Mapping cryptic phosphorylation sites in the human proteome.

ABSTRACT: Advances in computational and experimental methods have revealed the existence of transient, non-native protein folding intermediates that could play roles in disparate biological processes, from regulation of protein expression to disease-relevant misfolding mechanisms. Here, we tested the possibility that specific post-translational modifications may involve residues exposed during the folding process by assessing the solvent accessibility of 87,138 post-translationally modified amino acids in the human proteome. Unexpectedly, we found that one-third of phosphorylated proteins present at least one phosphosite completely buried within the protein's inner core. Computational and experimental analyses suggest that these cryptic phosphosites may become exposed during the folding process, whe

SUBMITTER: Gasparotto D 

PROVIDER: S-EPMC12624043 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature