Sign in
BioinformaticsbioRxiv
Preprint

Omic-Sig: Utilizing Omics Data to Explore and Visualize Kinase-Substrate Interactions

T. Mamie LihiD, David J. ClarkiD, Hui ZhangiD

Abstract

Protein phosphorylation is one of the most prevalent post-translational modifications, resulting from the activity of protein kinases phosphorylating specific substrates. Multiple cellular processes are regulated via protein phosphorylation, with aberrant signaling driven by dysregulation of phosphorylation events and associating with disease progression (e.g., cancer). Mass spectrometry-based phosphoprotomics approaches can be leveraged for studying alterations of kinase-substrate activity in clinical cohorts. However, the information gained via interrogation of global proteomes and transcriptomes can offer additional insight into the interaction of kinases and their respective substrates. Therefore, we have developed the bioinformatics, data visualization software tool, Omic-Sig, which can stratify prominent phospho-substrates and their associated kinases based on differential abundances between case and control samples (e.g., tumors and their normal adjacent tissues from a cancer cohort) in a multi-omics fashion. Omic-Sig is available at https://github.com/hzhangjhu/Omic-Sig.

PDFDOICode

02 /Specification & Classification

Click any tag to browse matching papers

Reproducibility ledger

Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.

Sign in to file a reproducibility report.

Similarity Map
SelectedSame fieldCross-field
THISMaier '25Wirbel '16Creixell '22Ayati '19Garrido‐Rod '24Kim '20
70% semantic matchBioinformatics
Benjamin Dominik Maier, Borgþór Pétursson, Alessandro Lussana+1 more·Molecular & Cellular Proteomics·May 15, 2025· 10 citations