UniProtKB - Q9NTG7 (SIR3_HUMAN)

BLAST

>sp|Q9NTG7|SIR3_HUMAN NAD-dependent protein deacetylase sirtuin-3, mitochondrial OS=Homo sapiens OX=9606 GN=SIRT3 PE=1 SV=2
MAFWGWRAAAALRLWGRVVERVEAGGGVGPFQACGCRLVLGGRDDVSAGLRGSHGARGEP
LDPARPLQRPPRPEVPRAFRRQPRAAAPSFFFSSIKGGRRSISFSVGASSVVGSGGSSDK
GKLSLQDVAELIRARACQRVVVMVGAGISTPSGIPDFRSPGSGLYSNLQQYDLPYPEAIF
ELPFFFHNPKPFFTLAKELYPGNYKPNVTHYFLRLLHDKGLLLRLYTQNIDGLERVSGIP
ASKLVEAHGTFASATCTVCQRPFPGEDIRADVMADRVPRCPVCTGVVKPDIVFFGEPLPQ
RFLLHVVDFPMADLLLILGTSLEVEPFASLTEAVRSSVPRLLINRDLVGPLAWHPRSRDV
AQLGDVVHGVESLVELLGWTEEMRDLVQRETGKLDGPDK

Align

Format
Add to basket Added to basket
History
Entry version 159 (12 Sep 2018)
Sequence version 2 (31 Oct 2003)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Gene

SIRT3

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

NAD-dependent protein deacetylase (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:23283301, PubMed:24121500, PubMed:24252090, PubMed:19535340). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:23283301, PubMed:24121500, PubMed:24252090). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5PO (PubMed:16788062, PubMed:18680753, PubMed:24121500, PubMed:24252090, PubMed:19535340). Contributes to the regulation of the cellular energy metabolism (PubMed:24252090). Important for regulating tissue-specific ATP levels (PubMed:18794531). In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription (PubMed:23283301).9 Publications

Miscellaneous

Has some ability to deacetylate histones in vitro, but seeing its subcellular location, this is unlikely in vivo.1 Publication

Catalytic activityⁱ

NAD⁺ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.PROSITE-ProRule annotation1 Publication7 Publications

Cofactorⁱ

Zn²⁺2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Kineticsⁱ

K_M=
600 µM for NAD
1 Publication
Manual assertion based on experiment inⁱ
- Ref.22
  "Crystal structures of human SIRT3 displaying substrate-induced conformational changes."
  Jin L., Wei W., Jiang Y., Peng H., Cai J., Mao C., Dai H., Choy W., Bemis J.E., Jirousek M.R., Milne J.C., Westphal C.H., Perni R.B.
  J. Biol. Chem. 284:24394-24405(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 118-399 IN COMPLEX WITH ZINC IONS AND ACSS1, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, NAD-BINDING.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	248	Proton acceptor	1
Metal bindingⁱ	256	Zinc	1
Metal bindingⁱ	259	Zinc	1
Metal bindingⁱ	280	Zinc	1
Metal bindingⁱ	283	Zinc	1
Binding siteⁱ	366	NAD; via amide nitrogenBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	145 – 165	NADAdd BLAST	21
Nucleotide bindingⁱ	228 – 231	NAD	4
Nucleotide bindingⁱ	319 – 321	NAD	3
Nucleotide bindingⁱ	344 – 346	NAD	3

GO - Molecular functionⁱ

enzyme binding Source: Ensembl
NAD+ ADP-ribosyltransferase activity
Source: ProtInc
Traceable author statementⁱ
- 10381378
NAD+ binding Source: InterPro
NAD-dependent histone deacetylase activity Source: InterPro
NAD-dependent protein deacetylase activity Source: Reactome
sequence-specific DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 29445193
zinc ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19535340

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aerobic respiration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 22309213
aging Source: Ensembl
mitochondrion organization Source: Reactome
negative regulation of ERK1 and ERK2 cascade Source: Ensembl
negative regulation of reactive oxygen species metabolic process Source: Ensembl
peptidyl-lysine deacetylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 22309213
positive regulation of insulin secretion Source: Ensembl
protein ADP-ribosylation
Source: ProtInc
Traceable author statementⁱ
- 10381378
protein deacetylation
Source: UniProtKB
Inferred from direct assayⁱ
- 16788062

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Ligand	Metal-binding, NAD, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
SABIO-RKⁱ	Q9NTG7
SIGNORⁱ	Q9NTG7

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: NAD-dependent protein deacetylase sirtuin-3, mitochondrial (EC:3.5.1.-7 Publications) Short name: hSIRT3 Alternative name(s): Regulatory protein SIR2 homolog 3 SIR2-like protein 3
Gene namesⁱ	Name:SIRT3 Synonyms:SIR2L3
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 11

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000142082.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:14931 SIRT3
MIMⁱ	604481 gene
neXtProtⁱ	NX_Q9NTG7

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	7	R → G or Q: Suppresses targeting to mitochondrion; when associated with G-13 or Q-13. 1 Publication	1
Mutagenesisⁱ	13	R → G or Q: Suppresses targeting to mitochondrion; when associated with G-7 or Q-7. 1 Publication	1
Mutagenesisⁱ	17	R → G or Q: Reduces targeting to mitochondrion; when associated with G-21 or Q-21. 1 Publication	1
Mutagenesisⁱ	21	R → G or Q: Reduces targeting to mitochondrion; when associated with G-17 or Q-17. 1 Publication	1
Mutagenesisⁱ	99 – 100	RR → GG: Abolishes processing by MPP (in vitro). 1 Publication	2
Mutagenesisⁱ	229	N → A: Loss of function. 1 Publication	1
Mutagenesisⁱ	248	H → Y: Loss of function. 3 Publications	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	23410
Open Targets More...OpenTargetsⁱ	ENSG00000142082
PharmGKBⁱ	PA37936

Chemistry databases

ChEMBLⁱ	CHEMBL4461
Drug and drug target database More...DrugBankⁱ	DB02059 Adenosine-5-Diphosphoribose
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2709

Polymorphism and mutation databases

BioMutaⁱ	SIRT3
DMDMⁱ	38258651

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000032612	? – 399	NAD-dependent protein deacetylase sirtuin-3, mitochondrial
Transit peptideⁱ	1 – ?	MitochondrionSequence analysis

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	122	N6-succinyllysineBy similarity		1

Post-translational modificationⁱ

Processed by mitochondrial processing peptidase (MPP) to give a 28 kDa product. Such processing is probably essential for its enzymatic activity.1 Publication

Proteomic databases

EPDⁱ	Q9NTG7
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9NTG7
PaxDbⁱ	Q9NTG7
PeptideAtlas More...PeptideAtlasⁱ	Q9NTG7
PRIDEⁱ	Q9NTG7
ProteomicsDBⁱ	82606 82607 [Q9NTG7-2]

PTM databases

iPTMnetⁱ	Q9NTG7
PhosphoSitePlusⁱ	Q9NTG7

Expressionⁱ

Tissue specificityⁱ

Widely expressed.2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000142082 Expressed in 214 organ(s), highest expression level in anterior cingulate cortex
CleanExⁱ	HS_SIRT3
ExpressionAtlasⁱ	Q9NTG7 baseline and differential
Genevisibleⁱ	Q9NTG7 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB037142 HPA026809

HPAⁱ

CAB037142
HPA026809

Interactionⁱ

Subunit structureⁱ

Upon metabolic stress, forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301). Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (PubMed:29445193). Interacts with NDUFA9, ACSS1, IDH2 and GDH (PubMed:16788062, PubMed:18794531, PubMed:19535340, PubMed:18680753). Interacts with PCCA (PubMed:23438705).7 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
ATP5F1A	P25705	2	EBI-724621,EBI-351437
OPA1	O60313	3	EBI-724621,EBI-1054131
SKP2	Q13309	5	EBI-724621,EBI-456291

GO - Molecular functionⁱ

enzyme binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	116982, 56 interactors
Database of interacting proteins More...DIPⁱ	DIP-46861N
IntActⁱ	Q9NTG7, 35 interactors
Molecular INTeraction database More...MINTⁱ	Q9NTG7
STRINGⁱ	9606.ENSP00000372191

Chemistry databases

BindingDBⁱ	Q9NTG7

BindingDBⁱ

Q9NTG7

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	125 – 133	Combined sources	9
Turnⁱ	134 – 136	Combined sources	3
Beta strandⁱ	140 – 144	Combined sources	5
Helixⁱ	146 – 152	Combined sources	7
Beta strandⁱ	157 – 159	Combined sources	3
Turnⁱ	160 – 162	Combined sources	3
Helixⁱ	164 – 168	Combined sources	5
Beta strandⁱ	171 – 175	Combined sources	5
Helixⁱ	176 – 180	Combined sources	5
Helixⁱ	182 – 187	Combined sources	6
Helixⁱ	190 – 199	Combined sources	10
Beta strandⁱ	201 – 203	Combined sources	3
Helixⁱ	208 – 218	Combined sources	11
Beta strandⁱ	222 – 227	Combined sources	6
Helixⁱ	233 – 236	Combined sources	4
Helixⁱ	241 – 243	Combined sources	3
Beta strandⁱ	244 – 246	Combined sources	3
Beta strandⁱ	249 – 256	Combined sources	8
Turnⁱ	257 – 259	Combined sources	3
Beta strandⁱ	262 – 264	Combined sources	3
Helixⁱ	265 – 273	Combined sources	9
Turnⁱ	281 – 283	Combined sources	3
Beta strandⁱ	286 – 291	Combined sources	6
Helixⁱ	300 – 304	Combined sources	5
Helixⁱ	305 – 311	Combined sources	7
Beta strandⁱ	313 – 319	Combined sources	7
Helixⁱ	327 – 330	Combined sources	4
Helixⁱ	331 – 333	Combined sources	3
Beta strandⁱ	340 – 346	Combined sources	7
Helixⁱ	349 – 353	Combined sources	5
Beta strandⁱ	359 – 364	Combined sources	6
Helixⁱ	366 – 377	Combined sources	12
Helixⁱ	380 – 391	Combined sources	12

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9NTG7
SMRⁱ	Q9NTG7
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9NTG7

EvolutionaryTraceⁱ

Q9NTG7

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	126 – 382	Deacetylase sirtuin-typePROSITE-ProRule annotationAdd BLAST		257

Sequence similaritiesⁱ

Belongs to the sirtuin family. Class I subfamily.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG2682 Eukaryota COG0846 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00870000136486
HOVERGENⁱ	HBG057095
InParanoidⁱ	Q9NTG7
KEGG Orthology (KO) More...KOⁱ	K11413
OMAⁱ	CTGIVKP
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07CT
PhylomeDBⁱ	Q9NTG7
TreeFamⁱ	TF106181

Family and domain databases

Gene3Dⁱ	3.30.1600.10, 2 hits
InterProⁱ	View protein in InterPro IPR029035 DHS-like_NAD/FAD-binding_dom IPR003000 Sirtuin IPR026591 Sirtuin_cat_small_dom_sf IPR017328 Sirtuin_class_I IPR026590 Ssirtuin_cat_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02146 SIR2, 1 hit
PIRSFⁱ	PIRSF037938 SIR2_euk, 1 hit
SUPFAMⁱ	SSF52467 SSF52467, 1 hit
PROSITEⁱ	View protein in PROSITE PS50305 SIRTUIN, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 9 potential isoforms that are computationally mapped.ⁱShow all

Isoform 1 (identifier: Q9NTG7-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFWGWRAAA ALRLWGRVVE RVEAGGGVGP FQACGCRLVL GGRDDVSAGL 
        60         70         80         90        100
RGSHGARGEP LDPARPLQRP PRPEVPRAFR RQPRAAAPSF FFSSIKGGRR 
       110        120        130        140        150
SISFSVGASS VVGSGGSSDK GKLSLQDVAE LIRARACQRV VVMVGAGIST 
       160        170        180        190        200
PSGIPDFRSP GSGLYSNLQQ YDLPYPEAIF ELPFFFHNPK PFFTLAKELY 
       210        220        230        240        250
PGNYKPNVTH YFLRLLHDKG LLLRLYTQNI DGLERVSGIP ASKLVEAHGT 
       260        270        280        290        300
FASATCTVCQ RPFPGEDIRA DVMADRVPRC PVCTGVVKPD IVFFGEPLPQ 
       310        320        330        340        350
RFLLHVVDFP MADLLLILGT SLEVEPFASL TEAVRSSVPR LLINRDLVGP 
       360        370        380        390 
LAWHPRSRDV AQLGDVVHGV ESLVELLGWT EEMRDLVQRE TGKLDGPDK

Length:399

Mass (Da):43,573

Last modified:October 31, 2003 - v2

Checksum:ⁱ4BA8BD3AC5FC7901

Isoform 2 (identifier: Q9NTG7-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-142: Missing.

« Hide

        10         20         30         40         50
MVGAGISTPS GIPDFRSPGS GLYSNLQQYD LPYPEAIFEL PFFFHNPKPF 
        60         70         80         90        100
FTLAKELYPG NYKPNVTHYF LRLLHDKGLL LRLYTQNIDG LERVSGIPAS 
       110        120        130        140        150
KLVEAHGTFA SATCTVCQRP FPGEDIRADV MADRVPRCPV CTGVVKPDIV 
       160        170        180        190        200
FFGEPLPQRF LLHVVDFPMA DLLLILGTSL EVEPFASLTE AVRSSVPRLL 
       210        220        230        240        250
INRDLVGPLA WHPRSRDVAQ LGDVVHGVES LVELLGWTEE MRDLVQRETG 

KLDGPDK

Show »

Length:257

Mass (Da):28,567

Checksum:ⁱ33043FAB6B3F0307

Computationally mapped potential isoform sequencesⁱ

There are 9 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation
E9PK80	E9PK80_HUMAN	NAD-dependent protein deacetylase NAD-dependent protein deacetylase, EC 3.5.1.-	SIRT3	318	Annotation score:
B7WNN4	B7WNN4_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	134	Annotation score:
E9PN58	E9PN58_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	353	Annotation score:
E9PM75	E9PM75_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	345	Annotation score:
E9PJS6	E9PJS6_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	95	Annotation score:
E9PIT6	E9PIT6_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	46	Annotation score:
E9PNA0	E9PNA0_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	93	Annotation score:
E9PM52	E9PM52_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	23	Annotation score:
E9PR48	E9PR48_HUMAN	NAD-dependent protein deacetylase s... NAD-dependent protein deacetylase sirtuin-3, mitochondrial	SIRT3	18	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_051977	80	R → W. Corresponds to variant dbSNP:rs28365927Ensembl.	1
Natural variantⁱVAR_051978	208	V → I. Corresponds to variant dbSNP:rs11246020Ensembl.	1
Natural variantⁱVAR_051979	369	G → S. Corresponds to variant dbSNP:rs3020901Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_043792	1 – 142	Missing in isoform 2. 1 PublicationAdd BLAST		142

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF083108 mRNA Translation: AAD40851.1 AK299438 mRNA Translation: BAH13032.1 AC136475 Genomic DNA No translation available. BC001042 mRNA Translation: AAH01042.1 AL137276 mRNA Translation: CAB70674.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS53590.1 [Q9NTG7-2] CCDS7691.1 [Q9NTG7-1]
PIRⁱ	T46348
NCBI Reference Sequences More...RefSeqⁱ	NP_001017524.1, NM_001017524.2 [Q9NTG7-2] NP_036371.1, NM_012239.5 [Q9NTG7-1] XP_016872919.1, XM_017017430.1 [Q9NTG7-2]
UniGeneⁱ	Hs.716456

Genome annotation databases

Ensemblⁱ	ENST00000382743; ENSP00000372191; ENSG00000142082 [Q9NTG7-1] ENST00000529382; ENSP00000437216; ENSG00000142082 [Q9NTG7-2]
GeneIDⁱ	23410
KEGGⁱ	hsa:23410
UCSC genome browser More...UCSCⁱ	uc001lok.5 human [Q9NTG7-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9NTG7	Isoform 2 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial		HUMAN		257	UniRef100_Q9NTG7
UPI0002782C30		HUMAN		274
UPI000C6F4485		HUMAN		274
UPI00035083A5		HUMAN		281
UPI00052E48FA		HUMAN		275
+2

Protein	Similar proteins		Species	Score	Length	Source
Q9NTG7	Isoform 2 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial		HUMAN		257	UniRef90_Q9NTG7
Sirtuin 3		RHIBE		478
NAD-dependent protein deacetylase		GORGO		399
NAD-dependent protein deacetylase		PANTR		399
NAD-dependent protein deacetylase		PONAB		399
+30

Protein	Similar proteins		Species	Score	Length	Source
Q9NTG7	Isoform 2 of NAD-dependent protein deacetylase sirtuin-3, mitochondrial		HUMAN		257	UniRef50_Q9NTG7
Sirtuin 3		RHIBE		478
NAD-dependent protein deacetylase		CERAT		399
NAD-dependent protein deacetylase		PANTR		399
NAD-dependent protein deacetylase		CHLSB		399
+66

Entry informationⁱ

Entry nameⁱ	SIR3_HUMAN
Accessionⁱ	Q9NTG7Primary (citable) accession number: Q9NTG7 Secondary accession number(s): B7Z5U6, Q9Y6E8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
	Last sequence update:	October 31, 2003
	Last modified:	September 12, 2018
	This is version 159 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9NTG7 (SIR3_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

NAD-dependent protein deacetylase sirtuin-3, mitochondrial

SIRT3

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Mitochondrion

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Computationally mapped potential isoform sequencesⁱ

Keywords - Coding sequence diversityⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ