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[PDF] Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder*S | Semantic Scholar

@article{Collins2008PhosphoproteomicAO,
  title={Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder*S},
  author={Mark O. Collins and Lu Yu and Iain D G Campuzano and Seth G. N. Grant and Jyoti S. Choudhary},
  journal={Molecular \& Cellular Proteomics},
  year={2008},
  volume={7},
  pages={1331 - 1348},
  url={https://api.semanticscholar.org/CorpusID:22193414}
}

Protein phosphorylation is significantly depleted in protein domains and significantly enriched in disordered protein sequences and that enrichment of intrinsic sequence disorder may be a common feature of phosphoproteomes is demonstrated, which supports the hypothesis that disordered regions in proteins allow kinases, phosphatases, and phosphate-dependent binding proteins to gain access to target sequences to regulate local protein conformation and activity.

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Proteomic Analysis of in Vivo Phosphorylated Synaptic Proteins*

Bioinformatic and in vitro phosphorylation assays of peptide arrays suggest that a small number of kinases phosphorylate many proteins and that each substrate is phosphorylated by many kinases, which support a model where the synapse phosphoproteome is functionally organized into a highly interconnected signaling network.