. Author manuscript; available in PMC: 2018 Aug 1.

Published in final edited form as: Trends Cell Biol. 2017 Apr 19;27(8):608–620. doi: 10.1016/j.tcb.2017.03.004

Table 1.

Metazoan target proteins of AMPylases

Species	Protein	Target(s)	Site(s) of modification	Consequence on cell signaling
*Histophilus somnii*	IbpA	Rho GTPases (Rac1, Cdc42, RhoA, RhoB, RhoC, RhoG, TC10)	Tyr32 of switch I region	cytotoxic; interferes with regulation of cytoskeleton
*Pasteurella multocida*	PfhB2	Rho GTPases (Cdc42, Rac1, RhoA, RhoG, TC10)	Tyr32 of switch I region	cytotoxic; interferes with regulation of cytoskeleton
*Vibrio parahaemolyticus*	VopS	Rho GTPases (Rac1, Cdc42, RhoA)	Thr35 of switch I region	cytotoxic; interferes with regulation of cytoskeleton
*Legionella pneumophila*	DrrA	Rab-1b	Tyr77 of switch II region	inhibits proper Rab- 1b downstream signaling
*Bartonella henselae*	BepA	40kDa protein / 50kDa protein	n.d.	increase in cellular cAMP levels
*Bartonella rochalimae*	Bep2	vimentin	Tyr53	n.d.
*Homo sapiens*	HYPE/FICD	BiP, Hsp70, Eef1A, Hsp40	BiP: Ser365/Thr3 66 or Thr518; Hsp70: n.d.; Eef1A:Thr26 1; HSP40: n.d.	BiP AMPylation negatively regulates UPR activation in the ER; HSP40 and HSP70 AMPylation interferes with chaperoning activities
*Drosophila melanogaster*	dfic	BiP	Thr366	Absence of dfic renders flies blind; BiP AMPylation negatively regulates UPR activation in ER
*Caenerobhaditis elegans*	Fic-1	Hsp-1, Hsp-3, Eef-1A.2	HSP-1: n.d.; Hsp-3: Thr176; eEF1A: Thr269, Thr432	AMPylation levels directly correlate to pathogen tolerance; HSP-1 and HSP-3 AMPylation interferes with cellular chaperoning machineries (cytosol, ER)