Curated Information

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PubMed Id: 10085070

This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus^®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus^®, click here.

Collins SP, Uhler MD (1999) Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their regulation of cyclic AMP response element-dependent gene transcription. J Biol Chem 274, 8391-404 10085070

S153-p - VASP (mouse)

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Orthologous residues

VASP (human): S157‑p, VASP (mouse): S153‑p, VASP (rat): S154‑p

Characterization

Methods used to characterize site in vivo: electrophoretic mobility shift, mutation of modification site

Relevant cell lines - cell types - tissues: CV1 (fibroblast) [PKG1 iso2 (mouse)], CV1 (fibroblast) [VASP (mouse)]

Cellular systems studied: cell lines

Species studied: human

Enzymes shown to modify site in vitro:

Type	Enzyme
KINASE	PKG1 iso2 (mouse)

Upstream Regulation

Potential in vivo enzymes for site:

Type	Enzyme	Evidence	Notes
KINASE	PKG1 iso2 (mouse)	transfection of constitutively active enzyme, co-immunoprecipitation

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
cGMP analog				increase

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