Sirtuin 5 (SIRT5)

SIR2L5; Silent Mating Type Information Regulation 2 Homolog 5; NAD-dependent protein deacylase sirtuin-5, mitochondrial; Regulatory protein SIR2 homolog 5; SIR2-like protein 5

SPN	R884
HGNC	14933
MGI	1915596
PubMed	22076378
RGD	1303285
UniProt	Q9NXA8
Wiki	SIRT5

SIRT5 encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.

The protein encoded by this gene is included in class III of the sirtuin family. Alternative splicing of this gene results in two transcript variants.

Reference

"Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity."
Biochem. Biophys. Res. Commun. 260:273-279(1999) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"The full-ORF clone resource of the German cDNA consortium."
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins."
Mol. Biol. Cell 16:4623-4635(2005) [PubMed] [Europe PMC] [Abstract]

"Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5."
J. Mol. Biol. 382:790-801(2008) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms."
Genes Cells 16:190-202(2011) [PubMed] [Europe PMC] [Abstract]

"The first identification of lysine malonylation substrates and its regulatory enzyme."
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]

"Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition."
PLoS ONE 7:E45098-E45098(2012) [PubMed] [Europe PMC] [Abstract]

"SIRT5 desuccinylates and activates SOD1 to eliminate ROS."
Biochem. Biophys. Res. Commun. 441:191-195(2013) [PubMed] [Europe PMC] [Abstract]

"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Crystal structure of human sirtuin homolog 5 in complex with NAD."
Submitted (FEB-2006) to the PDB data bank

"Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin."
Structure 15:377-389(2007) [PubMed] [Europe PMC] [Abstract]

"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]

"The bicyclic intermediate structure provides insights into the desuccinylation mechanism of human sirtuin 5 (SIRT5)."
J. Biol. Chem. 287:28307-28314(2012) [PubMed] [Europe PMC] [Abstract]

"Synthesis of carba-NAD and the structures of its ternary complexes with SIRT3 and SIRT5."
J. Org. Chem. 77:7319-7329(2012) [PubMed] [Europe PMC] [Abstract]

"A molecular mechanism for direct sirtuin activation by resveratrol."
PLoS ONE 7:E49761-E49761(2012) [PubMed] [Europe PMC] [Abstract]