PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16877378-4	2006	Here we show that cysteine substitution at Ala-395, Ala-367, and Ala-440 results in functional single and double cysteine transporters and that in the absence of glutamate or dl-threo-beta-benzyloxyaspartate (dl-TBOA), A395C in the highly conserved TM7 can be cross-linked to A367C in HP1 and to A440C in HP2.	Cysteine	18-26	chromobox 5	Homo sapiens	285-288	
25267718-4	2014	Using copper(II) (1,10-phenanthroline)3 (CuPh) for cross-linking cysteine pairs, we found strong inhibition of transport when A243C (TM4) was combined with S366C (HP1), I453C (HP2), or T456C (HP2).	Cysteine	65-73	chromobox 5	Homo sapiens	163-166	
20675861-3	2010	Here, we have identified intermolecular disulfide bond formation of HP1 cysteines in an isoform-specific manner.	Cysteine	72-81	chromobox 5	Homo sapiens	68-71	
20675861-4	2010	Cysteine 133 in HP1alpha and cysteine 177 in HP1gamma were involved in intermolecular homodimerization.	Cysteine	0-8	chromobox 5	Homo sapiens	16-24	
20675861-5	2010	Although both HP1alpha and HP1gamma contain reactive cysteine residues, only HP1gamma readily and reversibly formed disulfide homodimers under oxidative conditions.	Cysteine	53-61	chromobox 5	Homo sapiens	14-22	
2019582-1	1991	HP-1 is a 30-residue cysteine- and arginine-rich peptide of the human neutrophil primary granule and is the most abundant human representative of the family of peptides variously called defensins and corticostatins.	Cysteine	21-29	chromobox 5	Homo sapiens	0-4