NEDD8
entrez
4738
canonical
uniprot
Q15843
canonical
ensembl
ENSG00000129559
resolver
ensembl
ENSG00000285246
resolver
ensp
ENSP00000250495
resolver
ensp
ENSP00000496420
resolver
enst
ENST00000250495
resolver
enst
ENST00000643069
resolver
genesymbol
NEDD8
resolver
hgnc
HGNC:7732
resolver
uniprot
Q3SXN8
resolver
uniprot
Q6LES6
resolver
uniprot_entry
NEDD8_HUMAN
resolver
uniprot_sec
Q3SXN8
resolver
uniprot_sec
Q6LES6
resolver
amino_acid_sequence
MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLRQ
uniprot
proteins
function
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). {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}.
uniprot
proteins
mass_dalton
9072
uniprot
proteins
mutagenesis
MUTAGEN 7..9; /note="TLT->ALA: Decreased interaction with B.pseudomallei Cif protein, leading to decreased deamidation."; /evidence="ECO:0000269|PubMed:23175788"; MUTAGEN 11; /note="K->A: Decreased interaction with B.pseudomallei Cif protein, leading to decreased deamidation."; /evidence="ECO:0000269|PubMed:23175788"; MUTAGEN 31; /note="E->Q: Decreased interaction with B.pseudomallei Cif protein, leading to slightly decreased deamidation."; /evidence="ECO:0000269|PubMed:23175788"; MUTAGEN 40; /note="Q->E: Impaired ability to activate cullin-RING-based E3 ubiquitin-protein ligase complexes."; /evidence="ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597"; MUTAGEN 68; /note="H->A: Decreased interaction with B.pseudomallei Cif protein, leading to slightly decreased deamidation."; /evidence="ECO:0000269|PubMed:23175788"; MUTAGEN 72; /note="A->R: Prevents adenylation by UBE1C."; /evidence="ECO:0000269|PubMed:14690597
uniprot
proteins
post_translational_modification
PTM: Cleavage of precursor form by UCHL3 or SENP8 is necessary for function. {ECO:0000269|PubMed:12730221, ECO:0000269|PubMed:12759363, ECO:0000269|PubMed:9353319, ECO:0000269|PubMed:9790970}.; PTM: (Microbial infection) Deamidated at Gln-40 by bacterial cyclomodulin Cif produced by enteropathogenic E.coli, Y.pseudotuberculosis or B.pseudomallei, leading to impair NEDD8 ability to activate cullin-RING-based E3 ubiquitin-protein ligase complexes (CRL complexes) (PubMed:20688984, PubMed:21903097, PubMed:23175788, PubMed:23589306, PubMed:26632597). Deamidation occurs on NEDD8-modified cullins (PubMed:20850415, PubMed:21903097). NEDD8 deamidation prevents switching from the inactive to active state by maintaining the 'closed' structure of the CRL complexes (PubMed:23589306, PubMed:26632597). Deamidation may also impair its deconjugation by the COP9 signalosome; However this result needs additional evidence (PubMed:20850415, PubMed:21903097). {ECO:0000269|PubMed:20688984, ECO:0000269|PubMed:20850415, ECO:0000269|PubMed:21903097, ECO:0000269|PubMed:23175788, ECO:0000269|PubMed:23589306, ECO:0000269|PubMed:26632597}.
uniprot
proteins
protein_family
Ubiquitin family
uniprot
proteins
pubmed
10318914
uniprot
proteins
pubmed
10597293
uniprot
proteins
pubmed
11259415
uniprot
proteins
pubmed
11953428
uniprot
proteins
pubmed
12215427
uniprot
proteins
pubmed
12730221
uniprot
proteins
pubmed
12759363
uniprot
proteins
pubmed
14690597
uniprot
proteins
pubmed
15242646
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15567417
uniprot
proteins
pubmed
20688984
uniprot
proteins
pubmed
20850415
uniprot
proteins
pubmed
21903097
uniprot
proteins
pubmed
22691497
uniprot
proteins
pubmed
23175788
uniprot
proteins
pubmed
23589306
uniprot
proteins
pubmed
26632597
uniprot
proteins
pubmed
28891468
uniprot
proteins
pubmed
38316879
uniprot
proteins
pubmed
38605244
uniprot
proteins
pubmed
9353319
uniprot
proteins
pubmed
9694792
uniprot
proteins
pubmed
9790970
uniprot
proteins
pubmed
9857030
uniprot
proteins
sequence_length
81
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9353319}. Note=Mainly nuclear. {ECO:0000269|PubMed:9353319}.
uniprot
proteins