Any protein can be phosphorylated under specific cellular conditions

the verdict

SUPPORTED

the evidence backs this

Recorded sources

3 sources for · 0 against

Counts group repeated records of the same source within each side. They do not measure evidence strength or source independence.

Proteome-wide phosphoproteomic analyses and kinase assays demonstrate that a vast multitude of proteins can be phosphorylated under varying cellular conditions.

The analysis

The claim states that any protein can be phosphorylated under specific cellular conditions. Modern high-throughput phosphoproteomics databases like Scop3P map hundreds of thousands of phosphorylation sites across most of the human proteome, and global kinase assays confirm that accessibility to phosphorylation is a general property of proteins when subjected to appropriate enzymatic and cellular conditions. The provided literature strongly supports the ubiquity and broad scope of protein phosphorylation across the proteome.

Evidence for · 3

Scop3P in 2026: an expanded proteomics-informed resource contextualizing phosphorylation sites through sequence, structure, mutation, and experimental provenance

Recorded source metadata

Ramasamy P, Tichshenko N, Díaz A, Velghe K, Massignani E, Vranken WF, Martens L. Scop3P in 2026: an expanded proteomics-informed resource contextualizing phosphorylation sites through sequence, structure, mutation, and experimental provenance. 2026. https://doi.org/10.64898/2026.07.03.736340

Scop3P catalogs over 150,000 phosphorylation sites across tens of thousands of proteins, highlighting how widespread this modification is.

Source citation format

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More for · 2

Detecting protein higher-order structural changes using kinase as a phospho-labeler.

Recorded source metadata

Maeda A, Ogata K, Ishihama Y. Detecting protein higher-order structural changes using kinase as a phospho-labeler.. 2026. https://doi.org/10.1016/j.crmeth.2026.101466

Using kinase as a phospho-labeler allows site-resolved profiling of structural alterations across the proteome.

Source citation format

Protocol to study direct (de)phosphorylation events on a proteome-wide scale using on-bead in vitro enzyme assays.

Recorded source metadata

Brunner M, Hu Z, Caligaris M, Stumpe M, De Virgilio C, Dengjel J. Protocol to study direct (de)phosphorylation events on a proteome-wide scale using on-bead in vitro enzyme assays.. 2026. https://doi.org/10.1016/j.xpro.2026.104629

Protocols utilizing on-bead in vitro kinase assays facilitate the study of direct phosphorylation events on a proteome-wide scale under native conditions.

Source citation format

The paper trail · every fact has a biography

first checked01 Aug 2026

judged → SUPPORTED · 7501 Aug 2026

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