. Author manuscript; available in PMC: 2018 Nov 16.

Published in final edited form as: Cell Chem Biol. 2017 Sep 28;24(11):1388–1400.e7. doi: 10.1016/j.chembiol.2017.08.017

Table 1.

High-occupancy targets of inhibitors 1–3 identified by competitive ABPP-SILAC.

Gene name	Protein Class^A	Active Site Cysteine^B	Competed Target^C
CHEK2	Kinase	Yes^*	3
CLN3	Lysosomal membrane protein	-	3
CTSC	Cysteine Protease	Yes	1
CTSL1	Cysteine Protease	Yes	1
CTSH	Cysteine Protease	Yes	1
EGFR	Kinase	Yes	1, 2, 3
ERBB2	Kinase	Yes	1,2
IFI30	Thiol Reductase	Yes	1
NT5DC1	5'-Nucleotidase	-^*	3
RFTN1	Lipid raft protein	-	1
RTN4	ER membrane protein	-^*	3
SCARB1	Lipid receptor protein	-	1
TEC	Kinase	Yes	1, 2, 3
TEX264	Uncharacterized protein	-	1
TNK1	Kinase	Yes	3
TRMT61A	tRNA (adenine-N(1)-)-methyltransferase	-^*	3

Targets with a minimum of 80% competition (heavy:light ratios > 5) with at least one parent inhibitor are shown and described by:

^(A)

protein class,

^(B)

presence of an active-site cysteine or a ligandable cysteine (asterisks, (Backus et al., 2016)), and

^(C)

inhibitors that engage the protein target with high-occupancy.

, proteins also targeted by fragment electrophiles in a global chemical proteomic analysis (Backus et al., 2016).