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A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

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INDRA is developed by indralabs, a part of the Harvard Medical School Laboratory of Systems Pharmacology.

This project, indra_db, is also developed by the indralab team. For more information on how we procure our sources, you can go here. This work was funded by ARO grant W911NF‐15‐1‐0544 under the DARPA Communicating with Computers program.

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USP30 deubiquitinates OMM proteins. 3 / 3

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"Previous results from cell culture experiments and flies suggest that USP30 can deubiquitylate OMM proteins and antagonize Parkin’s activity ."

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"Recent advances have demonstrated that USP30 can counteract Parkin-dependent mitophagy by deubiquitylating OMM proteins, including TOMM20 ."

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"At present, the negative regulatory mechanisms against Parkin-mediated ubiquitination have been reported, with the discovery of several deubiquitinases including USP8, USP15 and USP30 that are able to cause the deubiquitination of Parkin and/or OMM proteins."

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USP30 deubiquitinates OMM proteins. 3 / 3

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