PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31644285-2	2019	The catalytic activity of a number of vital metabolic proteins, such as pyruvate dehydrogenase (PDH), depends on lysine lipoylation.	Lysine	113-119	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	72-94	
31644285-2	2019	The catalytic activity of a number of vital metabolic proteins, such as pyruvate dehydrogenase (PDH), depends on lysine lipoylation.	Lysine	113-119	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	96-99	
29330215-9	2018	Proteomic analysis of the total acetylome showed increased overall acetylation, and specific lysine acetylation of 2 central mitochondrial metabolic enzymes, PDH and ATP synthase, as well.	Lysine	93-99	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	158-161	
25152236-4	2014	SIRT3 deacetylates PDHA1 lysine 321 (K321), and a PDHA1 mutant mimicking a deacetylated lysine (PDHA1(K321R)) increases PDH activity, compared to the K321 acetylation mimic (PDHA1(K321Q)) or wild-type PDHA1.	Lysine	25-31	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	19-22	
24962578-5	2014	In particular, Tyr-381 phosphorylation of PDP1 dissociates deacetylase SIRT3 and recruits acetyltransferase ACAT1 to PDC, resulting in increased inhibitory lysine acetylation of PDHA1 and PDP1.	Lysine	156-162	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	42-46	
24962578-5	2014	In particular, Tyr-381 phosphorylation of PDP1 dissociates deacetylase SIRT3 and recruits acetyltransferase ACAT1 to PDC, resulting in increased inhibitory lysine acetylation of PDHA1 and PDP1.	Lysine	156-162	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	188-192	
24486017-3	2014	Here, we report that lysine acetylation of PDHA1 and PDP1 is common in epidermal growth factor (EGF)-stimulated cells and diverse human cancer cells.	Lysine	21-27	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	53-57