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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.

This Project

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.

IndraLab

Statements

OTULIN is dephosphorylated. 2 / 2

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"Furthermore, while OTULIN and the HOIP PUB domain form a gel filtration‐stable complex in vitro , the majority of OTULIN in cell lysates does not coelute with LUBAC indicating that OTULIN may be phosphorylated in cells, and dephosphorylation of OTULIN in cell extracts led to coelution of OTULIN with LUBAC xref ."

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"Although the responsible kinase(s) have not yet been identified, the dual specificity protein phosphatase 14 (DUSP14) has been reported to dephosphorylate OTULIN [ xref ]."

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Our Sources:

INDRA allows us to combine the results from a multitude of sources. In particular, the INDRA Database draws on the following...