Ser134
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Home > Phosphorylation Site Page: > Ser134  -  PLD2 (human)

Site Information
ARFAVAYsPARDAGN   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 456492

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 2 , 3 , 4 , 6 ) , mutation of modification site ( 5 , 6 ) , phospho-antibody ( 5 ) , western blotting ( 5 )
Disease tissue studied:
breast cancer ( 2 ) , luminal A breast cancer ( 1 ) , luminal B breast cancer ( 1 ) , breast cancer, surrounding tissue ( 1 ) , breast cancer, triple negative ( 2 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Putative in vivo kinases:
CDK5 (human) ( 5 )
Treatments:
EGF ( 5 )

Downstream Regulation
Effects of modification on PLD2:
enzymatic activity, induced ( 5 )

References 

1

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

2

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

3

Luerman GC, et al. (2014) Phosphoproteomic evaluation of pharmacological inhibition of leucine-rich repeat kinase 2 reveals significant off-target effects of LRRK-2-IN-1. J Neurochem 128, 561-76
24117733   Curated Info

4

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

5

Lee HY, et al. (2008) Cdk5 phosphorylates PLD2 to mediate EGF-dependent insulin secretion. Cell Signal 20, 1787-94
18625302   Curated Info

6

Chen JS, Exton JH (2005) Sites on phospholipase D2 phosphorylated by PKCalpha. Biochem Biophys Res Commun 333, 1322-6
15979581   Curated Info