Any protein can be phosphorylated under specific cellular conditions
the verdict
SUPPORTED
the evidence backs this
confidence 75/100
Proteome-wide phosphoproteomic analyses and kinase assays demonstrate that a vast multitude of proteins can be phosphorylated under varying cellular conditions.
Evidence for · 3
Scop3P in 2026: an expanded proteomics-informed resource contextualizing phosphorylation sites through sequence, structure, mutation, and experimental provenance
2026 · cited by 0
Scop3P catalogs over 150,000 phosphorylation sites across tens of thousands of proteins, highlighting how widespread this modification is.
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More for · 2
Detecting protein higher-order structural changes using kinase as a phospho-labeler.
2026 · cited by 0
Using kinase as a phospho-labeler allows site-resolved profiling of structural alterations across the proteome.
Protocol to study direct (de)phosphorylation events on a proteome-wide scale using on-bead in vitro enzyme assays.
2026 · cited by 0
Protocols utilizing on-bead in vitro kinase assays facilitate the study of direct phosphorylation events on a proteome-wide scale under native conditions.