PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25524207-6	2015	Moreover, proline mutations in the upper hinge region and removal of the Fc glycan enhanced the FVIII-mimetic activity, suggesting that flexibility of the upper hinge region and the Fc portion structure are important for the FVIII-mimetic activity.	Proline	10-17	coagulation factor VIII	Homo sapiens	96-101	
25524207-6	2015	Moreover, proline mutations in the upper hinge region and removal of the Fc glycan enhanced the FVIII-mimetic activity, suggesting that flexibility of the upper hinge region and the Fc portion structure are important for the FVIII-mimetic activity.	Proline	10-17	coagulation factor VIII	Homo sapiens	225-230	
1378653-3	1992	It was predicted to be immunogenic because a Hopp-Woods hydrophilicity analysis of the amino acid sequence of FVIII showed it to be very hydrophilic, and it contained a proline.	Proline	169-176	coagulation factor VIII	Homo sapiens	110-115	
3150544-2	1988	One of these new derivatives, FVIII delta II, in which amino acids 771(pro)-1666(asp) have been deleted, no longer contains the protease cleavage site at amino acid position 1648(arg)-1649(glu) known to be involved in the initial step of FVIII processing.	Proline	71-74	coagulation factor VIII	Homo sapiens	30-35	
6626500-2	1983	The following peptide was synthesized by classical methods in solution: Ac-Asp-Phe-Leu-Ala-Glu-Gly-Gly-Gly-Val-Arg-Gly-Pro-Arg-Val-NHCH3 (F-8).	Proline	119-122	coagulation factor VIII	Homo sapiens	138-141