Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  NAD-dependent protein deacetylase sirtuin-2  

UniProtKB / Swiss-Prot ID :  SIR2_MOUSE

Gene Name (Synonyms) : 
Sirt2, Sir2l2  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm, cytoskeleton. Note=Colocalizes with microtubules. 

Protein Function :  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 (By similarity). 

Protein Sequence MAEPDPSDPLETQAGKVQEAQDSDSDTEGGATGGEAEMDFLRNLFTQTLGLGSQKERLLDELTLEGVTRY...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
23PhosphoserineEAQDSDSDT
27.25Phosphositeplus
Link-
23PhosphoserineEAQDSDSDT
27.25SysPTM
Link-
23Phosphoserine.EAQDSDSDT
27.25UniProtKB
Link-
25PhosphoserineQDSDSDTEG
50.84Phosphositeplus
Link-
25PhosphoserineQDSDSDTEG
50.84SysPTM
Link-
27PhosphothreonineSDSDTEGGA
40.25Phosphositeplus
Link-
27PhosphothreonineSDSDTEGGA
40.25SysPTM
Link-
38Methionine sulfoneGEAEMDFLR
5.94SysPTM
Link-
53PhosphoserineLGLGSQKER
43.02Phosphositeplus
Link-
368PhosphoserineSTTISPGKS
26.05Phosphositeplus
Link-
372PhosphoserineSPGKSPPPA
48.86Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures