Curated Information
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Home > Curated Information Page > PubMed Id: 21945940
Thomson DM, et al. (2011) Phosphorylation of VASP by AMPK alters actin binding and occurs at a novel site. Biochem Biophys Res Commun 414, 215-9 21945940
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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S153-p - VASP (mouse)
Modsite: EHMERRVsNAGGPPA SwissProt Entrez-Gene
Orthologous residues
VASP (human): S157‑p, VASP (mouse): S153‑p, VASP (rat): S154‑p

S235-p - VASP (mouse)
Modsite: GAKLRKVsKQEEASG SwissProt Entrez-Gene
Orthologous residues
VASP (human): S239‑p, VASP (mouse): S235‑p, VASP (rat): S236‑p

T274-p - VASP (mouse)
Modsite: LARRRKAtQVGEKPP SwissProt Entrez-Gene
Orthologous residues
VASP (human): T278‑p, VASP (mouse): T274‑p, VASP (rat): T274‑p

S317-p - VASP (mouse)
Modsite: TtLPRMKssssVtTS SwissProt Entrez-Gene
Orthologous residues
VASP (human): S322‑p, VASP (mouse): S317‑p, VASP (rat): S318‑p
Characterization
Enzymes shown to modify site in vitro
Type Enzyme
KINASE AMPKA2 (human)
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  cell adhesion, induced
Comments:  increased actin filament binding in vitro, increased aggregation of cells, increased VASP at cell-cell adhesions