Descriptions

Sirtuin 2 (SIRT2) is a NAD+ dependent deacetylase that has been associated with neurodegeneration and cancer. The C-terminal region (CT) of SIRT2 functions as an autoinhibitory region that regulates the deacetylation activity of SIRT2. Phosphorylation at S331 of SIRT2 isoform 2 causes large conformational changes in the CT that enhance the autoinhibitory activity of the CT region. This serine residue is located within the naturally disordered C-terminal region (CT, residues 320-352 in isoform 2).

Autoinhibitory domains (AIDs)

Target domain

0-287 (Catalytic core domain)

Relief mechanism

Others

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q9I7I7

Entry ID Method Resolution Chain Position Source
AF-Q9I7I7-F1 Predicted AlphaFoldDB

No variants for Q9I7I7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9I7I7

No associated diseases with Q9I7I7

1 regional properties for Q9I7I7

Type Name Position InterPro Accession
domain Sirtuin family, catalytic core domain 28 - 306 IPR026590

Functions

Description
EC Number 2.3.1.286 Transferring groups other than amino-acyl groups
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

6 GO annotations of molecular function

Name Definition
histone deacetylase activity Catalysis of the reaction
metal ion binding Binding to a metal ion.
NAD+ binding Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.
NAD-dependent histone deacetylase activity Catalysis of the reaction
protein lysine deacetylase activity Catalysis of the reaction
transferase activity Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

3 GO annotations of biological process

Name Definition
determination of adult lifespan The pathways that regulate the duration of the adult phase of the life-cycle of an animal.
protein deacetylation The removal of an acetyl group from a protein amino acid. An acetyl group is CH3CO-, derived from acetic acid.
response to starvation Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nourishment.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9VK34 Sirt1 NAD-dependent histone deacetylase sirtuin-1 Drosophila melanogaster (Fruit fly) PR
Q8IXJ6 SIRT2 NAD-dependent protein deacetylase sirtuin-2 Homo sapiens (Human) EV
Q9NTG7 SIRT3 NAD-dependent protein deacetylase sirtuin-3, mitochondrial Homo sapiens (Human) SS
Q8VDQ8 Sirt2 NAD-dependent protein deacetylase sirtuin-2 Mus musculus (Mouse) SS
Q8R104 Sirt3 NAD-dependent protein deacetylase sirtuin-3 Mus musculus (Mouse) SS
Q5RJQ4 Sirt2 NAD-dependent protein deacetylase sirtuin-2 Rattus norvegicus (Rat) PR
Q7ZVK3 sirt2 NAD-dependent protein deacetylase sirtuin-2 Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MDKVRRFFAN TLHLGGSSDA KEEVKVEKVI PDLSFDGFAE HWRVHGFRKI VTMVGAGIST
70 80 90 100 110 120
SAGIPDFRSP GSGLYSNLKK YELPHPTAIF DLDYFEKNPA PFFALAKELY PGSFIPTPAH
130 140 150 160 170 180
YFIRLLNDKG LLQRHYTQNI DTLDRLTGLP EDKIIEAHGS FHTNHCIKCR KEYDMDWMKA
190 200 210 220 230 240
EIFADRLPKC QKCQGVVKPD IVFFGENLPK RFYSSPEEDF QDCDLLIIMG TSLEVQPFAS
250 260 270 280 290 300
LVWRPGPRCI RLLINRDAVG QASCVLFMDP NTRSLLFDKP NNTRDVAFLG DCDAGVMALA
310 320 330 340 350
KALGWDQELQ QLITSERKKL SGSQNSEELQ QGKEKPQSDP DKMTSGDRDK KDASL