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UniProtKB/Swiss-Prot entry Q8N6T7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SIRT6_HUMAN
Primary accession number Q8N6T7
Secondary accession numbers O75291 Q6IAF5 Q6PK99 Q8NCD2 Q9BSI5 Q9BWP3 Q9NRC7 Q9UQD1
Integrated into Swiss-Prot on October 31, 2003
Sequence was last modified on October 31, 2003 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Mono-ADP-ribosyltransferase sirtuin-6
Synonyms EC 2.4.2.31
SIR2-like protein 6
Gene name
Name: SIRT6
Synonyms: SIR2L6
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Spleen;
DOI=10.1006/bbrc.2000.3000; PubMed=10873683 [NCBI, ExPASy, EBI, Israel, Japan]
Frye R.A.;
"Phylogenetic classification of prokaryotic and eukaryotic Sir-2 like proteins.";
Biochem. Biophys. Res. Commun. 273:793-798(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-46.
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT ASN-46.
TISSUE=Blood, Eye, Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294 AND SER-303, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF233396; AAF43432.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK074810; BAC11222.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457200; CAG33481.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005620; AAC34468.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006930; AAD15478.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000090; AAH00090.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004218; AAH04218.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005026; AAH05026.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC028220; AAH28220.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_057623.1; -.
UniGene Hs.423756
3D structure databases
HSSP O28597; 1ICI. [HSSP ENTRY / PDB]
ModBase Q8N6T7.
Protein-protein interaction databases
IntAct Q8N6T7; -.
PTM databases
PhosphoSite Q8N6T7; -.
Organism-specific databases
H-InvDB HIX0014654; -.
HGNC HGNC:14934; SIRT6.
GenAtlas SIRT6.
MIM 606211; gene. [NCBI / EBI]
PharmGKB PA37939; -.
GeneCards Q8N6T7.
Gene expression databases
GermOnline ENSG00000077463; Homo sapiens.
Ontologies
GO
GO:0005677; Cellular component: chromatin silencing complex (inferred from electronic annotation from InterPro).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0003956; Molecular function: NAD(P)+-protein-arginine ADP-ribosyltransferase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0003950; Molecular function: NAD+ ADP-ribosyltransferase activity (traceable author statement from UniProtKB).
GO:0017136; Molecular function: NAD-dependent histone deacetylase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from sequence or structural similarity from UniProtKB).
GO:0006342; Biological process: chromatin silencing (inferred from electronic annotation from InterPro).
GO:0006471; Biological process: protein amino acid ADP-ribosylation (inferred from sequence or structural similarity from UniProtKB).
GO:0006476; Biological process: protein amino acid deacetylation (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003000; NAD-dep_histone_deAcase_SIR2.
Graphical view of domain structure.
PANTHER PTHR11085; SIR2; 1.
Pfam PF02146; SIR2; 1.
Pfam graphical view of domain structure.
PROSITE PS50305; SIRTUIN; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8N6T7.
Genome annotation databases
Ensembl ENSG00000077463; Homo sapiens. [Contig view]
GeneID 51548; -.
KEGG hsa:51548; -.
Phylogenomic databases
HOVERGEN Q8N6T7; -.
Other
NextBio 55327; -.
SOURCE SIRT6; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ADP-ribosylation; Alternative splicing; Glycosyltransferase; Metal-binding; NAD; NADP; Nucleus; Phosphoprotein; Polymorphism; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   355  355     Mono-ADP-ribosyltransferase sirtuin-6. PRO_0000110269
DOMAIN   35   274  240     Deacetylase sirtuin-type. 
NP_BIND   52    71  20     NAD (By similarity). 
NP_BIND   113   117  5     NAD (By similarity). 
COMPBIAS   287   345  59     Pro-rich. 
ACT_SITE   133   133        Proton acceptor (By similarity). 
METAL   141   141        Zinc (By similarity). 
METAL   144   144        Zinc (By similarity). 
METAL   166   166        Zinc (By similarity). 
METAL   177   177        Zinc (By similarity). 
MOD_RES   294   294        Phosphothreonine. 
MOD_RES   303   303        Phosphoserine. 
VAR_SEQ   23    64        Missing (in isoform 4). VSP_013659
VAR_SEQ   65   125        Missing (in isoform 3). VSP_008732
VAR_SEQ   179   205        Missing (in isoform 2 and isoform 4). VSP_008733
VAR_SEQ   206   248        NADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQP TKHDR -> SGPAGTCRWLPSAGEAAWSSSTCSPPSTTAMLTSASMA TLTRS (in isoform 3). VSP_008734
VAR_SEQ   249   355        Missing (in isoform 3). VSP_008735
VARIANT   46    46  1     S -> N (in dbSNP:rs352493 [NCBI]). VAR_017154 
CONFLICT   42    42        W -> R (in Ref. 3; CAG33481). 
CONFLICT   249   249        H -> Y (in Ref. 5; AAH04218). 
CONFLICT   267   267        K -> E (in Ref. 1; AAF43432). 
Sequence information
Length: 355 AA [This is the length of the unprocessed precursor] Molecular weight: 39119 Da [This is the MW of the unprocessed precursor] CRC64: 0C86AAC497130BBF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVNYAAGLS PYADKGKCGL PEIFDPPEEL ERKVWELARL VWQSSSVVFH TGAGISTASG 

        70         80         90        100        110        120 
IPDFRGPHGV WTMEERGLAP KFDTTFESAR PTQTHMALVQ LERVGLLRFL VSQNVDGLHV 

       130        140        150        160        170        180 
RSGFPRDKLA ELHGNMFVEE CAKCKTQYVR DTVVGTMGLK ATGRLCTVAK ARGLRACRGE 

       190        200        210        220        230        240 
LRDTILDWED SLPDRDLALA DEASRNADLS ITLGTSLQIR PSGNLPLATK RRGGRLVIVN 

       250        260        270        280        290        300 
LQPTKHDRHA DLRIHGYVDE VMTRLMKHLG LEIPAWDGPR VLERALPPLP RPPTPKLEPK 

       310        320        330        340        350 
EESPTRINGS IPAGPKQEPC AQHNGSEPAS PKRERPTSPA PHRPPKRVKA KAVPS 

Q8N6T7 in FASTA format

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