Search Results
Overview
| Uniprot ID | Q15843 |
|---|---|
| Protein Name | Ubiquitin-like protein NEDD8 |
| Gene Name | NEDD8 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 22 | IDIEPTDKVERIKER |
| 48 | QRLIYSGKQMNDEKT |
| 54 | GKQMNDEKTAADYKI |
| 6 | **MLIKVKTLTGKEI |
Function
Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53 (PubMed:10318914, PubMed:10597293, PubMed:11953428, PubMed:14690597, PubMed:15242646, PubMed:9694792, PubMed:38605244, PubMed:38316879). Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins (PubMed:10318914, PubMed:10597293, PubMed:11953428, PubMed:20688984, PubMed:9694792, PubMed:38605244, PubMed:38316879). Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity (PubMed:15242646). Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M (PubMed:14690597). Neddylates EGFR resulting in protein stabilization and translocation to the cell membrane (PubMed:28891468)
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:0098978 | glutamatergic synapse |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0098794 | postsynapse |
| Molecular Function | GO:0031386 | protein tag activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0009653 | anatomical structure morphogenesis |
| Biological Process | GO:0072757 | cellular response to camptothecin |
| Biological Process | GO:0019941 | modification-dependent protein catabolic process |
| Biological Process | GO:0036211 | protein modification process |
| Biological Process | GO:0045116 | protein neddylation |
| Biological Process | GO:0006508 | proteolysis |
| Biological Process | GO:0150052 | regulation of postsynapse assembly |
| Biological Process | GO:0030162 | regulation of proteolysis |
| Biological Process | GO:0006511 | ubiquitin-dependent protein catabolic process |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[4] 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.