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Q8N6T7

- SIR6_HUMAN

UniProt

Q8N6T7 - SIR6_HUMAN

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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

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

Zn2+By similarityNote: 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. chromatin binding Source: Ensembl
  2. NAD(P)+-protein-arginine ADP-ribosyltransferase activity Source: UniProtKB
  3. NAD+ ADP-ribosyltransferase activity Source: BHF-UCL
  4. NAD+ binding Source: UniProtKB
  5. NAD-dependent histone deacetylase activity Source: UniProtKB
  6. NAD-dependent histone deacetylase activity (H3-K9 specific) 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ8N6T7.
ExpressionAtlasiQ8N6T7. baseline.
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. 27 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 – 84Combined sources
Helixi27 – 4317Combined sources
Beta strandi47 – 515Combined sources
Helixi53 – 553Combined sources
Helixi57 – 593Combined sources
Beta strandi64 – 663Combined sources
Helixi70 – 745Combined sources
Turni75 – 773Combined sources
Turni86 – 883Combined sources
Helixi93 – 10311Combined sources
Beta strandi109 – 1124Combined sources
Helixi118 – 1214Combined sources
Beta strandi122 – 1254Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi138 – 1414Combined sources
Turni142 – 1443Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi161 – 1655Combined sources
Turni171 – 1744Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi188 – 1903Combined sources
Helixi194 – 20512Combined sources
Beta strandi208 – 2147Combined sources
Helixi222 – 2243Combined sources
Helixi225 – 2317Combined sources
Beta strandi235 – 2395Combined sources
Helixi247 – 2493Combined sources
Beta strandi251 – 2544Combined sources
Helixi258 – 26912Combined sources
Beta strandi280 – 2823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063706.
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

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

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:
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_001193285.1. [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:
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 .
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:
PDBei
RCSB PDBi
PDBji
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. 27 interactions.
DIPi DIP-47346N.
IntActi Q8N6T7. 15 interactions.
MINTi MINT-1374731.

Chemistry

BindingDBi Q8N6T7.
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.
GeneTreei ENSGT00530000063706.
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

Bgeei Q8N6T7.
ExpressionAtlasi Q8N6T7. baseline.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 122 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