
Development of Activity-Based Probes for Cathepsin X.
Neoplasms
Distinct functions of macrophage-derived and cancer cell-derived cathepsin Z combine to promote tumor malignancy via interactions with the extracellular matrix.
Neoplasms
Dysregulation of apoptotic signaling pathways by interaction of RPLP0 and cathepsin X/Z in gastric cancer.
Neoplasms
Identification and characterization of the novel reversible and selective cathepsin X inhibitors.
Neoplasms
IGF-I receptor phosphorylation is impaired in cathepsin X-deficient prostate cancer cells.
Neoplasms
Inhibition of cathepsin X reduces the strength of microglial-mediated neuroinflammation.
Neoplasms
Intracellular signaling by cathepsin X: Molecular mechanisms and diagnostic and therapeutic opportunities in cancer.
Neoplasms
Overexpression of cathepsin Z contributes to tumor metastasis by inducing epithelial-mesenchymal transition in hepatocellular carcinoma.
Neoplasms
Physical activity is associated with a large number of cardiovascular-specific proteins: Cross-sectional analyses in two independent cohorts.
Neoplasms
Profilin 1 as a target for cathepsin X activity in tumor cells.
Neoplasms
Structure-activity relationships of triazole-benzodioxine inhibitors of cathepsin X.
Neoplasms
Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice.
Neoplasms
Tumor cell-derived and macrophage-derived cathepsin B promotes progression and lung metastasis of mammary cancer.
Neoplasms
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer.
Neoplasms
Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia.
Neuroblastoma
Cathepsin X promotes 6-hydroxydopamine-induced apoptosis of PC12 and SH-SY5Y cells.
Neurodegenerative Diseases
Cathepsin X in serum from patients with colorectal cancer: relation to prognosis.
Neurodegenerative Diseases
Cathepsin X promotes 6-hydroxydopamine-induced apoptosis of PC12 and SH-SY5Y cells.
Neurodegenerative Diseases
Human cathepsin X/Z is a biologically active homodimer.
Neurodegenerative Diseases
Identification and characterization of the novel reversible and selective cathepsin X inhibitors.
Neurodegenerative Diseases
Neuroinflammation-Induced Upregulation of Glial Cathepsin X Expression and Activity in vivo.
Neurodegenerative Diseases
Structure-activity relationships of triazole-benzodioxine inhibitors of cathepsin X.
Neuroendocrine Tumors
Distinct functions of macrophage-derived and cancer cell-derived cathepsin Z combine to promote tumor malignancy via interactions with the extracellular matrix.
Neuroinflammatory Diseases
A role for cathepsin Z in neuroinflammation provides mechanistic support for an epigenetic risk factor in multiple sclerosis.
Neuroinflammatory Diseases
Inhibition of cathepsin X reduces the strength of microglial-mediated neuroinflammation.
Neuroinflammatory Diseases
Neuroinflammation-Induced Upregulation of Glial Cathepsin X Expression and Activity in vivo.
Neuroinflammatory Diseases
Upregulation of Cysteine Protease Cathepsin X in the 6-Hydroxydopamine Model of Parkinson's Disease.
Non-ST Elevated Myocardial Infarction
Lysophospholipids as Predictive Markers of ST-Elevation Myocardial Infarction (STEMI) and Non-ST-Elevation Myocardial Infarction (NSTEMI).
Osteoporosis
Cathepsin Z as a novel potential biomarker for osteoporosis.
Pancreatic Neoplasms
S100P-Binding Protein, S100PBP, Mediates Adhesion through Regulation of Cathepsin Z in Pancreatic Cancer Cells.
Parkinson Disease
Cathepsin X promotes 6-hydroxydopamine-induced apoptosis of PC12 and SH-SY5Y cells.
Parkinson Disease
Upregulation of Cysteine Protease Cathepsin X in the 6-Hydroxydopamine Model of Parkinson's Disease.
Pheochromocytoma
Cathepsin X promotes 6-hydroxydopamine-induced apoptosis of PC12 and SH-SY5Y cells.
Prostatic Intraepithelial Neoplasia
Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia.
Prostatic Neoplasms
Decreased levels of cathepsin Z mRNA expressed by immune blood cells: diagnostic and prognostic implications in prostate cancer.
Prostatic Neoplasms
Profilin 1 as a target for cathepsin X activity in tumor cells.
Prostatic Neoplasms
Structure-activity relationships of triazole-benzodioxine inhibitors of cathepsin X.
Prostatic Neoplasms
Up-regulation of cathepsin X in prostate cancer and prostatic intraepithelial neoplasia.
Sepsis
Increased expression and altered localization of cathepsin Z are associated with progression to jaundice stage in primary biliary cholangitis.
Stomach Neoplasms
Cathepsin X-deficient gastric epithelial cells in co-culture with macrophages: characterization of cytokine response and migration capability after helicobacter pylori infection.
Stomach Neoplasms
Regulation of cathepsin X overexpression in H. pylori-infected gastric epithelial cells and macrophages.
Stomach Neoplasms
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer.
Tuberculosis
Genetic susceptibility to tuberculosis associated with cathepsin Z haplotype in a Ugandan household contact study.
Tuberculosis
Mapping of a novel susceptibility locus suggests a role for MC3R and CTSZ in human tuberculosis.
Tuberculosis
Polymorphisms in MC3R promoter and CTSZ 3'UTR are associated with tuberculosis susceptibility.
Tuberculosis, Pulmonary
Association of CTSZ rs34069356 and MC3R rs6127698 gene polymorphisms with pulmonary tuberculosis.
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Edge, M.; Forder, C.; Hennam, J.; Lee, I.; Tonge, D.; Hardern, I.; Fitton, J.; Eckersley, K.; East, S.; Shufflebotham, A.; Blakey, D.; Slater, A.
Engineered human carboxypeptidase B enzymes that hydrolyse hippuryl-L-glutamic acid: reversed-polarity mutants
Protein Eng.
11
1229-1234
1998
Homo sapiens
brenda
Klemencic, I.; Carmona, A.K.; Cezari, M.H.; Juliano, M.A.; Juliano, L.; Guncar, G.; Turk, D.; Krizaj, I.; Turk, V.; Turk, B.
Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
Eur. J. Biochem.
267
5404-5412
2000
Homo sapiens
brenda
Guncar, G.; Klemencic, I.; Turk, B.; Turk, V.; Karaoglanovic-Carmona, A.; Juliano, L.; Turk, D.
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease
Structure Fold. Des.
8
305-313
2000
Homo sapiens
brenda
Devanathan, G.; Turnbull, J.L.; Ziomek, E.; Purisima, E.O.; Menard, R.; Sulea, T.
Carboxy-monopeptidase substrate specificity of human cathepsin X
Biochem. Biophys. Res. Commun.
329
445-452
2005
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Kos, J.; Sekirnik, A.; Premzl, A.; Zavasnik Bergant, V.; Langerholc, T.; Turk, B.; Werle, B.; Golouh, R.; Repnik, U.; Jeras, M.; Turk, V.
Carboxypeptidases cathepsins X and B display distinct protein profile in human cells and tissues
Exp. Cell Res.
306
103-113
2005
Homo sapiens
brenda
Obermajer, N.; Premzl, A.; Zavasnik Bergant, T.; Turk, B.; Kos, J.
Carboxypeptidase cathepsin X mediates beta(2)-integrin-dependent adhesion of differentiated U-937 cells
Exp. Cell Res.
312
2515-2527
2006
Homo sapiens
brenda
Ngler, D.K.; Lechner, A.M.; Oettl, A.; Kozaczynska, K.; Scheuber, H.P.; Gippner-Steppert, C.; Bogner, V.; Biberthaler, P.; Jochum, M.
An enzyme-linked immunosorbent assay for human cathepsin X, a potential new inflammatory marker
J. Immunol. Methods
308
241-250
2006
Homo sapiens
brenda
Krueger, S.; Kalinski, T.; Hundertmark, T.; Wex, T.; Kuster, D.; Peitz, U.; Ebert, M.; Nagler, D.K.; Kellner, U.; Malfertheiner, P.; Naumann, M.; Rocken, C.; Roessner, A.
Up-regulation of cathepsin X in Helicobacter pylori gastritis and gastric cancer
J. Pathol.
207
32-42
2005
Homo sapiens
brenda
Cooke, G.S.; Campbell, S.J.; Bennett, S.; Lienhardt, C.; McAdam, K.P.; Sow, O.; Gustafson, P.; Mwangulu, F.; van Helden, P.; Fine, P.; Hoal, E.G.; Hill, A.V.
Mapping of a novel susceptibility locus suggests a role for MC3R and CTSZ in human tuberculosis
Am. J. Respir. Crit. Care Med.
178
203-207
2008
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Nyfeler, B.; Hauri, H.P.
Visualization of protein interactions inside the secretory pathway
Biochem. Soc. Trans.
35
970-973
2007
Homo sapiens (Q9UBR2)
brenda
Wendt, W.; Zhu, X.R.; Luebbert, H.; Stichel, C.C.
Differential expression of cathepsin X in aging and pathological central nervous system of mice
Exp. Neurol.
204
525-540
2007
Homo sapiens, Mus musculus
brenda
Obermajer, N.; Repnik, U.; Jevnikar, Z.; Turk, B.; Kreft, M.; Kos, J.
Cysteine protease cathepsin X modulates immune response via activation of beta2 integrins
Immunology
124
76-88
2008
Homo sapiens
brenda
Lechner, A.M.; Assfalg-Machleidt, I.; Zahler, S.; Stoeckelhuber, M.; Machleidt, W.; Jochum, M.; Naegler, D.K.
RGD-dependent binding of procathepsin X to integrin alphavbeta3 mediates cell-adhesive properties
J. Biol. Chem.
281
39588-39597
2006
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Nyfeler, B.; Zhang, B.; Ginsburg, D.; Kaufman, R.J.; Hauri, H.P.
Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex
Traffic
7
1473-1481
2006
Homo sapiens (Q9UBR2)
brenda
Krueger, S.; Kuester, D.; Bernhardt, A.; Wex, T.; Roessner, A.
Regulation of cathepsin X overexpression in H. pylori-infected gastric epithelial cells and macrophages
J. Pathol.
217
581-588
2009
Homo sapiens
brenda
Kos, J.; Jevnikar, Z.; Obermajer, N.
The role of cathepsin X in cell signaling
Cell Adh. Migr.
3
164-166
2009
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Obermajer, N.; Jevnikar, Z.; Doljak, B.; Sadaghiani, A.M.; Bogyo, M.; Kos, J.
Cathepsin X-mediated beta2 integrin activation results in nanotube outgrowth
Cell. Mol. Life Sci.
66
1126-1134
2009
Homo sapiens (Q9UBR2)
brenda
Obermajer, N.; Magister, S.; Kopitar, A.N.; Tepes, B.; Ihan, A.; Kos, J.
Cathepsin X prevents an effective immune response against Helicobacter pylori infection
Eur. J. Cell Biol.
88
461-471
2009
Homo sapiens (Q9UBR2)
brenda
Jevnikar, Z.; Obermajer, N.; Pecar-Fonovi?, U.; Karaoglanovic-Carmona, A.; Kos, J.
Cathepsin X cleaves the beta2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and alpha-actinin-1 binding
Eur. J. Immunol.
39
3217-3227
2009
Homo sapiens
brenda
Staudt, N.D.; Aicher, W.K.; Kalbacher, H.; Stevanovic, S.; Carmona, A.K.; Bogyo, M.; Klein, G.
Cathepsin X is secreted by human osteoblasts, digests CXCL-12 and impairs adhesion of hematopoietic stem and progenitor cells to osteoblasts
Haematologica
95
1452-1460
2010
Homo sapiens (Q9UBR2), Homo sapiens
brenda
Naegler, D.K.; Kraus, S.; Feierler, J.; Mentele, R.; Lottspeich, F.; Jochum, M.; Faussner, A.
A cysteine-type carboxypeptidase, cathepsin X, generates peptide receptor agonists
Int. Immunopharmacol.
10
134-139
2010
Homo sapiens
brenda
Obermajer, N.; Doljak, B.; Jamnik, P.; Fonovic, U.P.; Kos, J.
Cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase and impairs survival and neuritogenesis of neuronal cells
Int. J. Biochem. Cell Biol.
41
1685-1696
2009
Homo sapiens
brenda
Zhao, C.F.; Herrington, D.M.
The function of cathepsins B, D, and X in atherosclerosis
Am. J. Cardiovasc. Dis.
6
163-170
2016
Homo sapiens (Q9UBR2)
brenda
Mitrovic, A.; Pecar Fonovic, U.; Kos, J.
Cysteine cathepsins B and X promote epithelial-mesenchymal transition of tumor cells
Eur. J. Cell Biol.
96
622-631
2017
Homo sapiens (Q9UBR2)
brenda
Pecar Fonovic, U.; Kos, J.
Cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis
PLoS ONE
10
e0137217
2015
Homo sapiens (Q9UBR2)
brenda