Ser202
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Home > Phosphorylation Site Page: > Ser202  -  PKM (human)

Site Information
tEVENGGsLGskkGV   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 15721963

In vivo Characterization
Methods used to characterize site in vivo:
immunoprecipitation ( 1 ) , mass spectrometry ( 1 , 2 , 3 , 4 , 5 ) , mutation of modification site ( 1 ) , phospho-antibody ( 1 ) , western blotting ( 1 )
Disease tissue studied:
breast cancer ( 4 ) , breast ductal carcinoma ( 4 ) , HER2 positive breast cancer ( 2 ) , luminal A breast cancer ( 2 ) , luminal B breast cancer ( 2 ) , breast cancer, triple negative ( 2 ) , lung cancer ( 1 ) , non-small cell lung cancer ( 1 ) , melanoma skin cancer ( 3 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Kinases, in vitro:
Akt1 (human) ( 1 )
Treatments:
IGF-1 ( 1 )

Downstream Regulation
Effects of modification on PKM:
intracellular localization ( 1 ) , molecular association, regulation ( 1 )
Induce interaction with:
STAT5A (human) ( 1 )

References 

1

Park YS, et al. (2016) AKT-induced PKM2 phosphorylation signals for IGF-1-stimulated cancer cell growth. Oncotarget 7, 48155-48167
27340866   Curated Info

2

Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62
27251275   Curated Info

3

Stuart SA, et al. (2015) A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells. Mol Cell Proteomics 14, 1599-615
25850435   Curated Info

4

Mertins P, et al. (2014) Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics 13, 1690-704
24719451   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