{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8N6T7","secondaryAccessions":["B2RCD0","O75291","Q6IAF5","Q6PK99","Q8NCD2","Q9BSI5","Q9BWP3","Q9NRC7","Q9UQD1"],"uniProtkbId":"SIR6_HUMAN","entryAudit":{"firstPublicDate":"2003-10-31","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-10-31","entryVersion":195,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"NAD-dependent protein deacylase sirtuin-6"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29555651"}],"value":"2.3.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"NAD-dependent protein deacetylase sirtuin-6"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337721"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23892288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27043296"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"}],"value":"2.3.1.286"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Protein mono-ADP-ribosyltransferase sirtuin-6"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21680843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27568560"}],"value":"2.4.2.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10873683"}],"value":"Regulatory protein SIR2 homolog 6"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"33122195"}],"value":"hSIRT6"}]},{"fullName":{"value":"SIR2-like protein 6"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10873683"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:14934"}],"value":"SIRT6"},"synonyms":[{"value":"SIR2L6"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P59941"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337721"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19135889"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19625767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21362626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21680843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21847107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22753495"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23142079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23217706"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23653361"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23892288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23911928"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24012758"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25009184"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25915124"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26456828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26787900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26898756"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27043296"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27180906"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27568560"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28406396"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29474172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29555651"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30374165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31995034"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32538779"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32789493"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33067423"}],"value":"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:21362626, PubMed:21680843, PubMed:23217706, PubMed:23552949, PubMed:23653361, PubMed:24052263, PubMed:27180906, PubMed:27322069, PubMed:29555651, PubMed:30374165). Displays protein-lysine deacetylase or defatty-acylase (demyristoylase and depalmitoylase) activity, depending on the context (PubMed:23552949, PubMed:24052263, PubMed:27322069). 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:21362626, PubMed:23892288, PubMed:23911928, PubMed:24012758, PubMed:26456828, PubMed:26898756, PubMed:27043296, PubMed:27180906, PubMed:30374165, PubMed:33067423). 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:29474172, PubMed:32789493). 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:23552949, PubMed:24052263, 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:27322069, PubMed:27568560). 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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-acetyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-acetyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43636"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:61930"},{"database":"ChEBI","id":"CHEBI:83767"}],"ecNumber":"2.3.1.286","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00236"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337721"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23142079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23892288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25009184"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26456828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26787900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27043296"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27912097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29474172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29555651"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30374165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32789493"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33067423"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33122195"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43637"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337721"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23142079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23892288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25009184"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26456828"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26787900"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27043296"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27912097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29474172"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29555651"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30374165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32789493"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33067423"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33122195"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-tetradecanoyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-tetradecanoyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:70567"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15437"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:141129"},{"database":"ChEBI","id":"CHEBI:189674"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29555651"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:70568"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29555651"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-hexadecanoyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-hexadecanoyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:70563"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:14175"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:138936"},{"database":"ChEBI","id":"CHEBI:189673"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:70564"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + NAD(+) = N(6)-(ADP-D-ribosyl)-L-lysyl-[protein] + nicotinamide + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58220"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15088"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:142515"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21680843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27568560"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:58221"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21680843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27322069"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27568560"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-[protein] + NAD(+) = N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19149"},{"database":"Rhea","id":"RHEA-COMP:10532"},{"database":"Rhea","id":"RHEA-COMP:15087"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29965"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:142554"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P59941"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:19150"},"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P59941"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21362626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27990725"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21362626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27990725"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21362626"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23892288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27043296"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27912097"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27990725"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30374165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30395713"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31844103"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33067423"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33122195"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33214841"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33649599"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33649600"}],"value":"Compared to the defatty-acylase activity, the protein deacetylase activity is weak in vitro, and requires activation (PubMed:21362626, PubMed:23552949, PubMed:23892288, PubMed:24052263). 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:30374165, PubMed:30395713, 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)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":3.4,"unit":"uM","substrate":"N6-tetradecanoyl-L-lysyl-peptide (myristoylated peptide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"}]},{"constant":0.9,"unit":"uM","substrate":"N6-hexadecanoyl-L-lysyl-peptide (palmitoylated peptide)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"}]},{"constant":2.4,"unit":"uM","substrate":"N6-tetradecanoyl-L-lysyl-TNF (TNF myristoylated on 'Lys-19')","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"}]},{"constant":4.5,"unit":"uM","substrate":"N6-tetradecanoyl-L-lysyl-TNF (TNF myristoylated on 'Lys-20')","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"}],"value":"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)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P59941"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19135889"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23911928"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31995034"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32538779"}],"value":"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)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37023208"}],"value":"(Microbial infection) Interacts with Kaposi's sarcoma-associated herpesvirus protein VIRF-1; this interaction prevents SIRT6 deubiquitination by USP10"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q8N6T7","intActId":"EBI-712415"},"interactantTwo":{"uniProtKBAccession":"P01106","geneName":"MYC","intActId":"EBI-447544"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q8N6T7","intActId":"EBI-712415"},"interactantTwo":{"uniProtKBAccession":"Q04206","geneName":"RELA","intActId":"EBI-73886"},"numberOfExperiments":4,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18337721"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21680843"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23552949"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23911928"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27043296"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27568560"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31995034"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32538779"}],"value":"Predominantly nuclear (PubMed:18337721). Associated with pericentric heterochromatin and telomeric heterochromatin regions (PubMed:18337721, PubMed:27043296). Localizes to DNA damage sites: directly recognizes and binds double-strand breaks (DSBs) sites via a tunnel-like structure that has high affinity for DSBs (PubMed:21680843, PubMed:23911928, PubMed:27568560, PubMed:31995034, PubMed:32538779). 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