DCUN1D1
entrez
54165
canonical
uniprot
Q96GG9
canonical
ensembl
ENSG00000043093
resolver
ensp
ENSP00000292782
resolver
ensp
ENSP00000419359
resolver
ensp
ENSP00000419440
resolver
ensp
ENSP00000488427
resolver
enst
ENST00000292782
resolver
enst
ENST00000460412
resolver
enst
ENST00000469954
resolver
enst
ENST00000632685
resolver
genesymbol
DCUN1D1
resolver
genesymbol_syn
DCN1
resolver
genesymbol_syn
DCUN1L1
resolver
genesymbol_syn
RP42
resolver
genesymbol_syn
SCCRO
resolver
hgnc
HGNC:18184
resolver
uniprot
B2RB37
resolver
uniprot
B4DM76
resolver
uniprot
C9JUW4
resolver
uniprot
C9JVE2
resolver
uniprot
Q7L3G9
resolver
uniprot
Q8TEX7
resolver
uniprot
Q9H6M1
resolver
uniprot
Q9HCT3
resolver
uniprot_entry
B4DM76_HUMAN
resolver
uniprot_entry
C9JVE2_HUMAN
resolver
uniprot_entry
DCNL1_HUMAN
resolver
uniprot_sec
B2RB37
resolver
uniprot_sec
C9JUW4
resolver
uniprot_sec
Q7L3G9
resolver
uniprot_sec
Q8TEX7
resolver
uniprot_sec
Q9H6M1
resolver
uniprot_sec
Q9HCT3
resolver
amino_acid_sequence
MNKLKSSQKDKVRQFMIFTQSSEKTAVSCLSQNDWKLDVATDNFFQNPELYIRESVKGSLDRKKLEQLYNRYKDPQDENKIGIDGIQQFCDDLALDPASISVLIIAWKFRAATQCEFSKQEFMDGMTELGCDSIEKLKAQIPKMEQELKEPGRFKDFYQFTFNFAKNPGQKGLDLEMAIAYWNLVLNGRFKFLDLWNKFLLEHHKRSIPKDTWNLLLDFSTMIADDMSNYDEEGAWPVLIDDFVEFARPQIAGTKSTTV
uniprot
proteins
function
FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation (PubMed:18826954). Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes (PubMed:19617556, PubMed:23201271, PubMed:23401859, PubMed:26906416). Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity (PubMed:25349211, PubMed:28581483). Also acts as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity). {ECO:0000250|UniProtKB:Q9QZ73, ECO:0000269|PubMed:18826954, ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:23401859, ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:28581483}.
uniprot
proteins
mass_dalton
30124
uniprot
proteins
mutagenesis
MUTAGEN 15; /note="F->A: Loss of ubiquitin binding; when associated with A-16, A-44 and A-45."; /evidence="ECO:0000269|PubMed:30587576"; MUTAGEN 16; /note="M->A: Loss of ubiquitin binding; when associated with A-15, A-44 and A-45."; /evidence="ECO:0000269|PubMed:30587576"; MUTAGEN 44; /note="F->A: Loss of ubiquitin binding; when associated with A-15, A-16 and A-45."; /evidence="ECO:0000269|PubMed:30587576"; MUTAGEN 45; /note="F->A: Loss of ubiquitin binding; when associated with A-15, A-16 and A-44."; /evidence="ECO:0000269|PubMed:30587576"; MUTAGEN 115; /note="C->A,G,I,L,T,V: Loss of ability to stimulate cullin neddylation."; /evidence="ECO:0000269|PubMed:28581483"; MUTAGEN 211; /note="D->A: Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with R-235 and A-241. Does not affect both nucleus and cytoplasm localization; when associated with R-235 and A-241. Reduces cullin neddylation; when associated with R-235 and A-241. Loss of interaction with CUL1, CUL2, CUL3, CULA4 and CULA4; when associated with R-235 and A-241. Loss of CUL2 interaction; when associated with R-235 and A-241. Reduces neddylation on CUL2; when associated with R-235 and A-241. Reduces interaction with VHL and HIF1A; when associated with R-235 and A-241. Does not affect interaction with SOCS1; when associated with R-235 and A-241. Does not affect DCUN1D1 monoubiquitylation; when associated with R-235 and A-241."; /evidence="ECO:0000269|PubMed:23401859, ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:30587576"; MUTAGEN 235; /note="A->R: Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with A-211 and A-241. Does not affect both nucleus and cytoplasm localization; when associated with A-211 and A-241. Reduces cullin neddylation; when associated with A-211 and A-241. Loss of interaction with CUL1, CUL2, CUL3, CULA4 and CULA4; when associated with A-211 and A-241. Loss of CUL2 interaction; when associated with A-211 and A-241. Reduces neddylation on CUL2; when associated with A-211 and A-241. Reduces interaction with VHL and HIF1A; when associated with A-211 and A-241. Does not affect interaction with SOCS1; when associated with A-211 and A-241. Does not affect DCUN1D1 monoubiquitylation; when associated with A-211 and A-241."; /evidence="ECO:0000269|PubMed:23401859, ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:30587576"; MUTAGEN 241; /note="D->A: Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with A-211 and R-235. Does not affect both nucleus and cytoplasm localization; when associated with A-211 and R-235. Reduces cullin neddylation; when associated with A-211 and R-235. Loss of interaction with CUL1, CUL2, CUL3, CULA4 and CULA4; when associated with A-211 and R-235. Loss of CUL2 interaction; when associated with A-211 and R-235. Reduces neddylation on CUL2; when associated with A-211 and R-235. Reduces interaction with VHL and HIF1A; when associated with A-211 and R-235. Does not affect interaction with SOCS1; when associated with A-211 and R-235. Does not affect DCUN1D1 monoubiquitylation; when associated with A-211 and R-235."; /evidence="ECO:0000269|PubMed:23401859, ECO:0000269|PubMed:26906416, ECO:0000269|PubMed:30587576"; MUTAGEN 241; /note="D->N: Loss of binding to CAND1 and CUL-RBX1 complex but retains binding to UBE2M."; /evidence="ECO:0000269|PubMed:18826954
uniprot
proteins
post_translational_modification
PTM: Mono- and poly-ubiquitinated by ARIH2 and ARIH1. Monoubiquitination by ARIH2 is mediated by an interaction between autoubiquitinated ARIH2 and the UBA-like domain. The monoubiquitinated form preferentially interacts with non-neddylated cullins and modulates cullin RING ligase (CRL) complex composition and activity. {ECO:0000269|PubMed:30587576}.
uniprot
proteins
pubmed
10777668
uniprot
proteins
pubmed
12796399
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15123463
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15511464
uniprot
proteins
pubmed
15623817
uniprot
proteins
pubmed
15657565
uniprot
proteins
pubmed
17018598
uniprot
proteins
pubmed
18826954
uniprot
proteins
pubmed
19617556
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21940857
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23201271
uniprot
proteins
pubmed
23401859
uniprot
proteins
pubmed
25349211
uniprot
proteins
pubmed
26906416
uniprot
proteins
pubmed
28581483
uniprot
proteins
pubmed
30587576
uniprot
proteins
sequence_length
259
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416}. Cytoplasm {ECO:0000269|PubMed:26906416}. Note=The ubiquitinated form is localized in the cytoplasm. {ECO:0000269|PubMed:30587576}.
uniprot
proteins