PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26797128-2	2016	Exposure to a high glucose concentration has recently been shown to increase phosphorylation of AMPK at Ser(485/491) of its alpha1/alpha2 subunit; however, the mechanism by which it does so is not known.	Serine	104-107	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	96-100	
26797128-4	2016	We sought to determine whether PKC or PKD1 is involved in inhibition of AMPK by causing Ser(485/491) phosphorylation in skeletal muscle cells.	Serine	88-91	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	72-76	
26797128-6	2016	This caused dose- and time-dependent increases in AMPK Ser(485/491) phosphorylation, which was associated with a ~60% decrease in AMPKalpha2 activity.	Serine	55-58	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	50-54	
26797128-6	2016	This caused dose- and time-dependent increases in AMPK Ser(485/491) phosphorylation, which was associated with a ~60% decrease in AMPKalpha2 activity.	Serine	55-58	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	130-140	
26797128-9	2016	Genetic knockdown of PKD1 also prevented Ser(485/491) phosphorylation of AMPK.	Serine	41-44	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	73-77	
26797128-12	2016	Finally, recombinant PKD1 phosphorylated AMPKalpha2 at Ser(491) in cell-free conditions.	Serine	55-58	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	41-51	
26797128-13	2016	These results identify PKD1 as a novel upstream kinase of AMPKalpha2 Ser(491) that plays a negative role in insulin signaling in muscle cells.	Serine	69-72	protein kinase AMP-activated catalytic subunit alpha 2	Homo sapiens	58-68