Curated Information
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Home > Curated Information Page > PubMed Id: 23946483
Takahashi M, et al. (2013) Protein Kinase A-dependent Phosphorylation of Rap1 Regulates Its Membrane Localization and Cell Migration. J Biol Chem 288, 27712-23 23946483
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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S179-p - RAP1B (cow)
Modsite: PGKARKKssCQLL__ SwissProt Entrez-Gene
Orthologous residues
RAP1B (human): S179‑p, RAP1B (mouse): S179‑p, RAP1B (rat): S179‑p, RAP1B (cow): S179‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, phospho-antibody, western blotting
Disease tissue studied:  lung cancer, non-small cell lung cancer
Relevant cell lines - cell types - tissues:  293 (epithelial), NCI-H1299 (pulmonary)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological activator of upstream enzyme, phospho-motif antibody, pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
NKH_477 increase
H-89 NKH_477 inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  activity, inhibited, intracellular localization
Effect of modification (process):  cell motility, induced
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
RASSF5 (human) Disrupts co-immunoprecipitation
Comments:  1) Cytosolic relocalization of Rap1 is phosphorylation dependent. 2) Rap1 phosphorylation is necessary for cell migration. 3) Binding of Rap1 to RapL is decreased by PKA-dependent phosphorylation of S180.

S180-p - RAP1B (cow)
Modsite: GKARKKssCQLL___ SwissProt Entrez-Gene
Orthologous residues
RAP1B (human): S180‑p, RAP1B (mouse): S180‑p, RAP1B (rat): S180‑p, RAP1B (cow): S180‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, phospho-antibody, western blotting
Disease tissue studied:  lung cancer, non-small cell lung cancer
Relevant cell lines - cell types - tissues:  293 (epithelial), NCI-H1299 (pulmonary)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological activator of upstream enzyme, phospho-motif antibody, pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
NKH_477 increase
H-89 NKH_477 inhibit treatment-induced increase
Downstream Regulation
Effect of modification (function):  activity, inhibited, intracellular localization
Effect of modification (process):  cell motility, induced
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
RASSF5 (human) Disrupts co-immunoprecipitation
Comments:  1) Cytosolic relocalization of Rap1 is phosphorylation dependent. 2) Rap1 phosphorylation is necessary for cell migration. 3) Binding of Rap1 to RapL is decreased by PKA-dependent phosphorylation of S180.