Tyr415

Site Information
ALGINSGysKRALML SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 10036101

In vivo Characterization
Methods used to characterize site in vivo:	immunoprecipitation ( 2 ) , mass spectrometry (in vitro) ( 4 ) , mutation of modification site ( 1 , 2 , 3 , 4 , 5 ) , western blotting ( 4 )
Disease tissue studied:	breast cancer ( 1 , 3 , 4 ) , lung cancer ( 3 ) , non-small cell lung cancer ( 3 )
Relevant cell line - cell type - tissue:	COS (fibroblast) ( 2 , 4 , 5 ) , MCF-7 (breast cell) ( 3 , 4 ) , MDA-MB-231 (breast cell) ( 3 ) , MTLn3 (breast cell) ( 1 , 3 , 4 ) , NCI-H1299 (pulmonary) ( 3 ) , neutrophil-blood ( 2 )

Downstream Regulation
Effects of modification on PLD2:	enzymatic activity, induced ( 3 , 4 , 5 ) , molecular association, regulation ( 1 )
Effects of modification on biological processes:	carcinogenesis, induced ( 3 ) , cell motility, induced ( 2 , 3 )
Induce interaction with:	JAK2 (human) ( 1 )

References
1	Hatton N, et al. (2015) Phosphatidic Acid Increases Epidermal Growth Factor Receptor Expression by Stabilizing mRNA Decay and by Inhibiting Lysosomal and Proteasomal Degradation of the Internalized Receptor. Mol Cell Biol 35, 3131-44 26124282 Curated Info
2	Mahankali M, Henkels KM, Gomez-Cambronero J (2013) A GEF-to-phospholipase molecular switch caused by phosphatidic acid, Rac and JAK tyrosine kinase that explains leukocyte cell migration. J Cell Sci 126, 1416-28 23378025 Curated Info
3	Henkels KM, et al. (2011) Cell Invasion of Highly Metastatic MTLn3 Cancer Cells Is Dependent on Phospholipase D2 (PLD2) and Janus Kinase 3 (JAK3). J Mol Biol 408, 850-62 21414324 Curated Info
4	Henkels KM, Peng HJ, Frondorf K, Gomez-Cambronero J (2010) A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation. Mol Cell Biol 30, 2251-63 20176813 Curated Info
5	Henkels KM, et al. (2009) PLD2 has both enzymatic and cell proliferation-inducing capabilities, that are differentially regulated by phosphorylation and dephosphorylation. Biochem Biophys Res Commun 389, 224-8 19715678 Curated Info