y-mtPTM

y-mtPTM catalogs posttranslational modifications (PTMs) of mitochondrial proteins in Saccharomyces cerevisiae, consolidating nearly 20,000 modified amino acid positions across approximately 20 PTM types for use in mitochondrial proteome research.

Key Features:

• Extensive coverage: Consolidates nearly 20,000 modified amino acid positions across approximately 20 types of PTMs in yeast mitochondrial proteins.
• PTM types cataloged: Includes specific modifications such as phosphorylation, succinylation, acetylation, and ubiquitination among other PTMs.
• Mass spectrometry integration: Incorporates PTM identifications derived from mass spectrometry datasets for assignment of modification sites.
• Residue mapping and provenance: Maps modified residues to primary sequence positions and 3D structure coordinates and links entries to original research references.

Scientific Applications:

• Studies of mitochondrial function: Enables investigation of how PTMs influence mitochondrial processes in Saccharomyces cerevisiae.
• Proteomic complexity analysis: Supports analysis of the diversity and distribution of PTMs to characterize mitochondrial proteome complexity.
• Functional significance of isoforms: Facilitates exploration of biochemical properties and functional implications of protein isoforms arising from PTMs.

Methodology:

Integration of PTM data identified by mass spectrometry to compile and map modified amino acid positions in yeast mitochondrial proteins.