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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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Methyltransferase activity methylates TP53. 4 / 4

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"P53 can be methylated on lysines and arginines by several different methylase enzymes, which can either activate or repress its activity depending on which site is methylated and the number of methyl groups added ( xref )."

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"In contrast, methylation of p53 by methyltransferases at histidines, arginines, and lysines, suppresses transcriptional activity of p53 [ xref ]."

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"Several histone lysine methyltransferases methylate p53 at specific C-terminal lysines, preventing or inducing p53 interaction with its co-activators."

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"Our study identified PRMT3 as a second arginine methyltransferase that can methylate p53."

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

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Statements

Methyltransferase activity methylates TP53. 4 / 4

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