PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15454439-4	2004	In the Kir3.1/Kir3.4 channel, mutation of an extracellular arginine residue, R155, in the Kir3.4 subunit markedly reduced K+ activation of the channel.	Arginine	59-67	potassium inwardly rectifying channel subfamily J member 3	Homo sapiens	7-13	
15454439-4	2004	In the Kir3.1/Kir3.4 channel, mutation of an extracellular arginine residue, R155, in the Kir3.4 subunit markedly reduced K+ activation of the channel.	Arginine	59-67	potassium inwardly rectifying channel subfamily J member 5	Homo sapiens	14-20	
15454439-4	2004	In the Kir3.1/Kir3.4 channel, mutation of an extracellular arginine residue, R155, in the Kir3.4 subunit markedly reduced K+ activation of the channel.	Arginine	59-67	potassium inwardly rectifying channel subfamily J member 5	Homo sapiens	90-96	
15454439-9	2004	Mutation of an extracellular histidine residue, H508, that mediates the inhibitory effect of protons on Kv1.4 current, abolished both K+ activation and the enhancement of K+ activation at acidic pH.	Histidine	29-38	potassium voltage-gated channel subfamily A member 4	Homo sapiens	104-109	
15454439-9	2004	Mutation of an extracellular histidine residue, H508, that mediates the inhibitory effect of protons on Kv1.4 current, abolished both K+ activation and the enhancement of K+ activation at acidic pH.	ranitidine hydrochloride	48-52	potassium voltage-gated channel subfamily A member 4	Homo sapiens	104-109	
15454439-11	2004	Furthermore, these data suggest that, at acidic pH, protonation of H508 inhibits current through the Kv1.4 channel by decreasing K+ access to the selectivity filter, thus favoring the collapse of the selectivity filter.	ranitidine hydrochloride	67-71	potassium voltage-gated channel subfamily A member 4	Homo sapiens	101-106