PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18258633-8	2008	The replacement of the residues of aspartic acid in position 5 or those of alanine in position 6 in the sequence of p10mer resulted in peptides with no activity in the activation experiments.	Aspartic Acid	35-48	S100 calcium binding protein A10	Homo sapiens	116-119	
6626500-1	1983	Kinetic evidence for involvement of aspartic acid at position P10.	Aspartic Acid	36-49	S100 calcium binding protein A10	Homo sapiens	62-65	
12506111-7	2003	We have found that cleavage of procaspase-9 at Asp(330) to generate p35, p10 or p37, p10 forms resulted in a significant increase (up to 8-fold) in apoptosome activity compared with p35/p12.	Aspartic Acid	47-50	S100 calcium binding protein A10	Homo sapiens	73-76	
12506111-7	2003	We have found that cleavage of procaspase-9 at Asp(330) to generate p35, p10 or p37, p10 forms resulted in a significant increase (up to 8-fold) in apoptosome activity compared with p35/p12.	Aspartic Acid	47-50	S100 calcium binding protein A10	Homo sapiens	85-88	
12506111-9	2003	In addition, cleavage at Asp(330) exposed a novel p10 NH(2)-terminal peptide motif (AISS) that retained the ability to mediate XIAP inhibition of caspase-9.	Aspartic Acid	25-28	S100 calcium binding protein A10	Homo sapiens	50-53