PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32958253-6	2020	We applied the NMR spectroscopy method to locate the binding area amid the S100A6m (mutant S100A6, cysteine at 3rd position of S100A6 is replaced with serine, C3S) and S100B proteins.	Serine	151-157	S100 calcium binding protein A6	Homo sapiens	75-81	
32958253-6	2020	We applied the NMR spectroscopy method to locate the binding area amid the S100A6m (mutant S100A6, cysteine at 3rd position of S100A6 is replaced with serine, C3S) and S100B proteins.	Serine	151-157	S100 calcium binding protein A6	Homo sapiens	91-97	
30118888-2	2019	This anti-inflammatory effect is inhibited by phosphorylation of PR-A at serine-344 and -345 (pSer344/345-PRA).	Serine	73-79	S100 calcium binding protein A6	Homo sapiens	65-69	
27653036-2	2016	Immunodetection of phosphoserine (pSer) PR forms in term myometrium revealed that the onset of labor is associated with increased phosphorylation of PR-A at serine-345 (pSer345-PRA) and that pSer345-PRA localized to the nucleus of myometrial cells.	Serine	26-32	S100 calcium binding protein A6	Homo sapiens	149-153	
27653036-6	2016	Taken together, the data show that human parturition involves the phosphorylation of PR-A at serine-345 in myometrial cells and that this process is ligand dependent and induced by a proinflammatory stimulus.	Serine	93-99	S100 calcium binding protein A6	Homo sapiens	85-89	
27653036-8	2016	Phosphorylation of PR-A at serine-345 may be an important functional link between tissue-level inflammation and PR-A-mediated functional progesterone withdrawal to trigger parturition.	Serine	27-33	S100 calcium binding protein A6	Homo sapiens	19-23	
27653036-8	2016	Phosphorylation of PR-A at serine-345 may be an important functional link between tissue-level inflammation and PR-A-mediated functional progesterone withdrawal to trigger parturition.	Serine	27-33	S100 calcium binding protein A6	Homo sapiens	112-116	
23880761-4	2013	GSK-3beta-mediated phosphorylation of serine 390 in PR-A regulates its subsequent ubiquitination and protein stability.	Serine	38-44	S100 calcium binding protein A6	Homo sapiens	52-56	
23880761-6	2013	Consistently, reduction of phosphorylation of serine 390 of PR-A and GSK-3beta activity is observed in the Brca1-deficient mammary gland.	Serine	46-52	S100 calcium binding protein A6	Homo sapiens	60-64	
16912968-4	2006	With this combined approach we were able to detect nine calcium-dependent interactions between Arg-Gly-Ser-(RGS)-His6 tagged proteins derived from the library and GST-tagged S100B and S100A6, respectively.	Serine	103-106	S100 calcium binding protein A6	Homo sapiens	184-190	
10628747-9	2000	This was unexpected because Ser 294 and flanking sequences are identical on both proteins, suggesting that a distinct conformation of the N-terminal domain of PR-A inhibits phosphorylation of this site.	Serine	28-31	S100 calcium binding protein A6	Homo sapiens	159-163	
10628747-10	2000	That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B.	Serine	5-8	S100 calcium binding protein A6	Homo sapiens	95-99	
10628747-10	2000	That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B.	Serine	5-8	S100 calcium binding protein A6	Homo sapiens	221-225	
10628747-10	2000	That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B.	Serine	160-163	S100 calcium binding protein A6	Homo sapiens	95-99	
10628747-10	2000	That Ser 294 lies within an inhibitory domain that mediates the unique repressive functions of PR-A raises the possibility that differential phosphorylation of Ser 294 is involved in the distinct functional properties of PR-A and PR-B.	Serine	160-163	S100 calcium binding protein A6	Homo sapiens	221-225