Extended Data Fig. 6: Phosphoregulation of HNRNPA1. | Nature Chemical Biology

Extended Data Fig. 6: Phosphoregulation of HNRNPA1.

From: Systematic discovery of biomolecular condensate-specific protein phosphorylation

Extended Data Fig. 6: Phosphoregulation of HNRNPA1.The alternative text for this image may have been generated using AI.

(a) Visualization of the RNA-bound fraction of identified phosphopeptides and unmodified protein of HNRNPA1. Top: schematic representation of the protein with its domains and known phosphosites from Uniprot is shown. Median RNA-bound fraction (of three independent measurements, y-axis) of phosphopeptides (solid lines with points representing the site) and unmodified protein (dotted line) in log2 scale is represented along the linear sequence of the protein (x-axis). (b) IUpred, prediction of intrinsic disorder (top) and net charge per residue (NCPR, calculated over 5 aa window) along the linear sequence of HNRNPA1. (c) Barplot representing the relative protein abundance (in log2 scale, y-axis) of heterologously expressed GFP-tagged phosphomutants (x-axis) of HNRNPA1 (proxy for intracellular protein expression) compared to the wild type (wt) from three independent biological replicates. (d) Comparison of coefficient of variation (CV, in log2 scale) of intensity with the mean intensity of (segmented-) nucleus (n > 100) from two independent trials. (f) Comparison of coefficient of variation (CV) of intensity with the area of the (segmented-) nucleus (n > 100) from two independent trials.

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