PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
35281082-1	2022	Caspases are a family of cysteine proteases that predominantly cleave their substrates after aspartic acid residues.	Aspartic Acid	93-106	caspase 2	Homo sapiens	0-8	
14599290-8	2004	Like caspase-3, caspase-2 cleaves alphaII-spectrin in vitro at residue Asp-1185.	Aspartic Acid	71-74	caspase 2	Homo sapiens	16-25	
22825847-4	2012	We confirmed that Asp(563) in eukaryotic translation initiation factor 4B (eIF4B) is a cleavage site preferred by caspase-2 not only in COFRADIC setup but also upon co-expression in HEK 293T cells.	Aspartic Acid	18-21	caspase 2	Homo sapiens	114-123	
21726810-4	2011	PIDD-induced Caspase-2 directly cleaves the E3 ubiquitin ligase Mdm2 at Asp 367, leading to loss of the C-terminal RING domain responsible for p53 ubiquitination.	Aspartic Acid	72-75	caspase 2	Homo sapiens	13-22