Degradation Determinants Are Abundant in Human Noncanonical Proteins and Minor Annotated Isoforms.

ABSTRACT: The comprehensive characterization of human proteins, a key objective in contemporary biology, has been revolutionized by the identification of thousands of potential novel proteins through ribosome profiling and proteomics. Determining the physiological activity of these noncanonical proteins has proven difficult, because they are encoded by different types of coding regions and tend to share no sequence similarity with canonical polypeptides. Evidence from immunopeptidomic assays combined with a better understanding of the quality control of protein synthesis suggest that many noncanonical proteins may possess low stability in the cellular environment. Here, we tested this hypothesis by analyzing the frequency of multiple sequence features eliciting either proteasomal degradation or auto

SUBMITTER: Casola C 

PROVIDER: S-EPMC12863090 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature