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). {ECO:0000269|PubMed:10318914, ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:11953428, ECO:0000269|PubMed:14690597, ECO:0000269|PubMed:15242646, ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:28891468, ECO:0000269|PubMed:38316879, ECO:0000269|PubMed:38605244, ECO:0000269|PubMed:9694792}. This is the function of NEDD8 (NEDD8 ubiquitin like modifier, ENSG00000129559).