Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 10617634 
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
This page summarizes selected information from the record 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.
Download Sites

S71-p - RAC1 (human)
Orthologous residues
RAC1 (human): S71‑p, RAC1 iso2 (human): S71‑p, RAC1 (mouse): S71‑p, RAC1 (rat): S71‑p
 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):  activity, inhibited
 Comments:  Phosphorylation of this site inhibits GTP binding activity of Rac1 without affecting its GTPase activity.

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.