DCUN1D5
entrez
84259
canonical
uniprot
Q9BTE7
canonical
ensembl
ENSG00000137692
resolver
ensp
ENSP00000260247
resolver
ensp
ENSP00000435035
resolver
enst
ENST00000260247
resolver
genesymbol
DCUN1D5
resolver
genesymbol_syn
SCCRO5
resolver
hgnc
HGNC:28409
resolver
uniprot
B4DP84
resolver
uniprot
Q3ZTT2
resolver
uniprot_entry
B4DP84_HUMAN
resolver
uniprot_entry
DCNL5_HUMAN
resolver
uniprot_sec
Q3ZTT2
resolver
amino_acid_sequence
MPVKKKRKSPGVAAAVAEDGGLKKCKISSYCRSQPPARLISGEEHFSSKKCLAWFYEYAGPDEVVGPEGMEKFCEDIGVEPENIIMLVLAWKLEAESMGFFTKEEWLKGMTSLQCDCTEKLQNKFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTWPLFSVFYQYLEQSKYRVMNKDQWYNVLEFSRTVHADLSNYDEDGAWPVLLDEFVEWQKVRQTS
uniprot
proteins
function
FUNCTION: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs) (PubMed:19617556, PubMed:23201271, PubMed:26906416). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth (PubMed:23098533, PubMed:24192928). {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23098533, ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:24192928, ECO:0000269|PubMed:26906416}.
uniprot
proteins
mass_dalton
27508
uniprot
proteins
mutagenesis
MUTAGEN 5..8; /note="KKRK->AAAA: Affects nucleus localization."; /evidence="ECO:0000269|PubMed:26906416"; MUTAGEN 195; /note="D->A: Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with R-219 and A-225. Does not affect localization at nucleus; when associated with R-219 and A-225."; /evidence="ECO:0000269|PubMed:26906416"; MUTAGEN 195; /note="D->N: Loss of interaction with RBX1, CUL1 and CAND1."; /evidence="ECO:0000269|PubMed:24192928"; MUTAGEN 219; /note="A->R: Loss of interaction with RBX1, CUL1 and CAND1. Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with A-195 and A-225. Does not affect localization at nucleus; when associated with A-195 and A-225."; /evidence="ECO:0000269|PubMed:24192928, ECO:0000269|PubMed:26906416"; MUTAGEN 225; /note="D->A: Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with A-195 and R-219. Does not affect localization at nucleus; when associated with A-195 and R-219."; /evidence="ECO:0000269|PubMed:26906416"; MUTAGEN 225; /note="D->N: Loss of interaction with RBX1, CUL1, CUL2, CUL3 and CAND1. Does not affect interaction with UBE2M and NEDD8. Fails to augment Cul3 neddylation beyond basal levels."; /evidence="ECO:0000269|PubMed:24192928"; MUTAGEN 226; /note="E->A: Loss of interaction with RBX1, CUL1, CUL2, CUL3 and CAND1. Does not affect interaction with UBE2M and NEDD8. Fails to augment Cul3 neddylation beyond basal levels."; /evidence="ECO:0000269|PubMed:24192928
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-41 is independent of cullin's interaction. Phosphorylated in response to both TICAM1 and MYD88 dependent Toll-like receptor (TLR) pathway activation (By similarity). Phosphorylated in response to IL1B stimulation (PubMed:29958295). {ECO:0000250|UniProtKB:Q9CXV9, ECO:0000269|PubMed:29958295}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16533400
uniprot
proteins
pubmed
18445686
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19617556
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23098533
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23201271
uniprot
proteins
pubmed
24192928
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26906416
uniprot
proteins
pubmed
29958295
uniprot
proteins
sequence_length
237
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:23098533, ECO:0000269|PubMed:26906416}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}. Note=Subcellular localization is independent of the interaction with cullins. {ECO:0000269|PubMed:26906416}.
uniprot
proteins