Q9U3C8 · DCN1_CAEEL

  • Protein
    Defective in cullin neddylation protein 1
  • Gene
    dcn-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with rbx-1 to recruit the Nedd8-charged E2 enzyme to the cullin component of SCF-type complexes.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular Componentubiquitin ligase complex
Molecular Functioncullin family protein binding
Molecular Functionubiquitin binding
Molecular Functionubiquitin conjugating enzyme binding
Molecular Functionubiquitin-like protein binding
Biological Processastral microtubule organization
Biological Processestablishment of mitotic spindle localization
Biological Processprotein catabolic process
Biological Processprotein neddylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Defective in cullin neddylation protein 1

Gene names

    • Name
      dcn-1
    • ORF names
      H38K22.2

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q9U3C8
  • Secondary accessions
    • Q9U3C9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001295071-295Defective in cullin neddylation protein 1

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with the cullin cul-3. Interacts with ubiquitin via its UBA-like domain. Interacts with ned-8/nedd8.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-45UBA-like
Domain60-272DCUN1

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9U3C8-1

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.

  • Length
    295
  • Mass (Da)
    34,133
  • Last updated
    2003-06-01 v2
  • Checksum
    F5C50912727235E4
MNRLKSDQKTKLRQFVQWTQVTEAVSLNFLAKANWNIEYAMTLYFDNPNLFAGSTPQPSVDRSNIERLFNQYVDPKDKVGEKRMGPHGINRLLTDLGYEATDRRVLVLAWKFTAQTQCEFSLDEWVKGMTALQADTVQNLRQRIDSINSGLESDKAKFHELYLFAFNYAKSAACRNLDLETAICCWDVLFGQRSTIMTQWIDFLWAQENAAASRLAQNVGASNAKQFKSVWISRDTWNLFWDFILLSKPDLSDYDDEGAWPVLIDQFVDYCRENLNYPKPGNASNDQQMETPSYY

Q9U3C8-2

  • Name
    b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-64: MNRLKSDQKTKLRQFVQWTQVTEAVSLNFLAKANWNIEYAMTLYFDNPNLFAGSTPQPSVDRSN → MNRLKSDQKTK

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0153191-64in isoform b

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL024499
EMBL· GenBank· DDBJ
CAB54261.2
EMBL· GenBank· DDBJ
Genomic DNA
AL024499
EMBL· GenBank· DDBJ
CAB54260.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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