Search Results
Overview
| Uniprot ID | P52758 |
|---|---|
| Protein Name | 2-iminobutanoate/2-iminopropanoate deaminase |
| Gene Name | RIDA |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | EIYKQYFKSNFPARA |
| 117 | YQVAALPKGSRIEIE |
| 13 | RRVISTAKAPGAIGP |
| 60 | EEAKQALKNMGEILK |
| 67 | KNMGEILKAAGCDFT |
Function
Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005777 | peroxisome |
| Molecular Function | GO:0120242 | 2-iminobutanoate deaminase activity |
| Molecular Function | GO:0120243 | 2-iminopropanoate deaminase activity |
| Molecular Function | GO:0019239 | deaminase activity |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0016892 | RNA endonuclease activity producing 3'-phosphomonoesters, hydrolytic mechanism |
| Biological Process | GO:0019518 | L-threonine catabolic process to glycine |
| Biological Process | GO:0006629 | lipid metabolic process |
| Biological Process | GO:0006402 | mRNA catabolic process |
| Biological Process | GO:0061157 | mRNA destabilization |
| Biological Process | GO:0017148 | negative regulation of translation |
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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.