Q93725 · NEDD8_CAEEL

Function

function

Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex uba-3-ula-1 and linkage to the E2 enzyme ubc-12. Attachment of ned-8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

Features

Showing features for site.

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MLIKVKTLTGKEIELDIEPNDRVERIKEKVEEKEGIPPPQQRLIFAGKQMNDDKTAADYKVLGGSVLHLVLALRGGF
TypeIDPosition(s)Description
Site8Interaction with uba-3
Site44Interaction with uba-3

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
Molecular Functionprotein tag activity
Molecular Functionubiquitin protein ligase binding
Biological Processmodification-dependent protein catabolic process
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of DNA damage response, signal transduction by p53 class mediator
Biological Processnegative regulation of gene expression
Biological Processpositive regulation of apoptotic process
Biological Processprotein neddylation
Biological Processregulation of proteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NEDD8
  • Alternative names
    • Neddylin
    • Protein NED-8
    • Ubiquitin-like protein Nedd8

Gene names

    • Name
      ned-8
    • ORF names
      F45H11.2

Organism names

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

Accessions

  • Primary accession
    Q93725

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Note: Mainly nuclear during interphase, also cytoplasmic during interphase and mitosis.

Keywords

Phenotypes & Variants

Disruption phenotype

Worms either arrest during embryonic development, or show vulval eversion at the L4 stage and burst at the vulva during the L4-to-adult molt. Those who survive to the adult stage display severe defects in terminal differentiation of seam cells, vulva and male tail.

PTM/Processing

Features

Showing features for chain, cross-link, propeptide.

TypeIDPosition(s)Description
ChainPRO_00000427771-76NEDD8
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
PropeptidePRO_000004277877

Post-translational modification

Cleavage of precursor form is necessary for function.

Keywords

Proteomic databases

Expression

Developmental stage

Expressed throughout development.

Gene expression databases

Interaction

Subunit

Interacts with dcn-1 (PubMed:15988528).
Covalently attached to cullins (PubMed:12781129).
May interact with atx-3 (PubMed:17935801).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region70-72Interaction with uba-3

Sequence similarities

Belongs to the ubiquitin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    77
  • Mass (Da)
    8,629
  • Last updated
    1997-02-01 v1
  • Checksum
    F3387DE33C671C78
MLIKVKTLTGKEIELDIEPNDRVERIKEKVEEKEGIPPPQQRLIFAGKQMNDDKTAADYKVLGGSVLHLVLALRGGF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z78420
EMBL· GenBank· DDBJ
CAB01708.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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