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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

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

NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). 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). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). 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 similarity6 Publications

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

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

  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
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei102SubstrateUniRule annotation1
    Binding sitei105SubstrateUniRule annotation1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei158Proton acceptorUniRule annotation2 Publications1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi58 – 77NADUniRule annotation3 PublicationsAdd BLAST20
    Nucleotide bindingi140 – 143NADUniRule annotation3 Publications4
    Nucleotide bindingi249 – 251NADUniRule annotation3 Publications3
    Nucleotide bindingi275 – 277NADUniRule annotation3 Publications3

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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    LigandMetal-binding, NAD, Zinc

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9NXA8

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

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    NAD-dependent protein deacylase sirtuin-5, mitochondrialUniRule annotation (EC:3.5.1.-UniRule annotation3 Publications)
    Alternative name(s):
    Regulatory protein SIR2 homolog 5UniRule annotation
    SIR2-like protein 5UniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:SIRT5UniRule annotation
    Synonyms:SIR2L5
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000124523.14

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:14933 SIRT5

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    604483 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9NXA8

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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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. 4 Publications1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    23408

    Open Targets

    More...
    OpenTargetsi
    ENSG00000124523

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA37938

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2163183

    Drug and drug target database

    More...
    DrugBanki
    DB03478 2'-O-Acetyl Adenosine-5-Diphosphoribose
    DB02059 Adenosine-5-Diphosphoribose
    DB02701 Nicotinamide
    DB04786 Suramin

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2711

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    SIRT5

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    38258652

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 36MitochondrionUniRule annotationAdd BLAST36
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000011026637 – 310NAD-dependent protein deacylase sirtuin-5, mitochondrialAdd BLAST274

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9NXA8

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9NXA8

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q9NXA8

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q9NXA8

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9NXA8

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9NXA8

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    83064
    83065 [Q9NXA8-2]
    83066 [Q9NXA8-3]
    83067 [Q9NXA8-4]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9NXA8

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q9NXA8

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

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000124523 Expressed in 218 organ(s), highest expression level in myocardium

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_SIRT5

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9NXA8 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9NXA8 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA021798
    HPA022002
    HPA022992

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

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with CPS1 (By similarity). Interacts with PCCA (PubMed:23438705). Monomer (PubMed:17355872). Homodimer (PubMed:17355872). Forms homodimers upon suramin binding (PubMed:17355872).By similarity7 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    116980, 26 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q9NXA8, 5 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000368552

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9NXA8

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

    Secondary structure

    1310
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    5XHSX-ray2.19A34-302[»]
    6EQSX-ray1.32A/B/C/D34-302[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9NXA8

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9NXA8

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q9NXA8

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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini41 – 309Deacetylase sirtuin-typeUniRule annotationAdd BLAST269

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

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

    Belongs to the sirtuin family. Class III subfamily.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2684 Eukaryota
    COG0846 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000156080

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000085950

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG056009

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9NXA8

    KEGG Orthology (KO)

    More...
    KOi
    K11415

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    SMQVYPA

    Database of Orthologous Groups

    More...
    OrthoDBi
    1459156at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9NXA8

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF106183

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01412 SIRT5_Af1_CobB, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1600.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01121 Sirtuin_ClassIII, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR003000 Sirtuin
    IPR026591 Sirtuin_cat_small_dom_sf
    IPR027546 Sirtuin_class_III
    IPR026590 Ssirtuin_cat_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02146 SIR2, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52467 SSF52467, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50305 SIRTUIN, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    Q7Z3A0Q7Z3A0_HUMAN
    NAD-dependent protein deacylase sir...
    SIRT5 DKFZp686L2375
    79Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    U3KQT8U3KQT8_HUMAN
    NAD-dependent protein deacylase sir...
    SIRT5
    41Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti53I → M in BAG63757 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029042285F → L. Corresponds to variant dbSNP:rs9464003Ensembl.1
    Natural variantiVAR_051980305E → G. Corresponds to variant dbSNP:rs34162626Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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 No translation available.
    CH471087 Genomic DNA Translation: EAW55332.1
    BC000126 mRNA Translation: AAH00126.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS4526.1 [Q9NXA8-1]
    CCDS4527.1 [Q9NXA8-2]
    CCDS54966.1 [Q9NXA8-3]
    CCDS56398.1 [Q9NXA8-4]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_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]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.567431
    Hs.594133

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000359782; ENSP00000352830; ENSG00000124523 [Q9NXA8-3]
    ENST00000379262; ENSP00000368564; ENSG00000124523 [Q9NXA8-2]
    ENST00000397350; ENSP00000380509; ENSG00000124523 [Q9NXA8-4]
    ENST00000606117; ENSP00000476228; ENSG00000124523 [Q9NXA8-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    23408

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:23408

    UCSC genome browser

    More...
    UCSCi
    uc003naw.4 human [Q9NXA8-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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 No translation available.
    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[»]
    5XHSX-ray2.19A34-302[»]
    6EQSX-ray1.32A/B/C/D34-302[»]
    ProteinModelPortaliQ9NXA8
    SMRiQ9NXA8
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116980, 26 interactors
    IntActiQ9NXA8, 5 interactors
    STRINGi9606.ENSP00000368552

    Chemistry databases

    BindingDBiQ9NXA8
    ChEMBLiCHEMBL2163183
    DrugBankiDB03478 2'-O-Acetyl Adenosine-5-Diphosphoribose
    DB02059 Adenosine-5-Diphosphoribose
    DB02701 Nicotinamide
    DB04786 Suramin
    GuidetoPHARMACOLOGYi2711

    PTM databases

    iPTMnetiQ9NXA8
    PhosphoSitePlusiQ9NXA8

    Polymorphism and mutation databases

    BioMutaiSIRT5
    DMDMi38258652

    Proteomic databases

    EPDiQ9NXA8
    jPOSTiQ9NXA8
    MaxQBiQ9NXA8
    PaxDbiQ9NXA8
    PeptideAtlasiQ9NXA8
    PRIDEiQ9NXA8
    ProteomicsDBi83064
    83065 [Q9NXA8-2]
    83066 [Q9NXA8-3]
    83067 [Q9NXA8-4]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    23408
    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

    Comparative Toxicogenomics Database

    More...
    CTDi
    23408
    DisGeNETi23408
    EuPathDBiHostDB:ENSG00000124523.14

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    SIRT5
    HGNCiHGNC:14933 SIRT5
    HPAiHPA021798
    HPA022002
    HPA022992
    MIMi604483 gene
    neXtProtiNX_Q9NXA8
    OpenTargetsiENSG00000124523
    PharmGKBiPA37938

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2684 Eukaryota
    COG0846 LUCA
    GeneTreeiENSGT00940000156080
    HOGENOMiHOG000085950
    HOVERGENiHBG056009
    InParanoidiQ9NXA8
    KOiK11415
    OMAiSMQVYPA
    OrthoDBi1459156at2759
    PhylomeDBiQ9NXA8
    TreeFamiTF106183

    Enzyme and pathway databases

    ReactomeiR-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
    SABIO-RKiQ9NXA8

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    SIRT5 human
    EvolutionaryTraceiQ9NXA8

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    SIRT5

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    23408

    Protein Ontology

    More...
    PROi
    PR:Q9NXA8

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000124523 Expressed in 218 organ(s), highest expression level in myocardium
    CleanExiHS_SIRT5
    ExpressionAtlasiQ9NXA8 baseline and differential
    GenevisibleiQ9NXA8 HS

    Family and domain databases

    CDDicd01412 SIRT5_Af1_CobB, 1 hit
    Gene3Di3.30.1600.10, 1 hit
    HAMAPiMF_01121 Sirtuin_ClassIII, 1 hit
    InterProiView protein in InterPro
    IPR029035 DHS-like_NAD/FAD-binding_dom
    IPR003000 Sirtuin
    IPR026591 Sirtuin_cat_small_dom_sf
    IPR027546 Sirtuin_class_III
    IPR026590 Ssirtuin_cat_dom
    PfamiView protein in Pfam
    PF02146 SIR2, 1 hit
    SUPFAMiSSF52467 SSF52467, 1 hit
    PROSITEiView protein in PROSITE
    PS50305 SIRTUIN, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

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

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSIR5_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9NXA8
    Secondary accession number(s): B4DFM4
    , B4DYJ5, F5H5Z9, Q5T294, Q5T295, Q9Y6E6
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: October 31, 2003
    Last modified: January 16, 2019
    This is version 158 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    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. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
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