CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017060
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 
Gene Name
 SIRT2 
Gene Synonyms/Alias
 SIR2L; SIR2L2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55TLSLGSQKERLLDELubiquitination[1, 2]
158FMRLLKDKGLLLRCYubiquitination[1]
287TPRLLINKEKAGQSDubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
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. 
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.
 METAL 195 195 Zinc.
 METAL 200 200 Zinc.
 METAL 221 221 Zinc.
 METAL 224 224 Zinc.
 BINDING 324 324 NAD; via amide nitrogen (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 23 23 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Metal-binding; Microtubule; Mitosis; NAD; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 389 AA 
Protein Sequence
MAEPDPSHPL ETQAGKVQEA QDSDSDSEGG AAGGEADMDF LRNLFSQTLS LGSQKERLLD 60
ELTLEGVARY MQSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYDNLEKY HLPYPEAIFE 120
ISYFKKHPEP FFALAKELYP GQFKPTICHY FMRLLKDKGL LLRCYTQNID TLERIAGLEQ 180
EDLVEAHGTF YTSHCVSASC RHEYPLSWMK EKIFSEVTPK CEDCQSLVKP DIVFFGESLP 240
ARFFSCMQSD FLKVDLLLVM GTSLQVQPFA SLISKAPLST PRLLINKEKA GQSDPFLGMI 300
MGLGGGMDFD SKKAYRDVAW LGECDQGCLA LAELLGWKKE LEDLVRREHA SIDAQSGAGV 360
PNPSTSASPK KSPPPAKDEA RTTEREKPQ 389 
Gene Ontology
 GO:0005677; C:chromatin silencing complex; NAS:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0070403; F:NAD+ binding; IDA:UniProtKB.
 GO:0017136; F:NAD-dependent histone deacetylase activity; IDA:UniProtKB.
 GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
 GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000183; P:chromatin silencing at rDNA; NAS:UniProtKB.
 GO:0006348; P:chromatin silencing at telomere; NAS:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0045843; P:negative regulation of striated muscle tissue development; IDA:UniProtKB.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
 GO:0006471; P:protein ADP-ribosylation; NAS:UniProtKB.
 GO:0007096; P:regulation of exit from mitosis; NAS:UniProtKB.
 GO:0042325; P:regulation of phosphorylation; NAS:UniProtKB.
 GO:0051775; P:response to redox state; NAS:UniProtKB. 
Interpro
 IPR017328; NAD-dep_deAcase_SIR2_class_I.
 IPR003000; Sirtuin.
 IPR026590; Ssirtuin_cat_dom. 
Pfam
 PF02146; SIR2 
SMART
  
PROSITE
 PS50305; SIRTUIN 
PRINTS