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Protein Page:
SIRT2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
SIRT2 NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA. Interacts with HDAC6, suggesting that these proteins belong to a large complex that deacetylate the cytoskeleton. Widely expressed. Highly expressed in heart, brain and skeletal muscle, while it is weakly expressed in placenta and lung. Down-regulated in many gliomas suggesting that it may act as a tumor suppressor gene in human gliomas possibly through the regulation of microtubule network. Inhibited by Sirtinol, A3 and M15 small molecules. Inhibited by nicotinamide. Belongs to the sirtuin family. Class I subfamily. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.5.1.-; Deacetylase
Cellular Component: chromatin silencing complex; microtubule; cytoplasm
Molecular Function: histone acetyltransferase binding; ubiquitin binding; protein binding; tubulin deacetylase activity; zinc ion binding; NAD-dependent histone deacetylase activity; histone deacetylase binding; protein deacetylase activity; transcription factor binding; NAD+ ADP-ribosyltransferase activity
Biological Process: chromatin silencing at rDNA; mitosis; proteasomal ubiquitin-dependent protein catabolic process; regulation of phosphorylation; chromatin silencing; regulation of exit from mitosis; histone deacetylation; response to redox state; gene silencing; negative regulation of striated muscle development; chromatin silencing at telomere; protein amino acid ADP-ribosylation; substantia nigra development; protein amino acid deacetylation; negative regulation of transcription, DNA-dependent
Reference #:  Q8IXJ6 (UniProtKB)
Alt. Names/Synonyms: NAD-dependent deacetylase sirtuin-2; silencing information regulator 2-like; silent information regulator 2; SIR2; SIR2-like protein 2; sir2-related protein type 2; SIR2L; SIR2L2; SIRT2; sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae); sirtuin type 2
Gene Symbols: SIRT2
Molecular weight: 43,182 Da
Basal Isoelectric point: 5.22  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Mitochondrial Control of Apoptosis  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SIRT2

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
cell adhesion, altered: S368‑p
cell growth, altered: S368‑p
cell motility, altered: S368‑p
enzymatic activity, induced: S372‑p
enzymatic activity, inhibited: S368‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 16 S23-p KVQEAQDsDsDsEGG
0 13 S25-p QEAQDsDsDsEGGAA
0 7 S27-p AQDsDsDsEGGAAGG
0 1 S53 SQTLSLGSQkERLLD
0 5 K55-u TLSLGSQkERLLDEL
1 0 T101-p PDFRSPStGLyDNLE
0 3 Y104-p RSPStGLyDNLEKYH
0 1 K126 FEISYFKKHPEPFFA
0 1 K144 ELYPGQFKPTICHYF
0 1 H202 CVSASCRHEYPLSWM
0 1 K210 EYPLSWMKEKIFSEV
0 2 S274-p QPFASLIsKAPLSTP
0 1 K287 TPRLLINKEKAGQSD
0 6 K338-a LAELLGWkKELEDLV
0 1 K339 AELLGWkKELEDLVR
0 1 S356-p HASIDAQsGAGVPNP
0 3 S364-p GAGVPNPsTsAsPKK
0 2 S366-p GVPNPsTsAsPKKsP
4 11 S368-p PNPsTsAsPKKsPPP
0 1 K371 sTsAsPKKsPPPAKD
1 9 S372-p TsAsPKKsPPPAKDE
  mouse

► Hide Isoforms
 
S23-p KVQEAQDsDsDtEGG
S25-p QEAQDsDsDtEGGAT
T27-p AQDsDsDtEGGATGG
S53-p TQTLGLGsQkERLLD
K55-u TLGLGsQkERLLDEL
T101 PDFRSPSTGLYANLE
Y104 RSPSTGLYANLEKYH
K126-u FEISYFKkHPEPFFA
K144-u ELYPGQFkPTICHYF
K202-u CVNTSCRkEYTMGWM
K210-u EYTMGWMkEKIFSEA
S274 QPFASLISKAPLATP
K287-u TPRLLINkEKTGQTD
K338-a LADLLGWkkELEDLV
K339-u ADLLGWkkELEDLVR
S356-p HANIDAQsGSQAPNP
S364-p GSQAPNPsTTIsPGk
T366 QAPNPsTTIsPGksP
S368-p PNPsTTIsPGksPPP
K371-u sTTIsPGksPPPAKE
S372-p TTIsPGksPPPAKEA
  SIRT2 iso2  
- gap
- gap
- gap
S16 TQTLGLGSQKERLLD
K18 TLGLGSQKERLLDEL
T64 PDFRSPSTGLYANLE
Y67 RSPSTGLYANLEKYH
K89 FEISYFKKHPEPFFA
K107 ELYPGQFKPTICHYF
K165 CVNTSCRKEYTMGWM
K173 EYTMGWMKEKIFSEA
S237 QPFASLISKAPLATP
K250 TPRLLINKEKTGQTD
K301 LADLLGWKKELEDLV
K302 ADLLGWKKELEDLVR
S319 HANIDAQSGSQAPNP
S327 GSQAPNPSTTIsPGK
T329 QAPNPSTTIsPGKSP
S331-p PNPSTTIsPGKSPPP
K334 STTIsPGKSPPPAKE
S335 TTIsPGKSPPPAKEA
  rat

 
- gap
- gap
- gap
S16 TQTLGLGSQkERLLD
K18-u TLGLGSQkERLLDEL
T64 PDFRSPSTGLYANLE
Y67 RSPSTGLYANLEKYH
K89 FEISYFKKHPEPFFA
K107 ELYPGQFKPTICHYF
K165 CVNTSCGKEYTMSWM
K173 EYTMSWMKEKIFSEA
S237 QPFASLISKAPLATP
K250 TPRLLINKEKTGQTD
K301 LADLLGWKELEDLVR
- gap
S318 HANIDAQSGSQASNP
S326 GSQASNPSATVSPRK
T328 QASNPSATVSPRKSP
S330 SNPSATVSPRKSPPP
K333 SATVSPRKSPPPAKE
S334 ATVSPRKSPPPAKEA
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