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Literature summary for 3.4.24.36 extracted from

  • Halle, M.; Gomez, M.A.; Stuible, M.; Shimizu, H.; McMaster, W.R.; Olivier, M.; Tremblay, M.L.
    The Leishmania surface protease GP63 cleaves multiple intracellular proteins and actively participates in p38 mitogen-activated protein kinase inactivation (2009), J. Biol. Chem., 284, 6893-6908.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Leishmania major gp63 is the principal catalyst of proteolysis during infection. It plays a central role in a number of host cell molecular events that likely contribute to the infectivity of Leishmania ?
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Organism

Organism UniProt Comment Textmining
Leishmania major
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information gp63 is the principal catalyst of proteolysis during infection. It plays a central role in a number of host cell molecular events that likely contribute to the infectivity of Leishmania Leishmania major ?
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p130Cas + H2O phosphorylated adaptor protein of fibroblasts Leishmania major ?
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protein-tyrosine phosphatase-PEST + H2O fibroblast protein cleaved upon infection by Leishmania major. cleavage augments its catalytic activity. Cleavage occurs likely near its C-terminal nuclear localization signal. Removal of the nuclear localization signal could allow the phosphatase to access additional substrates and also enhance its catalytic activity Leishmania major ?
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