sirtuin 2 | 3.5.1.- Histone deacetylases (HDACs) | IUPHAR/BPS Guide to PHARMACOLOGY

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sirtuin 2

Target not currently curated in GtoImmuPdb

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

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
ChEMBL Target
Ensembl Gene
Entrez Gene
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.-

Download all structure-activity data for this target as a CSV file

Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Value Parameter 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]
Immuno Process Associations
Immuno Process:  Inflammation
GO Annotations:  Associated to 1 GO processes, IEA only
click arrow to show/hide IEA associations
GO:0045087 innate immune response IEA
Immuno Process:  Antigen presentation
GO Annotations:  Associated to 1 GO processes
GO:0099149 regulation of postsynaptic neurotransmitter receptor internalization IDA
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 (8): 945-66. [PMID:24962284]

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. Science, 317 (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 10/08/2020. IUPHAR/BPS Guide to PHARMACOLOGY,