Ser201
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Home > Phosphorylation Site Page: > Ser201  -  RRas (human)

Site Information
QEQELPPsPPsAPRK   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 18015221

In vivo Characterization
Methods used to characterize site in vivo:
immunoprecipitation ( 1 ) , mass spectrometry ( 2 , 3 , 5 , 6 ) , mutation of modification site ( 1 ) , phospho-antibody ( 1 ) , western blotting ( 1 )
Disease tissue studied:
cervical cancer ( 6 ) , cervical adenocarcinoma ( 6 )
Relevant cell line - cell type - tissue:
HEK293T (epithelial) ( 1 ) , HeLa (cervical) ( 1 , 2 , 5 ) , HeLa S3 (cervical) ( 6 ) , liver ( 3 )

Upstream Regulation
Putative in vivo kinases:
ERK1 (human) ( 1 ) , ERK2 (mouse) ( 1 )
Kinases, in vitro:
ERK1 (human) ( 1 )

Downstream Regulation
Effects of modification on RRas:
activity, induced ( 1 )

References 

1

Frémin C, et al. (2016) ERK1/2-induced phosphorylation of R-Ras GTPases stimulates their oncogenic potential. Oncogene 35, 5692-5698
27086924   Curated Info

2

Sharma K, et al. (2014) Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Rep 8, 1583-94
25159151   Curated Info

3

Bian Y, et al. (2014) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics 96, 253-62
24275569   Curated Info

4

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

5

Kettenbach AN, et al. (2011) Quantitative phosphoproteomics identifies substrates and functional modules of aurora and polo-like kinase activities in mitotic cells. Sci Signal 4, rs5
21712546   Curated Info

6

Olsen JV, et al. (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3, ra3
20068231   Curated Info

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