Curated Information
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Home > Curated Information Page > PubMed Id: 15166227
Park SY, Avraham HK, Avraham S (2004) RAFTK/Pyk2 activation is mediated by trans-acting autophosphorylation in a Src-independent manner. J Biol Chem 279, 33315-22 15166227
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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Y402-p - Pyk2 (human)
Modsite: CsIEsDIyAEIPDEt SwissProt Entrez-Gene
Orthologous residues
Pyk2 (human): Y402‑p, Pyk2 iso2 (human): Y402‑p, Pyk2 (mouse): Y402‑p, Pyk2 (rat): Y402‑p
Characterization
Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
Disease tissue studied:  adrenal cancer, pheochromocytoma
Relevant cell lines - cell types - tissues:  293 (epithelial), PC-12 (chromaffin), SYF (fibroblast)
Cellular systems studied:  cell lines
Species studied:  human, mouse, rat
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Pyk2 (human) co-immunoprecipitation, transfection of wild-type enzyme, phospho-antibody, transfection of inactive enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
depolarization increase