PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30723194-4	2019	High-resolution crystal structures of Zn2+-bound ERp44 reveal that Zn2+ binds to a conserved histidine-cluster.	Histidine	93-102	endoplasmic reticulum protein 44	Homo sapiens	49-54	
30723194-7	2019	Histidine mutations in the Zn2+-binding sites compromise ERp44 activity and localization.	Histidine	0-9	endoplasmic reticulum protein 44	Homo sapiens	57-62	
25097228-4	2014	Here, we show that conserved histidine residues in the C-terminal tail also regulate ERp44 in vivo.	Histidine	29-38	endoplasmic reticulum protein 44	Homo sapiens	85-90	
28373561-11	2017	We propose that the protonation states of the essential histidines regulate the ERp44-client interaction by altering the C-tail dynamics and surface electrostatic potential of ERp44.	Histidine	56-66	endoplasmic reticulum protein 44	Homo sapiens	80-85	
28373561-11	2017	We propose that the protonation states of the essential histidines regulate the ERp44-client interaction by altering the C-tail dynamics and surface electrostatic potential of ERp44.	Histidine	56-66	endoplasmic reticulum protein 44	Homo sapiens	176-181