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. 2016 Aug 9;45(Database issue):D204–D209. doi: 10.1093/nar/gkw706

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© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — (A) ADP-ribosylated proteins are significantly enriched in non-membranous compartments, such as the nucleolus (38) and stress granules (39), as determined by Fisher's Exact Test, with significant P-values highlighted in red. These organelle proteomes are also enriched in low complexity domain-containing proteins. A similar analysis was performed with proteins that have experimentally validated N-glyosylation sites (N-GlyocsylDB) deposited in dbPTM (46). As expected, N-glyocsylated proteins were found enriched in the golgi, endoplasmic reticulum, lysosomes and membrane fractions as defined by UniProtKB (51). No enrichment of experimentally validated ADP-ribosylation sites or N-glycosylation sites was found in the mitochondrial proteome (52). (B) Low complexity domain-containing proteins are significantly enriched in ADPriboDB in contrast to N-GlycosylDB, suggesting a link between ADP-ribosylation and low complexity domain-containing proteins.