Q17391 · CUL3_CAEEL

Function

function

Probable core component of multiple cullin-RING-based BCB (BTB-CUL3-BTB) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:13679922).
Probably acts as a scaffold protein which may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:13679922).
Required to target mei-3/katanin for degradation at the meiosis to mitosis transition via its neddylation and deneddylation (PubMed:12781129).
Functions in ubiquitin-mediated degradation of CKIs to target cki-1 for degradation (PubMed:12781129).
Regulates microtubule stability in the early embryo (PubMed:12781129).
In body wall muscles, involved in the organization of myosin thick filaments, likely by regulating the degradation of microtubule severing protein mei-1 downstream of unc-89 (PubMed:22621901).
Together with spop-1, may promote the ubiquitination and proteasomal degradation of target bromodomain-containing proteins such as bet-1 (PubMed:34593637).

Pathway

Protein modification; protein ubiquitination.

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 ComponentCul3-RING ubiquitin ligase complex
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular FunctionPOZ domain binding
Molecular Functionubiquitin protein ligase binding
Biological Processprogrammed cell death involved in cell development
Biological Processprotein catabolic process
Biological Processprotein polyubiquitination
Biological Processprotein ubiquitination
Biological Processstriated muscle myosin thick filament assembly
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cullin-3
  • Short names
    CUL-3

Gene names

    • Name
      cul-3
    • ORF names
      Y108G3AL.1

Organism names

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

Accessions

  • Primary accession
    Q17391
  • Secondary accessions
    • Q95Y32

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

RNAi-mediated knockdown at L1 larval stage results in the disorganization of myosin thick filaments in adult body wall muscles characterized by the formation of abnormal myosin heavy chain myo-3 aggregates and V-shaped crossing of A-bands (PubMed:22621901).
RNAi-mediated knockdown suppresses the age-dependent paralysis and growth arrest induced by exogenous dipeptide repeat protein PR50 (PubMed:34593637).

PTM/Processing

Features

Showing features for chain, cross-link.

TypeIDPosition(s)Description
ChainPRO_00001197821-777Cullin-3
Cross-link721Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

Post-translational modification

Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.

Keywords

Proteomic databases

Expression

Developmental stage

Highest levels in embryos and lower levels in larvae and adults.

Gene expression databases

Interaction

Subunit

Probable component of multiple cullin-RING-based BCB (BTB-CUL3-BTB) E3 ubiquitin-protein ligase complexes formed by cul-3, rbx-1 and a variable BTB domain-containing protein acting as both, adapter to cullin and substrate recognition component (PubMed:13679922).
Interacts with bath-15, bath-40, bath-41, bath-42, C17F4.8, tag-303, D2045.8, F57C2.1, ZC239.15 and B0281.5 (PubMed:13679922).
Interacts with mel-26 (via BTB domain) (PubMed:13679922, PubMed:22621901).
Interacts with dcn-1 (PubMed:13679922).

Binary interactions

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region568-596Disordered

Sequence similarities

Belongs to the cullin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    777
  • Mass (Da)
    90,236
  • Last updated
    2003-06-20 v2
  • Checksum
    3D90A41092E540A7
MSGRSGNGGQQKMRIRPFMATIDEQYVTQTWELLKRAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGERLYNGLKDVIQDHMASVRIRIIESMNSGSFLETVAESWADHTVAMVMIRDILMYMDRIYVAQNNHVLPVYNLGLDAYRTEILRQNGIGDRIRDALLELIKLDRKSNQINWHGIKNACDMLISLGIDSRTVYEDEFERPLLKETSDYYRDVCKNWLSGDNDACFYLAQVEIAMHDEASRASRYLDKMTEAKILQVMDDVMVAEHIQTIVYMQNGGVKFMLEHKKIEDLTRIFRIFKRIGDSVTVPGGGLKALLKAVSEYLNETGSNIVKNEDLLKNPVNFVNELLQLKDYFSSLLTTAFADDRDFKNRFQHDFETFLNSNRQSPEFVALYMDDMLRSGLKCVSDAEMDNKLDNVMILFRYLQEKDVFEKYFKQYLAKRLLLDKSCSDDVEKALLAKLKTECGCQFTQKLENMFRDKELWLTLATSFRDWREAQPTKMSIDISLRVLTAGVWPTVQCNPVVLPQELSVAYEMFTQYYTEKHTGRKLTINTLLGNADVKATFYPPPKASMSNEENGPGPSSSGESMKERKPEHKILQVNTHQMIILLQFNHHNRISCQQLMDELKIPERELKRNLQSLALGKASQRILVRKNKGKDAIDMSDEFAVNDNFQSKLTRVKVQMVTGKVESEPEIRETRQKVEDDRKLEVEAAIVRIMKARKKLNHNNLVAEVTQQLRHRFMPSPIIIKQRIETLIEREYLARDEHDHRAYQYIA

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0K3ASX8A0A0K3ASX8_CAEELcul-3240
A0A0K3AV81A0A0K3AV81_CAEELcul-3113
A0A0K3AY70A0A0K3AY70_CAEELcul-3717

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict586in Ref. 1; AAC47122
Sequence conflict614in Ref. 1; AAC47122
Sequence conflict623in Ref. 1; AAC47122

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U58085
EMBL· GenBank· DDBJ
AAC47122.1
EMBL· GenBank· DDBJ
mRNA
BX284605
EMBL· GenBank· DDBJ
CCD74336.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp