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Protein

NAD-dependent protein deacetylase sirtuin-3, mitochondrial

Gene

SIRT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation3 Publications

Cofactori

Zn2+Note: 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

    • NAD+ ADP-ribosyltransferase activity Source: ProtInc
    • NAD+ binding Source: InterPro
    • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: Ensembl
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • aerobic respiration Source: UniProtKB
    • aging Source: Ensembl
    • mitochondrion organization Source: Reactome
    • organelle organization Source: Reactome
    • peptidyl-lysine deacetylation Source: UniProtKB
    • protein ADP-ribosylation Source: ProtInc
    • protein deacetylation Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_264212. 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 Componenti: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:14931. SIRT3.

    Subcellular locationi

    GO - Cellular componenti

    • membrane Source: Ensembl
    • mitochondrial matrix Source: Reactome
    • 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.

    Polymorphism and mutation databases

    BioMutaiSIRT3.
    DMDMi38258651.

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei122 – 1221N6-succinyllysineBy similarity

    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.
    GenevisibleiQ9NTG7. HS.

    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. 102 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 – 1339Combined sources
    Turni134 – 1363Combined sources
    Beta strandi140 – 1445Combined sources
    Helixi146 – 1527Combined sources
    Beta strandi157 – 1593Combined sources
    Turni160 – 1623Combined sources
    Helixi164 – 1685Combined sources
    Beta strandi171 – 1755Combined sources
    Helixi176 – 1805Combined sources
    Helixi182 – 1876Combined sources
    Helixi190 – 19910Combined sources
    Beta strandi201 – 2033Combined sources
    Helixi208 – 21811Combined sources
    Beta strandi222 – 2276Combined sources
    Helixi233 – 2364Combined sources
    Helixi241 – 2433Combined sources
    Beta strandi244 – 2463Combined sources
    Beta strandi249 – 2568Combined sources
    Turni257 – 2593Combined sources
    Beta strandi262 – 2643Combined sources
    Helixi265 – 2739Combined sources
    Turni281 – 2833Combined sources
    Beta strandi286 – 2916Combined sources
    Helixi300 – 3045Combined sources
    Helixi305 – 3117Combined sources
    Beta strandi313 – 3197Combined sources
    Helixi327 – 3304Combined sources
    Helixi331 – 3333Combined sources
    Beta strandi340 – 3467Combined sources
    Helixi349 – 3535Combined sources
    Beta strandi359 – 3646Combined sources
    Helixi366 – 37712Combined sources
    Helixi380 – 39112Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4O8ZX-ray2.00A116-399[»]
    4V1CX-ray2.95A/B/E/G/I/K121-394[»]
    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.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view]
    PANTHERiPTHR11085. PTHR11085. 1 hit.
    PfamiPF02146. SIR2. 1 hit.
    [Graphical view]
    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. AlignAdd to basket

    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:
    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.
    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]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    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.
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4O8ZX-ray2.00A116-399[»]
    4V1CX-ray2.95A/B/E/G/I/K121-394[»]
    ProteinModelPortaliQ9NTG7.
    SMRiQ9NTG7. Positions 121-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116982. 102 interactions.
    DIPiDIP-46861N.
    IntActiQ9NTG7. 26 interactions.
    MINTiMINT-4540133.
    STRINGi9606.ENSP00000372191.

    Chemistry

    BindingDBiQ9NTG7.
    ChEMBLiCHEMBL4461.

    PTM databases

    PhosphoSiteiQ9NTG7.

    Polymorphism and mutation databases

    BioMutaiSIRT3.
    DMDMi38258651.

    Proteomic databases

    MaxQBiQ9NTG7.
    PaxDbiQ9NTG7.
    PRIDEiQ9NTG7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi23410.
    GeneCardsiGC11M000264.
    HGNCiHGNC:14931. SIRT3.
    HPAiCAB037142.
    HPA026809.
    MIMi604481. gene.
    neXtProtiNX_Q9NTG7.
    PharmGKBiPA37936.
    GenAtlasiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    ReactomeiREACT_264212. Transcriptional activation of mitochondrial biogenesis.

    Miscellaneous databases

    ChiTaRSiSIRT3. human.
    EvolutionaryTraceiQ9NTG7.
    GeneWikiiSIRT3.
    GenomeRNAii23410.
    NextBioi45597.
    PROiQ9NTG7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NTG7.
    CleanExiHS_SIRT3.
    ExpressionAtlasiQ9NTG7. baseline and differential.
    GenevisibleiQ9NTG7. HS.

    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.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view]
    PANTHERiPTHR11085. PTHR11085. 1 hit.
    PfamiPF02146. SIR2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    PROSITEiPS50305. SIRTUIN. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    17. "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.
    18. "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: June 24, 2015
    This is version 128 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.