Raw data related to DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination

Published: 10-09-2020| Version 2 | DOI: 10.17632/sxpfkty7dw.2
Syed Feroj Ahmed,
Lori Buetow,
Danny Huang


Crosstalk between ubiquitination and ADP-ribosylation regulates spatio-temporal recruitment of key players during DNA damage repair (DDR). The Deltex family of ubiquitin ligases (DTX1–4 and DTX3L), are characterized by a RING domain followed by a C-terminal domain (DTC) of unknown function; four Deltex proteins have other domains or partner proteins for binding poly-ADP-ribose (PAR), suggesting a role for these proteins in mediating crosstalk between ubiquitination and ADP-ribosylation. Here, we use two label-free mass spectrometry techniques to identify substrates of human DTX2 and uncover a new ADP-ribose-binding domain that facilitates PAR-dependent ubiquitination.