InstaNovo-P: a de novo peptide sequencing model for phosphoproteomics

peer-reviewed · Nature Communications · 2026

peer-reviewed · Nature Communications · 2026. Jesper Lauridsen et al. Phosphorylation, a crucial post-translational modification (PTM), plays a central role in cellular signaling…
Date 2026-07-10
Type peer-reviewed
Venue Nature Communications
Publisher Springer Nature
Contribution algorithm
DOI 10.1038/s41467-026-75138-x
Citations (OpenAlex) 5
Venue 2-year citedness 15.88

Abstract

Phosphorylation, a crucial post-translational modification (PTM), plays a central role in cellular signaling and disease mechanisms. Mass spectrometry-based phosphoproteomics is widely used for system-wide characterization of phosphorylation events. However, traditional methods struggle with accurate phosphorylated site localization, complex search spaces, and detecting sequences outside the reference database. Advances in de novo peptide sequencing offer opportunities to address these limitations, but have yet to become integrated and adapted for phosphoproteomics datasets. Here, we present InstaNovo-P, a phosphorylation specific version of our transformer-based InstaNovo model, fine-tuned on extensive phosphoproteomics datasets. InstaNovo-P significantly surpasses existing methods in phosphorylated peptide detection and phosphorylated site localization accuracy across multiple datasets, including complex experimental scenarios. Our model robustly identifies peptides with single and multiple phosphorylated sites, effectively localizing phosphorylation events on serine, threonine, and tyrosine residues. We experimentally validate our model predictions by studying FGFR2 signaling, further demonstrating that InstaNovo-P uncovers phosphorylated sites previously missed by traditional database searches. These predictions align with critical biological processes, confirming the model’s capacity to yield valuable biological insights. InstaNovo-P adds value to phosphoproteomics experiments by effectively identifying biologically relevant phosphorylation events without prior information, providing a powerful analytical tool for the dissection of signaling pathways.

Authors

  1. Jesper Lauridsen · Technical University of Denmark
  2. Vahap Canbay · Technical University of Denmark
  3. Rachel Catzel · InstaDeep Ltd
  4. Pathmanaban Ramasamy · Ghent University, ULB-VUB, VIB, Vrije Universiteit Brussel
  5. Amandla Mabona · InstaDeep Ltd
  6. Kevin Eloff · InstaDeep Ltd
  7. Paul Fullwood · The University of Manchester
  8. Jennifer Ferguson · The University of Manchester
  9. Annekatrine Kirketerp-Møller · Technical University of Denmark
  10. Ida Sofie Goldschmidt · Technical University of Denmark
  11. Tine Claeys · Ghent University, VIB
  12. Sam van Puyenbroeck · Ghent University, VIB
  13. Nicolas Lopez Carranza · InstaDeep Ltd
  14. Erwin M. Schoof · Technical University of Denmark
  15. Lennart Martens · Ghent University, Infrastructure Nationale de Protéomique (ProFI-FR2048), University of Strasbourg, VIB
  16. Jeroen Van Goey · InstaDeep Ltd
  17. Chiara Francavilla · The University of Manchester
  18. Timothy P. Jenkins · Technical University of Denmark
  19. Konstantinos Kalogeropoulos · Delft University of Technology, Kavli Institute of Nanoscience, Technical University of Denmark

Methods and tools

Cites (6)

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