PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1706595-0	1991	Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which "buries" Ser-378, its site of phosphorylation by protein kinase A. Activation of blood platelets by thrombin was previously shown to specifically release protein kinase A, which in human plasma singles out and phosphorylates one protein, identified as vitronectin.	Serine	122-125	vitronectin	Homo sapiens	51-62	
1706595-0	1991	Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which "buries" Ser-378, its site of phosphorylation by protein kinase A. Activation of blood platelets by thrombin was previously shown to specifically release protein kinase A, which in human plasma singles out and phosphorylates one protein, identified as vitronectin.	Serine	122-125	vitronectin	Homo sapiens	365-376	
1706595-3	1991	1 mol/mol), that it is targeted to one site (Ser-378) at the C-terminal edge of the heparin-binding domain, and that it distinguishes between the two physiologically occurring forms of vitronectin: the one-chain (75 kDa) form, and the nicked two-chain (65 + 10 kDa) form, held together by an interchain disulphide bridge.	Serine	45-48	vitronectin	Homo sapiens	185-196	
1706595-5	1991	Cleavage of the Arg-379-Ala-380 bond results therefore in a conformationally distinct form of vitronectin in which Ser-378 is "buried".	Serine	115-118	vitronectin	Homo sapiens	94-105	
1706595-6	1991	This is demonstrated by our finding that Ser-378 is present in the 65 kDa chain of clipped vitronectin but inaccessible to phosphorylation at physiological pH.	Serine	41-44	vitronectin	Homo sapiens	91-102