TY - JOUR
T1 - ProteoSushi
T2 - A Software Tool to Biologically Annotate and Quantify Modification-Specific, Peptide-Centric Proteomics Data Sets
AU - Seymour, Robert W.
AU - van der Post, Sjoerd
AU - Mooradian, Arshag D.
AU - Held, Jason M.
N1 - Publisher Copyright:
© 2021 American Chemical Society
PY - 2021/7/2
Y1 - 2021/7/2
N2 - Large-scale proteomic profiling of protein post-translational modifications has provided important insights into the regulation of cell signaling and disease. These modification-specific proteomics workflows nearly universally enrich modified peptides prior to mass spectrometry analysis, but protein-centric proteomic software tools have many limitations evaluating and interpreting these peptide-centric data sets. We, therefore, developed ProteoSushi, a software tool tailored to analysis of each modified site in peptide-centric proteomic data sets that is compatible with any post-translational modification or chemical label. ProteoSushi uses a unique approach to assign identified peptides to shared proteins and genes, minimizing redundancy by prioritizing shared assignments based on UniProt annotation score and optional user-supplied protein/gene lists. ProteoSushi simplifies quantitation by summing or averaging intensities for each modified site, merging overlapping peptide charge states, missed cleavages, spectral matches, and variable modifications into a single value. ProteoSushi also annotates each PTM site with the most up-to-date biological information available from UniProt, such as functional roles or known modifications, the protein domain in which the site resides, the protein’s subcellular location and function, and more. ProteoSushi has a graphical user interface for ease of use. ProteoSushi’s flexibility and combination of analysis features streamlines peptide-centric data processing and knowledge mining of large modification-specific proteomics data sets.
AB - Large-scale proteomic profiling of protein post-translational modifications has provided important insights into the regulation of cell signaling and disease. These modification-specific proteomics workflows nearly universally enrich modified peptides prior to mass spectrometry analysis, but protein-centric proteomic software tools have many limitations evaluating and interpreting these peptide-centric data sets. We, therefore, developed ProteoSushi, a software tool tailored to analysis of each modified site in peptide-centric proteomic data sets that is compatible with any post-translational modification or chemical label. ProteoSushi uses a unique approach to assign identified peptides to shared proteins and genes, minimizing redundancy by prioritizing shared assignments based on UniProt annotation score and optional user-supplied protein/gene lists. ProteoSushi simplifies quantitation by summing or averaging intensities for each modified site, merging overlapping peptide charge states, missed cleavages, spectral matches, and variable modifications into a single value. ProteoSushi also annotates each PTM site with the most up-to-date biological information available from UniProt, such as functional roles or known modifications, the protein domain in which the site resides, the protein’s subcellular location and function, and more. ProteoSushi has a graphical user interface for ease of use. ProteoSushi’s flexibility and combination of analysis features streamlines peptide-centric data processing and knowledge mining of large modification-specific proteomics data sets.
KW - PTMs
KW - acetylation
KW - bioinformatics
KW - chemoproteomics
KW - modification-specific proteomics
KW - phosphorylation
KW - post-translational modifications
KW - proteomics
KW - proteosushi
UR - http://www.scopus.com/inward/record.url?scp=85108439119&partnerID=8YFLogxK
U2 - 10.1021/acs.jproteome.1c00203
DO - 10.1021/acs.jproteome.1c00203
M3 - Article
C2 - 34056901
AN - SCOPUS:85108439119
SN - 1535-3893
VL - 20
SP - 3621
EP - 3628
JO - Journal of Proteome Research
JF - Journal of Proteome Research
IS - 7
ER -