PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33799982-2	2021	Loss-of-function mutations in ATP13A2 result in lysosomal deficiency as a consequence of impaired lysosomal export of the polyamines spermine/spermidine.	Spermidine	142-152	ATPase cation transporting 13A2	Homo sapiens	30-37	
22265822-7	2012	Acridine orange fluorescence intensity suggested that ATP13A2 induced the expansion of acidic vesicles that become more alkaline upon external addition of spermidine.	Spermidine	155-165	ATPase cation transporting 13A2	Homo sapiens	54-61	
23205587-0	2013	Parkinson"s disease-associated human P5B-ATPase ATP13A2 increases spermidine uptake.	Spermidine	66-76	ATPase cation transporting 13A2	Homo sapiens	48-55	
22265822-8	2012	Polyamine uptake is proposed to be initiated by a plasma membrane carrier followed by sequestration into acidic vesicles of the late endocytic compartment through an unidentified active mechanism; because ATP13A2 is located in lysosomes and late endosomes, our results open the possibility that ATP13A2 could be one of those active transporters capable of transporting polyamines like spermidine as well as its toxic analog paraquat.	Spermidine	385-395	ATPase cation transporting 13A2	Homo sapiens	205-212