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Literature summary extracted from

  • Park, H.M.; Kim, G.Y.; Nam, M.K.; Seong, G.H.; Han, C.; Chung, K.C.; Kang, S.; Rhim, H.
    The serine protease HtrA2/Omi cleaves Parkin and irreversibly inactivates its E3 ubiquitin ligase activity (2009), Biochem. Biophys. Res. Commun., 387, 537-542.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.108 parkin + H2O Homo sapiens using cleavage and binding assays, it is demonstrated that HtrA2 specifically binds to and directly cleaves the E3 ubiquitin ligase Parkin ?
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 ?
3.4.21.108 parkin + H2O Mus musculus HtrA2/Omi cleaves E3 ubiquitin ligase Parkin ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.108 Homo sapiens
-
-
-
3.4.21.108 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.108 parkin + H2O using cleavage and binding assays, it is demonstrated that HtrA2 specifically binds to and directly cleaves the E3 ubiquitin ligase Parkin Homo sapiens ?
-
 ?
3.4.21.108 parkin + H2O HtrA2/Omi cleaves E3 ubiquitin ligase Parkin Mus musculus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.108 HtrA2
-
 Homo sapiens
3.4.21.108 HtrA2
-
 Mus musculus

General Information

EC Number General Information Comment Organism
3.4.21.108 malfunction endogenous levels of Parkin are significantly decreased in wild-type (HtrA2+/+) mouse embryonic fibroblasts compared with those in HtrA2-knockout (HtrA2-/-) mouse embryonic fibroblasts under the same stress conditions Mus musculus
3.4.21.108 physiological function the HtrA2-mediated Parkin cleavage irreversibly disrupts Parkin-mediated synphilin-1 ubiquitination and autoubiquitination, indicating that HtrA2 may play a critical role in the Parkin-related pathway involved in the ubiquitin proteasome system Homo sapiens