Q92564 · DCNL4_HUMAN
- ProteinDCN1-like protein 4
- GeneDCUN1D4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids292 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 are necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | cullin family protein binding | |
Molecular Function | ubiquitin conjugating enzyme binding | |
Molecular Function | ubiquitin-like protein binding | |
Biological Process | positive regulation of protein neddylation | |
Biological Process | protein neddylation |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDCN1-like protein 4
- Short namesDCNL4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ92564
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 250 | Does not affect localization at nucleus; when associated with R-274 and A-280. | ||||
Sequence: D → A | ||||||
Mutagenesis | 274 | Does not affect localization at nucleus; when associated with A-250 and A-280. | ||||
Sequence: A → R | ||||||
Mutagenesis | 280 | Does not affect localization at nucleus; when associated with A-250 and R-274. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 335 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000129503 | 1-292 | UniProt | DCN1-like protein 4 | |||
Sequence: MHSDAAAVNFQLNSHLSTLANIHKIYHTLNKLNLTEDIGQDDHQTGSLRSCSSSDCFNKVMPPRKKRRPASGDDLSAKKSRHDSMYRKYDSTRIKTEEEAFSSKRCLEWFYEYAGTDDVVGPEGMEKFCEDIGVEPENVVMLVLAWKLDAQNMGYFTLQEWLKGMTSLQCDTTEKLRNTLDYLRSFLNDSTNFKLIYRYAFDFAREKDQRSLDINTAKCMLGLLLGKIWPLFPVFHQFLEQSKYKVINKDQWCNVLEFSRTINLDLSNYDEDGAWPVLLDEFVEWYKDKQMS | |||||||
Modified residue (large scale data) | 71 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 95 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts (via the DCUN1 domain) with the unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these interactions promote the cullin neddylation and the identity of the cullin dictates the affinity of the interaction (PubMed:23201271, PubMed:26906416).
Interacts with RBX1 and RNF7 (PubMed:26906416).
Interacts with CAND1; this interaction is bridged by cullins such as CUL3 and strongly inhibits the neddylation of CUL3. These CAND-cullin-DCNL complexes can only be neddylated in the presence of a substrate adapter (PubMed:26906416).
Interacts (via DCUN1 domain) with UBE2M (N-terminally acetylated form) and probably with UBE2F (N-terminally acetylated form) (PubMed:23201271).
Interacts with RBX1 and RNF7 (PubMed:26906416).
Interacts with CAND1; this interaction is bridged by cullins such as CUL3 and strongly inhibits the neddylation of CUL3. These CAND-cullin-DCNL complexes can only be neddylated in the presence of a substrate adapter (PubMed:26906416).
Interacts (via DCUN1 domain) with UBE2M (N-terminally acetylated form) and probably with UBE2F (N-terminally acetylated form) (PubMed:23201271).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q92564 | PRO_0000037946 P29991 | 3 | EBI-2654610, EBI-8826488 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 43-57 | Polar residues | ||||
Sequence: HQTGSLRSCSSSDCF | ||||||
Region | 43-83 | Disordered | ||||
Sequence: HQTGSLRSCSSSDCFNKVMPPRKKRRPASGDDLSAKKSRHD | ||||||
Compositional bias | 60-83 | Basic and acidic residues | ||||
Sequence: VMPPRKKRRPASGDDLSAKKSRHD | ||||||
Domain | 101-287 | DCUN1 | ||||
Sequence: FSSKRCLEWFYEYAGTDDVVGPEGMEKFCEDIGVEPENVVMLVLAWKLDAQNMGYFTLQEWLKGMTSLQCDTTEKLRNTLDYLRSFLNDSTNFKLIYRYAFDFAREKDQRSLDINTAKCMLGLLLGKIWPLFPVFHQFLEQSKYKVINKDQWCNVLEFSRTINLDLSNYDEDGAWPVLLDEFVEWYK |
Domain
The DCUN1 domain, also known as PONY domain, mediates the interaction with different cullins (PubMed:23201271).
The DCUN1 domain mediates the interaction with the N-terminally acetylated NEDD8-conjugating E2s enzyme leading to the NEDD8 transfer from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes; the neddylation efficiency correlates with the DCUN1D5-cullin and DCUN1D5-E2 interaction affinities (PubMed:23201271).
The DCUN1 domain mediates the interaction with the N-terminally acetylated NEDD8-conjugating E2s enzyme leading to the NEDD8 transfer from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes; the neddylation efficiency correlates with the DCUN1D5-cullin and DCUN1D5-E2 interaction affinities (PubMed:23201271).
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q92564-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length292
- Mass (Da)34,068
- Last updated2005-10-25 v2
- Checksum1927AA612E075E9C
Q92564-2
- Name2
- Differences from canonical
- 206-240: Missing
Q92564-3
- Name3
- Differences from canonical
- 1-9: MHSDAAAVN → MEVEAALGCSGQGRGCGGVAPAGRGRERASERGTRVRISKGLSGAGGSVRKAD
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_054381 | 1-9 | in isoform 3 | |||
Sequence: MHSDAAAVN → MEVEAALGCSGQGRGCGGVAPAGRGRERASERGTRVRISKGLSGAGGSVRKAD | ||||||
Compositional bias | 43-57 | Polar residues | ||||
Sequence: HQTGSLRSCSSSDCF | ||||||
Compositional bias | 60-83 | Basic and acidic residues | ||||
Sequence: VMPPRKKRRPASGDDLSAKKSRHD | ||||||
Alternative sequence | VSP_016016 | 206-240 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D87466 EMBL· GenBank· DDBJ | BAA13405.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK294894 EMBL· GenBank· DDBJ | BAG57986.1 EMBL· GenBank· DDBJ | mRNA | ||
BX537944 EMBL· GenBank· DDBJ | CAD97912.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC027271 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC053897 EMBL· GenBank· DDBJ | AAH53897.2 EMBL· GenBank· DDBJ | mRNA |