HUMAN:SIR3

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	SIRT3 (synonyms: SIR2L3)
Protein Name(s)	NAD-dependent protein deacetylase sirtuin-3, mitochondrial hSIRT3 Regulatory protein SIR2 homolog 3 SIR2-like protein 3
External Links
UniProt	Q9NTG7
EMBL	AF083108 AK299438 AC136475 BC001042 AL137276
CCDS	CCDS53590.1 CCDS7691.1
PIR	T46348
RefSeq	NP_001017524.1 NP_036371.1
UniGene	Hs.716456
PDB	3GLR 3GLS 3GLT 3GLU 4BN4 4BN5 4BV3 4BVB 4BVE 4BVF 4BVG 4BVH 4C78 4C7B 4FVT 4FZ3 4HD8 4JSR 4JT8 4JT9 4V1C
PDBsum	3GLR 3GLS 3GLT 3GLU 4BN4 4BN5 4BV3 4BVB 4BVE 4BVF 4BVG 4BVH 4C78 4C7B 4FVT 4FZ3 4HD8 4JSR 4JT8 4JT9 4V1C
ProteinModelPortal	Q9NTG7
SMR	Q9NTG7
BioGrid	116982
DIP	DIP-46861N
IntAct	Q9NTG7
MINT	MINT-4540133
STRING	9606.ENSP00000372191
BindingDB	Q9NTG7
ChEMBL	CHEMBL4461
PhosphoSite	Q9NTG7
DMDM	38258651
MaxQB	Q9NTG7
PaxDb	Q9NTG7
PRIDE	Q9NTG7
Ensembl	ENST00000382743 ENST00000529382
GeneID	23410
KEGG	hsa:23410
UCSC	uc001loj.4
CTD	23410
GeneCards	GC11M000264
HGNC	HGNC:14931
HPA	CAB037142 HPA026809
MIM	604481
neXtProt	NX_Q9NTG7
PharmGKB	PA37936
eggNOG	COG0846
GeneTree	ENSGT00740000115546
HOVERGEN	HBG057095
InParanoid	Q9NTG7
KO	K11413
OMA	LAWHPRS
OrthoDB	EOG7WX09C
PhylomeDB	Q9NTG7
TreeFam	TF106181
Reactome	REACT_200608
ChiTaRS	SIRT3
EvolutionaryTrace	Q9NTG7
GeneWiki	SIRT3
GenomeRNAi	23410
NextBio	45597
PRO	PR:Q9NTG7
Proteomes	UP000005640
Bgee	Q9NTG7
CleanEx	HS_SIRT3
ExpressionAtlas	Q9NTG7
Genevestigator	Q9NTG7
GO	GO:0016020 GO:0005759 GO:0005739 GO:0003950 GO:0070403 GO:0032041 GO:0008270 GO:0009060 GO:0007568 GO:0034983 GO:0006471 GO:0006476
Gene3D	3.30.1600.10 3.40.50.1220
InterPro	IPR029035 IPR003000 IPR026591 IPR017328 IPR026590
PANTHER	PTHR11085
Pfam	PF02146
PIRSF	PIRSF037938
SUPFAM	SSF52467
PROSITE	PS50305

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0090311	regulation of protein deacetylation	PMID:16790548^[1]	ECO:0000315			P		Fig. 3	complete CACAO 8108
	GO:1902553	positive regulation of catalase activity	PMID:25210848^[2]	ECO:0000314			P		Figure 2(H-I) shows that pSIRT3 transfection increases gene & protein levels of CAT. 2J indicates enzymatic activity of CAT is also enhanced.	complete CACAO 11337
	GO:1901671	positive regulation of superoxide dismutase activity	PMID:25210848^[2]	ECO:0000314			P		Figure 2(E-F) shows that pSIRT3 transfection increases gene & protein levels of MnSOD. 2G indicates enzymatic activity of MnSOD is also enhanced.	complete CACAO 11338
	GO:1903206	negative regulation of hydrogen peroxide-induced cell death	PMID:25210848^[2]	ECO:0000316		UniProtKB:P04040 UniProtKB:P04179	P		Figure 3J & 3K show that transfection with the SIRT3 expression construct significantly reduces hydrogen peroxide-induced apoptosis by enhancing antioxidant activity of CAT and MnSOD	complete CACAO 11339
	GO:0005759	mitochondrial matrix	PMID:12186850^[3]	ECO:0000314			C		Figure 5	complete CACAO 11346
part_of	GO:0005759	mitochondrial matrix	PMID:29445193^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:29445193^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0042149)	Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:29445193^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:23283301^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0042149)	Seeded From UniProt	complete
involved_in	GO:0034983	peptidyl-lysine deacetylation	PMID:22309213^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009060	aerobic respiration	PMID:22309213^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:19535340^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006476	protein deacetylation	PMID:16788062^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16079181^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0070403	NAD+ binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000119154 PomBase:SPBC16D10.07c UniProtKB:Q8IXJ6	F		Seeded From UniProt	complete
enables	GO:0043565	sequence-specific DNA binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1927665 PANTHER:PTN002476415 UniProtKB:Q9NTG7	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1927665 PANTHER:PTN002476415 UniProtKB:Q9NTG7	C		Seeded From UniProt	complete
enables	GO:0017136	NAD-dependent histone deacetylase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0024291 FB:FBgn0038788 MGI:MGI:2135607 PANTHER:PTN000119154 SGD:S000002200 SGD:S000005429 SGD:S000005551 SGD:S000005936 UniProtKB:Q96EB6	F		Seeded From UniProt	complete
enables	GO:0017136	NAD-dependent histone deacetylase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0024291 FB:FBgn0038788 MGI:MGI:2135607 PANTHER:PTN000119154 SGD:S000002200 SGD:S000005429 SGD:S000005551 SGD:S000005936 UniProtKB:Q8IXJ6 UniProtKB:Q96EB6	F		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1927665 PANTHER:PTN002476415 UniProtKB:Q9NTG7	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1927665 PANTHER:PTN002476415 RGD:1308374 UniProtKB:Q9NTG7	C		Seeded From UniProt	complete
involved_in	GO:0016575	histone deacetylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0017136	P		Seeded From UniProt	complete
involved_in	GO:0016575	histone deacetylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0017136	P		Seeded From UniProt	complete
involved_in	GO:0016575	histone deacetylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0017136	P		Seeded From UniProt	complete
involved_in	GO:2000378	negative regulation of reactive oxygen species metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C6ZII9 ensembl:ENSRNOP00000018861	P		Seeded From UniProt	complete
involved_in	GO:0070373	negative regulation of ERK1 and ERK2 cascade	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C6ZII9 ensembl:ENSRNOP00000018861	P		Seeded From UniProt	complete
involved_in	GO:0032024	positive regulation of insulin secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C6ZII9 ensembl:ENSRNOP00000018861	P		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C6ZII9 ensembl:ENSRNOP00000018861	F		Seeded From UniProt	complete
involved_in	GO:0007568	aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C6ZII9 ensembl:ENSRNOP00000018861	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:C6ZII9 ensembl:ENSRNOP00000018861	C		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017328	F		Seeded From UniProt	complete
enables	GO:0017136	NAD-dependent histone deacetylase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017328	F		Seeded From UniProt	complete
enables	GO:0070403	NAD+ binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003000	F		Seeded From UniProt	complete
involved_in	GO:0006471	protein ADP-ribosylation	PMID:10381378^[11] PMID:17456799^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003950	NAD+ ADP-ribosyltransferase activity	PMID:10381378^[11] PMID:17456799^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007005	mitochondrion organization	Reactome:R-HSA-1592230	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	Reactome:R-HSA-5688289 Reactome:R-HSA-1605535	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-9620532	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Hallows, WC et al. (2006) Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. U.S.A. 103 10230-5 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Wang, XQ et al. (2014) Decreased SIRT3 in aged human mesenchymal stromal/stem cells increases cellular susceptibility to oxidative stress. J. Cell. Mol. Med. 18 2298-310 PubMed GONUTS page
↑ Schwer, B et al. (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158 647-57 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Celestini, V et al. (2018) Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy. Cell Death Dis 9 231 PubMed GONUTS page
↑ Peserico, A et al. (2013) A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels. Cell. Mol. Life Sci. 70 2015-29 PubMed GONUTS page
↑ ^6.0 ^6.1 Scott, I et al. (2012) Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1. Biochem. J. 443 655-61 PubMed GONUTS page
↑ Jin, L et al. (2009) Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J. Biol. Chem. 284 24394-405 PubMed GONUTS page
↑ Schwer, B et al. (2006) Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U.S.A. 103 10224-9 PubMed GONUTS page
↑ Michishita, E et al. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16 4623-35 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^11.0 ^11.1 Frye, RA (1999) 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. 260 273-9 PubMed GONUTS page
↑ ^12.0 ^12.1 Yamamoto, H et al. (2007) Sirtuin functions in health and disease. Mol. Endocrinol. 21 1745-55 PubMed GONUTS page

[PMID:16790548-1] Hallows, WC et al. (2006) Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. U.S.A. 103 10230-5 PubMed GONUTS page

[PMID:25210848-2] 2.0 ^2.1 ^2.2 Wang, XQ et al. (2014) Decreased SIRT3 in aged human mesenchymal stromal/stem cells increases cellular susceptibility to oxidative stress. J. Cell. Mol. Med. 18 2298-310 PubMed GONUTS page

[PMID:12186850-3] Schwer, B et al. (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J. Cell Biol. 158 647-57 PubMed GONUTS page

[PMID:29445193-4] 4.0 ^4.1 ^4.2 Celestini, V et al. (2018) Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy. Cell Death Dis 9 231 PubMed GONUTS page

[PMID:23283301-5] Peserico, A et al. (2013) A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels. Cell. Mol. Life Sci. 70 2015-29 PubMed GONUTS page

[PMID:22309213-6] 6.0 ^6.1 Scott, I et al. (2012) Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1. Biochem. J. 443 655-61 PubMed GONUTS page

[PMID:19535340-7] Jin, L et al. (2009) Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J. Biol. Chem. 284 24394-405 PubMed GONUTS page

[PMID:16788062-8] Schwer, B et al. (2006) Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U.S.A. 103 10224-9 PubMed GONUTS page

[PMID:16079181-9] Michishita, E et al. (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell 16 4623-35 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 ^10.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:10381378-11] 11.0 ^11.1 Frye, RA (1999) 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. 260 273-9 PubMed GONUTS page

[PMID:17456799-12] 12.0 ^12.1 Yamamoto, H et al. (2007) Sirtuin functions in health and disease. Mol. Endocrinol. 21 1745-55 PubMed GONUTS page

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HUMAN:SIR3

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