Search Results
Overview
| Uniprot ID | O60701 |
|---|---|
| Protein Name | UDP-glucose 6-dehydrogenase |
| Gene Name | UGDH |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 107 | KGRAADLKYIEACAR |
| 124 | VQNSNGYKIVTEKST |
| 129 | GYKIVTEKSTVPVRA |
| 207 | EHWVPREKILTTNTW |
| 279 | FGGSCFQKDVLNLVY |
| 329 | LFNTVTDKKIAILGF |
| 370 | HLHIYDPKVPREQIV |
| 431 | DYERIHKKMLKPAFI |
| 481 | APSGEIPKFSLQDPP |
| 490 | SLQDPPNKKPKV*** |
| 491 | LQDPPNKKPKV**** |
| 493 | DPPNKKPKV****** |
| 58 | PIYEPGLKEVVESCR |
| 6 | **MFEIKKICCIGAG |
Function
Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716)
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:0042802 | identical protein binding |
| Molecular Function | GO:0051287 | NAD binding |
| Molecular Function | GO:0003979 | UDP-glucose 6-dehydrogenase activity |
| Biological Process | GO:0050650 | chondroitin sulfate proteoglycan biosynthetic process |
| Biological Process | GO:0001702 | gastrulation with mouth forming second |
| Biological Process | GO:0006024 | glycosaminoglycan biosynthetic process |
| Biological Process | GO:0015012 | heparan sulfate proteoglycan biosynthetic process |
| Biological Process | GO:0048666 | neuron development |
| Biological Process | GO:0034214 | protein hexamerization |
| Biological Process | GO:0006065 | UDP-glucuronate biosynthetic 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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[5] 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.