Q9NXA8 (SIR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NAD-dependent protein deacylase sirtuin-5, mitochondrial
EC=3.5.1.-

Alternative name(s):
Regulatory protein SIR2 homolog 5
SIR2-like protein 5

Gene names

Name:	SIRT5
Synonyms:	SIR2L5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NAD-dependent lysine demalonylase and desuccinylase that specifically removes malonyl and succinyl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro. Ref.8 Ref.11 Ref.14
Catalytic activity	NAD+ + a malonylprotein = nicotinamide + O-malonyl-ADP-ribose + a protein. Ref.13 Ref.14 NAD+ + a succinylprotein = nicotinamide + O-succinyl-ADP-ribose + a protein. Ref.13 Ref.14
Cofactor	Binds 1 zinc ion per subunit. Ref.14
Enzyme regulation	Inhibited by suramin. Ref.13
Subunit structure	Interacts with CPS1 By similarity. Monomer. Homodimer. Forms homodimers upon suramin binding. Ref.13
Subcellular location	Mitochondrion matrix. Mitochondrion intermembrane space Ref.7 Ref.8 Ref.10. Isoform 1: Cytoplasm. Mitochondrion Ref.7 Ref.8 Ref.10. Isoform 2: Mitochondrion Ref.7 Ref.8 Ref.10.
Tissue specificity	Widely expressed. Ref.1
Domain	In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-102 and Arg-105) that bind to malonylated and succinylated substrates and define the specificity (Ref.14). HAMAP-Rule MF_03160
Sequence similarities	Belongs to the sirtuin family. Class III subfamily. Contains 1 deacetylase sirtuin-type domain.
Biophysicochemical properties	Kinetic parameters: KM=6.1 µM for a synthetic histone H3K9 malonyllysine peptide Ref.14 KM=5.8 µM for a synthetic histone H3K9 succinyllysine peptide KM=8.7 µM for a synthetic GLUD1 peptide malonylated at 'Lys-503' KM=14 µM for a synthetic GLUD1 peptide succinylated at 'Lys-503' KM=150 µM for a synthetic ACSS1 peptide malonylated at 'Lys-628' KM=450 µM for a synthetic ACSS1 peptide succinylated at 'Lys-628'

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	Metal-binding NAD Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin silencing Traceable author statement Ref.1. Source: ProtInc protein ADP-ribosylation Traceable author statement Ref.1. Source: ProtInc protein deacetylation Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	mitochondrial intermembrane space Inferred from direct assay Ref.8. Source: UniProtKB mitochondrial matrix Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	NAD+ ADP-ribosyltransferase activity Traceable author statement Ref.1. Source: ProtInc NAD+ binding Inferred from direct assay Ref.11Ref.14. Source: UniProtKB protein-malonyllysine demalonylase activity Inferred from direct assay Ref.11Ref.14. Source: UniProtKB protein-succinyllysine desuccinylase activity Inferred from direct assay Ref.11Ref.14. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NXA8-1)

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: Q9NXA8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     286-299: RFHFQGPCGTTLPE → SHLISISSLIIIKN
     300-310: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9NXA8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     189-206: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q9NXA8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 36

36

Mitochondrion By similarity

Chain

37 – 310

274

NAD-dependent protein deacylase sirtuin-5, mitochondrial HAMAP-Rule MF_03160

PRO_0000110266

Regions

Domain

41 – 309

269

Deacetylase sirtuin-type

Nucleotide binding

58 – 77

20

NAD HAMAP-Rule MF_03160

Nucleotide binding

140 – 143

4

NAD By similarity

Nucleotide binding

249 – 251

3

NAD HAMAP-Rule MF_03160

Nucleotide binding

275 – 277

3

NAD HAMAP-Rule MF_03160

Sites

Active site

158

1

Proton acceptor

Metal binding

166

1

Zinc

Metal binding

169

1

Zinc

Metal binding

207

1

Zinc

Metal binding

212

1

Zinc

Binding site

102

1

Substrate

Binding site

105

1

Substrate

Binding site

293

1

NAD; via amide nitrogen

Natural variations

Alternative sequence

1 – 108

108

Missing in isoform 4.

VSP_042291

Alternative sequence

189 – 206

18

Missing in isoform 3.

VSP_042292

Alternative sequence

286 – 299

14

RFHFQ…TTLPE → SHLISISSLIIIKN in isoform 2.

VSP_008730

Alternative sequence

300 – 310

11

Missing in isoform 2.

VSP_008731

Natural variant

285

1

F → L.
Corresponds to variant rs9464003 [ dbSNP | Ensembl ].

VAR_029042

Natural variant

305

1

E → G.
Corresponds to variant rs34162626 [ dbSNP | Ensembl ].

VAR_051980

Experimental info

Mutagenesis

102

1

Y → F: Increases the KM for desuccinylation. Ref.14

Mutagenesis

105

1

R → M: Increases the KM for desuccinylation. Ref.14

Mutagenesis

158

1

H → A: Abolishes desuccinylation activity. Ref.11 Ref.14

Sequence conflict

53

1

I → M in BAG63757. Ref.2

Secondary structure

1

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310

Helix Strand Turn

Details...

Helix

40 – 49

10

Beta strand

51 – 57

7

Helix

59 – 61

3

Helix

63 – 65

3

Beta strand

70 – 72

3

Helix

73 – 75

3

Helix

82 – 85

4

Helix

88 – 93

6

Helix

95 – 109

15

Helix

116 – 129

14

Turn

130 – 132

3

Beta strand

134 – 140

7

Helix

145 – 149

5

Beta strand

153 – 156

4

Beta strand

159 – 166

8

Turn

167 – 169

3

Beta strand

172 – 174

3

Beta strand

178 – 181

4

Helix

182 – 184

3

Beta strand

190 – 193

4

Helix

201 – 203

3

Helix

209 – 211

3

Beta strand

215 – 220

6

Helix

229 – 241

13

Beta strand

243 – 249

7

Beta strand

252 – 255

4

Helix

257 – 259

3

Helix

260 – 266

7

Beta strand

271 – 277

7

Helix

282 – 284

3

Beta strand

285 – 291

7

Helix

293 – 301

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2003. Version 2. Checksum: 022DA32CDB43AC3A	FASTA	310	33,881
	10 20 30 40 50 60 MRPLQIVPSR LISQLYCGLK PPASTRNQIC LKMARPSSSM ADFRKFFAKA KHIVIISGAG 70 80 90 100 110 120 VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE FYHYRREVMG SKEPNAGHRA 130 140 150 160 170 180 IAECETRLGK QGRRVVVITQ NIDELHRKAG TKNLLEIHGS LFKTRCTSCG VVAENYKSPI 190 200 210 220 230 240 CPALSGKGAP EPGTQDASIP VEKLPRCEEA GCGGLLRPHV VWFGENLDPA ILEEVDRELA 250 260 270 280 290 300 HCDLCLVVGT SSVVYPAAMF APQVAARGVP VAEFNTETTP ATNRFRFHFQ GPCGTTLPEA 310 LACHENETVS
	Isoform 2 [UniParc]. Checksum: 2EE7C311AAA34CBA	FASTA	299	32,674
	10 20 30 40 50 60 MRPLQIVPSR LISQLYCGLK PPASTRNQIC LKMARPSSSM ADFRKFFAKA KHIVIISGAG 70 80 90 100 110 120 VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE FYHYRREVMG SKEPNAGHRA 130 140 150 160 170 180 IAECETRLGK QGRRVVVITQ NIDELHRKAG TKNLLEIHGS LFKTRCTSCG VVAENYKSPI 190 200 210 220 230 240 CPALSGKGAP EPGTQDASIP VEKLPRCEEA GCGGLLRPHV VWFGENLDPA ILEEVDRELA 250 260 270 280 290 HCDLCLVVGT SSVVYPAAMF APQVAARGVP VAEFNTETTP ATNRFSHLIS ISSLIIIKN
	Isoform 3 [UniParc]. Checksum: D89A65C251224735	FASTA	292	31,994
	10 20 30 40 50 60 MRPLQIVPSR LISQLYCGLK PPASTRNQIC LKMARPSSSM ADFRKFFAKA KHIVIISGAG 70 80 90 100 110 120 VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE FYHYRREVMG SKEPNAGHRA 130 140 150 160 170 180 IAECETRLGK QGRRVVVITQ NIDELHRKAG TKNLLEIHGS LFKTRCTSCG VVAENYKSPI 190 200 210 220 230 240 CPALSGKGCE EAGCGGLLRP HVVWFGENLD PAILEEVDRE LAHCDLCLVV GTSSVVYPAA 250 260 270 280 290 MFAPQVAARG VPVAEFNTET TPATNRFRFH FQGPCGTTLP EALACHENET VS
	Isoform 4 [UniParc]. Checksum: 051C7D4BE508D66B	FASTA	202	21,689
	10 20 30 40 50 60 MGSKEPNAGH RAIAECETRL GKQGRRVVVI TQNIDELHRK AGTKNLLEIH GSLFKTRCTS 70 80 90 100 110 120 CGVVAENYKS PICPALSGKG APEPGTQDAS IPVEKLPRCE EAGCGGLLRP HVVWFGENLD 130 140 150 160 170 180 PAILEEVDRE LAHCDLCLVV GTSSVVYPAA MFAPQVAARG VPVAEFNTET TPATNRFRFH 190 200 FQGPCGTTLP EALACHENET VS

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Testis.
[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] (ISOFORMS 2; 3 AND 4). Tissue: Amygdala, Hepatoblastoma and Testis.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[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] (ISOFORM 1). Tissue: Eye.
[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]	"Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5." Schlicker C., Gertz M., Papatheodorou P., Kachholz B., Becker C.F.W., Steegborn C. J. Mol. Biol. 382:790-801(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms." Matsushita N., Yonashiro R., Ogata Y., Sugiura A., Nagashima S., Fukuda T., Inatome R., Yanagi S. Genes Cells 16:190-202(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
[11]	"The first identification of lysine malonylation substrates and its regulatory enzyme." Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y. Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, NAD-BINDING, MUTAGENESIS OF HIS-158.
[12]	"Crystal structure of human sirtuin homolog 5 in complex with NAD." Structural genomics consortium (SGC) Submitted (FEB-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 34-302 IN COMPLEX WITH NAD AND ZINC IONS.
[13]	"Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin." Schuetz A., Min J., Antoshenko T., Wang C.-L., Allali-Hassani A., Dong A., Loppnau P., Vedadi M., Bochkarev A., Sternglanz R., Plotnikov A.N. Structure 15:377-389(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 34-302 IN COMPLEXES WITH ZINC IONS; SURAMIN AND ADP-RIBOSE, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
[14]	"Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase." Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H. Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-302 IN COMPLEX WITH NAD; ZINC IONS AND SUCCINYLATED PEPTIDE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-102; ARG-105 AND HIS-158.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF083110 mRNA. Translation: AAD40853.1.
AK000355 mRNA. Translation: BAA91107.1.
AK294162 mRNA. Translation: BAG57485.1.
AK302467 mRNA. Translation: BAG63757.1.
AM393414 mRNA. Translation: CAL38292.1.
AL441883 Genomic DNA. Translation: CAI19837.1.
AL441883 Genomic DNA. Translation: CAI19838.1.
CH471087 Genomic DNA. Translation: EAW55332.1.
BC000126 mRNA. Translation: AAH00126.1.

IPI

IPI00010331.
IPI00016807.

RefSeq

NP_001180196.1. NM_001193267.2.
NP_001229756.1. NM_001242827.1.
NP_036373.1. NM_012241.4.
NP_112534.1. NM_031244.3.

UniGene

Hs.567431.
Hs.594133.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B4Y	X-ray	1.90	A/B/C/D	34-302	[»]
2NYR	X-ray	2.06	A/B	34-302	[»]
3RIG	X-ray	2.00	A/B	34-302	[»]
3RIY	X-ray	1.55	A/B	34-302	[»]
4F4U	X-ray	2.00	A/B	34-302	[»]
4F56	X-ray	1.70	A/B	34-302	[»]
4G1C	X-ray	1.94	A/B	36-302	[»]
4HDA	X-ray	2.60	A/B	34-302	[»]

ProteinModelPortal

Q9NXA8.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000368552.

PTM databases

PhosphoSite

Q9NXA8.

Polymorphism databases

DMDM

38258652.

Proteomic databases

PaxDb

Q9NXA8.

PRIDE

Q9NXA8.

Protocols and materials databases

DNASU

23408.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359782; ENSP00000352830; ENSG00000124523.
ENST00000379250; ENSP00000368552; ENSG00000124523.
ENST00000379262; ENSP00000368564; ENSG00000124523.
ENST00000397350; ENSP00000380509; ENSG00000124523.

GeneID

23408.

KEGG

hsa:23408.

UCSC

uc003naw.3. human.
uc003nax.3. human.
uc011dit.2. human.

Organism-specific databases

CTD

23408.

GeneCards

GC06P013574.

HGNC

HGNC:14933. SIRT5.

HPA

HPA021798.
HPA022002.
HPA022992.

MIM

604483. gene.

neXtProt

NX_Q9NXA8.

PharmGKB

PA37938.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0846.

HOGENOM

HOG000085950.

HOVERGEN

HBG056009.

InParanoid

Q9NXA8.

KO

K11415.

OMA

VLHMHGE.

PhylomeDB

Q9NXA8.

Enzyme and pathway databases

Pathway_Interaction_DB

hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Gene expression databases

Bgee

Q9NXA8.

CleanEx

HS_SIRT5.

Genevestigator

Q9NXA8.

GermOnline

ENSG00000124523. Homo sapiens.

Family and domain databases

Gene3D

3.30.1600.10. 2 hits.

HAMAP

MF_01121. Sirtuin_ClassIII.

InterPro

IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR027546. Sirtuin_ClassIII.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]

PANTHER

PTHR11085. PTHR11085. 1 hit.

Pfam

PF02146. SIR2. 1 hit.
[Graphical view]

PROSITE

PS50305. SIRTUIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB04786. Suramin.

EvolutionaryTrace

Q9NXA8.

GenomeRNAi

23408.

NextBio

45587.

SOURCE

Search...

Entry information

Entry name

SIR5_HUMAN

Accession

Primary (citable) accession number: Q9NXA8
Secondary accession number(s): B4DFM4 , B4DYJ5, F5H5Z9, Q5T294, Q5T295, Q9Y6E6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	October 31, 2003
Last modified:	May 29, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.