DCUN1D3
entrez
123879
canonical
uniprot
Q8IWE4
canonical
ensembl
ENSG00000188215
resolver
ensp
ENSP00000319482
resolver
ensp
ENSP00000454762
resolver
ensp
ENSP00000570915
resolver
ensp
ENSP00000570916
resolver
ensp
ENSP00000587330
resolver
ensp
ENSP00000587331
resolver
ensp
ENSP00000587332
resolver
ensp
ENSP00000587333
resolver
ensp
ENSP00000587334
resolver
ensp
ENSP00000587335
resolver
ensp
ENSP00000617841
resolver
ensp
ENSP00000617842
resolver
ensp
ENSP00000617843
resolver
ensp
ENSP00000617844
resolver
enst
ENST00000324344
resolver
enst
ENST00000563934
resolver
enst
ENST00000900856
resolver
enst
ENST00000900857
resolver
enst
ENST00000917271
resolver
enst
ENST00000917272
resolver
enst
ENST00000917273
resolver
enst
ENST00000917274
resolver
enst
ENST00000917275
resolver
enst
ENST00000917276
resolver
enst
ENST00000947782
resolver
enst
ENST00000947783
resolver
enst
ENST00000947784
resolver
enst
ENST00000947785
resolver
genesymbol
DCUN1D3
resolver
genesymbol_syn
SCCRO3
resolver
hgnc
HGNC:28734
resolver
uniprot
B3KVY4
resolver
uniprot_entry
DCNL3_HUMAN
resolver
uniprot_sec
B3KVY4
resolver
amino_acid_sequence
MGQCVTKCKNPSSTLGSKNGDREPSNKSHSRRGAGHREEQVPPCGKPGGDILVNGTKKAEAATEACQLPTSSGDAGRESKSNAEESSLQRLEELFRRYKDEREDAILEEGMERFCNDLCVDPTEFRVLLLAWKFQAATMCKFTRKEFFDGCKAISADSIDGICARFPSLLTEAKQEDKFKDLYRFTFQFGLDSEEGQRSLHREIAIALWKLVFTQNNPPVLDQWLNFLTENPSGIKGISRDTWNMFLNFTQVIGPDLSNYSEDEAWPSLFDTFVEWEMERRKREGEGRGALSSGPEGLCPEEQT
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 and may play a role in the cell cycle progression by regulating the SCF ubiquitin E3 ligase complex, after UV damage (PubMed:18823379, PubMed:19617556, PubMed:23201271, PubMed:27542266). At the cell membrane, can promote and as well inhibit cullins neddylation (PubMed:19617556, PubMed:25349211, PubMed:26906416). {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:27542266}.
uniprot
proteins
mass_dalton
34291
uniprot
proteins
mutagenesis
MUTAGEN 1..26; /note="Missing: No effect on CAND1-, CUL1-, CUL3- and RBX1-binding."; /evidence="ECO:0000269|PubMed:25349211"; MUTAGEN 2; /note="G->A: No effect on CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of localization at the cell membrane. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation. Loss of myristoylation. Loss of myristoylation; when associated with A-4. Loss of myristoylation; when associated with A-8. Loss of palmitoylation. Affects cell membrane localization, and localizes throughout the cytoplasm. Does not relocalizes CUL3 to the cell membrane."; /evidence="ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:25349211"; MUTAGEN 4; /note="C->A: Does not affect myristoylation; when associated with A-8. Loss of myristoylation; when associated with A-2. Loss of palmitoylation; when associated with A-8. Reduces cell membrane localization."; /evidence="ECO:0000269|PubMed:19617556"; MUTAGEN 8; /note="C->A: Does not affect myristoylation; when associated with A-4. Loss of myristoylation; when associated with A-2. Loss of palmitoylation; when associated with A-4. Reduces cell membrane localization."; /evidence="ECO:0000269|PubMed:19617556"; MUTAGEN 241; /note="D->A: Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5, CAND1 and RBX1; when associated with R-265 and A-271. Does not affect both nucleus and cytoplasm localization; when associated with R-265 and A-271. Loss of interaction with CUL3; when associated with R-265 and A-271."; /evidence="ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:26906416"; MUTAGEN 241; /note="D->N: Loss of CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation, but no effect on localization at the cell membrane; when associated with R-265 and N-271."; /evidence="ECO:0000269|PubMed:25349211"; MUTAGEN 265; /note="A->R: Loss of CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation, but no effect on localization at the cell membrane; when associated with N-241 and N-271. Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5, CAND1 and RBX1; when associated with A-241 and A-271. Does not affect both nucleus and cytoplasm localization; when associated with A-241 and A-271. Loss of interaction with CUL3; when associated with A-241 and A-271."; /evidence="ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416"; MUTAGEN 271; /note="D->A: Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CALD1 and RBX1; when associated with A-241 and R-265. Does not affect both nucleus and cytoplasm localization; when associated with A-241 and R-265. Loss of interaction with CUL3; when associated with A-241 and A-271."; /evidence="ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:26906416"; MUTAGEN 271; /note="D->N: Loss of CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation, but no effect on localization at the cell membrane; when associated with N-241 and R-265."; /evidence="ECO:0000269|PubMed:25349211
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16533400
uniprot
proteins
pubmed
18823379
uniprot
proteins
pubmed
19617556
uniprot
proteins
pubmed
23201271
uniprot
proteins
pubmed
25349211
uniprot
proteins
pubmed
26906416
uniprot
proteins
pubmed
27542266
uniprot
proteins
sequence_length
304
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416}. Cytoplasm {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Nucleus {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18823379}. Note=After UVC treatment, the protein enters to the nucleus gradually (PubMed:18823379). Cell membrane localization is essential for CUL3 neddylation (PubMed:19617556). {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:19617556}.
uniprot
proteins