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Q9NTG7

- SIR3_HUMAN

UniProt

Q9NTG7 - SIR3_HUMAN

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Protein

NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Gene

SIRT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NAD-dependent protein deacetylase. Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues. Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5O. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels.6 Publications

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.3 PublicationsPROSITE-ProRule annotation

Cofactori

Binds 1 zinc ion per subunit.

Kineticsi

  1. KM=600 µM for NAD1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei248 – 2481Proton acceptor
Metal bindingi256 – 2561Zinc
Metal bindingi259 – 2591Zinc
Metal bindingi280 – 2801Zinc
Metal bindingi283 – 2831Zinc
Binding sitei366 – 3661NAD; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi145 – 16521NADAdd
BLAST
Nucleotide bindingi228 – 2314NAD
Nucleotide bindingi319 – 3213NAD
Nucleotide bindingi344 – 3463NAD

GO - Molecular functioni

  1. NAD+ ADP-ribosyltransferase activity Source: ProtInc
  2. NAD+ binding Source: InterPro
  3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: Ensembl
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. aerobic respiration Source: UniProtKB
  2. peptidyl-lysine deacetylation Source: UniProtKB
  3. protein ADP-ribosylation Source: ProtInc
  4. protein deacetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiREACT_200608. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylase sirtuin-3, mitochondrial (EC:3.5.1.-)
Short name:
hSIRT3
Alternative name(s):
Regulatory protein SIR2 homolog 3
SIR2-like protein 3
Gene namesi
Name:SIRT3
Synonyms:SIR2L3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14931. SIRT3.

Subcellular locationi

Mitochondrion matrix 4 Publications

GO - Cellular componenti

  1. membrane Source: Ensembl
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71R → G or Q: Suppresses targeting to mitochondrion; when associated with G-13 or Q-13. 1 Publication
Mutagenesisi13 – 131R → G or Q: Suppresses targeting to mitochondrion; when associated with G-7 or Q-7. 1 Publication
Mutagenesisi17 – 171R → G or Q: Reduces targeting to mitochondrion; when associated with G-21 or Q-21. 1 Publication
Mutagenesisi21 – 211R → G or Q: Reduces targeting to mitochondrion; when associated with G-17 or Q-17. 1 Publication
Mutagenesisi99 – 1002RR → GG: Abolishes processing by MPP (in vitro). 1 Publication
Mutagenesisi229 – 2291N → A: Loss of function. 1 Publication
Mutagenesisi248 – 2481H → Y: Loss of function. 3 Publications

Organism-specific databases

PharmGKBiPA37936.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 399NAD-dependent protein deacetylase sirtuin-3, mitochondrialPRO_0000032612
Transit peptidei1 – ?MitochondrionSequence Analysis

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

MaxQBiQ9NTG7.
PaxDbiQ9NTG7.
PRIDEiQ9NTG7.

PTM databases

PhosphoSiteiQ9NTG7.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiQ9NTG7.
CleanExiHS_SIRT3.
ExpressionAtlasiQ9NTG7. baseline and differential.
GenevestigatoriQ9NTG7.

Organism-specific databases

HPAiCAB037142.
HPA026809.

Interactioni

Subunit structurei

Interacts with NDUFA9, ACSS1, IDH2 and GDH.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP5A1P257052EBI-724621,EBI-351437
SKP2Q133095EBI-724621,EBI-456291

Protein-protein interaction databases

BioGridi116982. 99 interactions.
DIPiDIP-46861N.
IntActiQ9NTG7. 26 interactions.
MINTiMINT-4540133.
STRINGi9606.ENSP00000372191.

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi125 – 1339
Turni134 – 1363
Beta strandi140 – 1445
Helixi146 – 1527
Beta strandi157 – 1593
Turni160 – 1623
Helixi164 – 1685
Beta strandi171 – 1755
Helixi176 – 1805
Helixi182 – 1876
Helixi190 – 19910
Beta strandi201 – 2033
Helixi208 – 21811
Beta strandi222 – 2276
Helixi233 – 2364
Helixi241 – 2433
Beta strandi244 – 2463
Beta strandi249 – 2568
Turni257 – 2593
Beta strandi262 – 2643
Helixi265 – 2739
Turni281 – 2833
Beta strandi286 – 2916
Helixi300 – 3045
Helixi305 – 3117
Beta strandi313 – 3197
Helixi327 – 3304
Helixi331 – 3333
Beta strandi340 – 3467
Helixi349 – 3535
Beta strandi359 – 3646
Helixi366 – 37712
Helixi380 – 39112

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GLRX-ray1.80A118-399[»]
3GLSX-ray2.70A/B/C/D/E/F118-399[»]
3GLTX-ray2.10A118-399[»]
3GLUX-ray2.50A118-399[»]
4BN4X-ray1.30A116-399[»]
4BN5X-ray3.25A/B/C/D/E/F/G/H/I/J/K/L119-399[»]
4BV3X-ray2.00A116-399[»]
4BVBX-ray2.00A116-399[»]
4BVEX-ray2.05A116-399[»]
4BVFX-ray2.70A116-399[»]
4BVGX-ray2.50A116-399[»]
4BVHX-ray1.90A/B/C116-399[»]
4C78X-ray2.00A116-399[»]
4C7BX-ray2.10A117-399[»]
4FVTX-ray2.47A122-395[»]
4FZ3X-ray2.10A118-399[»]
4HD8X-ray2.30A116-399[»]
4JSRX-ray1.70A118-399[»]
4JT8X-ray2.26A118-399[»]
4JT9X-ray2.24A118-399[»]
ProteinModelPortaliQ9NTG7.
SMRiQ9NTG7. Positions 121-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NTG7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini126 – 382257Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the sirtuin family. Class I subfamily.Curated
Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0846.
GeneTreeiENSGT00740000115546.
HOVERGENiHBG057095.
InParanoidiQ9NTG7.
KOiK11413.
OMAiLAWHPRS.
OrthoDBiEOG7WX09C.
PhylomeDBiQ9NTG7.
TreeFamiTF106181.

Family and domain databases

Gene3Di3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
PIRSFiPIRSF037938. SIR2_euk. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

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

Isoform 1 (identifier: Q9NTG7-1) [UniParc]FASTAAdd 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
GO
Isoform 2 (identifier: Q9NTG7-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:257
Mass (Da):28,567
Checksum:i33043FAB6B3F0307
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801R → W.
Corresponds to variant rs28365927 [ dbSNP | Ensembl ].
VAR_051977
Natural varianti208 – 2081V → I.
Corresponds to variant rs11246020 [ dbSNP | Ensembl ].
VAR_051978
Natural varianti369 – 3691G → S.
Corresponds to variant rs3020901 [ dbSNP | Ensembl ].
VAR_051979

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 142142Missing in isoform 2. 1 PublicationVSP_043792Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS53590.1. [Q9NTG7-2]
CCDS7691.1. [Q9NTG7-1]
PIRiT46348.
RefSeqiNP_001017524.1. NM_001017524.2. [Q9NTG7-2]
NP_036371.1. NM_012239.5. [Q9NTG7-1]
UniGeneiHs.716456.

Genome annotation databases

EnsembliENST00000382743; ENSP00000372191; ENSG00000142082. [Q9NTG7-1]
ENST00000529382; ENSP00000437216; ENSG00000142082. [Q9NTG7-2]
GeneIDi23410.
KEGGihsa:23410.
UCSCiuc001loj.4. human. [Q9NTG7-1]

Polymorphism databases

DMDMi38258651.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53590.1. [Q9NTG7-2 ]
CCDS7691.1. [Q9NTG7-1 ]
PIRi T46348.
RefSeqi NP_001017524.1. NM_001017524.2. [Q9NTG7-2 ]
NP_036371.1. NM_012239.5. [Q9NTG7-1 ]
UniGenei Hs.716456.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3GLR X-ray 1.80 A 118-399 [» ]
3GLS X-ray 2.70 A/B/C/D/E/F 118-399 [» ]
3GLT X-ray 2.10 A 118-399 [» ]
3GLU X-ray 2.50 A 118-399 [» ]
4BN4 X-ray 1.30 A 116-399 [» ]
4BN5 X-ray 3.25 A/B/C/D/E/F/G/H/I/J/K/L 119-399 [» ]
4BV3 X-ray 2.00 A 116-399 [» ]
4BVB X-ray 2.00 A 116-399 [» ]
4BVE X-ray 2.05 A 116-399 [» ]
4BVF X-ray 2.70 A 116-399 [» ]
4BVG X-ray 2.50 A 116-399 [» ]
4BVH X-ray 1.90 A/B/C 116-399 [» ]
4C78 X-ray 2.00 A 116-399 [» ]
4C7B X-ray 2.10 A 117-399 [» ]
4FVT X-ray 2.47 A 122-395 [» ]
4FZ3 X-ray 2.10 A 118-399 [» ]
4HD8 X-ray 2.30 A 116-399 [» ]
4JSR X-ray 1.70 A 118-399 [» ]
4JT8 X-ray 2.26 A 118-399 [» ]
4JT9 X-ray 2.24 A 118-399 [» ]
ProteinModelPortali Q9NTG7.
SMRi Q9NTG7. Positions 121-394.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116982. 99 interactions.
DIPi DIP-46861N.
IntActi Q9NTG7. 26 interactions.
MINTi MINT-4540133.
STRINGi 9606.ENSP00000372191.

Chemistry

BindingDBi Q9NTG7.
ChEMBLi CHEMBL4461.

PTM databases

PhosphoSitei Q9NTG7.

Polymorphism databases

DMDMi 38258651.

Proteomic databases

MaxQBi Q9NTG7.
PaxDbi Q9NTG7.
PRIDEi Q9NTG7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000382743 ; ENSP00000372191 ; ENSG00000142082 . [Q9NTG7-1 ]
ENST00000529382 ; ENSP00000437216 ; ENSG00000142082 . [Q9NTG7-2 ]
GeneIDi 23410.
KEGGi hsa:23410.
UCSCi uc001loj.4. human. [Q9NTG7-1 ]

Organism-specific databases

CTDi 23410.
GeneCardsi GC11M000264.
HGNCi HGNC:14931. SIRT3.
HPAi CAB037142.
HPA026809.
MIMi 604481. gene.
neXtProti NX_Q9NTG7.
PharmGKBi PA37936.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0846.
GeneTreei ENSGT00740000115546.
HOVERGENi HBG057095.
InParanoidi Q9NTG7.
KOi K11413.
OMAi LAWHPRS.
OrthoDBi EOG7WX09C.
PhylomeDBi Q9NTG7.
TreeFami TF106181.

Enzyme and pathway databases

Reactomei REACT_200608. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

ChiTaRSi SIRT3. human.
EvolutionaryTracei Q9NTG7.
GeneWikii SIRT3.
GenomeRNAii 23410.
NextBioi 45597.
PROi Q9NTG7.
SOURCEi Search...

Gene expression databases

Bgeei Q9NTG7.
CleanExi HS_SIRT3.
ExpressionAtlasi Q9NTG7. baseline and differential.
Genevestigatori Q9NTG7.

Family and domain databases

Gene3Di 3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view ]
PANTHERi PTHR11085. PTHR11085. 1 hit.
Pfami PF02146. SIR2. 1 hit.
[Graphical view ]
PIRSFi PIRSF037938. SIR2_euk. 1 hit.
SUPFAMi SSF52467. SSF52467. 1 hit.
PROSITEi PS50305. SIRTUIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Frye R.A.
    Biochem. Biophys. Res. Commun. 260:273-279(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-399 (ISOFORM 1).
    Tissue: Testis.
  6. "The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase."
    Schwer B., North B.J., Frye R.A., Ott M., Verdin E.
    J. Cell Biol. 158:647-657(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING BY MPP, MUTAGENESIS OF ARG-7; ARG-13; ARG-17; ARG-21; 99-ARG-ARG-100; ASN-229 AND HIS-248.
  7. "SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria."
    Onyango P., Celic I., McCaffery J.M., Boeke J.D., Feinberg A.P.
    Proc. Natl. Acad. Sci. U.S.A. 99:13653-13658(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins."
    Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., Horikawa I.
    Mol. Biol. Cell 16:4623-4635(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2."
    Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E.
    Proc. Natl. Acad. Sci. U.S.A. 103:10224-10229(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-248, INTERACTION WITH ACSS1.
  10. "The human SIRT3 protein deacetylase is exclusively mitochondrial."
    Cooper H.M., Spelbrink J.N.
    Biochem. J. 411:279-285(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5."
    Schlicker C., Gertz M., Papatheodorou P., Kachholz B., Becker C.F.W., Steegborn C.
    J. Mol. Biol. 382:790-801(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis."
    Ahn B.-H., Kim H.-S., Song S., Lee I.H., Liu J., Vassilopoulos A., Deng C.-X., Finkel T.
    Proc. Natl. Acad. Sci. U.S.A. 105:14447-14452(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-248, FUNCTION, INTERACTION WITH NDUFA9.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "SIRT3 deacetylates ATP synthase F1 complex proteins in response to nutrient and exercise-induced stress."
    Vassilopoulos A., Pennington D.J., Andresson T., Rees D., Fearnley I., Ham A., Yan Y., Flynn C.R., Jones K., Kim H.S., Deng C., Walker J., Gius D.
    Antioxid. Redox Signal. 21:551-564(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating conserved lysines near the active site."
    Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M., Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E., Gibson B.W., Hirschey M.D., Goetzman E.S.
    J. Biol. Chem. 288:33837-33847(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "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, BIOPHYSICOCHEMICAL PROPERTIES, NAD-BINDING.
  17. "Structures of human sirtuin 3 complexes with ADP-ribose and with carba-NAD+ and SRT1720: binding details and inhibition mechanism."
    Nguyen G.T., Schaefer S., Gertz M., Weyand M., Steegborn C.
    Acta Crystallogr. D 69:1423-1432(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 116-399 IN COMPLEX WITH INHIBITOR, NAD-BINDING SITES, ZINC-BINDING SITES.

Entry informationi

Entry nameiSIR3_HUMAN
AccessioniPrimary (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: October 29, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3