Q3UJK6 · Q3UJK6_MOUSE
- ProteinNAD-dependent protein deacetylase
- GeneSirt2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids351 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
NAD-dependent protein deacetylase.
Catalytic activity
- H2O + N6-acetyl-L-lysyl-[protein] + NAD+ = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
- H2O + N6-hexadecanoyl-L-lysyl-[protein] + NAD+ = 2''-O-hexadecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
- H2O + N6-tetradecanoyl-L-lysyl-[protein] + NAD+ = 2''-O-tetradecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamideThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48-52 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: AGIST | ||||||
Binding site | 58-60 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DFR | ||||||
Binding site | 130-133 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNID | ||||||
Active site | 150 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 158 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 163 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 184 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 187 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 224-225 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TS | ||||||
Binding site | 248-250 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NKE | ||||||
Binding site | 286 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | centriole | |
Cellular Component | microtubule | |
Cellular Component | midbody | |
Cellular Component | myelin sheath | |
Cellular Component | spindle | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent histone deacetylase activity | |
Molecular Function | NAD-dependent protein demyristoylase activity | |
Molecular Function | NAD-dependent protein depalmitoylase activity | |
Molecular Function | zinc ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-dependent protein deacetylase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3UJK6
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-300 | Deacetylase sirtuin-type | ||||
Sequence: RLLDELTLEGVTRYMQSERCRKVICLVGAGISTSAGIPDFRSPSTGLYANLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFIRLLKEKGLLLRCYTQNIDTLERVAGLEPQDLVEAHGTFYTSHCVNTSCRKEYTMGWMKEKIFSEATPRCEQCQSVVKPDIVFFGENLPSRFSCMQSDFSKVDLLIIMGTSLQVQPFASLISKAPLATPRLLINKEKTGQTDPFLGMMMGLGGGMDFDSKKAYRDVAWLGDCDQGCLALADLLGWK | ||||||
Region | 312-351 | Disordered | ||||
Sequence: ANIDAQSGSQAPNPSTTISPGKSPPPAKEAARTKEKEEQQ | ||||||
Compositional bias | 314-328 | Polar residues | ||||
Sequence: IDAQSGSQAPNPSTT |
Sequence similarities
Belongs to the sirtuin family. Class I subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length351
- Mass (Da)39,406
- Last updated2005-10-11 v1
- ChecksumA610628E55831D1D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 314-328 | Polar residues | ||||
Sequence: IDAQSGSQAPNPSTT |