Fig. 5: Site-specific properties of ADPr in HPF1 and ARH3 knockout cells.
From: The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
a Overview of the abundance fraction of ADPr modifying serine residues. n = 4 cell culture replicates, data are presented as mean values ± SD. b As a, but visualizing the fraction of serine ADPr in (lysine–serine) KS motifs. c Pie-chart analysis showing the distribution of ADPr sites across different amino acid residue types. d IceLogo analysis visualizes relative preference for ADPr to be targeted to different amino acid residue types. Amino acid residues displayed above the line were enriched for HPF1 KO, and those displayed below were enriched for ARH3 KO. Displayed amino acids were determined to be significantly changed at p < 0.05 as determined by two-tailed Student’s t testing using iceLogo software77, n = 50 and n = 1054 HPF1 KO and ARH3 KO ADP-ribosylation sites, respectively. p-Values for all amino acids were re-assessed using via two-tailed Fisher Exact testing with Benjamini–Hochberg correction, and are listed in the Source Data. Gray: not significantly different in the second statistical test. e Term enrichment analysis visualizing the Gene Ontology subcellular localization of ADPr target proteins across experimental conditions. n = 99 (control), n = 35 (HPF1 KO), n = 575 (ARH3 KO), n = 429 (control + H2O2), n = 45 (HPF1 KO + H2O2), n = 756 (ARH3 KO + H2O2) ADPr target proteins, tested versus a background of n = 21,297 proteins, with Gene Ontology subcellular localization annotated for n = 402 chromosomal, n = 5298 nuclear, n = 1166 mitochondrial, and n = 5027 cytoplasmic proteins. Significance was determined via two-tailed Fisher Exact testing with Benjamini–Hochberg correction for multiple hypotheses testing, *p < 0.05. Individual p-values are listed in the Source Data. Source data are provided as a Source Data file.
