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UniProtKB - Q8N6T7 (SIR6_HUMAN)

Entry version 175 (25 May 2022)
Sequence version 2 (31 Oct 2003)
Previous versions | rss
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Protein

NAD-dependent protein deacylase sirtuin-6

Gene

SIRT6

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 deacetylase, deacylase and mono-ADP-ribosyltransferase that plays an essential role in DNA damage repair, telomere maintenance, metabolic homeostasis, inflammation, tumorigenesis and aging (PubMed:18337721, PubMed:19135889, PubMed:19625767, PubMed:21680843, PubMed:23217706, PubMed:23653361, PubMed:24052263, PubMed:27322069, PubMed:27180906, PubMed:21362626, PubMed:23552949, PubMed:30374165, PubMed:29555651).

Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context (PubMed:24052263, PubMed:27322069, PubMed:23552949).

Acts as a key histone deacetylase by catalyzing deacetylation of histone H3 at 'Lys-9', 'Lys-18' and 'Lys-56' (H3K9ac, H3K18ac and H3K56ac, respectively), suppressing target gene expression of several transcription factors, including NF-kappa-B (PubMed:19625767, PubMed:24012758, PubMed:23892288, PubMed:23911928, PubMed:27043296, PubMed:26898756, PubMed:27180906, PubMed:33067423, PubMed:21362626, PubMed:30374165, PubMed:26456828).

Acts as an inhibitor of transcription elongation by mediating deacetylation of H3K9ac and H3K56ac, preventing release of NELFE from chromatin and causing transcriptional pausing (By similarity).

Involved in DNA repair by promoting double-strand break (DSB) repair: acts as a DSB sensor by recognizing and binding DSB sites, leading to (1) recruitment of DNA repair proteins, such as SMARCA5/SNF2H, and (2) deacetylation of histone H3K9ac and H3K56ac (PubMed:23911928, PubMed:31995034, PubMed:32538779).

SIRT6 participation to DSB repair is probably involved in extension of life span (By similarity).

Also promotes DNA repair by deacetylating non-histone proteins, such as DDB2 and p53/TP53 (PubMed:32789493, PubMed:29474172).

Specifically deacetylates H3K18ac at pericentric heterochromatin, thereby maintaining pericentric heterochromatin silencing at centromeres and protecting against genomic instability and cellular senescence (PubMed:27043296).

Involved in telomere maintenance by catalyzing deacetylation of histone H3 in telomeric chromatin, regulating telomere position effect and telomere movement in response to DNA damage (PubMed:18337721, PubMed:19625767, PubMed:21847107).

Required for embryonic stem cell differentiation by mediating histone deacetylation of H3K9ac (PubMed:25915124, PubMed:29555651).

Plays a major role in metabolism by regulating processes such as glycolysis, gluconeogenesis, insulin secretion and lipid metabolism (PubMed:24012758, PubMed:26787900).

Inhibits glycolysis via histone deacetylase activity and by acting as a corepressor of the transcription factor HIF1A, thereby controlling the expression of multiple glycolytic genes (By similarity).

Has tumor suppressor activity by repressing glycolysis, thereby inhibiting the Warburg effect (PubMed:23217706).

Also regulates glycolysis and tumorigenesis by mediating deacetylation and nuclear export of non-histone proteins, such as isoform M2 of PKM (PKM2) (PubMed:26787900).

Acts as a negative regulator of gluconeogenesis by mediating deacetylation of non-histone proteins, such as FOXO1 and KAT2A/GCN5 (PubMed:23142079, PubMed:25009184).

Promotes beta-oxidation of fatty acids during fasting by catalyzing deacetylation of NCOA2, inducing coactivation of PPARA (By similarity).

Acts as a regulator of lipid catabolism in brown adipocytes, both by catalyzing deacetylation of histones and non-histone proteins, such as FOXO1 (By similarity).

Also acts as a regulator of circadian rhythms, both by regulating expression of clock-controlled genes involved in lipid and carbohydrate metabolism, and by catalyzing deacetylation of PER2 (By similarity).

The defatty-acylase activity is specifically involved in regulation of protein secretion (PubMed:24052263, PubMed:23552949, PubMed:27322069, PubMed:28406396).

Has high activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as RRAS2 and TNF, thereby regulating their secretion (PubMed:23552949, PubMed:28406396).

Also acts as a mono-ADP-ribosyltransferase by mediating mono-ADP-ribosylation of PARP1, TRIM28/KAP1 or SMARCC2/BAF170 (PubMed:21680843, PubMed:22753495, PubMed:27568560, PubMed:27322069).

Mono-ADP-ribosyltransferase activity is involved in DNA repair, cellular senescence, repression of LINE-1 retrotransposon elements and regulation of transcription (PubMed:21680843, PubMed:22753495, PubMed:27568560).

By similarity32 Publications

Caution

Upon DNA damage, was reported to promote DNA end resection via deacetylation of RBBP8. However, this study was later retracted.2 Publications
The binding-mode of MDL-801 selective activator is subject to discussion (PubMed:30374165, PubMed:33649599, PubMed:33649600). According to a group, MDL-801 binds around the acyl channel exit and acts as an allosteric activator (PubMed:30374165, PubMed:33649600). According to another group, the binding mode of MDL-801 remains undefined (PubMed:33649599).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+3 PublicationsNote: Binds 1 zinc ion per subunit.3 Publications

<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

Compared to the defatty-acylase activity, the protein deacetylase activity is weak in vitro, and requires activation (PubMed:24052263, PubMed:23892288, PubMed:21362626, PubMed:23552949). The histone deacetylase activity is strongly activated upon binding to nucleosomes and chromatin in vivo (PubMed:23892288, PubMed:27043296, PubMed:33067423). Two molecules of SIRT6 associate with the acidic patch of one nucleosome, while the C-terminal disordered region of SIRT6 associates with nucleosomal DNA, leading to efficient histone deacetylation (PubMed:33067423). The protein-lysine deacetylase activity is also activated by long-chain free fatty-acids (PubMed:24052263). The histone deacetylase activity is specifically repressed by long non-coding RNA lncPRESS1, which binds to SIRT6 and prevents chromatin-binding, thereby promoting stem cell pluripotency (PubMed:27912097). Due to its essential role as tumor suppressor and involvement in DNA repair and life span, extensive research is made for the identification of small compound regulators of SIRT6 (PubMed:27990725, PubMed:30395713, PubMed:30374165, PubMed:31844103, PubMed:33214841, PubMed:33649599, PubMed:33649600). Nitro-fatty acids (nitro-oleic acid and nitro-conjugated linoleic acid) strongly stimulate the protein-lysine deacetylase activity by forming a covalent Michael adduct formation with Cys-18 (PubMed:33122195). Activated by UBCS039 (4-(pyridin-3-yl)-4,5- dihydropyrrolo[1,2-a]quinoxaline) (PubMed:27990725). Inhibited by non-selective hydroxamate trichostatin A inhibitor (PubMed:30395713). Deacetylase activity is activated by fluvastatin and quercetin-based compounds (PubMed:31844103, PubMed:33214841). The protein-lysine deacetylase activity, but not the defatty-acylase activity, is specifically activated by MDL-800 and MDL-801 activators in vivo, enhancing the histone deacetylase and tumor suppressor activities (PubMed:30374165, PubMed:33649599, PubMed:33649600). MDL-800 and MDL-801 selectively activate SIRT6 and not other members of the sirtuin family (PubMed:30374165). The binding-mode of MDL-801 is however subject to discussion (PubMed:30374165, PubMed:33649599, PubMed:33649600).15 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

kcat is 0.0049 sec(-1) for N6-tetradecanoyl-L-lysyl-peptide (myristoylated peptide) (PubMed:23552949). kcat is 0.0027 sec(-1) for N6-hexadecanoyl-L-lysyl-peptide (palmitoylated peptide) (PubMed:23552949). kcat is 0.0020 sec(-1) for N6-tetradecanoyl-L-lysyl-TNF (TNF myristoylated on 'Lys-19') (PubMed:23552949). kcat is 0.0050 sec(-1) for N6-tetradecanoyl-L-lysyl-TNF (TNF myristoylated on 'Lys-20') (PubMed:23552949).1 Publication
  1. KM=3.4 µM for N6-tetradecanoyl-L-lysyl-peptide (myristoylated peptide)1 Publication
  2. KM=0.9 µM for N6-hexadecanoyl-L-lysyl-peptide (palmitoylated peptide)1 Publication
  3. KM=2.4 µM for N6-tetradecanoyl-L-lysyl-TNF (TNF myristoylated on 'Lys-19')1 Publication
  4. KM=4.5 µM for N6-tetradecanoyl-L-lysyl-TNF (TNF myristoylated on 'Lys-20')1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei18Formation of an covalent adduct with nitro-fatty acid activators1 Publication1
<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 sitei53NAD; via amide nitrogenCombined sources1 Publication1
Binding sitei57NADCombined sources1 Publication1 Publication1
Binding sitei64NADCombined sources1 Publication1 Publication1
Binding sitei65NADCombined sources1 Publication1 Publication1
Binding sitei71NADCombined sources1 Publication1 Publication1
Binding sitei113NAD; via carbonyl oxygenCombined sources1 Publication1 Publication1
<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 sitei133Proton acceptor4 Publications1 Publication1
Binding sitei133NADCombined sources1 Publication1 Publication1
<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 bindingi141ZincPROSITE-ProRule annotationCombined sources3 Publications1
Metal bindingi144ZincPROSITE-ProRule annotationCombined sources3 Publications1
Metal bindingi166ZincPROSITE-ProRule annotationCombined sources3 Publications1
Metal bindingi177ZincPROSITE-ProRule annotationCombined sources3 Publications1
Binding sitei214NADCombined sources1 Publication1 Publication1
Binding sitei216NADCombined sources1 Publication1 Publication1
Binding sitei240NADCombined sources1 Publication1 Publication1
Binding sitei242NADCombined sources1 Publication1 Publication1
Binding sitei258NAD; via amide nitrogenCombined sources1 Publication1 Publication1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAcyltransferase, Chromatin regulator, Developmental protein, DNA-binding, RNA-binding, Transferase
Biological processDNA damage, DNA repair
LigandMetal-binding, NAD, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.B41, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q8N6T7

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1912408, Pre-NOTCH Transcription and Translation
R-HSA-5693607, Processing of DNA double-strand break ends

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q8N6T7

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q8N6T7

<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 deacylase sirtuin-6Curated (EC:2.3.1.-4 Publications)
Alternative name(s):
NAD-dependent protein deacetylase sirtuin-6Curated (EC:2.3.1.2867 Publications)
Protein mono-ADP-ribosyltransferase sirtuin-6Curated (EC:2.4.2.-3 Publications)
Regulatory protein SIR2 homolog 61 Publication
Short name:
hSIRT61 Publication
SIR2-like protein 6
<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:SIRT61 PublicationImported
Synonyms:SIR2L6
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:14934, SIRT6

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606211, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q8N6T7

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000077463

<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

Keywords - Cellular componenti

Chromosome, Endoplasmic reticulum, Nucleus, Telomere

<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>Mutagenesisi10S → A: Abolihes ability to promote DNA repair and recruit PARP1 to double-strand breaks (DSBs). 1 Publication1
Mutagenesisi10S → E: Mimics phosphorylation; increased ability to promote DNA repair and recruit PARP1 to double-strand breaks (DSBs). 1 Publication1
Mutagenesisi13A → W: Increased protein-lysine demyristoylase activity. 1 Publication1
Mutagenesisi15K → R: Does not affect acetylation level. 1 Publication1
Mutagenesisi17K → R: Does not affect acetylation level. 1 Publication1
Mutagenesisi33K → Q: Mimics acetylation, leading to impaired ability to recognize and bind double-strand breaks (DSBs) sites. 1 Publication1
Mutagenesisi33K → R: Decreased acetylation level. 1 Publication1
Mutagenesisi45S → A in AAA mutant; strongly decreased nucleosome-binding; when associated with 206-A--A-208. 1 Publication1
Mutagenesisi56S → Y: Abolished NAD-dependent protein deacetylase, defatty-acylase and mono-ADP-ribosyltransferase activities. 4 Publications1
Mutagenesisi60G → A: Does not affect the NAD-dependent protein defatty-acylase activity. Abolished NAD-dependent protein deacetylase and mono-ADP-ribosyltransferase activities. 4 Publications1
Mutagenesisi65R → A: Does not affect the mono-ADP-ribosyltransferase activity. Abolished NAD-dependent protein deacetylase and defatty-acylase activities. 3 Publications1
Mutagenesisi82F → A or E: Reduced MDL-800 and MDL-801 compounds-binding. 1 Publication1
Mutagenesisi86F → E: Strongly reduced MDL-800 and MDL-801 compounds-binding. 1 Publication1
Mutagenesisi86F → Q: Slightly reduced MDL-800 and MDL-801 compounds-binding. 1 Publication1
Mutagenesisi133H → Y: Abolished NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase activities. Impaired ability to recognize and bind double-strand breaks (DSBs) sites. 13 Publications1
Mutagenesisi170K → R: Decreased ubiquitination. 1 Publication1
Mutagenesisi206 – 208Missing in AAA mutant; strongly decreased nucleosome-binding; when associated with A-45. 1 Publication3
Mutagenesisi294T → A: Does not affect ability to promote DNA repair. 1 Publication1
Mutagenesisi296 – 300KLEPK → RLEPR in 4KR mutant; abolished sumoylation, leading to increased H3K56ac; when associated with R-316 and R-332. 1 Publication5
Mutagenesisi303S → A: Does not affect ability to promote DNA repair. 1 Publication1
Mutagenesisi316K → R in 4KR mutant; abolished sumoylation, leading to increased H3K56ac; when associated with 296-R--R-300 and R-332. 1 Publication1
Mutagenesisi330S → A: Does not affect ability to promote DNA repair. 1 Publication1
Mutagenesisi332K → R in 4KR mutant; abolished sumoylation, leading to increased H3K56ac; when associated with 296-R--R-300 and R-316. 1 Publication1
Mutagenesisi338S → A: Does not affect ability to promote DNA repair. 1 Publication1

Keywords - Diseasei

Disease variant, Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		51548

MalaCards human disease database

More...MalaCardsi		SIRT6

Open Targets

More...OpenTargetsi		ENSG00000077463

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		580933, Lethal brain and heart developmental defects

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37939

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q8N6T7, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2163182

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2712

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		SIRT6

Domain mapping of disease mutations (DMDM)

More...DMDMi		38258612

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001102692 – 355NAD-dependent protein deacylase sirtuin-6Add BLAST354

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 residuei2N-acetylserineCombined sources1
Modified residuei10Phosphoserine; by MAPK8Combined sources1 Publication1
Modified residuei33N6-acetyllysine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei294PhosphothreonineCombined sources1
Modified residuei303PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1

<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

Acetylated at Lys-33 (PubMed:32538779). Deacetylation at Lys-33 by SIRT1 promotes homomultimerization and binding to double-strand breaks (DSBs) sites (PubMed:32538779).1 Publication
Phosphorylation at Ser-10 by MAPK8/JNK1 in response to oxidative stress stimulates the mono-ADP-ribosyltransferase activity on PARP1, leading to PARP1 recruitment to double-strand breaks (DSBs).1 Publication
Monoubiquitinated at Lys-170 by STUB1/CHIP, preventing its degradation by the proteasome.1 Publication
Sumoylated, leading to specifically decrease ability to deacetylate histone H3 at 'Lys-56' (H3K56ac).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q8N6T7

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q8N6T7

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q8N6T7

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q8N6T7

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

More...PaxDbi		Q8N6T7

PeptideAtlas

More...PeptideAtlasi		Q8N6T7

PRoteomics IDEntifications database

More...PRIDEi		Q8N6T7

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		72232 [Q8N6T7-1]
72233 [Q8N6T7-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q8N6T7

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

More...PhosphoSitePlusi		Q8N6T7

<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

Down-regulated in a number of cancers, such as pancreatic cancer or colon carcinomas (PubMed:23217706). Post-transcriptionally regulated by miR-766 (PubMed:23653361). Expression is post-transcriptionally repressed by miR-122 (PubMed:26748705).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000077463, Expressed in mucosa of transverse colon and 181 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q8N6T7, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8N6T7, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000077463, 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

Homodimer; binds to nucleosomes and DNA ends as a homodimer (PubMed:31995034, PubMed:32538779).

Interacts with RELA; interferes with RELA binding to target DNA (PubMed:19135889).

Interacts with SMARCA5; promoting recruitment of SMARCA5/SNF2H to double-strand breaks (DSBs) sites (PubMed:23911928).

Interacts with the mTORC2 complex; preventing the ability of SIRT6 to deacetylate FOXO1.

Interacts with the CLOCK-BMAL1 complex; recruited by the CLOCK-BMAL1 complex to regulate expression of clock-controlled genes.

Interacts with CSNK2A2; preventing CSNK2A2 localization to the nucleus (By similarity).

By similarity4 Publications

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

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		119603, 224 interactors

Database of interacting proteins

More...DIPi		DIP-47346N

Protein interaction database and analysis system

More...IntActi		Q8N6T7, 71 interactors

Molecular INTeraction database

More...MINTi		Q8N6T7

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000337332

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q8N6T7

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q8N6T7, 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

1355
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q8N6T7

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

More...SMRi		Q8N6T7

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q8N6T7

<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>Domaini35 – 274Deacetylase sirtuin-typePROSITE-ProRule annotationAdd BLAST240

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni284 – 355Disordered1 PublicationAdd BLAST72

<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

The C-terminal disordered region mediates non-specific DNA-binding.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 IV subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1905, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160088

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_023643_6_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8N6T7

Identification of Orthologs from Complete Genome Data

More...OMAi		EQCKKCR

Database of Orthologous Groups

More...OrthoDBi		1503290at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8N6T7

TreeFam database of animal gene trees

More...TreeFami		TF106184

Family and domain databases

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00486

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02146, SIR2, 2 hits

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%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 (2+)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.

<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 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 2 <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 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8N6T7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><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.

« Hide
        10         20         30         40         50
MSVNYAAGLS PYADKGKCGL PEIFDPPEEL ERKVWELARL VWQSSSVVFH 
        60         70         80         90        100
TGAGISTASG IPDFRGPHGV WTMEERGLAP KFDTTFESAR PTQTHMALVQ 
       110        120        130        140        150
LERVGLLRFL VSQNVDGLHV RSGFPRDKLA ELHGNMFVEE CAKCKTQYVR 
       160        170        180        190        200
DTVVGTMGLK ATGRLCTVAK ARGLRACRGE LRDTILDWED SLPDRDLALA 
       210        220        230        240        250
DEASRNADLS ITLGTSLQIR PSGNLPLATK RRGGRLVIVN LQPTKHDRHA 
       260        270        280        290        300
DLRIHGYVDE VMTRLMKHLG LEIPAWDGPR VLERALPPLP RPPTPKLEPK 
       310        320        330        340        350
EESPTRINGS IPAGPKQEPC AQHNGSEPAS PKRERPTSPA PHRPPKRVKA 

KAVPS
Length:355
Mass (Da):39,119
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:i0C86AAC497130BBF
GO
Isoform 2 (identifier: Q8N6T7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-205: Missing.

Show »
Length:328
Mass (Da):36,065
Checksum:i503805C898FD7769
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0QZ09M0QZ09_HUMAN
NAD-dependent protein deacetylase s...
SIRT6
275Annotation score:

Annotation score:2 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>
M0R1N9M0R1N9_HUMAN
NAD-dependent protein deacetylase s...
SIRT6 hCG_2004101
176Annotation 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>
M0R1F6M0R1F6_HUMAN
NAD-dependent protein deacetylase s...
SIRT6
186Annotation 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>
M0QXA0M0QXA0_HUMAN
NAD-dependent protein deacetylase s...
SIRT6
187Annotation 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>
M0R0B2M0R0B2_HUMAN
NAD-dependent protein deacetylase s...
SIRT6
43Annotation 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 AAC34468 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAD15478 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAH04218 differs from that shown. Reason: Erroneous translation. Wrong choice of CCDS.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 conflicti42W → R in CAG33481 (Ref. 3) Curated1
Sequence conflicti249H → Y in AAH04218 (PubMed:15489334).Curated1
Sequence conflicti267K → E in AAF43432 (PubMed:10873683).Curated1

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Variability among SIRT6 alleles may account for variations in life span (PubMed:25541994). A minor allele (rs107251) is associated with a decreased life span of 5.5 and 5.9 years when homozygous (TT); when compared to the major allele homozygous (CC) and heterozygous (CT) genotypes, respectively (PubMed:25541994).1 Publication

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_08608325D → N Found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity. 1 Publication1
Natural variantiVAR_08608436E → V Found in kidney cancer; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity. 1 Publication1
Natural variantiVAR_01715446S → N Does not affect histone deacetylase activity. 4 PublicationsCorresponds to variant dbSNP:rs352493Ensembl.1
Natural variantiVAR_08608563D → H Found in a family presenting with four cases of perinatal lethality caused by severe neurodevelopmental and cardiac anomalies; abolished histone deacetylase activity; abolished protein demyristoylase activity; decreased ability to recognize and bind double-strand breaks (DSBs) sites; does not affect nuclear localization. 2 Publications1
Natural variantiVAR_08608663D → Y Found in non-small cell lung cancer; somatic mutation; does not affect ability to recognize and bind double-strand breaks (DSBs) sites; strongly reduced histone deacetylase activity; strongly reduced the protein-lysine demyristoylase activity. 2 Publications1
Natural variantiVAR_08608789A → S Found in non-small cell lung cancer; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity. 1 Publication1
Natural variantiVAR_086088116D → N Found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin; strongly reduced histone deacetylase activity; strongly reduced the protein-lysine demyristoylase activity. 1 Publication1
Natural variantiVAR_086089260 – 355Missing Found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin. 1 PublicationAdd BLAST96
Natural variantiVAR_086090263T → P Found in cervical cancer; somatic mutation; reduced histone deacetylase activity; slightly reduced the protein-lysine demyristoylase activity. 1 Publication1
Natural variantiVAR_086091274P → L Found in melanoma; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity. 1 Publication1

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_008733179 – 205Missing in isoform 2. 1 PublicationAdd BLAST27

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
AF233396 mRNA Translation: AAF43432.1
AK074810 mRNA Translation: BAC11222.1
AK315048 mRNA Translation: BAG37527.1
CR457200 mRNA Translation: CAG33481.1
AC005620 Genomic DNA Translation: AAC34468.1 Sequence problems.
AC006930 Genomic DNA Translation: AAD15478.1 Sequence problems.
CH471139 Genomic DNA Translation: EAW69252.1
BC004218 mRNA Translation: AAH04218.1 Sequence problems.
BC005026 mRNA Translation: AAH05026.1
BC028220 mRNA Translation: AAH28220.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12122.1 [Q8N6T7-1]
CCDS54199.1 [Q8N6T7-2]

NCBI Reference Sequences

More...RefSeqi		NP_001180214.1, NM_001193285.2 [Q8N6T7-2]
NP_001307987.1, NM_001321058.1
NP_001307988.1, NM_001321059.1
NP_001307989.1, NM_001321060.1
NP_001307990.1, NM_001321061.1
NP_001307991.1, NM_001321062.1
NP_001307992.1, NM_001321063.1
NP_001307993.1, NM_001321064.1
NP_057623.2, NM_016539.3 [Q8N6T7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000305232.10; ENSP00000305310.5; ENSG00000077463.15 [Q8N6T7-2]
ENST00000337491.7; ENSP00000337332.1; ENSG00000077463.15

Database of genes from NCBI RefSeq genomes

More...GeneIDi		51548

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:51548

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000337491.7; ENSP00000337332.1; NM_016539.4; NP_057623.2

UCSC genome browser

More...UCSCi		uc002lzo.4, human [Q8N6T7-1]

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
AF233396 mRNA Translation: AAF43432.1
AK074810 mRNA Translation: BAC11222.1
AK315048 mRNA Translation: BAG37527.1
CR457200 mRNA Translation: CAG33481.1
AC005620 Genomic DNA Translation: AAC34468.1 Sequence problems.
AC006930 Genomic DNA Translation: AAD15478.1 Sequence problems.
CH471139 Genomic DNA Translation: EAW69252.1
BC004218 mRNA Translation: AAH04218.1 Sequence problems.
BC005026 mRNA Translation: AAH05026.1
BC028220 mRNA Translation: AAH28220.1
CCDSiCCDS12122.1 [Q8N6T7-1]
CCDS54199.1 [Q8N6T7-2]
RefSeqiNP_001180214.1, NM_001193285.2 [Q8N6T7-2]
NP_001307987.1, NM_001321058.1
NP_001307988.1, NM_001321059.1
NP_001307989.1, NM_001321060.1
NP_001307990.1, NM_001321061.1
NP_001307991.1, NM_001321062.1
NP_001307992.1, NM_001321063.1
NP_001307993.1, NM_001321064.1
NP_057623.2, NM_016539.3 [Q8N6T7-1]

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
3K35X-ray2.00A/B/C/D/E/F3-318[»]
3PKIX-ray2.04A/B/C/D/E/F2-355[»]
3PKJX-ray2.12A/B/C/D/E/F2-355[»]
3ZG6X-ray2.20A1-296[»]
5MF6X-ray1.87A/B13-308[»]
5MFPX-ray1.98A/B13-308[»]
5MFZX-ray2.10A/B13-308[»]
5MGNX-ray2.07A/B13-308[»]
5X16X-ray1.97A3-318[»]
5Y2FX-ray2.53A3-318[»]
6HOYX-ray1.70A/B13-308[»]
6QCDX-ray1.84A/B13-308[»]
6QCEX-ray1.90A/B13-308[»]
6QCHX-ray2.10A/B13-308[»]
6QCJX-ray2.01A/B13-308[»]
6XUYX-ray2.13A/B13-308[»]
6XV1X-ray1.95A/B13-308[»]
6XV6X-ray1.75A/B/C/D/E/F3-318[»]
6XVGX-ray2.10A/B/C/D/E/F3-318[»]
6ZU4X-ray2.46A/B13-308[»]
7CL0X-ray2.53A1-355[»]
7CL1X-ray3.20A1-355[»]
AlphaFoldDBiQ8N6T7
SMRiQ8N6T7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi119603, 224 interactors
DIPiDIP-47346N
IntActiQ8N6T7, 71 interactors
MINTiQ8N6T7
STRINGi9606.ENSP00000337332

Chemistry databases

BindingDBiQ8N6T7
ChEMBLiCHEMBL2163182
GuidetoPHARMACOLOGYi2712

PTM databases

iPTMnetiQ8N6T7
PhosphoSitePlusiQ8N6T7

Genetic variation databases

BioMutaiSIRT6
DMDMi38258612

Proteomic databases

EPDiQ8N6T7
jPOSTiQ8N6T7
MassIVEiQ8N6T7
MaxQBiQ8N6T7
PaxDbiQ8N6T7
PeptideAtlasiQ8N6T7
PRIDEiQ8N6T7
ProteomicsDBi72232 [Q8N6T7-1]
72233 [Q8N6T7-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		11389, 699 antibodies from 42 providers

The DNASU plasmid repository

More...DNASUi		51548

Genome annotation databases

EnsembliENST00000305232.10; ENSP00000305310.5; ENSG00000077463.15 [Q8N6T7-2]