PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12270713-5	2002	Previously, we solved the NMR structure of the central proline-rich P-domain of CRT comprising residues 189-288.	Proline	55-62	calreticulin	Homo sapiens	80-83	
24100026-4	2013	Although both interactions involve the glycan-binding site or its vicinity, the arm-like proline-rich (P-) domain of calreticulin contributes to binding non/deglycosylated proteins.	Proline	89-96	calreticulin	Homo sapiens	117-129	
34050860-2	2021	The structure of Calr is unusual, reflecting different functions of the protein: a proline-rich beta-hairpin arm and an acidic C-terminal tail protrude from a globular core, composed of a beta-sheet sandwich and an alpha-helix.	Proline	83-90	calreticulin	Homo sapiens	17-21	
9521669-11	1998	Finally, deletion mutagenesis of calnexin and calreticulin identified a central proline-rich region characterized by two tandem repeat motifs as a segment capable of binding oligosaccharide.	Proline	80-87	calreticulin	Homo sapiens	46-58	
8006073-3	1994	Here we demonstrate that calreticulin can be co-localized by immunofluorescence as well as co-purified with integrins, that recombinant calreticulin can also interact with integrins, and that the interaction occurs predominantly via the N-domain of calreticulin, to a much lesser extent with the C-domain, but not at all with the proline-rich P-domain.	Proline	330-337	calreticulin	Homo sapiens	25-37	
8006073-3	1994	Here we demonstrate that calreticulin can be co-localized by immunofluorescence as well as co-purified with integrins, that recombinant calreticulin can also interact with integrins, and that the interaction occurs predominantly via the N-domain of calreticulin, to a much lesser extent with the C-domain, but not at all with the proline-rich P-domain.	Proline	330-337	calreticulin	Homo sapiens	136-148	
8006073-3	1994	Here we demonstrate that calreticulin can be co-localized by immunofluorescence as well as co-purified with integrins, that recombinant calreticulin can also interact with integrins, and that the interaction occurs predominantly via the N-domain of calreticulin, to a much lesser extent with the C-domain, but not at all with the proline-rich P-domain.	Proline	330-337	calreticulin	Homo sapiens	136-148