Search Results
Overview
| Uniprot ID | O75356 |
|---|---|
| Protein Name | Nucleoside diphosphate phosphatase ENTPD5 |
| Gene Name | ENTPD5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 128 | KKTPVVLKATAGLRL |
| 142 | LLPEHKAKALLFEVK |
| 248 | SYLGFGLKAARLATL |
| 314 | VLRVVRGKLHQPEEV |
| 388 | SYITALLKDGFGFAD |
Function
Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (PubMed:10400613, PubMed:15698960). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Molecular Function | GO:0043262 | ADP phosphatase activity |
| Molecular Function | GO:0036384 | CDP phosphatase activity |
| Molecular Function | GO:0004382 | GDP phosphatase activity |
| Molecular Function | GO:1990003 | IDP phosphatase activity |
| Molecular Function | GO:0045134 | UDP phosphatase activity |
| Biological Process | GO:0051084 | 'de novo' post-translational protein folding |
| Biological Process | GO:0006487 | protein N-linked glycosylation |
| Biological Process | GO:0006256 | UDP catabolic process |
| Biological Process | GO:0006011 | UDP-alpha-D-glucose 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.