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. 2017 Feb 3;8:23. doi: 10.3389/fphar.2017.00023

Figure 1.

Figure 1

UGT1A interaction network investigated by untargeted proteomics. (A) The nine UGT1A enzymes are distinguished by the amino acid sequence of their substrate binding domain (unique peptides) whereas they share identical C-terminal co-substrate and transmembrane domains (common peptides). The anti-UGT1A antibody used in this study was raised against a C-terminal peptide common to all nine UGT1A enzymes but does not recognize the main spliced alternative isoforms 2 or UGT1A_i2s. (B) Experimental approach to establish endogenous UGT1A protein interactomes in drug metabolizing tissues and in the colon cancer cell model HT-29. Immunoprecipitation of UGT1A enzymes was conducted with the anti-UGT1A antibody. The numbers of common and unique UGT1A protein partners identified by mass spectrometry and above confidence threshold are represented in the Venn diagrams. Datasets were established on a minimum of two biological replicates. A Venn diagram for the 4 matrices is presented in Supplementary Figure 2. A list of proteins in each group is provided in Supplementary Table 3.