Thr108
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.7.5
Powered by Cell Signaling Technology
Home > Phosphorylation Site Page: > Thr108  -  RAC1 (human)

Site Information
VrHHCPNtPIILVGT   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 27458396

In vivo Characterization
Methods used to characterize site in vivo:
[32P] ATP in vitro ( 4 ) , immunoprecipitation ( 3 ) , mutation of modification site ( 1 , 2 , 3 , 4 ) , western blotting ( 3 )
Disease tissue studied:
breast cancer ( 4 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Putative in vivo kinases:
ERK1 (human) ( 4 )
Kinases, in vitro:
ERK1 (human) ( 2 , 4 )
Treatments:
EGF ( 1 , 4 ) , U0126 ( 4 )

Downstream Regulation
Effects of modification on RAC1:
enzymatic activity, inhibited ( 4 ) , intracellular localization ( 1 , 4 ) , molecular association, regulation ( 1 , 4 )
Effects of modification on biological processes:
RNA splicing, induced ( 1 )
Induce interaction with:
SFRS2 (human) ( 1 ) , hnRNP A1 (human) ( 1 ) , snRNP A' (human) ( 1 )
Inhibit interaction with:
PLCG1 (human) ( 4 )

References 

1

Abdrabou A, Wang Z (2021) Regulation of the nuclear speckle localization and function of Rac1. FASEB J 35, e21235
33417283   Curated Info

2

Brandwein D, et al. (2018) An In Vitro Kinase Assay to Assess Rac1 Phosphorylation by ERK. Methods Mol Biol 1821, 131-140
30062409   Curated Info

3

Tong J, Li L, Ballermann B, Wang Z (2016) Phosphorylation and Activation of RhoA by ERK in Response to Epidermal Growth Factor Stimulation. PLoS One 11, e0147103
26816343   Curated Info

4

Tong J, Li L, Ballermann B, Wang Z (2013) Phosphorylation of Rac1 T108 by extracellular signal-regulated kinase in response to epidermal growth factor: a novel mechanism to regulate Rac1 function. Mol Cell Biol 33, 4538-51
24043306   Curated Info

5

Shiromizu T, et al. (2013) Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res 12, 2414-21
23312004   Curated Info