Curated Information
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Home > Curated Information Page > PubMed Id: 17803936
Wang WJ, et al. (2007) The tumor suppressor DAPK is reciprocally regulated by tyrosine kinase Src and phosphatase LAR. Mol Cell 27, 701-16 17803936
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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Y490-p - DAPK1 (human)
Modsite: HCAAWHGyySVAKAL SwissProt Entrez-Gene
Orthologous residues
DAPK1 (human): Y490‑p, DAPK1 iso3 (human): Y490‑p, DAPK1 (mouse): Y490‑p, DAPK1 (rat): Y490‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
Disease tissue studied:  lung cancer
Relevant cell lines - cell types - tissues:  3T3 (fibroblast), CL1-0 (pulmonary), CL1-5 (pulmonary), HEK293T (epithelial), SYF (fibroblast)
Cellular systems studied:  cell lines
Species studied:  human, mouse
Enzymes shown to modify site in vitro
Type Enzyme
PHOSPHATASE PTPRF (human)
KINASE Src (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Src (human) pharmacological inhibitor of upstream enzyme, phospho-antibody, siRNA inhibition of enzyme
PHOSPHATASE PTPRF (human) genetic knockout/knockin of upstream enzyme, phospho-antibody
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PP2 decrease
SU6656 decrease
EGF (human) increase
siRNA EGF (human) inhibit treatment-induced increase Src-specific siRNA
Downstream Regulation
Effect of modification (function):  enzymatic activity, inhibited, protein conformation
Effect of modification (process):  apoptosis, inhibited, carcinogenesis, induced, cell adhesion, induced, cell motility, induced
Associated Diseases
Diseases Alterations Comments
colorectal cancer increased there is a positive correlation between elevated Src activity and DAPK Y491/492 hyperphosphorylation in human cancers

Y491-p - DAPK1 (human)
Modsite: CAAWHGyySVAKALC SwissProt Entrez-Gene
Orthologous residues
DAPK1 (human): Y491‑p, DAPK1 iso3 (human): Y491‑p, DAPK1 (mouse): Y491‑p, DAPK1 (rat): Y491‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
Disease tissue studied:  lung cancer
Relevant cell lines - cell types - tissues:  3T3 (fibroblast), CL1-0 (pulmonary), CL1-5 (pulmonary), HEK293T (epithelial), SYF (fibroblast)
Cellular systems studied:  cell lines
Species studied:  human, mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE Src (human)
PHOSPHATASE PTPRF (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
PHOSPHATASE PTPRF (human) genetic knockout/knockin of upstream enzyme, phospho-antibody
KINASE Src (human) pharmacological inhibitor of upstream enzyme, phospho-antibody, siRNA inhibition of enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PP2 decrease
SU6656 decrease
EGF (human) increase
siRNA EGF (human) inhibit treatment-induced increase Src-specific siRNA
Downstream Regulation
Effect of modification (function):  enzymatic activity, inhibited, protein conformation
Effect of modification (process):  apoptosis, inhibited, carcinogenesis, induced, cell adhesion, induced, cell motility, induced
Associated Diseases
Diseases Alterations Comments
colorectal cancer increased there is a positive correlation between elevated Src activity and DAPK Y491/492 hyperphosphorylation in human cancers