NAD-dependent lysine demalonylase and desuccinylase that specifically removes malonyl and succinyl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Has weak NAD- dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro. Belongs to the sirtuin family. Class III subfamily. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.5.1.-; Deacetylase; Mitochondrial
Cellular Component: mitochondrion; mitochondrial matrix; mitochondrial intermembrane space
Molecular Function: zinc ion binding; NAD+ ADP-ribosyltransferase activity
Biological Process: protein amino acid ADP-ribosylation; protein amino acid deacetylation; chromatin silencing
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.