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Sirt5 - sirtuin 5 (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-17
Description
Predicted to enable NAD+ binding activity; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; and zinc ion binding activity. Involved in negative regulation of cardiac muscle cell apoptotic process and response to nutrient levels. Predicted to be located in cytosol; mitochondrial inner membrane; and mitochondrial intermembrane space. Predicted to be active in mitochondrial matrix. Orthologous to human SIRT5 (sirtuin 5).

1 Names and Identifiers

1.1 Synonyms

  • NAD-dependent protein deacylase sirtuin-5, mitochondrial
  • NAD-dependent deacetylase sirtuin-5
  • NAD-dependent lysine demalonylase and desuccinylase sirtuin-5, mitochondrial
  • SIR2-like protein 5
  • regulatory protein SIR2 homolog 5

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Bgee Gene ID

1.2.4 Enzyme Commission (EC) Number

1.2.5 RGD ID

1.2.6 Wikidata

3 Proteins

3.1 Protein Function

NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. 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 such as UOX.

3.2 Protein 3D Structures

3.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

3.3 Protein Targets

4 Interactions and Pathways

4.1 Interactions

4.2 Pathways

5 Biochemical Reactions

6 Expression

7 Literature

7.1 Gene-Chemical Co-Occurrences in Literature

7.2 Gene-Gene Co-Occurrences in Literature

7.3 Gene-Disease Co-Occurrences in Literature

8 Patents

8.1 Gene-Chemical Co-Occurrences in Patents

8.2 Gene-Gene Co-Occurrences in Patents

8.3 Gene-Disease Co-Occurrences in Patents

9 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  4. NCBI Gene Expression Omnibus (GEO)
  5. Rat Genome Database (RGD)
    LICENSE
    Creative Commons Attribution 4.0 International license (CC BY 4.0)
    https://creativecommons.org/licenses/by/4.0/
  6. STRING: functional protein association networks
  7. Swiss Institute of Bioinformatics Bgee
    LICENSE
    Creative Commons Zero license (CC0)
    https://www.bgee.org/about/
  8. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  9. Wikidata
  10. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  11. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
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