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Entry version 169 (17 Jun 2020)
Sequence version 1 (01 Oct 2000)
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Protein

NAD-dependent protein deacetylase sirtuin-7

Gene

SIRT7

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 protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase and deglutarylase), depending on the context (PubMed:22722849, PubMed:26907567, PubMed:30653310, PubMed:31542297). Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac) (PubMed:22722849, PubMed:30420520). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression (PubMed:22722849, PubMed:30653310). H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor (PubMed:22722849). Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells (PubMed:22722849). Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes (PubMed:30653310). Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53 (PubMed:24207024, PubMed:26867678, PubMed:28147277, PubMed:28886238, PubMed:28426094, PubMed:30540930, PubMed:31075303, PubMed:30944854, PubMed:28790157). Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex (PubMed:16618798, PubMed:19174463, PubMed:24207024). Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:16618798, PubMed:19174463, PubMed:24207024). In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription (PubMed:24207024). Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis (PubMed:19174463). Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex (PubMed:26867678). Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65 (PubMed:31075303). Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation (PubMed:30944854). Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B) (PubMed:28886238). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (PubMed:28426094). Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL (PubMed:30540930). Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51 (PubMed:28147277). Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). In addition to protein deacetylase activity, also acts as protein-lysine deacylase (PubMed:27436229, PubMed:27997115, PubMed:31542297). Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (PubMed:31542297). Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair (PubMed:27436229). Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ) (By similarity). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina (PubMed:31226208). Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability (PubMed:29728458). Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity).By similarity20 Publications

Caution

Was originally termed SIR-T8/SIRT8 (PubMed:11953824). This was later retracted (PubMed:12454780, PubMed:12454781).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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+By similarityNote: Binds 1 zinc ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

NAD-dependent protein-lysine deacetylase and deacylase activities are activated by nucleic acids (PubMed:26907567, PubMed:27997115). Histone deacetylase activity is activated by DNA (PubMed:27997115). Protein-lysine deacylase activity is activated by RNA (PubMed:26907567). H3K18Ac histone deacetylase activity is inhibited by methylation at Arg-388 (PubMed:30420520). H3K18Ac histone deacetylase activity is inhibited by deubiquitination by USP7 (PubMed:28655758).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei187Proton acceptor4 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi195ZincPROSITE-ProRule annotation1
Metal bindingi198ZincPROSITE-ProRule annotation1
Metal bindingi225ZincPROSITE-ProRule annotation1
Metal bindingi228ZincPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei315NAD; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi107 – 126NADBy similarityAdd BLAST20
Nucleotide bindingi167 – 170NADBy similarity4
Nucleotide bindingi268 – 270NADBy similarity3
Nucleotide bindingi297 – 299NADBy similarity3

<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 functionChromatin regulator, Repressor, Transferase
Biological processDNA damage, DNA repair, Transcription, Transcription regulation
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9NRC8

<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%5Fand%5Ftaxonomy%5Fsection">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 deacetylase sirtuin-7 (EC:2.3.1.2866 Publications)
Alternative name(s):
NAD-dependent protein deacylase sirtuin-7 (EC:2.3.1.-2 Publications)
Regulatory protein SIR2 homolog 7
SIR2-like protein 7
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:SIRT71 PublicationImported
Synonyms:SIR2L7
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000187531.13

Human Gene Nomenclature Database

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HGNCi
HGNC:14935 SIRT7

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606212 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9NRC8

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi111S → A: Catalytically inactive mutant; abolishes activation of pre-rRNA synthesis. Abolishes deacetylation of DDB1. Abolished histone desuccinylase activity; when associated with Y-187. 4 Publications1
Mutagenesisi187H → Y: Abolishes deacylase and deacetylase activities and activation of pre-rRNA synthesis. Abolished histone desuccinylase activity; when associated with A-111. 5 Publications1
Mutagenesisi388R → F: Mimics methylation status; impaired histone deacetylase activity. 1 Publication1
Mutagenesisi388R → K: Decreased methylation; does not affect histone deacetylase activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
51547

Open Targets

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OpenTargetsi
ENSG00000187531

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37940

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q9NRC8 Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2163184

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SIRT7

Domain mapping of disease mutations (DMDM)

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DMDMi
38258650

<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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001102711 – 400NAD-dependent protein deacetylase sirtuin-7Add BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei388Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei388Omega-N-methylarginine; alternateCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated during mitosis.1 Publication
Methylation at Arg-388 by PRMT6 inhibits the H3K18Ac histone deacetylase activity, promoting mitochondria biogenesis and maintaining mitochondria respiration.1 Publication
Ubiquitinated via 'Lys-63'-linked ubiquitin chains (PubMed:28655758). Deubiquitinated by USP7, inhibiting the H3K18Ac histone deacetylase activity and regulating gluconeogenesis (PubMed:28655758).1 Publication

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9NRC8

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9NRC8

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9NRC8

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9NRC8

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

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PaxDbi
Q9NRC8

PeptideAtlas

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PeptideAtlasi
Q9NRC8

PRoteomics IDEntifications database

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PRIDEi
Q9NRC8

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
82334 [Q9NRC8-1]
82335 [Q9NRC8-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9NRC8

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

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PhosphoSitePlusi
Q9NRC8

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Overexpressed in thyroid carcinoma cell lines and tissues, but not in adenomas.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000187531 Expressed in lower esophagus mucosa and 202 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9NRC8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9NRC8 HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000187531 Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with UBTF and the RNA polymerase I complex (PubMed:16618798, PubMed:19174463).

Interacts with components of the B-WICH complex, such as MYBBP1A, SMARCA5/SNF2H and BAZ1B/WSTF (PubMed:22586326).

Interacts with ELK4, leading to stabilization at target promoters for H3K18Ac deacetylation (PubMed:22722849).

Interacts with histone H2A and/or histone H2B (PubMed:22722849).

Interacts with DNMT1 (By similarity).

Interacts with SIRT1 (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
119602, 679 interactors

Database of interacting proteins

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DIPi
DIP-59906N

Protein interaction database and analysis system

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IntActi
Q9NRC8, 10 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000329466

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9NRC8

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q9NRC8 protein

<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

1400
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q9NRC8

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini90 – 331Deacetylase sirtuin-typePROSITE-ProRule annotationAdd BLAST242

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi8 – 74Arg-richAdd BLAST67

<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 IV subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1905 Eukaryota
COG0846 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159703

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_023643_6_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9NRC8

KEGG Orthology (KO)

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KOi
K11417

Identification of Orthologs from Complete Genome Data

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OMAi
RGCAKRA

Database of Orthologous Groups

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OrthoDBi
1459156at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9NRC8

TreeFam database of animal gene trees

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TreeFami
TF106184

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029035 DHS-like_NAD/FAD-binding_dom
IPR003000 Sirtuin
IPR026590 Ssirtuin_cat_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF02146 SIR2, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52467 SSF52467, 1 hit

PROSITE; a protein domain and family database

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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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry describes 3 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9NRC8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MAAGGLSRSE RKAAERVRRL REEQQRERLR QVSRILRKAA AERSAEEGRL
60 70 80 90 100
LAESADLVTE LQGRSRRREG LKRRQEEVCD DPEELRGKVR ELASAVRNAK
110 120 130 140 150
YLVVYTGAGI STAASIPDYR GPNGVWTLLQ KGRSVSAADL SEAEPTLTHM
160 170 180 190 200
SITRLHEQKL VQHVVSQNCD GLHLRSGLPR TAISELHGNM YIEVCTSCVP
210 220 230 240 250
NREYVRVFDV TERTALHRHQ TGRTCHKCGT QLRDTIVHFG ERGTLGQPLN
260 270 280 290 300
WEAATEAASR ADTILCLGSS LKVLKKYPRL WCMTKPPSRR PKLYIVNLQW
310 320 330 340 350
TPKDDWAALK LHGKCDDVMR LLMAELGLEI PAYSRWQDPI FSLATPLRAG
360 370 380 390 400
EEGSHSRKSL CRSREEAPPG DRGAPLSSAP ILGGWFGRGC TKRTKRKKVT
Length:400
Mass (Da):44,898
Last modified:October 1, 2000 - v1
<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:i55D7736A864AFE6F
GO
Isoform 2 (identifier: Q9NRC8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-183: QHVVSQNCDGLHLRSGLPRTAI → RALGGWYTCQGPGRAPWCPVGN
     184-400: Missing.

Show »
Length:183
Mass (Da):20,404
Checksum:iEC211D79031585C2
GO
Isoform 3 (identifier: Q9NRC8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MAAGGLSRSERKAAERVRRLREEQQRERLR → MPGPRRRSPSACP
     336-400: WQDPIFSLATPLRAGEEGSHSRKSLCRSREEAPPGDRGAPLSSAPILGGWFGRGCTKRTKRKKVT → VL

Show »
Length:320
Mass (Da):35,851
Checksum:iC0E80615256EEA7A
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
I3L480I3L480_HUMAN
NAD-dependent protein deacetylase s...
SIRT7
150Annotation 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>
I3L2A4I3L2A4_HUMAN
NAD-dependent protein deacetylase s...
SIRT7
116Annotation 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAB70848 differs from that shown.Curated

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 conflicti71L → Q in BAG52860 (PubMed:14702039).Curated1
Sequence conflicti384G → S in BAF82954 (PubMed:14702039).Curated1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0443961 – 30MAAGG…RERLR → MPGPRRRSPSACP in isoform 3. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_008736162 – 183QHVVS…PRTAI → RALGGWYTCQGPGRAPWCPV GN in isoform 2. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_008737184 – 400Missing in isoform 2. 1 PublicationAdd BLAST217
Alternative sequenceiVSP_044397336 – 400WQDPI…RKKVT → VL in isoform 3. 1 PublicationAdd BLAST65

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF233395 mRNA Translation: AAF43431.1
AK002027 mRNA Translation: BAA92044.1
AK094326 mRNA Translation: BAG52860.1
AK290265 mRNA Translation: BAF82954.1
AC145207 Genomic DNA No translation available.
BC017305 mRNA Translation: AAH17305.1
BC101791 mRNA Translation: AAI01792.1
BC101793 mRNA Translation: AAI01794.1
AL137626 mRNA Translation: CAB70848.2 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11792.1 [Q9NRC8-1]

Protein sequence database of the Protein Information Resource

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PIRi
T46324

NCBI Reference Sequences

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RefSeqi
NP_057622.1, NM_016538.2 [Q9NRC8-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000328666; ENSP00000329466; ENSG00000187531 [Q9NRC8-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
51547

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:51547

UCSC genome browser

More...
UCSCi
uc002kcj.3 human [Q9NRC8-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF233395 mRNA Translation: AAF43431.1
AK002027 mRNA Translation: BAA92044.1
AK094326 mRNA Translation: BAG52860.1
AK290265 mRNA Translation: BAF82954.1
AC145207 Genomic DNA No translation available.
BC017305 mRNA Translation: AAH17305.1
BC101791 mRNA Translation: AAI01792.1
BC101793 mRNA Translation: AAI01794.1
AL137626 mRNA Translation: CAB70848.2 Sequence problems.
CCDSiCCDS11792.1 [Q9NRC8-1]
PIRiT46324
RefSeqiNP_057622.1, NM_016538.2 [Q9NRC8-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IQZX-ray2.33A5-73[»]
6G0SX-ray1.48D269-279[»]
SMRiQ9NRC8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi119602, 679 interactors
DIPiDIP-59906N
IntActiQ9NRC8, 10 interactors
STRINGi9606.ENSP00000329466

Chemistry databases

BindingDBiQ9NRC8
ChEMBLiCHEMBL2163184

PTM databases

iPTMnetiQ9NRC8
PhosphoSitePlusiQ9NRC8

Polymorphism and mutation databases

BioMutaiSIRT7
DMDMi38258650

Proteomic databases

EPDiQ9NRC8
jPOSTiQ9NRC8
MassIVEiQ9NRC8
MaxQBiQ9NRC8
PaxDbiQ9NRC8
PeptideAtlasiQ9NRC8
PRIDEiQ9NRC8
ProteomicsDBi82334 [Q9NRC8-1]
82335 [Q9NRC8-2]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
Q9NRC8 1 sequenced antibody

Antibodypedia a portal for validated antibodies

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Antibodypediai
19848 468 antibodies

The DNASU plasmid repository

More...
DNASUi
51547

Genome annotation databases

EnsembliENST00000328666; ENSP00000329466; ENSG00000187531 [Q9NRC8-1]
GeneIDi51547
KEGGihsa:51547
UCSCiuc002kcj.3 human [Q9NRC8-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
51547
DisGeNETi51547
EuPathDBiHostDB:ENSG00000187531.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SIRT7
HGNCiHGNC:14935 SIRT7
HPAiENSG00000187531 Low tissue specificity
MIMi606212 gene
neXtProtiNX_Q9NRC8
OpenTargetsiENSG00000187531
PharmGKBiPA37940

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1905 Eukaryota
COG0846 LUCA
GeneTreeiENSGT00940000159703
HOGENOMiCLU_023643_6_2_1
InParanoidiQ9NRC8
KOiK11417
OMAiRGCAKRA
OrthoDBi1459156at2759
PhylomeDBiQ9NRC8
TreeFamiTF106184

Enzyme and pathway databases

SIGNORiQ9NRC8

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
51547 9 hits in 791 CRISPR screens

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

More...
ChiTaRSi
SIRT7 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SIRT7

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

More...
GenomeRNAii
51547
PharosiQ9NRC8 Tbio

Protein Ontology

More...
PROi
PR:Q9NRC8
RNActiQ9NRC8 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000187531 Expressed in lower esophagus mucosa and 202 other tissues
ExpressionAtlasiQ9NRC8 baseline and differential
GenevisibleiQ9NRC8 HS

Family and domain databases

InterProiView protein in InterPro
IPR029035 DHS-like_NAD/FAD-binding_dom
IPR003000 Sirtuin
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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiSIR7_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: Q9NRC8
Secondary accession number(s): A8K2K0
, B3KSU8, Q3MIK4, Q9NSZ6, Q9NUS6
<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%5Fand%5Fisoforms">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 1, 2000
Last modified: June 17, 2020
This is version 169 of the entry and version 1 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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