Tag | Content |
---|
CPLM ID | CPLM-013348 |
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 | QtsA-13614 |
Created Date | July 27, 2013 |
Organism | Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) |
NCBI Taxa ID | 9541 |
Lysine Modification | Position | Peptide | Type | References |
---|
55 | TLSLGSQKERLLDEL | ubiquitination | [1] | 126 | FEISYFKKHPEPFFA | ubiquitination | [1] | 158 | FMRLLKDKGLLLRCY | ubiquitination | [1] | 212 | PLSWMKEKIFSEVTP | ubiquitination | [1] |
|
Reference | [1] 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 (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 (By similarity). |
Keyword | Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Hydrolase; Metal-binding; Microtubule; Mitosis; NAD; Phosphoprotein; 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 LGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LAELLGWKKE LEDLVRREHA SIDAQSGAEA 360 PNPSTSASPR KSPPPAQDEA RTTEREKPQ 389 |
Gene Ontology | GO:0005737; C:cytoplasm; ISS:UniProtKB. GO:0005874; C:microtubule; IEA:UniProtKB-KW. GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro. GO:0070403; F:NAD+ binding; IEA:InterPro. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0051301; P:cell division; IEA:UniProtKB-KW. GO:0007067; P:mitosis; IEA:UniProtKB-KW. GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. GO:0006476; P:protein deacetylation; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |