PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32891431-3	2020	Deletion mutants for RIM8, RIM9, RIM13, RIM20, RIM21 and RIM101 causes yeast cells to be sensitive to calcium stress, but how they regulate calcium sensitivity remain unknown.	Calcium	102-109	Rim21p	Saccharomyces cerevisiae S288C	47-52
32891431-3	2020	Deletion mutants for RIM8, RIM9, RIM13, RIM20, RIM21 and RIM101 causes yeast cells to be sensitive to calcium stress, but how they regulate calcium sensitivity remain unknown.	Calcium	140-147	Rim21p	Saccharomyces cerevisiae S288C	47-52
27803246-8	2017	Furthermore, the sensitivity of cells to tunicamycin without ER-PM contact was considerably elevated by the deletion of RIM21.	Tunicamycin	41-52	Rim21p	Saccharomyces cerevisiae S288C	120-125
31787665-0	2020	N-glycosylation of Rim21 at an unconventional site fine-tunes its behavior in the plasma membrane.	Nitrogen	0-1	Rim21p	Saccharomyces cerevisiae S288C	19-24
31787665-2	2020	Rim21 is known to undergo N-glycosylation, but the site and function of the glycosylation modification is not known.	Nitrogen	26-27	Rim21p	Saccharomyces cerevisiae S288C	0-5
31787665-3	2020	Using a systematic mutation analysis, we found that Rim21 is N-glycosylated at an unconventional motif located in the N-terminal extracellular region.	Nitrogen	61-62	Rim21p	Saccharomyces cerevisiae S288C	52-57
31787665-3	2020	Using a systematic mutation analysis, we found that Rim21 is N-glycosylated at an unconventional motif located in the N-terminal extracellular region.	Nitrogen	118-119	Rim21p	Saccharomyces cerevisiae S288C	52-57
31787665-4	2020	The Rim21 mutant protein that failed to receive N-glycosylation showed prolonged protein lifetime compared to that of WT Rim21 protein.	Nitrogen	48-49	Rim21p	Saccharomyces cerevisiae S288C	4-9
31787665-7	2020	Further, compared to WT Rim21, mutant Rim21 was more easily solubilized with digitonin but was conversely more resistant to solubilization with Triton X-100.	Digitonin	77-86	Rim21p	Saccharomyces cerevisiae S288C	38-43
31787665-7	2020	Further, compared to WT Rim21, mutant Rim21 was more easily solubilized with digitonin but was conversely more resistant to solubilization with Triton X-100.	Polyethylene Glycols	144-150	Rim21p	Saccharomyces cerevisiae S288C	38-43
31787665-9	2020	Collectively, N-glycosylation of Rim21 is not indispensable for its activity as a sensor protein, but modulates the residence of Rim21 protein to some microdomains within the plasma membrane with distinct lipid conditions, thereby affecting its turnover.	Nitrogen	14-15	Rim21p	Saccharomyces cerevisiae S288C	33-38
31787665-9	2020	Collectively, N-glycosylation of Rim21 is not indispensable for its activity as a sensor protein, but modulates the residence of Rim21 protein to some microdomains within the plasma membrane with distinct lipid conditions, thereby affecting its turnover.	Nitrogen	14-15	Rim21p	Saccharomyces cerevisiae S288C	129-134
26527678-6	2015	Among them, three consecutive Glu residues (EEE motif) were essential for Rim21 function and dissociation of Rim21C from the plasma membrane in response to changes in lipid asymmetry.	Glutamic Acid	30-33	Rim21p	Saccharomyces cerevisiae S288C	74-79
26527678-6	2015	Among them, three consecutive Glu residues (EEE motif) were essential for Rim21 function and dissociation of Rim21C from the plasma membrane in response to changes in lipid asymmetry.	Glutamic Acid	30-33	Rim21p	Saccharomyces cerevisiae S288C	109-115