Reviewed, UniProtKB/Swiss-Prot Q8IXJ6 (SIRT2_HUMAN)

Names and origin

Protein names

Recommended name:
    NAD-dependent deacetylase sirtuin-2
    EC=3.5.1.-
Alternative name(s):
    SIR2-like protein 2
      Short name=SIR2-like

Gene names

Name:	SIRT2
Synonyms:	SIR2L, SIR2L2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	NAD-dependent protein deacetylase, which deacetylates the '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. Ref.12 Ref.13
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	Cytoplasm › cytoskeleton. Note: Colocalizes with microtubules. Ref.12 Ref.2 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.2 Ref.1 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 Ref.16
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. Contains 1 deacetylase sirtuin-type domain.
Sequence caution	The sequence AAF67015.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding NAD Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing at rDNA Ref.17 Non-traceable author statement. Source: UniProtKB chromatin silencing at telomere Ref.17 Non-traceable author statement. Source: UniProtKB histone deacetylation Ref.13 Traceable author statement. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of striated muscle tissue development Inferred from direct assay. Source: UniProtKB protein amino acid ADP-ribosylation Ref.1 Non-traceable author statement. Source: UniProtKB redox signal response Non-traceable author statement. Source: UniProtKB regulation of exit from mitosis Ref.13 Non-traceable author statement. Source: UniProtKB regulation of phosphorylation Ref.13 Non-traceable author statement. Source: UniProtKB
Cellular component	chromatin silencing complex Ref.13 Non-traceable author statement. Source: UniProtKB cytoplasm Ref.13 Ref.15 Inferred from direct assay. Source: UniProtKB microtubule Ref.12 Inferred from direct assay. Source: UniProtKB
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro NAD-dependent histone deacetylase activity Ref.13 Inferred from direct assay. Source: UniProtKB histone acetyltransferase binding Inferred from physical interaction. Source: UniProtKB histone deacetylase binding Ref.12 Inferred from physical interaction. Source: UniProtKB transcription factor binding Inferred from physical interaction. Source: UniProtKB tubulin deacetylase activity Ref.12 Inferred from direct assay. Source: UniProtKB ubiquitin binding Ref.13 Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9Y569	1	EBI-477232,EBI-1052090
GYS1	P13807	1	EBI-477232,EBI-963094
HDAC6	Q9UBN7	1	EBI-477232,EBI-301697
KAT2A	Q92830-1	1	EBI-477232,EBI-477636
KAT2A	Q92830-2	1	EBI-477232,EBI-477641
KAT2B	Q92831	2	EBI-477232,EBI-477430
KRT78	Q8N1N4	1	EBI-477232,EBI-1056564
PHB2	Q99623	1	EBI-477232,EBI-358348
RTN4	Q9NQC3	1	EBI-477232,EBI-715945
SARS	P49591	1	EBI-477232,EBI-1053431
SPOP	O43791	1	EBI-477232,EBI-743549

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 389

389

NAD-dependent deacetylase sirtuin-2

PRO_0000110258

Regions

Domain

65 – 340

276

Deacetylase sirtuin-type

Nucleotide binding

84 – 104

21

NAD By similarity

Nucleotide binding

167 – 171

5

NAD By similarity

Sites

Active site

187

1

Proton acceptor

Metal binding

195

1

Zinc

Metal binding

200

1

Zinc

Metal binding

221

1

Zinc

Metal binding

224

1

Zinc

Amino acid modifications

Modified residue

23

1

Phosphoserine By similarity

Modified residue

25

1

Phosphoserine Ref.16

Modified residue

27

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

1 – 38

38

MAEPD…GEADM → MPLAECPSCRCLSSFRSV in isoform 3.

VSP_008726

Alternative sequence

1 – 37

37

Missing in isoform 2.

VSP_008724

Alternative sequence

266 – 271

6

VQPFAS → GRGLAG in isoform 4.

VSP_008727

Alternative sequence

272 – 389

118

Missing in isoform 4.

VSP_008728

Experimental info

Mutagenesis

97

1

R → A: No effect on deacetylase activity. Ref.17

Mutagenesis

167

1

Q → A: Reduced deacetylase activity. Ref.17

Mutagenesis

168

1

N → A: Abolishes acetylation of alpha-tubulin. Ref.12 Ref.17

Mutagenesis

170

1

D → A or N: Reduced deacetylase activity. Ref.17

Mutagenesis

187

1

H → Y or A: Loss of function. Abolishes acetylation of alpha-tubulin. No effect on phosphorylation. Ref.12 Ref.13 Ref.11 Ref.1 Ref.17

Sequence conflict

199

1

S → N Ref.5

Sequence conflict

219

1

P → L in CAD43717. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

389

Helix Strand Turn

Details...

Helix

35 – 44

10

Beta strand

60 – 63

4

Helix

64 – 72

9

Beta strand

79 – 83

5

Helix

85 – 87

3

Helix

89 – 91

3

Turn

105 – 109

5

Helix

115 – 119

5

Helix

121 – 126

6

Helix

129 – 138

10

Beta strand

139 – 142

4

Helix

147 – 157

11

Beta strand

161 – 166

6

Helix

172 – 175

4

Helix

180 – 182

3

Beta strand

183 – 185

3

Beta strand

188 – 196

9

Turn

198 – 200

3

Helix

206 – 214

9

Turn

222 – 224

3

Beta strand

227 – 232

6

Helix

241 – 249

9

Helix

250 – 252

3

Beta strand

255 – 262

8

Helix

267 – 273

7

Beta strand

282 – 288

7

Helix

295 – 304

10

Beta strand

309 – 311

3

Beta strand

316 – 322

7

Helix

324 – 334

11

Helix

338 – 354

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2003. Version 2. Checksum: A392442A8F6316F1	FASTA	389	43,182
	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
	Isoform 2. Checksum: FFED07DEF9E3416A	FASTA	352	39,515
	10 20 30 40 50 60 MDFLRNLFSQ TLSLGSQKER LLDELTLEGV ARYMQSERCR RVICLVGAGI STSAGIPDFR 70 80 90 100 110 120 SPSTGLYDNL EKYHLPYPEA IFEISYFKKH PEPFFALAKE LYPGQFKPTI CHYFMRLLKD 130 140 150 160 170 180 KGLLLRCYTQ NIDTLERIAG LEQEDLVEAH GTFYTSHCVS ASCRHEYPLS WMKEKIFSEV 190 200 210 220 230 240 TPKCEDCQSL VKPDIVFFGE SLPARFFSCM QSDFLKVDLL LVMGTSLQVQ PFASLISKAP 250 260 270 280 290 300 LSTPRLLINK EKAGQSDPFL GMIMGLGGGM DFDSKKAYRD VAWLGECDQG CLALAELLGW 310 320 330 340 350 KKELEDLVRR EHASIDAQSG AGVPNPSTSA SPKKSPPPAK DEARTTEREK PQ
	Isoform 3. Checksum: 0805580CAAB59A51	FASTA	369	41,353
	10 20 30 40 50 60 MPLAECPSCR CLSSFRSVDF LRNLFSQTLS LGSQKERLLD ELTLEGVARY MQSERCRRVI 70 80 90 100 110 120 CLVGAGISTS AGIPDFRSPS TGLYDNLEKY HLPYPEAIFE ISYFKKHPEP FFALAKELYP 130 140 150 160 170 180 GQFKPTICHY FMRLLKDKGL LLRCYTQNID TLERIAGLEQ EDLVEAHGTF YTSHCVSASC 190 200 210 220 230 240 RHEYPLSWMK EKIFSEVTPK CEDCQSLVKP DIVFFGESLP ARFFSCMQSD FLKVDLLLVM 250 260 270 280 290 300 GTSLQVQPFA SLISKAPLST PRLLINKEKA GQSDPFLGMI MGLGGGMDFD SKKAYRDVAW 310 320 330 340 350 360 LGECDQGCLA LAELLGWKKE LEDLVRREHA SIDAQSGAGV PNPSTSASPK KSPPPAKDEA RTTEREKPQ
	Isoform 4. Checksum: FF4641368029BD94	FASTA	271	30,379
	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 ARFFSCMQSD FLKVDLLLVM GTSLQGRGLA G

References

	« Hide 'large scale' referencesShow '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: 10381378] [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: 10393250] [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: 12065666] [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. , 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: 10931946] [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. , 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: 14702039] [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. , 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: 15489334] [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: 11483616] [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: 11812793] [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: 12620231] [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: 12697818] [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: 12963026] [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: 16079181] [Abstract] Cited for: SUBCELLULAR LOCATION.
[16]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, MASS SPECTROMETRY. Tissue: Platelet.
[17]	"Structure of the histone deacetylase SIRT2." Finnin M.S., Donigian J.R., Pavletich N.P. Nat. Struct. Biol. 8:621-625(2001) [PubMed: 11427894] [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

EMBLGenBankDDBJ

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.

IPI

IPI00179109.
IPI00382551.
IPI00382553.
IPI00472047.

RefSeq

NP_036369.2.
NP_085096.1.

UniGene

Hs.466693

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J8F	X-ray	1.70	A/B/C	34-356	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IXJ6. 13 interactions.

STRING

Q8IXJ6.

PTM databases

PhosphoSite

Q8IXJ6.

Proteomic databases

PRIDE

Q8IXJ6.

Genome annotation databases

Ensembl

ENST00000249396; ENSP00000249396; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000358931; ENSP00000351809; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000381766; ENSP00000401203; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000392081; ENSP00000375931; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000402684; ENSP00000384002; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000407552; ENSP00000385146; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000414941; ENSP00000404309; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000420440; ENSP00000400338; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000423526; ENSP00000409690; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000437828; ENSP00000397022; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000443898; ENSP00000411393; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000447739; ENSP00000408023; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000451193; ENSP00000407272; ENSG00000068903; Homo sapiens. [Genome view]
ENST00000456703; ENSP00000400725; ENSG00000068903; Homo sapiens. [Genome view]

GeneID

22933.

KEGG

hsa:22933.

UCSC

uc002ojs.1. human.
uc002ojt.1. human.
uc002oju.1. human.
uc010egh.1. human.

Organism-specific databases

CTD

22933.

GeneCards

GC19M044061.

H-InvDB

HIX0015103.

HGNC

HGNC:10886. SIRT2.

HPA

CAB004573.
HPA011165.

MIM

604480. gene.

PharmGKB

PA35786.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q8IXJ6.

HOVERGEN

Q8IXJ6.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

Gene expression databases

ArrayExpress

Q8IXJ6.

Bgee

Q8IXJ6.

CleanEx

HS_SIRT2.

Genevestigator

Q8IXJ6.

GermOnline

ENSG00000068903. Homo sapiens.

Family and domain databases

InterPro

IPR017328. NAD-dep_deAcase_SIR2_euk.
IPR003000. NAD-dep_histone_deAcase_SIR2.
[Graphical view]

PANTHER

PTHR11085. SIR2. 1 hit.

Pfam

PF02146. SIR2. 1 hit.
[Graphical view]

PIRSF

PIRSF037938. SIR2_euk. 1 hit.

PROSITE

PS50305. SIRTUIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

43669.

SOURCE

Search...

Entry information

Entry name

SIRT2_HUMAN

Accession

Primary (citable) accession number: Q8IXJ6
Secondary accession number(s): A8K3V1 , B2RB45, O95889, Q924Y7, Q9P0G8, Q9UNT0, Q9Y6E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	October 31, 2003
Last modified:	November 3, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.