PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31924651-4	2020	Although the tetramer form of PKM2 converts phosphoenolpyruvate to pyruvate, the dimeric form of PKM2 has alternative, nonglycolysis functions as a transcriptional coactivator to enhance the transcription of several proinflammatory cytokines.	Phosphoenolpyruvate	44-63	pyruvate kinase, muscle	Mus musculus	30-34	
29455645-1	2018	Originally identified as a metabolic enzyme that catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP in the glycolytic pathway, pyruvate kinase M2-type (PKM2) has been shown to exhibit novel biological activities in the nucleus and outside the cells.	Phosphoenolpyruvate	98-117	pyruvate kinase, muscle	Mus musculus	158-187	
25713368-5	2015	Based on these results, we found that both in vitro and in MIN6 cells, L-cysteine specifically inhibited the activity of pyruvate kinase muscle isoform 2 (PKM2), an isoform of pyruvate kinases that catalyze the conversion of phosphoenolpyruvate to pyruvate.	Phosphoenolpyruvate	225-244	pyruvate kinase, muscle	Mus musculus	121-153	
25713368-5	2015	Based on these results, we found that both in vitro and in MIN6 cells, L-cysteine specifically inhibited the activity of pyruvate kinase muscle isoform 2 (PKM2), an isoform of pyruvate kinases that catalyze the conversion of phosphoenolpyruvate to pyruvate.	Phosphoenolpyruvate	225-244	pyruvate kinase, muscle	Mus musculus	155-159