PhosphOrtholog

PhosphOrtholog maps orthologous protein post-translational modification (PTM) sites across species to enable comparative proteomics and identification of conserved modification sites including phosphorylation, acetylation, ubiquitination, and methylation.

Key Features:

• Cross-Species Mapping: Maps both known and novel orthologous PTM sites between species, enabling site-level comparisons even in structurally disordered protein domains.
• Database-Independent Automated Mapping: Performs automated mapping independently of pre-existing PTM databases by employing pairwise sequence alignment of orthologous protein residues.
• PTM-Type Agnostic: Applicable to multiple PTM types including phosphorylation, acetylation, ubiquitination, and methylation.
• High Mapping Efficiency: Demonstrates higher mapping efficiency than PhosphoSitePlus, more than doubling the number of cross-species mapped sites in analyses of human and rat muscle phosphoproteomes and a mouse phosphoproteome.

Scientific Applications:

• Comparative Proteomics: Enables comprehensive cross-species comparisons of large-scale PTM datasets to assess conservation and divergence of modification sites.
• Model-to-Human Translation: Facilitates translation of PTM data between model organisms and humans to support inference of conserved biological mechanisms.
• Functional PTM Site Identification: Supports identification and expansion of candidate conserved functional PTM sites for studies of signal transduction and protein regulation.

Methodology:

Maps PTM sites by pairwise sequence alignment of orthologous protein residues without relying on pre-existing PTM databases, enabling mapping of both known and novel modification sites.