Cellular BioAnalysis

Highlights • Identification of novel kinase interactors by BioID. • Applying two orthogonal filters, kinase perturbation and phosphorylation motif. • Identification of novel CK2 and PKA substrates. • A universal method for the identification of endogenous substrates for all kinases. Abstract Mass-spectrometry-based phosphoproteomics can identify more than 10,000 phosphorylated sites in a single experiment.

For reproducibility and sustainability of scientific research, the public sharing of raw data obtained by researchers is of paramount significance (1). The FAIRness (Findable, Accessible, Interoperable and Re-usable) of datasets is the most important principle that supports open science in the future (1–3). For genomics, the sharing of raw data from next generation sequencers (NGS) is implemented through public repositories (4).

Emerging evidence indicates that heterogeneity in ribosome composition can give rise to specialized functions. Until now, research mainly focused on differences in core ribosomal proteins and associated factors. The effect of posttranslational modifications has not been studied systematically. Analyzing ribosome heterogeneity is challenging because individual proteins can be part of different subcomplexes (40S, 60S, 80S, and polysomes).