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Protein

NAD-dependent protein deacylase sirtuin-5, mitochondrial

Gene

SIRT5

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

Functioni

NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX.By similarity5 Publications

Catalytic activityi

NAD+ + a malonylprotein = nicotinamide + O-malonyl-ADP-ribose + a protein.UniRule annotation
NAD+ + a succinylprotein = nicotinamide + O-succinyl-ADP-ribose + a protein.UniRule annotation
NAD+ + a glutarylprotein = nicotinamide + O-glutaryl-ADP-ribose + a protein.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation1 PublicationNote: Binds 1 zinc ion per subunit.UniRule annotation1 Publication

Enzyme regulationi

Inhibited by suramin. NAD-dependent lysine desuccinylase activity is inhibited by physiological nicotinamide concentrations, while deacetylase activity is not. In contrast, resveratrol activates deacetylase activity, while inhibiting desuccinylase activity.3 Publications

Kineticsi

  1. KM=6.1 µM for a synthetic histone H3K9 malonyllysine peptide1 Publication
  2. KM=5.8 µM for a synthetic histone H3K9 succinyllysine peptide1 Publication
  3. KM=8.7 µM for a synthetic GLUD1 peptide malonylated at 'Lys-503'1 Publication
  4. KM=14 µM for a synthetic GLUD1 peptide succinylated at 'Lys-503'1 Publication
  5. KM=150 µM for a synthetic ACSS1 peptide malonylated at 'Lys-628'1 Publication
  6. KM=450 µM for a synthetic ACSS1 peptide succinylated at 'Lys-628'1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei102SubstrateUniRule annotation1
    Binding sitei105SubstrateUniRule annotation1
    Active sitei158Proton acceptorUniRule annotation1 Publication1
    Metal bindingi166ZincUniRule annotation1
    Metal bindingi169ZincUniRule annotation1
    Metal bindingi207ZincUniRule annotation1
    Metal bindingi212ZincUniRule annotation1
    Binding sitei293NAD; via amide nitrogenUniRule annotation3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi58 – 77NADUniRule annotation3 PublicationsAdd BLAST20
    Nucleotide bindingi140 – 143NADUniRule annotation3 Publications4
    Nucleotide bindingi249 – 251NADUniRule annotation3 Publications3
    Nucleotide bindingi275 – 277NADUniRule annotation3 Publications3

    GO - Molecular functioni

    • NAD+ ADP-ribosyltransferase activity Source: ProtInc
    • NAD+ binding Source: UniProtKB
    • protein-glutaryllysine deglutarylase activity Source: UniProtKB
    • protein-malonyllysine demalonylase activity Source: UniProtKB
    • protein-succinyllysine desuccinylase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • chromatin silencing Source: ProtInc
    • negative regulation of cardiac muscle cell apoptotic process Source: Ensembl
    • negative regulation of reactive oxygen species metabolic process Source: UniProtKB
    • peptidyl-lysine demalonylation Source: UniProtKB
    • peptidyl-lysine desuccinylation Source: UniProtKB
    • protein ADP-ribosylation Source: ProtInc
    • protein deacetylation Source: UniProtKB
    • protein deglutarylation Source: UniProtKB
    • protein demalonylation Source: UniProtKB
    • protein desuccinylation Source: UniProtKB
    • regulation of ketone biosynthetic process Source: UniProtKB
    • response to nutrient levels Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000124523-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD-dependent protein deacylase sirtuin-5, mitochondrialUniRule annotation (EC:3.5.1.-UniRule annotation1 Publication)
    Alternative name(s):
    Regulatory protein SIR2 homolog 5UniRule annotation
    SIR2-like protein 5UniRule annotation
    Gene namesi
    Name:SIRT5UniRule annotation
    Synonyms:SIR2L5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14933. SIRT5.

    Subcellular locationi

    Isoform 1 :
    Isoform 2 :

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • mitochondrial inner membrane Source: Ensembl
    • mitochondrial intermembrane space Source: UniProtKB
    • mitochondrial matrix Source: UniProtKB
    • mitochondrion Source: UniProtKB
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi69T → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi102Y → F: Increases the KM for desuccinylation. 1 Publication1
    Mutagenesisi105R → M: Increases the KM for desuccinylation. Does not affect deacetylase activity. 2 Publications1
    Mutagenesisi158H → A: Abolishes desuccinylation and deglutarylation activity. 3 Publications1

    Organism-specific databases

    DisGeNETi23408.
    OpenTargetsiENSG00000124523.
    PharmGKBiPA37938.

    Chemistry databases

    ChEMBLiCHEMBL2163183.
    DrugBankiDB02701. Nicotinamide.
    DB04786. Suramin.
    GuidetoPHARMACOLOGYi2711.

    Polymorphism and mutation databases

    BioMutaiSIRT5.
    DMDMi38258652.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 36MitochondrionUniRule annotationAdd BLAST36
    ChainiPRO_000011026637 – 310NAD-dependent protein deacylase sirtuin-5, mitochondrialAdd BLAST274

    Proteomic databases

    EPDiQ9NXA8.
    MaxQBiQ9NXA8.
    PaxDbiQ9NXA8.
    PeptideAtlasiQ9NXA8.
    PRIDEiQ9NXA8.

    PTM databases

    iPTMnetiQ9NXA8.
    PhosphoSitePlusiQ9NXA8.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiENSG00000124523.
    CleanExiHS_SIRT5.
    ExpressionAtlasiQ9NXA8. baseline and differential.
    GenevisibleiQ9NXA8. HS.

    Organism-specific databases

    HPAiHPA021798.
    HPA022002.
    HPA022992.

    Interactioni

    Subunit structurei

    Interacts with CPS1 (By similarity). Monomer. Homodimer. Forms homodimers upon suramin binding.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi116980. 20 interactors.
    IntActiQ9NXA8. 5 interactors.
    STRINGi9606.ENSP00000368552.

    Chemistry databases

    BindingDBiQ9NXA8.

    Structurei

    Secondary structure

    1310
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi40 – 49Combined sources10
    Beta strandi51 – 57Combined sources7
    Helixi59 – 63Combined sources5
    Turni64 – 66Combined sources3
    Beta strandi70 – 72Combined sources3
    Helixi73 – 75Combined sources3
    Helixi82 – 85Combined sources4
    Helixi88 – 93Combined sources6
    Helixi95 – 108Combined sources14
    Helixi109 – 111Combined sources3
    Helixi116 – 129Combined sources14
    Turni130 – 132Combined sources3
    Beta strandi134 – 139Combined sources6
    Helixi145 – 148Combined sources4
    Beta strandi153 – 156Combined sources4
    Beta strandi159 – 166Combined sources8
    Turni167 – 169Combined sources3
    Beta strandi172 – 174Combined sources3
    Beta strandi178 – 181Combined sources4
    Helixi182 – 184Combined sources3
    Beta strandi190 – 193Combined sources4
    Helixi201 – 203Combined sources3
    Turni210 – 212Combined sources3
    Beta strandi215 – 220Combined sources6
    Helixi229 – 241Combined sources13
    Beta strandi243 – 250Combined sources8
    Beta strandi252 – 254Combined sources3
    Helixi257 – 259Combined sources3
    Helixi261 – 266Combined sources6
    Beta strandi271 – 277Combined sources7
    Beta strandi284 – 291Combined sources8
    Helixi293 – 300Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2B4YX-ray1.90A/B/C/D34-302[»]
    2NYRX-ray2.06A/B34-302[»]
    3RIGX-ray2.00A/B34-302[»]
    3RIYX-ray1.55A/B34-302[»]
    4F4UX-ray2.00A/B34-302[»]
    4F56X-ray1.70A/B34-302[»]
    4G1CX-ray1.94A/B36-302[»]
    4HDAX-ray2.60A/B34-302[»]
    5BWLX-ray1.55A33-302[»]
    ProteinModelPortaliQ9NXA8.
    SMRiQ9NXA8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NXA8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini41 – 309Deacetylase sirtuin-typeUniRule annotationAdd BLAST269

    Domaini

    In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-102 and Arg-105) that bind to malonylated and succinylated substrates and define the specificity (PubMed:22076378).1 Publication

    Sequence similaritiesi

    Belongs to the sirtuin family. Class III subfamily.UniRule annotation
    Contains 1 deacetylase sirtuin-type domain.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG2684. Eukaryota.
    COG0846. LUCA.
    GeneTreeiENSGT00850000132288.
    HOGENOMiHOG000085950.
    HOVERGENiHBG056009.
    InParanoidiQ9NXA8.
    KOiK11415.
    OMAiLIHMHGE.
    OrthoDBiEOG091G0KF2.
    PhylomeDBiQ9NXA8.
    TreeFamiTF106183.

    Family and domain databases

    CDDicd01412. SIRT5_Af1_CobB. 1 hit.
    Gene3Di3.30.1600.10. 2 hits.
    3.40.50.1220. 3 hits.
    HAMAPiMF_01121. Sirtuin_ClassIII. 1 hit.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR003000. Sirtuin.
    IPR026591. Sirtuin_cat_small_dom.
    IPR027546. Sirtuin_class_III.
    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NXA8-1) [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
    MRPLQIVPSR LISQLYCGLK PPASTRNQIC LKMARPSSSM ADFRKFFAKA
    60 70 80 90 100
    KHIVIISGAG VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE
    110 120 130 140 150
    FYHYRREVMG SKEPNAGHRA IAECETRLGK QGRRVVVITQ NIDELHRKAG
    160 170 180 190 200
    TKNLLEIHGS LFKTRCTSCG VVAENYKSPI CPALSGKGAP EPGTQDASIP
    210 220 230 240 250
    VEKLPRCEEA GCGGLLRPHV VWFGENLDPA ILEEVDRELA HCDLCLVVGT
    260 270 280 290 300
    SSVVYPAAMF APQVAARGVP VAEFNTETTP ATNRFRFHFQ GPCGTTLPEA
    310
    LACHENETVS
    Length:310
    Mass (Da):33,881
    Last modified:October 31, 2003 - v2
    Checksum:i022DA32CDB43AC3A
    GO
    Isoform 2 (identifier: Q9NXA8-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         286-299: RFHFQGPCGTTLPE → SHLISISSLIIIKN
         300-310: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:299
    Mass (Da):32,674
    Checksum:i2EE7C311AAA34CBA
    GO
    Isoform 3 (identifier: Q9NXA8-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         189-206: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:292
    Mass (Da):31,994
    Checksum:iD89A65C251224735
    GO
    Isoform 4 (identifier: Q9NXA8-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:202
    Mass (Da):21,689
    Checksum:i051C7D4BE508D66B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti53I → M in BAG63757 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_029042285F → L.Corresponds to variant rs9464003dbSNPEnsembl.1
    Natural variantiVAR_051980305E → G.Corresponds to variant rs34162626dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0422911 – 108Missing in isoform 4. 1 PublicationAdd BLAST108
    Alternative sequenceiVSP_042292189 – 206Missing in isoform 3. 1 PublicationAdd BLAST18
    Alternative sequenceiVSP_008730286 – 299RFHFQ…TTLPE → SHLISISSLIIIKN in isoform 2. 1 PublicationAdd BLAST14
    Alternative sequenceiVSP_008731300 – 310Missing in isoform 2. 1 PublicationAdd BLAST11

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF083110 mRNA. Translation: AAD40853.1.
    AK000355 mRNA. Translation: BAA91107.1.
    AK294162 mRNA. Translation: BAG57485.1.
    AK302467 mRNA. Translation: BAG63757.1.
    AM393414 mRNA. Translation: CAL38292.1.
    AL441883 Genomic DNA. Translation: CAI19837.1.
    AL441883 Genomic DNA. Translation: CAI19838.1.
    CH471087 Genomic DNA. Translation: EAW55332.1.
    BC000126 mRNA. Translation: AAH00126.1.
    CCDSiCCDS4526.1. [Q9NXA8-1]
    CCDS4527.1. [Q9NXA8-2]
    CCDS54966.1. [Q9NXA8-3]
    CCDS56398.1. [Q9NXA8-4]
    RefSeqiNP_001180196.1. NM_001193267.2. [Q9NXA8-3]
    NP_001229756.1. NM_001242827.1. [Q9NXA8-4]
    NP_036373.1. NM_012241.4. [Q9NXA8-1]
    NP_112534.1. NM_031244.3. [Q9NXA8-2]
    XP_005249025.1. XM_005248968.4. [Q9NXA8-1]
    UniGeneiHs.567431.
    Hs.594133.

    Genome annotation databases

    EnsembliENST00000359782; ENSP00000352830; ENSG00000124523. [Q9NXA8-3]
    ENST00000379262; ENSP00000368564; ENSG00000124523. [Q9NXA8-2]
    ENST00000397350; ENSP00000380509; ENSG00000124523. [Q9NXA8-4]
    ENST00000606117; ENSP00000476228; ENSG00000124523. [Q9NXA8-1]
    GeneIDi23408.
    KEGGihsa:23408.
    UCSCiuc003naw.4. human. [Q9NXA8-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF083110 mRNA. Translation: AAD40853.1.
    AK000355 mRNA. Translation: BAA91107.1.
    AK294162 mRNA. Translation: BAG57485.1.
    AK302467 mRNA. Translation: BAG63757.1.
    AM393414 mRNA. Translation: CAL38292.1.
    AL441883 Genomic DNA. Translation: CAI19837.1.
    AL441883 Genomic DNA. Translation: CAI19838.1.
    CH471087 Genomic DNA. Translation: EAW55332.1.
    BC000126 mRNA. Translation: AAH00126.1.
    CCDSiCCDS4526.1. [Q9NXA8-1]
    CCDS4527.1. [Q9NXA8-2]
    CCDS54966.1. [Q9NXA8-3]
    CCDS56398.1. [Q9NXA8-4]
    RefSeqiNP_001180196.1. NM_001193267.2. [Q9NXA8-3]
    NP_001229756.1. NM_001242827.1. [Q9NXA8-4]
    NP_036373.1. NM_012241.4. [Q9NXA8-1]
    NP_112534.1. NM_031244.3. [Q9NXA8-2]
    XP_005249025.1. XM_005248968.4. [Q9NXA8-1]
    UniGeneiHs.567431.
    Hs.594133.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2B4YX-ray1.90A/B/C/D34-302[»]
    2NYRX-ray2.06A/B34-302[»]
    3RIGX-ray2.00A/B34-302[»]
    3RIYX-ray1.55A/B34-302[»]
    4F4UX-ray2.00A/B34-302[»]
    4F56X-ray1.70A/B34-302[»]
    4G1CX-ray1.94A/B36-302[»]
    4HDAX-ray2.60A/B34-302[»]
    5BWLX-ray1.55A33-302[»]
    ProteinModelPortaliQ9NXA8.
    SMRiQ9NXA8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116980. 20 interactors.
    IntActiQ9NXA8. 5 interactors.
    STRINGi9606.ENSP00000368552.

    Chemistry databases

    BindingDBiQ9NXA8.
    ChEMBLiCHEMBL2163183.
    DrugBankiDB02701. Nicotinamide.
    DB04786. Suramin.
    GuidetoPHARMACOLOGYi2711.

    PTM databases

    iPTMnetiQ9NXA8.
    PhosphoSitePlusiQ9NXA8.

    Polymorphism and mutation databases

    BioMutaiSIRT5.
    DMDMi38258652.

    Proteomic databases

    EPDiQ9NXA8.
    MaxQBiQ9NXA8.
    PaxDbiQ9NXA8.
    PeptideAtlasiQ9NXA8.
    PRIDEiQ9NXA8.

    Protocols and materials databases

    DNASUi23408.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000359782; ENSP00000352830; ENSG00000124523. [Q9NXA8-3]
    ENST00000379262; ENSP00000368564; ENSG00000124523. [Q9NXA8-2]
    ENST00000397350; ENSP00000380509; ENSG00000124523. [Q9NXA8-4]
    ENST00000606117; ENSP00000476228; ENSG00000124523. [Q9NXA8-1]
    GeneIDi23408.
    KEGGihsa:23408.
    UCSCiuc003naw.4. human. [Q9NXA8-1]

    Organism-specific databases

    CTDi23408.
    DisGeNETi23408.
    GeneCardsiSIRT5.
    HGNCiHGNC:14933. SIRT5.
    HPAiHPA021798.
    HPA022002.
    HPA022992.
    MIMi604483. gene.
    neXtProtiNX_Q9NXA8.
    OpenTargetsiENSG00000124523.
    PharmGKBiPA37938.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2684. Eukaryota.
    COG0846. LUCA.
    GeneTreeiENSGT00850000132288.
    HOGENOMiHOG000085950.
    HOVERGENiHBG056009.
    InParanoidiQ9NXA8.
    KOiK11415.
    OMAiLIHMHGE.
    OrthoDBiEOG091G0KF2.
    PhylomeDBiQ9NXA8.
    TreeFamiTF106183.

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000124523-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ9NXA8.
    GeneWikiiSIRT5.
    GenomeRNAii23408.
    PROiQ9NXA8.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000124523.
    CleanExiHS_SIRT5.
    ExpressionAtlasiQ9NXA8. baseline and differential.
    GenevisibleiQ9NXA8. HS.

    Family and domain databases

    CDDicd01412. SIRT5_Af1_CobB. 1 hit.
    Gene3Di3.30.1600.10. 2 hits.
    3.40.50.1220. 3 hits.
    HAMAPiMF_01121. Sirtuin_ClassIII. 1 hit.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR003000. Sirtuin.
    IPR026591. Sirtuin_cat_small_dom.
    IPR027546. Sirtuin_class_III.
    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...

    Entry informationi

    Entry nameiSIR5_HUMAN
    AccessioniPrimary (citable) accession number: Q9NXA8
    Secondary accession number(s): B4DFM4
    , B4DYJ5, F5H5Z9, Q5T294, Q5T295, Q9Y6E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: October 31, 2003
    Last modified: November 2, 2016
    This is version 141 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

    The mechanism of demalonylation and desuccinylation involves the presence of a 1',2'-cyclic intermediate, suggesting that sirtuins use the ADP-ribose-peptidylamidate mechanism to remove acyl groups from substrate lysine residues.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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

    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 one 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.