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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.

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Statements

AKT phosphorylates NOS3 on S615. 4 / 4

1 1 | 2

➶

phosphoelm

No evidence text available

12171920

➶

reach

"Upon stimulation, Akt and protein kinase B (PKB) phosphorylates eNOS at Ser 1177 (1179) and possibly Ser 615 (617), and consequently activates eNOS [XREF_BIBR]."

25460366

➶

reach

"Upon stimulation, Akt and protein kinase B (PKB) phosphorylates eNOS at Ser 1177 (1179) and possibly Ser 615 (617), and consequently activates eNOS [XREF_BIBR]."

25460366

➶

signor

"The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites"

24379783

Our Sources:

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