sirtuin 2

Target id: 2708

Nomenclature: sirtuin 2

Family: 3.5.1.- Histone deacetylases (HDACs)

Annotation status:  image of a grey circle Awaiting annotation/under development. Please contact us if you can help with annotation.  » Email us

   GtoImmuPdb view: OFF :     Currently no data for sirtuin 2 in GtoImmuPdb

Gene and Protein Information
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 389 19q13 SIRT2 sirtuin 2
Mouse - 389 7 B1-2 Sirt2 sirtuin 2
Rat - 350 1q21 Sirt2 sirtuin 2
Database Links
Ensembl Gene
Entrez Gene
GenitoUrinary Development Molecular Anatomy Project
Human Protein Atlas
KEGG Enzyme
RefSeq Nucleotide
RefSeq Protein
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  Human SIRT2 histone deacetylase
PDB Id:  1J8F
Resolution:  1.7Å
Species:  Human
References:  4
Enzyme Reaction
EC Number: 3.5.1.-

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Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
compound 86 [PMID: 26982234] Hs Inhibition 7.1 pKi 1
pKi 7.1 (Ki 7.3x10-8 M) [1]
compound 17 [PMID: 23570514] Hs Inhibition 8.7 pIC50 3
pIC50 8.7 (IC50 1.8x10-9 M) [3]
AGK2 Hs Inhibition 4.5 – 5.8 pIC50 2,6
pIC50 4.5 – 5.8 (IC50 3.5x10-5 – 1.56x10-6 M) [2,6]
General Comments
SIRT2 is NAD+-dependent protein deacetylase, which deacetylates internal lysines on histone, α-tubulin and some transcription factors. SIRT2 is the most abundant sirtuin in the brain [7]. Selective pharmacological blockade of SIRT2 is being investigated for potential clinical benefit in neurodegenerative diseases (and cancers [5]), with initial research focussing on the synucleinopathy, Parkinson's disease [6].


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1. Ai T, Wilson DJ, More SS, Xie J, Chen L. (2016) 5-((3-Amidobenzyl)oxy)nicotinamides as Sirtuin 2 Inhibitors. J. Med. Chem.59 (7): 2928-41. [PMID:26982234]

2. Cui H, Kamal Z, Ai T, Xu Y, More SS, Wilson DJ, Chen L. (2014) Discovery of potent and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach. J. Med. Chem.57 (20): 8340-57. [PMID:25275824]

3. Disch JS, Evindar G, Chiu CH, Blum CA, Dai H, Jin L, Schuman E, Lind KE, Belyanskaya SL, Deng J et al.. (2013) Discovery of thieno[3,2-d]pyrimidine-6-carboxamides as potent inhibitors of SIRT1, SIRT2, and SIRT3. J. Med. Chem.56 (9): 3666-79. [PMID:23570514]

4. Finnin MS, Donigian JR, Pavletich NP. (2001) Structure of the histone deacetylase SIRT2. Nat. Struct. Biol.8 (7): 621-5. [PMID:11427894]

5. Hu J, Jing H, Lin H. (2014) Sirtuin inhibitors as anticancer agents. Future Med. Chem.6: 945-966.

6. Outeiro TF, Kontopoulos E, Altmann SM, Kufareva I, Strathearn KE, Amore AM, Volk CB, Maxwell MM, Rochet JC, McLean PJ et al.. (2007) Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science317 (5837): 516-9. [PMID:17588900]

7. Pandithage R, Lilischkis R, Harting K, Wolf A, Jedamzik B, Lüscher-Firzlaff J, Vervoorts J, Lasonder E, Kremmer E, Knöll B et al.. (2008) The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility. J. Cell Biol.180 (5): 915-29. [PMID:18332217]

How to cite this page

3.5.1.- Histone deacetylases (HDACs): sirtuin 2. Last modified on 14/07/2016. Accessed on 23/02/2018. IUPHAR/BPS Guide to PHARMACOLOGY,