Search Results
Overview
| Uniprot ID | Q9UKK9 |
|---|---|
| Protein Name | ADP-sugar pyrophosphatase |
| Gene Name | NUDT5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 218 | PFEVPFLKF****** |
| 33 | GKWVKLEKTTYMDPT |
| 42 | TYMDPTGKTRTWESV |
| 50 | TRTWESVKRTTRKEQ |
| 55 | SVKRTTRKEQTADGV |
Function
Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate (PubMed:27257257). In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10567213, PubMed:10722730, PubMed:17052728, PubMed:12717453, PubMed:19699693, PubMed:21389046, PubMed:38635563). Can also hydrolyze other nucleotide sugars with low activity (PubMed:12717453, PubMed:19699693, PubMed:21389046). In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place when dephosphorylated at Thr-45 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257). In vitro, it has decapping activity on 11-mer RNA capped with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) by hydrolyzing the pyrophosphate bridge of the sugar cap (PubMed:38716860). Does not play a role in U8 snoRNA decapping (By similarity). Binds U8 snoRNA (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0044715 | 8-oxo-dGDP phosphatase activity |
| Molecular Function | GO:0047631 | ADP-ribose diphosphatase activity |
| Molecular Function | GO:0019144 | ADP-sugar diphosphatase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0016779 | nucleotidyltransferase activity |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0030515 | snoRNA binding |
| Biological Process | GO:1990966 | ATP generation from poly-ADP-D-ribose |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0019303 | D-ribose catabolic process |
| Biological Process | GO:0055086 | nucleobase-containing small molecule metabolic process |
| Biological Process | GO:0006753 | nucleoside phosphate metabolic process |
| Biological Process | GO:0009117 | nucleotide metabolic process |
| Biological Process | GO:0009191 | ribonucleoside diphosphate catabolic process |
| Biological Process | GO:0019693 | ribose phosphate metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.