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Q9NTG7

- SIR3_HUMAN

UniProt

Q9NTG7 - SIR3_HUMAN

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
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (31 Oct 2003)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    5. 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

    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. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: UniProtKB

    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).
    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

    ArrayExpressiQ9NTG7.
    BgeeiQ9NTG7.
    CleanExiHS_SIRT3.
    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. 94 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.
    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

    MAFWGWRAAA ALRLWGRVVE RVEAGGGVGP FQACGCRLVL GGRDDVSAGL    50
    RGSHGARGEP LDPARPLQRP PRPEVPRAFR RQPRAAAPSF FFSSIKGGRR 100
    SISFSVGASS VVGSGGSSDK GKLSLQDVAE LIRARACQRV VVMVGAGIST 150
    PSGIPDFRSP GSGLYSNLQQ YDLPYPEAIF ELPFFFHNPK PFFTLAKELY 200
    PGNYKPNVTH YFLRLLHDKG LLLRLYTQNI DGLERVSGIP ASKLVEAHGT 250
    FASATCTVCQ RPFPGEDIRA DVMADRVPRC PVCTGVVKPD IVFFGEPLPQ 300
    RFLLHVVDFP MADLLLILGT SLEVEPFASL TEAVRSSVPR LLINRDLVGP 350
    LAWHPRSRDV AQLGDVVHGV ESLVELLGWT EEMRDLVQRE TGKLDGPDK 399
    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. 94 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 GC11M000241.
    HGNCi HGNC:14931. SIRT3.
    HPAi CAB037142.
    HPA026809.
    MIMi 604481. gene.
    neXtProti NX_Q9NTG7.
    PharmGKBi PA37936.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0846.
    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

    ArrayExpressi Q9NTG7.
    Bgeei Q9NTG7.
    CleanExi HS_SIRT3.
    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

    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. 0:0-0(2013) [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 1, 2014
    This is version 121 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