CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018178
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NAD-dependent protein deacetylase sirtuin-2 
Protein Synonyms/Alias
 Regulatory protein SIR2 homolog 2; SIR2-like protein 2; mSIR2L2 
Gene Name
 Sirt2 
Gene Synonyms/Alias
 Sir2l2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
55TLGLGSQKERLLDELubiquitination[1]
126FEISYFKKHPEPFFAubiquitination[1]
144ELYPGQFKPTICHYFubiquitination[1]
202CVNTSCRKEYTMGWMubiquitination[1]
210EYTMGWMKEKIFSEAubiquitination[1]
287TPRLLINKEKTGQTDubiquitination[1]
339ADLLGWKKELEDLVRubiquitination[1]
371STTISPGKSPPPAKEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 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). 
Sequence Annotation
 DOMAIN 65 340 Deacetylase sirtuin-type.
 NP_BIND 84 104 NAD (By similarity).
 NP_BIND 167 170 NAD (By similarity).
 NP_BIND 261 263 NAD (By similarity).
 NP_BIND 286 288 NAD (By similarity).
 ACT_SITE 187 187 Proton acceptor (By similarity).
 METAL 195 195 Zinc (By similarity).
 METAL 200 200 Zinc (By similarity).
 METAL 221 221 Zinc (By similarity).
 METAL 224 224 Zinc (By similarity).
 BINDING 324 324 NAD; via amide nitrogen (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 23 23 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Hydrolase; Metal-binding; Microtubule; Mitosis; NAD; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 389 AA 
Protein Sequence
MAEPDPSDPL ETQAGKVQEA QDSDSDTEGG ATGGEAEMDF LRNLFTQTLG LGSQKERLLD 60
ELTLEGVTRY MQSERCRKVI CLVGAGISTS AGIPDFRSPS TGLYANLEKY HLPYPEAIFE 120
ISYFKKHPEP FFALAKELYP GQFKPTICHY FIRLLKEKGL LLRCYTQNID TLERVAGLEP 180
QDLVEAHGTF YTSHCVNTSC RKEYTMGWMK EKIFSEATPR CEQCQSVVKP DIVFFGENLP 240
SRFFSCMQSD FSKVDLLIIM GTSLQVQPFA SLISKAPLAT PRLLINKEKT GQTDPFLGMM 300
MGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LADLLGWKKE LEDLVRREHA NIDAQSGSQA 360
PNPSTTISPG KSPPPAKEAA RTKEKEEQQ 389 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005874; C:microtubule; ISS:UniProtKB.
 GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
 GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
 GO:0070403; F:NAD+ binding; IEA:InterPro.
 GO:0017136; F:NAD-dependent histone deacetylase activity; ISS:UniProtKB.
 GO:0008134; F:transcription factor binding; ISS:UniProtKB.
 GO:0042903; F:tubulin deacetylase activity; ISS:UniProtKB.
 GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0045843; P:negative regulation of striated muscle tissue development; ISS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. 
Interpro
 IPR017328; NAD-dep_deAcase_SIR2_class_I.
 IPR003000; Sirtuin.
 IPR026590; Ssirtuin_cat_dom. 
Pfam
 PF02146; SIR2 
SMART
  
PROSITE
 PS50305; SIRTUIN 
PRINTS