PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30783087-2	2019	We show here that a fraction of kindlin-2 localizes to mitochondria and interacts with pyrroline-5-carboxylate reductase 1 (PYCR1), a key enzyme for proline synthesis.	Proline	149-156	pyrroline-5-carboxylate reductase 1	Homo sapiens	87-122	
30783087-2	2019	We show here that a fraction of kindlin-2 localizes to mitochondria and interacts with pyrroline-5-carboxylate reductase 1 (PYCR1), a key enzyme for proline synthesis.	Proline	149-156	pyrroline-5-carboxylate reductase 1	Homo sapiens	124-129	
30783087-3	2019	Extracellular matrix (ECM) stiffening promotes kindlin-2 translocation into mitochondria and its interaction with PYCR1, resulting in elevation of PYCR1 level and consequent increase of proline synthesis and cell proliferation.	Proline	186-193	pyrroline-5-carboxylate reductase 1	Homo sapiens	114-119	
30783087-7	2019	Our findings reveal a mechanoresponsive kindlin-2-PYCR1 complex that links mechano-environment to proline metabolism and signaling, and suggest a strategy to inhibit tumor growth.	Proline	98-105	pyrroline-5-carboxylate reductase 1	Homo sapiens	50-55