Tag | Content |
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CPLM ID | CPLM-022322 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NAD-dependent protein deacylase sirtuin-5, mitochondrial |
Protein Synonyms/Alias | Regulatory protein SIR2 homolog 5; SIR2-like protein 5 |
Gene Name | SIRT5 |
Gene Synonyms/Alias | SIR2L5 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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203 | DASIPVEKLPRCEEA | ubiquitination | [1] |
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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 lysine demalonylase and desuccinylase that specifically removes malonyl and succinyl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Has weak NAD- dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro. |
Sequence Annotation | DOMAIN 41 309 Deacetylase sirtuin-type. NP_BIND 58 77 NAD. NP_BIND 140 143 NAD (By similarity). NP_BIND 249 251 NAD. NP_BIND 275 277 NAD. ACT_SITE 158 158 Proton acceptor. METAL 166 166 Zinc. METAL 169 169 Zinc. METAL 207 207 Zinc. METAL 212 212 Zinc. BINDING 102 102 Substrate. BINDING 105 105 Substrate. BINDING 293 293 NAD; via amide nitrogen. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Mitochondrion; NAD; Polymorphism; Reference proteome; Transit peptide; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 310 AA |
Protein Sequence | MRPLQIVPSR LISQLYCGLK PPASTRNQIC LKMARPSSSM ADFRKFFAKA KHIVIISGAG 60 VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE FYHYRREVMG SKEPNAGHRA 120 IAECETRLGK QGRRVVVITQ NIDELHRKAG TKNLLEIHGS LFKTRCTSCG VVAENYKSPI 180 CPALSGKGAP EPGTQDASIP VEKLPRCEEA GCGGLLRPHV VWFGENLDPA ILEEVDRELA 240 HCDLCLVVGT SSVVYPAAMF APQVAARGVP VAEFNTETTP ATNRFRFHFQ GPCGTTLPEA 300 LACHENETVS 310 |
Gene Ontology | GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB. GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. GO:0003950; F:NAD+ ADP-ribosyltransferase activity; TAS:ProtInc. GO:0070403; F:NAD+ binding; IDA:UniProtKB. GO:0036054; F:protein-malonyllysine demalonylase activity; IDA:UniProtKB. GO:0036055; F:protein-succinyllysine desuccinylase activity; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IDA:UniProtKB. GO:0006342; P:chromatin silencing; TAS:ProtInc. GO:0006471; P:protein ADP-ribosylation; TAS:ProtInc. GO:0006476; P:protein deacetylation; IDA:UniProtKB. |
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