PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31575700-4	2019	Sirtuin 5 (Sirt5), which localizes to both mitochondria and peroxisomes, reverses post-translational lysine acylation on several enzymes involved in fatty acid oxidation.	Lysine	101-107	sirtuin 5	Mus musculus	0-9	
32301534-0	2020	SIRT5 impairs aggregation and activation of the signaling adaptor MAVS through catalyzing lysine desuccinylation.	Lysine	90-96	sirtuin 5	Mus musculus	0-5	
32301534-5	2020	SIRT5-catalyzed desuccinylation of MAVS at Lysine 7 diminishes the formation of MAVS aggregation after viral infection, resulting in the inhibition of MAVS activation and leading to the impairment of type I IFN production and antiviral gene expression.	Lysine	43-49	sirtuin 5	Mus musculus	0-5	
33479498-2	2021	SIRT5 removes negatively charged malonyl, succinyl, and glutaryl groups from lysine residues and thereby regulates multiple enzymes involved in cellular metabolism and other biological processes.	Lysine	77-83	sirtuin 5	Mus musculus	0-5	
30471144-1	2019	Sirt5 is known to functionally regulate mitochondrial proteins by altering posttranslational modifications, including lysine desuccinylation.	Lysine	118-124	sirtuin 5	Mus musculus	0-5	
30759120-1	2019	Sirtuin 5 (SIRT5) is a member of the NAD+-dependent sirtuin family of protein deacylase that catalyzes removal of post-translational modifications, such as succinylation, malonylation, and glutarylation on lysine residues.	Lysine	206-212	sirtuin 5	Mus musculus	0-9	
30759120-1	2019	Sirtuin 5 (SIRT5) is a member of the NAD+-dependent sirtuin family of protein deacylase that catalyzes removal of post-translational modifications, such as succinylation, malonylation, and glutarylation on lysine residues.	Lysine	206-212	sirtuin 5	Mus musculus	11-16	
27051063-2	2016	One such PTM is lysine succinylation, which is regulated by sirtuin 5 (SIRT5).	Lysine	16-22	sirtuin 5	Mus musculus	60-69	
30515162-2	2018	SIRT5 resides mainly in the mitochondria where it catalyzes deacetylation, demalonylation, desuccinylation, and deglutarylation of lysine to regulate metabolic and oxidative stress response pathways.	Lysine	131-137	sirtuin 5	Mus musculus	0-5	
30279144-4	2018	METHODS: The hepatic SIRT5-overexpressing ob/ob mouse model (ob/ob-SIRT5 OE) was established by CRISPR/Cas9 gene editing tool Protein malonylation and succinylation lysine sites were identified by immunoprecipitation coupled lipid chromatography - tandem mass spectrometry (LC-MS/MS) methods.	Lysine	165-171	sirtuin 5	Mus musculus	21-26	
27051063-2	2016	One such PTM is lysine succinylation, which is regulated by sirtuin 5 (SIRT5).	Lysine	16-22	sirtuin 5	Mus musculus	71-76	
24703693-0	2014	Lysine glutarylation is a protein posttranslational modification regulated by SIRT5.	Lysine	0-6	sirtuin 5	Mus musculus	78-83	
26073543-3	2015	Using affinity enrichment and label free quantitative proteomics, we characterized the SIRT5-regulated lysine malonylome in wild-type (WT) and Sirt5(-/-) mice.	Lysine	103-109	sirtuin 5	Mus musculus	87-92	
26073543-9	2015	These data demonstrate that SIRT5 is a global regulator of lysine malonylation and provide a mechanism for regulation of energetic flux through glycolysis.	Lysine	59-65	sirtuin 5	Mus musculus	28-33	
35613279-6	2022	SIRT5 was engineered to resist acylation-driven inhibition via lysine to arginine mutagenesis.	Lysine	63-69	sirtuin 5	Mus musculus	0-5	
34644302-4	2021	Here, we mapped the known SIRT3/SIRT5-targeted lysine residues onto the recently solved TFP crystal structure which revealed that many of the target sites are involved in substrate channeling within the TFPalpha subunit.	Lysine	47-53	sirtuin 5	Mus musculus	32-37	
34807744-0	2021	Sirtuin 5-Mediated Lysine Desuccinylation Protects Mitochondrial Metabolism Following Subarachnoid Hemorrhage in Mice.	Lysine	19-25	sirtuin 5	Mus musculus	0-9	
34807744-16	2021	CONCLUSIONS: Protein lysine succinylation is a biochemical hallmark of metabolic crisis after SAH, and disruption of lysine succinylation through activation of Sirt5 might be a promising therapeutic strategy for the treatment of SAH.	Lysine	21-27	sirtuin 5	Mus musculus	160-165	
34807744-16	2021	CONCLUSIONS: Protein lysine succinylation is a biochemical hallmark of metabolic crisis after SAH, and disruption of lysine succinylation through activation of Sirt5 might be a promising therapeutic strategy for the treatment of SAH.	Lysine	117-123	sirtuin 5	Mus musculus	160-165	
34642466-0	2022	Repression of p53 function by SIRT5-mediated desuccinylation at Lysine 120 in response to DNA damage.	Lysine	64-70	sirtuin 5	Mus musculus	30-35	
35157847-0	2022	Deglutarylation of glutaryl-CoA dehydrogenase by deacylating enzyme SIRT5 promotes lysine oxidation in mice.	Lysine	83-89	sirtuin 5	Mus musculus	68-73