PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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