PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17548063-1	2007	SULT1A3 is an enzyme that catalyzes the sulfonation of many endogenous and exogenous phenols and catechols.	Phenols	85-92	sulfotransferase family 1A member 3	Homo sapiens	0-7	
10441143-7	1999	The mutation E146A in SULT1A3 resulted in a SULT1A1-like protein with respect to the Michaelis constant for both simple phenols and monoamine compounds.	Phenols	120-127	sulfotransferase family 1A member 3	Homo sapiens	22-29	
10608851-4	1999	To further our understanding of the molecular basis for the unique substrate selectivity of this enzyme, we have solved the crystal structure of human SULT1A3, complexed with 3"-phosphoadenosine 5"-phosphate (PAP), at 2.5 A resolution and carried out quantitative structure-activity relationship (QSAR) analysis with a series of phenols and catechols.	Phenols	329-336	sulfotransferase family 1A member 3	Homo sapiens	151-158	
14502490-3	2003	The evaluated SULT1A3 substrate data set consisted of 95 different substituted phenols, catechols, catecholamines, steroids, and related structures for which the K(m) values were available.	Phenols	79-86	sulfotransferase family 1A member 3	Homo sapiens	14-21