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Q8IXJ6 (SIR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD-dependent protein deacetylase sirtuin-2

EC=3.5.1.-
Alternative name(s):
Regulatory protein SIR2 homolog 2
SIR2-like protein 2
Gene names
Name:SIRT2
Synonyms:SIR2L, SIR2L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins such as ACLY, PCK1 and RELA. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA. Ref.12 Ref.13 Ref.20 Ref.21 Ref.22

Catalytic activity

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein. Ref.11

Cofactor

Binds 1 zinc ion per subunit.

Enzyme regulation

Inhibited by Sirtinol, A3 and M15 small molecules. Inhibited by nicotinamide.

Subunit structure

Interacts with HDAC6, suggesting that these proteins belong to a large complex that deacetylate the cytoskeleton. Ref.12

Subcellular location

Cytoplasmcytoskeleton. Note: Colocalizes with microtubules. Ref.2 Ref.12 Ref.15

Tissue specificity

Widely expressed. Highly expressed in heart, brain and skeletal muscle, while it is weakly expressed in placenta and lung. Down-regulated in many gliomas suggesting that it may act as a tumor suppressor gene in human gliomas possibly through the regulation of microtubule network. Ref.1 Ref.2 Ref.14

Developmental stage

Peaks during mitosis. After mitosis, it is probably degraded by the 26S proteasome. Ref.13

Post-translational modification

Phosphorylated at the G2/M transition of the cell cycle. Ref.13

Miscellaneous

Has some ability to deacetylate histones in vitro, but seeing its subcellular location, this is unlikely in vivo.

Sequence similarities

Belongs to the sirtuin family. Class I subfamily.

Contains 1 deacetylase sirtuin-type domain.

Sequence caution

The sequence AAD45971.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAF67015.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
NAD
Zinc
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing

Non-traceable author statement Ref.13. Source: UniProtKB

chromatin silencing at rDNA

Non-traceable author statement Ref.23. Source: UniProtKB

chromatin silencing at telomere

Non-traceable author statement Ref.23. Source: UniProtKB

gene silencing

Non-traceable author statement Ref.1. Source: UniProtKB

histone deacetylation

Traceable author statement Ref.13. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of striated muscle tissue development

Inferred from direct assay PubMed 12887892. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12887892. Source: UniProtKB

peptidyl-lysine deacetylation

Inferred from direct assay Ref.22. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 21841822. Source: UniProtKB

protein ADP-ribosylation

Non-traceable author statement Ref.1. Source: UniProtKB

protein deacetylation

Inferred from direct assay PubMed 17172643. Source: UniProtKB

regulation of exit from mitosis

Non-traceable author statement Ref.13. Source: UniProtKB

regulation of phosphorylation

Non-traceable author statement Ref.13. Source: UniProtKB

response to redox state

Non-traceable author statement PubMed 12887892. Source: UniProtKB

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentchromatin silencing complex

Non-traceable author statement Ref.13. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.13Ref.15. Source: UniProtKB

microtubule

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionNAD+ binding

Inferred from direct assay Ref.23. Source: UniProtKB

NAD-dependent histone deacetylase activity

Inferred from direct assay Ref.23Ref.13. Source: UniProtKB

NAD-dependent protein deacetylase activity

Inferred from direct assay Ref.22. Source: UniProtKB

histone acetyltransferase binding

Inferred from physical interaction PubMed 12887892. Source: UniProtKB

histone deacetylase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

protein deacetylase activity

Inferred from direct assay PubMed 17172643. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 12887892PubMed 15126506. Source: UniProtKB

tubulin deacetylase activity

Inferred from direct assay Ref.12. Source: UniProtKB

ubiquitin binding

Inferred from direct assay Ref.13. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.23. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IXJ6-1)

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.
Isoform 2 (identifier: Q8IXJ6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.
Isoform 3 (identifier: Q8IXJ6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADM → MPLAECPSCRCLSSFRSV
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8IXJ6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     266-271: VQPFAS → GRGLAG
     272-389: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 389388NAD-dependent protein deacetylase sirtuin-2
PRO_0000110258

Regions

Domain65 – 340276Deacetylase sirtuin-type
Nucleotide binding84 – 10421NAD By similarity
Nucleotide binding167 – 1704NAD By similarity
Nucleotide binding261 – 2633NAD By similarity
Nucleotide binding286 – 2883NAD By similarity

Sites

Active site1871Proton acceptor
Metal binding1951Zinc
Metal binding2001Zinc
Metal binding2211Zinc
Metal binding2241Zinc
Binding site3241NAD; via amide nitrogen By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.18

Natural variations

Alternative sequence1 – 3838MAEPD…GEADM → MPLAECPSCRCLSSFRSV in isoform 3.
VSP_008726
Alternative sequence1 – 3737Missing in isoform 2.
VSP_008724
Alternative sequence266 – 2716VQPFAS → GRGLAG in isoform 4.
VSP_008727
Alternative sequence272 – 389118Missing in isoform 4.
VSP_008728

Experimental info

Mutagenesis971R → A: No effect on deacetylase activity. Ref.23
Mutagenesis1671Q → A: Reduced deacetylase activity. Ref.23
Mutagenesis1681N → A: Abolishes acetylation of alpha-tubulin. Ref.12 Ref.23
Mutagenesis1701D → A or N: Reduced deacetylase activity. Ref.23
Mutagenesis1871H → Y or A: Loss of function. Abolishes acetylation of alpha-tubulin. No effect on phosphorylation. Ref.1 Ref.11 Ref.12 Ref.13 Ref.23
Sequence conflict1991S → N Ref.5
Sequence conflict2191P → L in CAD43717. Ref.4

Secondary structure

................................................................ 389
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2003. Version 2.
Checksum: A392442A8F6316F1

FASTA38943,182
        10         20         30         40         50         60 
MAEPDPSHPL ETQAGKVQEA QDSDSDSEGG AAGGEADMDF LRNLFSQTLS LGSQKERLLD 

        70         80         90        100        110        120 
ELTLEGVARY MQSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYDNLEKY HLPYPEAIFE 

       130        140        150        160        170        180 
ISYFKKHPEP FFALAKELYP GQFKPTICHY FMRLLKDKGL LLRCYTQNID TLERIAGLEQ 

       190        200        210        220        230        240 
EDLVEAHGTF YTSHCVSASC RHEYPLSWMK EKIFSEVTPK CEDCQSLVKP DIVFFGESLP 

       250        260        270        280        290        300 
ARFFSCMQSD FLKVDLLLVM GTSLQVQPFA SLISKAPLST PRLLINKEKA GQSDPFLGMI 

       310        320        330        340        350        360 
MGLGGGMDFD SKKAYRDVAW LGECDQGCLA LAELLGWKKE LEDLVRREHA SIDAQSGAGV 

       370        380 
PNPSTSASPK KSPPPAKDEA RTTEREKPQ 

« Hide

Isoform 2 [UniParc].

Checksum: FFED07DEF9E3416A
Show »

FASTA35239,515
Isoform 3 [UniParc].

Checksum: 0805580CAAB59A51
Show »

FASTA36941,353
Isoform 4 [UniParc].

Checksum: FF4641368029BD94
Show »

FASTA27130,379

References

« Hide 'large scale' references
[1]"Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity."
Frye R.A.
Biochem. Biophys. Res. Commun. 260:273-279(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF HIS-187.
Tissue: Testis.
[2]"Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2."
Afshar G., Murnane J.P.
Gene 234:161-168(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression."
De Smet C., Nishimori H., Furnari F.B., Boegler O., Huang H.-J.S., Cavenee W.K.
J. Neurochem. 81:575-588(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Response of autologous T cells to a human melanoma is dominated by individual mutant antigens."
Lennerz V., Fatho M., Gentilini C., Lifke A., Woelfel C., Woelfel T.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Adrenal gland.
[6]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Brain and Lung.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 2).
Tissue: Lung.
[9]Mei G., Yu W., Gibbs R.A.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-389 (ISOFORM 4).
Tissue: Brain.
[10]"Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening."
Grozinger C.M., Chao E.D., Blackwell H.E., Moazed D., Schreiber S.L.
J. Biol. Chem. 276:38837-38843(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY SIRTINOL; A3 AND M15.
[11]"Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases."
Borra M.T., O'Neill F.J., Jackson M.D., Marshall B.L., Verdin E., Foltz K.R., Denu J.M.
J. Biol. Chem. 277:12632-12641(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-187.
[12]"The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase."
North B.J., Marshall B.L., Borra M.T., Denu J.M., Verdin E.
Mol. Cell 11:437-444(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC6, MUTAGENESIS OF ASN-168 AND HIS-187.
[13]"Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle."
Dryden S.C., Nahhas F.A., Nowak J.E., Goustin A.-S., Tainsky M.A.
Mol. Cell. Biol. 23:3173-3185(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, MUTAGENESIS OF HIS-187.
[14]"Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene."
Hiratsuka M., Inoue T., Toda T., Kimura N., Shirayoshi Y., Kamitani H., Watanabe T., Ohama E., Tahimic C.G.T., Kurimasa A., Oshimura M.
Biochem. Biophys. Res. Commun. 309:558-566(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[15]"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.
[16]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310."
Rothgiesser K.M., Erener S., Waibel S., Luscher B., Hottiger M.O.
J. Cell Sci. 123:4251-4258(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEACETYLATION OF RELA.
[21]"Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase."
Jiang W., Wang S., Xiao M., Lin Y., Zhou L., Lei Q., Xiong Y., Guan K.L., Zhao S.
Mol. Cell 43:33-44(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEACETYLATION OF PCK1.
[22]"Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth."
Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.
Mol. Cell 51:506-518(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"Structure of the histone deacetylase SIRT2."
Finnin M.S., Donigian J.R., Pavletich N.P.
Nat. Struct. Biol. 8:621-625(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 34-356 IN COMPLEX WITH ZINC, MUTAGENESIS OF ARG-97; GLN-167; ASN-168; ASP-170 AND HIS-187.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083107 mRNA. Translation: AAD40850.2.
AF095714 mRNA. Translation: AAD45971.1. Different initiation.
AY030277 mRNA. Translation: AAK51133.1.
AJ505014 mRNA. Translation: CAD43717.1.
AF160214 mRNA. Translation: AAF67015.1. Frameshift.
AK290716 mRNA. Translation: BAF83405.1.
AK314492 mRNA. Translation: BAG37092.1.
CH471126 Genomic DNA. Translation: EAW56833.1.
CH471126 Genomic DNA. Translation: EAW56835.1.
BC003012 mRNA. Translation: AAH03012.1.
BC003547 mRNA. Translation: AAH03547.1.
AF131800 mRNA. Translation: AAD20046.1.
RefSeqNP_001180215.1. NM_001193286.1.
NP_036369.2. NM_012237.3.
NP_085096.1. NM_030593.2.
UniGeneHs.466693.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J8FX-ray1.70A/B/C34-356[»]
3ZGOX-ray1.63A/B/C34-356[»]
3ZGVX-ray2.27A/B34-356[»]
4L3OX-ray2.52A/B/C/D55-356[»]
ProteinModelPortalQ8IXJ6.
SMRQ8IXJ6. Positions 54-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116593. 93 interactions.
DIPDIP-33350N.
IntActQ8IXJ6. 14 interactions.
MINTMINT-3037896.
STRING9606.ENSP00000249396.

Chemistry

BindingDBQ8IXJ6.
ChEMBLCHEMBL4462.

PTM databases

PhosphoSiteQ8IXJ6.

Polymorphism databases

DMDM38258608.

Proteomic databases

PaxDbQ8IXJ6.
PRIDEQ8IXJ6.

Protocols and materials databases

DNASU22933.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249396; ENSP00000249396; ENSG00000068903. [Q8IXJ6-1]
ENST00000358931; ENSP00000351809; ENSG00000068903. [Q8IXJ6-4]
ENST00000392081; ENSP00000375931; ENSG00000068903. [Q8IXJ6-2]
GeneID22933.
KEGGhsa:22933.
UCSCuc002ojs.2. human. [Q8IXJ6-3]
uc002ojt.2. human. [Q8IXJ6-1]
uc010egh.2. human. [Q8IXJ6-4]

Organism-specific databases

CTD22933.
GeneCardsGC19M039369.
HGNCHGNC:10886. SIRT2.
HPACAB004573.
HPA011165.
MIM604480. gene.
neXtProtNX_Q8IXJ6.
PharmGKBPA35786.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0846.
HOVERGENHBG057095.
KOK11412.
OMATICHYFM.
OrthoDBEOG7WX09C.
PhylomeDBQ8IXJ6.
TreeFamTF106181.

Enzyme and pathway databases

SABIO-RKQ8IXJ6.

Gene expression databases

ArrayExpressQ8IXJ6.
BgeeQ8IXJ6.
CleanExHS_SIRT2.
GenevestigatorQ8IXJ6.

Family and domain databases

InterProIPR003000. Sirtuin.
IPR017328. Sirtuin_class_I.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERPTHR11085. PTHR11085. 1 hit.
PfamPF02146. SIR2. 1 hit.
[Graphical view]
PIRSFPIRSF037938. SIR2_euk. 1 hit.
PROSITEPS50305. SIRTUIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSIRT2. human.
EvolutionaryTraceQ8IXJ6.
GeneWikiSIRT2.
GenomeRNAi22933.
NextBio43669.
PROQ8IXJ6.
SOURCESearch...

Entry information

Entry nameSIR2_HUMAN
AccessionPrimary (citable) accession number: Q8IXJ6
Secondary accession number(s): A8K3V1 expand/collapse secondary AC list , B2RB45, O95889, Q924Y7, Q9P0G8, Q9UNT0, Q9Y6E9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM