PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18702519-5	2008	We previously reported the serendipitous creation of a protein, His15Asp histidine-containing protein (HPr), which undergoes phosphorylation-catalyzed formation of a succinimide whose hydrolysis is seemingly exclusive for aspartate formation.	succinimide	166-177	haptoglobin-related protein	Homo sapiens	103-106	
18702519-6	2008	Here, through the high-resolution structure of postsuccinimide His15Asp HPr, we confirm the absence of isoaspartate residues and propose mechanisms for phosphorylation-catalyzed succinimide formation and its directed hydrolysis to aspartate.	succinimide	51-62	haptoglobin-related protein	Homo sapiens	72-75	
18702519-7	2008	His15Asp HPr represents the first characterized protein example of an isoaspartate-free succinimide and lends credence to the hypothesis that intramolecular cyclization could represent a physiological mechanism of autophosphatase activity.	succinimide	88-99	haptoglobin-related protein	Homo sapiens	9-12	
12068021-8	2002	Deletion of the C-terminal residue of this protein does not influence the ability for phosphorylation or ring formation, but it does allow for isoaspartyl formation, verifying a succinimide as the cyclic intermediate in H15D HPr.	succinimide	178-189	haptoglobin-related protein	Homo sapiens	225-228