PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12475240-10	2002	Inactivation of the human ASBT due to MTS modification of cysteine 270 was shown to be largely abolished when the transporter was preincubated with 2164U90, suggesting that the binding of this benzothiazepine is in the vicinity of position 270.	Cysteine	58-66	solute carrier family 10 member 2	Homo sapiens	26-30	
15952798-0	2005	Site-directed mutagenesis and use of bile acid-MTS conjugates to probe the role of cysteines in the human apical sodium-dependent bile acid transporter (SLC10A2).	Cysteine	83-92	solute carrier family 10 member 2	Homo sapiens	153-160	
15952798-2	2005	Biochemical modification of conserved cysteine residues has suggested their direct involvement in hASBT function.	Cysteine	38-46	solute carrier family 10 member 2	Homo sapiens	98-103	
22354836-3	2012	The ability of electrophilic derivatives to interact with hASBT was evaluated by 2-aminoethyl-methanethiosulfonate (MTSEA)-biotin labeling of thiol groups in TM7 cysteine mutants.	Cysteine	162-170	solute carrier family 10 member 2	Homo sapiens	58-63	
18311924-1	2008	We report the involvement of transmembrane domain 4 (TM4) of hASBT in forming the putative translocation pathway, using cysteine-scanning mutagenesis in conjunction with solvent-accessibility studies using the membrane-impermeant, sulfhydryl-specific methanethiosulfonate reagents.	Cysteine	120-128	solute carrier family 10 member 2	Homo sapiens	61-66	
18311924-2	2008	We individually mutated each of the 21 amino acids in TM4 to cysteine on a fully functional, MTS-resistant C270A-hASBT template.	Cysteine	61-69	solute carrier family 10 member 2	Homo sapiens	113-118	
29198943-4	2018	We generated a cysteine-less form of hASBT by creating point mutations at all 13 endogenous cysteines in a stepwise manner.	Cysteine	15-23	solute carrier family 10 member 2	Homo sapiens	37-42	
34346218-5	2021	The results from the TC uptake assay using N-acetylcysteine suggested that the inhibitory effect of TF2A and TF2B was attributed to the oxidization of their benzotropolone rings and their covalent bonding with ASBT"s cysteine.	Cysteine	217-225	solute carrier family 10 member 2	Homo sapiens	210-214	
34346218-6	2021	TC uptake was reduced in the COS-7 cells expressing recombinant ASBT whose cysteine residues were mutated to alanine.	Cysteine	75-83	solute carrier family 10 member 2	Homo sapiens	64-68	
29198943-4	2018	We generated a cysteine-less form of hASBT by creating point mutations at all 13 endogenous cysteines in a stepwise manner.	Cysteine	92-101	solute carrier family 10 member 2	Homo sapiens	37-42