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Q8N6T7

- SIR6_HUMAN

UniProt

Q8N6T7 - SIR6_HUMAN

Protein

NAD-dependent protein deacetylase sirtuin-6

Gene

SIRT6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (31 Oct 2003)
      Previous versions | rss
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    Functioni

    NAD-dependent protein deacetylase. Has deacetylase activity towards histone H3K9Ac and H3K56Ac. Modulates acetylation of histone H3 in telomeric chromatin during the S-phase of the cell cycle. Deacetylates histone H3K9Ac at NF-kappa-B target promoters and may down-regulate the expression of a subset of NF-kappa-B target genes. Acts as a corepressor of the transcription factor HIF1A to control the expression of multiple glycolytic genes to regulate glucose homeostasis. Required for genomic stability. Regulates the production of TNF protein. Has a role in the regulation of life span By similarity. Deacetylation of nucleosomes interferes with RELA binding to target DNA. May be required for the association of WRN with telomeres during S-phase and for normal telomere maintenance. Required for genomic stability. Required for normal IGF1 serum levels and normal glucose homeostasis. Modulates cellular senescence and apoptosis. On DNA damage, promotes DNA end resection via deacetylation of RBBP8. Has very weak deacetylase activity and can bind NAD+ in the absence of acetylated substrate.By similarity5 Publications

    Catalytic activityi

    NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.1 PublicationPROSITE-ProRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei133 – 1331Proton acceptor
    Metal bindingi141 – 1411Zinc1 PublicationPROSITE-ProRule annotation
    Metal bindingi144 – 1441Zinc1 PublicationPROSITE-ProRule annotation
    Metal bindingi166 – 1661Zinc1 PublicationPROSITE-ProRule annotation
    Metal bindingi177 – 1771Zinc1 PublicationPROSITE-ProRule annotation
    Binding sitei258 – 2581NAD; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi52 – 7120NADAdd
    BLAST
    Nucleotide bindingi113 – 1164NAD
    Nucleotide bindingi214 – 2163NAD
    Nucleotide bindingi240 – 2423NAD

    GO - Molecular functioni

    1. NAD(P)+-protein-arginine ADP-ribosyltransferase activity Source: UniProtKB
    2. NAD+ ADP-ribosyltransferase activity Source: BHF-UCL
    3. NAD+ binding Source: UniProtKB
    4. NAD-dependent histone deacetylase activity Source: UniProtKB
    5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. histone deacetylation Source: GOC
    2. histone H3 deacetylation Source: GOC
    3. protein ADP-ribosylation Source: UniProtKB
    4. regulation of double-strand break repair via homologous recombination Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD-dependent protein deacetylase sirtuin-6 (EC:3.5.1.-)
    Alternative name(s):
    Regulatory protein SIR2 homolog 6
    SIR2-like protein 6
    Gene namesi
    Name:SIRT6
    Synonyms:SIR2L6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:14934. SIRT6.

    Subcellular locationi

    Nucleusnucleoplasm 3 Publications
    Note: Predominantly nuclear. Associated with telomeric heterochromatin regions.

    GO - Cellular componenti

    1. nuclear telomeric heterochromatin Source: UniProtKB
    2. nucleoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331H → Y: Loss of enzyme activity. Abolishes RBBP8 deacetylation and promotion of DNA end resection after DNA damage. 2 Publications

    Organism-specific databases

    PharmGKBiPA37939.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 355354NAD-dependent protein deacetylase sirtuin-6PRO_0000110269Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei303 – 3031Phosphoserine1 Publication
    Modified residuei330 – 3301Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8N6T7.
    PaxDbiQ8N6T7.
    PRIDEiQ8N6T7.

    PTM databases

    PhosphoSiteiQ8N6T7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8N6T7.
    BgeeiQ8N6T7.
    GenevestigatoriQ8N6T7.

    Interactioni

    Subunit structurei

    Interacts with RELA. Interacts with RBBP8; the interaction deacetylates RBBP8.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYCP011063EBI-712415,EBI-447544
    RELAQ042064EBI-712415,EBI-73886

    Protein-protein interaction databases

    BioGridi119603. 17 interactions.
    DIPiDIP-47346N.
    IntActiQ8N6T7. 15 interactions.
    MINTiMINT-1374731.

    Structurei

    Secondary structure

    1
    355
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni5 – 84
    Helixi27 – 4317
    Beta strandi47 – 515
    Helixi53 – 553
    Helixi57 – 593
    Beta strandi64 – 663
    Helixi70 – 745
    Turni75 – 773
    Turni86 – 883
    Helixi93 – 10311
    Beta strandi109 – 1124
    Helixi118 – 1214
    Beta strandi122 – 1254
    Helixi126 – 1283
    Beta strandi129 – 1313
    Beta strandi138 – 1414
    Turni142 – 1443
    Beta strandi147 – 1493
    Beta strandi161 – 1655
    Turni171 – 1744
    Beta strandi180 – 1834
    Beta strandi188 – 1903
    Helixi194 – 20512
    Beta strandi208 – 2147
    Helixi222 – 2243
    Helixi225 – 2317
    Beta strandi235 – 2395
    Helixi247 – 2493
    Beta strandi251 – 2544
    Helixi258 – 26912
    Beta strandi280 – 2823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ8N6T7.
    SMRiQ8N6T7. Positions 13-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N6T7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 274240Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi287 – 34559Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the sirtuin family. Class IV subfamily.Curated
    Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0846.
    HOVERGENiHBG060028.
    InParanoidiQ8N6T7.
    KOiK11416.
    OMAiPSKTHMA.
    PhylomeDBiQ8N6T7.
    TreeFamiTF106184.

    Family and domain databases

    Gene3Di3.40.50.1220. 2 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR003000. Sirtuin.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view]
    PANTHERiPTHR11085. PTHR11085. 1 hit.
    PfamiPF02146. SIR2. 2 hits.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    PROSITEiPS50305. SIRTUIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

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

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSVNYAAGLS PYADKGKCGL PEIFDPPEEL ERKVWELARL VWQSSSVVFH    50
    TGAGISTASG IPDFRGPHGV WTMEERGLAP KFDTTFESAR PTQTHMALVQ 100
    LERVGLLRFL VSQNVDGLHV RSGFPRDKLA ELHGNMFVEE CAKCKTQYVR 150
    DTVVGTMGLK ATGRLCTVAK ARGLRACRGE LRDTILDWED SLPDRDLALA 200
    DEASRNADLS ITLGTSLQIR PSGNLPLATK RRGGRLVIVN LQPTKHDRHA 250
    DLRIHGYVDE VMTRLMKHLG LEIPAWDGPR VLERALPPLP RPPTPKLEPK 300
    EESPTRINGS IPAGPKQEPC AQHNGSEPAS PKRERPTSPA PHRPPKRVKA 350
    KAVPS 355
    Length:355
    Mass (Da):39,119
    Last modified:October 31, 2003 - v2
    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.

    Note: No experimental confirmation available.

    Show »
    Length:328
    Mass (Da):36,065
    Checksum:i503805C898FD7769
    GO

    Sequence cautioni

    The sequence AAC34468.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAD15478.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421W → R in CAG33481. 1 PublicationCurated
    Sequence conflicti249 – 2491H → Y in AAH04218. (PubMed:15489334)Curated
    Sequence conflicti267 – 2671K → E in AAF43432. (PubMed:10873683)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461S → N.3 Publications
    Corresponds to variant rs352493 [ dbSNP | Ensembl ].
    VAR_017154

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei179 – 20527Missing in isoform 2. 1 PublicationVSP_008733Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_001193285.1. [Q8N6T7-2]
    NP_057623.2. NM_016539.2. [Q8N6T7-1]
    UniGeneiHs.423756.

    Genome annotation databases

    EnsembliENST00000305232; ENSP00000305310; ENSG00000077463. [Q8N6T7-2]
    ENST00000337491; ENSP00000337332; ENSG00000077463. [Q8N6T7-1]
    GeneIDi51548.
    KEGGihsa:51548.
    UCSCiuc002lzo.3. human. [Q8N6T7-1]
    uc002lzq.3. human. [Q8N6T7-2]

    Polymorphism databases

    DMDMi38258612.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12122.1. [Q8N6T7-1 ]
    CCDS54199.1. [Q8N6T7-2 ]
    RefSeqi NP_001180214.1. NM_001193285.1. [Q8N6T7-2 ]
    NP_057623.2. NM_016539.2. [Q8N6T7-1 ]
    UniGenei Hs.423756.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3K35 X-ray 2.00 A/B/C/D/E/F 3-318 [» ]
    3PKI X-ray 2.04 A/B/C/D/E/F 2-355 [» ]
    3PKJ X-ray 2.12 A/B/C/D/E/F 2-355 [» ]
    3ZG6 X-ray 2.20 A 1-296 [» ]
    ProteinModelPortali Q8N6T7.
    SMRi Q8N6T7. Positions 13-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119603. 17 interactions.
    DIPi DIP-47346N.
    IntActi Q8N6T7. 15 interactions.
    MINTi MINT-1374731.

    Chemistry

    ChEMBLi CHEMBL2163182.

    PTM databases

    PhosphoSitei Q8N6T7.

    Polymorphism databases

    DMDMi 38258612.

    Proteomic databases

    MaxQBi Q8N6T7.
    PaxDbi Q8N6T7.
    PRIDEi Q8N6T7.

    Protocols and materials databases

    DNASUi 51548.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305232 ; ENSP00000305310 ; ENSG00000077463 . [Q8N6T7-2 ]
    ENST00000337491 ; ENSP00000337332 ; ENSG00000077463 . [Q8N6T7-1 ]
    GeneIDi 51548.
    KEGGi hsa:51548.
    UCSCi uc002lzo.3. human. [Q8N6T7-1 ]
    uc002lzq.3. human. [Q8N6T7-2 ]

    Organism-specific databases

    CTDi 51548.
    GeneCardsi GC19M004125.
    H-InvDB HIX0014654.
    HGNCi HGNC:14934. SIRT6.
    MIMi 606211. gene.
    neXtProti NX_Q8N6T7.
    PharmGKBi PA37939.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0846.
    HOVERGENi HBG060028.
    InParanoidi Q8N6T7.
    KOi K11416.
    OMAi PSKTHMA.
    PhylomeDBi Q8N6T7.
    TreeFami TF106184.

    Miscellaneous databases

    ChiTaRSi SIRT6. human.
    EvolutionaryTracei Q8N6T7.
    GeneWikii SIRT6.
    GenomeRNAii 51548.
    NextBioi 55327.
    PROi Q8N6T7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N6T7.
    Bgeei Q8N6T7.
    Genevestigatori Q8N6T7.

    Family and domain databases

    Gene3Di 3.40.50.1220. 2 hits.
    InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR003000. Sirtuin.
    IPR026590. Ssirtuin_cat_dom.
    [Graphical view ]
    PANTHERi PTHR11085. PTHR11085. 1 hit.
    Pfami PF02146. SIR2. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52467. SSF52467. 1 hit.
    PROSITEi PS50305. SIRTUIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phylogenetic classification of prokaryotic and eukaryotic Sir-2 like proteins."
      Frye R.A.
      Biochem. Biophys. Res. Commun. 273:793-798(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Spleen.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-46.
      Tissue: Heart and Teratocarcinoma.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-46.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ASN-46.
      Tissue: Blood, Eye and Lung.
    7. "Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins."
      Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., Horikawa I.
      Mol. Biol. Cell 16:4623-4635(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-133, SUBCELLULAR LOCATION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span."
      Kawahara T.L.A., Michishita E., Adler A.S., Damian M., Berber E., Lin M., McCord R.A., Ongaigui K.C.L., Boxer L.D., Chang H.Y., Chua K.F.
      Cell 136:62-74(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RELA, SUBCELLULAR LOCATION.
    12. "Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6."
      Michishita E., McCord R.A., Boxer L.D., Barber M.F., Hong T., Gozani O., Chua K.F.
      Cell Cycle 8:2664-2666(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Human SIRT6 promotes DNA end resection through CtIP deacetylation."
      Kaidi A., Weinert B.T., Choudhary C., Jackson S.P.
      Science 329:1348-1353(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RBBP8, MUTAGENESIS OF HIS-133.
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-318 IN COMPLEX WITH ZINC AND ADP-RIBOSE, FUNCTION.

    Entry informationi

    Entry nameiSIR6_HUMAN
    AccessioniPrimary (citable) accession number: Q8N6T7
    Secondary accession number(s): B2RCD0
    , O75291, Q6IAF5, Q6PK99, Q8NCD2, Q9BSI5, Q9BWP3, Q9NRC7, Q9UQD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: October 31, 2003
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The reported ADP-ribosyltransferase activity of sirtuins is likely some inefficient side reaction of the deacetylase activity and may not be physiologically relevant.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3