PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25905420-6	2000	MCT10 also transports aromatic amino acids and its physiological role in tissue TH transport remains to be established.	Amino Acids, Aromatic	22-42	solute carrier family 16 member 10	Homo sapiens	0-5	
18337592-2	2008	Monocarboxylate transporter 10 (MCT10) has been reported to transport aromatic amino acids but not iodothyronines.	Amino Acids, Aromatic	70-90	solute carrier family 16 member 10	Homo sapiens	0-30	
18337592-2	2008	Monocarboxylate transporter 10 (MCT10) has been reported to transport aromatic amino acids but not iodothyronines.	Amino Acids, Aromatic	70-90	solute carrier family 16 member 10	Homo sapiens	32-37	
11827462-7	2002	Expression of human TAT1 in Xenopus laevis oocytes demonstrated the Na+-independent transport of tryptophan, tyrosine, phenylalanine, and L-dopa, indicating that human TAT1 is a transporter subserving system T. Because human TAT1 is proposed to be crucial to the efficient absorption of aromatic amino acids from intestine and kidney, its defect could be involved in the disruption of aromatic amino-acid transport, such as in blue diaper syndrome.	Amino Acids, Aromatic	287-307	solute carrier family 16 member 10	Homo sapiens	20-24	
11827462-7	2002	Expression of human TAT1 in Xenopus laevis oocytes demonstrated the Na+-independent transport of tryptophan, tyrosine, phenylalanine, and L-dopa, indicating that human TAT1 is a transporter subserving system T. Because human TAT1 is proposed to be crucial to the efficient absorption of aromatic amino acids from intestine and kidney, its defect could be involved in the disruption of aromatic amino-acid transport, such as in blue diaper syndrome.	Amino Acids, Aromatic	287-307	solute carrier family 16 member 10	Homo sapiens	168-172	
11827462-7	2002	Expression of human TAT1 in Xenopus laevis oocytes demonstrated the Na+-independent transport of tryptophan, tyrosine, phenylalanine, and L-dopa, indicating that human TAT1 is a transporter subserving system T. Because human TAT1 is proposed to be crucial to the efficient absorption of aromatic amino acids from intestine and kidney, its defect could be involved in the disruption of aromatic amino-acid transport, such as in blue diaper syndrome.	Amino Acids, Aromatic	287-307	solute carrier family 16 member 10	Homo sapiens	168-172	
11827462-7	2002	Expression of human TAT1 in Xenopus laevis oocytes demonstrated the Na+-independent transport of tryptophan, tyrosine, phenylalanine, and L-dopa, indicating that human TAT1 is a transporter subserving system T. Because human TAT1 is proposed to be crucial to the efficient absorption of aromatic amino acids from intestine and kidney, its defect could be involved in the disruption of aromatic amino-acid transport, such as in blue diaper syndrome.	Amino Acids, Aromatic	385-404	solute carrier family 16 member 10	Homo sapiens	20-24	
11827462-7	2002	Expression of human TAT1 in Xenopus laevis oocytes demonstrated the Na+-independent transport of tryptophan, tyrosine, phenylalanine, and L-dopa, indicating that human TAT1 is a transporter subserving system T. Because human TAT1 is proposed to be crucial to the efficient absorption of aromatic amino acids from intestine and kidney, its defect could be involved in the disruption of aromatic amino-acid transport, such as in blue diaper syndrome.	Amino Acids, Aromatic	385-404	solute carrier family 16 member 10	Homo sapiens	168-172	
11827462-7	2002	Expression of human TAT1 in Xenopus laevis oocytes demonstrated the Na+-independent transport of tryptophan, tyrosine, phenylalanine, and L-dopa, indicating that human TAT1 is a transporter subserving system T. Because human TAT1 is proposed to be crucial to the efficient absorption of aromatic amino acids from intestine and kidney, its defect could be involved in the disruption of aromatic amino-acid transport, such as in blue diaper syndrome.	Amino Acids, Aromatic	385-404	solute carrier family 16 member 10	Homo sapiens	168-172	
17574005-7	2007	Although it was long hypothesized that a T-type amino acid transporter also transports iodothyronines, it only recently became clear that MCT10 is involved in the bidirectional transport of aromatic amino acids and iodothyronines.	Amino Acids, Aromatic	190-210	solute carrier family 16 member 10	Homo sapiens	138-143	
15918515-5	2005	The hLAT2 transports all neutral amino acids and hTAT1 transports aromatic amino acids.	Amino Acids, Aromatic	66-86	solute carrier family 16 member 10	Homo sapiens	49-54	
15918515-6	2005	The basolateral location of the hLAT2 and hTAT1 proteins in the renal proximal tubule as well as the amino acid transport activity of hLAT2 and hTAT1 suggests that these transporters contribute to the renal reabsorption of neutral and aromatic amino acids in the basolateral domain of epithelial proximal tubule cells, respectively.	Amino Acids, Aromatic	235-255	solute carrier family 16 member 10	Homo sapiens	42-47	
15918515-6	2005	The basolateral location of the hLAT2 and hTAT1 proteins in the renal proximal tubule as well as the amino acid transport activity of hLAT2 and hTAT1 suggests that these transporters contribute to the renal reabsorption of neutral and aromatic amino acids in the basolateral domain of epithelial proximal tubule cells, respectively.	Amino Acids, Aromatic	235-255	solute carrier family 16 member 10	Homo sapiens	144-149	
15727804-10	2005	TAT1, also called MCT10, has been characterized to transport aromatic amino acids but no iodothyronines.	Amino Acids, Aromatic	61-81	solute carrier family 16 member 10	Homo sapiens	0-4	
15727804-10	2005	TAT1, also called MCT10, has been characterized to transport aromatic amino acids but no iodothyronines.	Amino Acids, Aromatic	61-81	solute carrier family 16 member 10	Homo sapiens	18-23	
23177990-2	2012	MCT1 through MCT4 (MCTs 1-4) are H(+)-coupled monocarboxylate transporters, MCT8 and MCT10 transport thyroid hormone and aromatic amino acids, while the substrate specificity and function of other MCTs have yet to be determined.	Amino Acids, Aromatic	121-141	solute carrier family 16 member 10	Homo sapiens	85-90	
21835054-4	2011	They transport TH as secondary substrates and include the aromatic amino acid transporting MCT10, the organic anion transporting polypeptides (e.g. OATP1C1, OATP1A2, OPTP1A4) and the large neutral amino acid transporters (LAT1 and LAT2).	Amino Acids, Aromatic	58-77	solute carrier family 16 member 10	Homo sapiens	91-96	
25390336-3	2014	Out of 14 known mammalian MCTs, six isoforms have been functionally characterized to transport monocarboxylates and short chain fatty acids (MCT1-4), thyroid hormones (MCT8, -10) and aromatic amino acids (MCT10).	Amino Acids, Aromatic	183-203	solute carrier family 16 member 10	Homo sapiens	205-210