Curated Information

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Curated Information Page

PubMed Id: 10617634

This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus^®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus^®, click here.

Kwon T, et al. (2000) Akt protein kinase inhibits Rac1-GTP binding through phosphorylation at serine 71 of Rac1. J Biol Chem 275, 423-8 10617634

S71-p - Rac1 (human)

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Orthologous residues

Rac1 (human): S71‑p, RAC1 iso2 (human): S71‑p, Rac1 (mouse): S71‑p, Rac1 (rat): S71‑p

Characterization

Species studied: no information

Comments: While this paper does not prove directly that this site is phosphorylated in vivo, it does present strong circumstantial evidence to support this argument. Additionally, CST has verified that it is phosphorylated in living cells (CST cat# 2461).

Enzymes shown to modify site in vitro:

Type	Enzyme
KINASE	Akt1 (human)

Downstream Regulation

Effect of modification (function): inhibition

Comments: Phosphorylation of this site inhibits GTP binding activity of Rac1 without affecting its GTPase activity.

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