Q17391 · CUL3_CAEEL
- ProteinCullin-3
- Genecul-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids777 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 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 | Cul3-RING ubiquitin ligase complex | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | POZ domain binding | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | programmed cell death involved in cell development | |
Biological Process | protein catabolic process | |
Biological Process | protein polyubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | striated muscle myosin thick filament assembly | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCullin-3
- Short namesCUL-3
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ17391
- Secondary accessions
Proteomes
Organism-specific databases
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000119782 | 1-777 | Cullin-3 | |||
Sequence: MSGRSGNGGQQKMRIRPFMATIDEQYVTQTWELLKRAIQEIQRKNNSGLSFEELYRNAYTMVLHKHGERLYNGLKDVIQDHMASVRIRIIESMNSGSFLETVAESWADHTVAMVMIRDILMYMDRIYVAQNNHVLPVYNLGLDAYRTEILRQNGIGDRIRDALLELIKLDRKSNQINWHGIKNACDMLISLGIDSRTVYEDEFERPLLKETSDYYRDVCKNWLSGDNDACFYLAQVEIAMHDEASRASRYLDKMTEAKILQVMDDVMVAEHIQTIVYMQNGGVKFMLEHKKIEDLTRIFRIFKRIGDSVTVPGGGLKALLKAVSEYLNETGSNIVKNEDLLKNPVNFVNELLQLKDYFSSLLTTAFADDRDFKNRFQHDFETFLNSNRQSPEFVALYMDDMLRSGLKCVSDAEMDNKLDNVMILFRYLQEKDVFEKYFKQYLAKRLLLDKSCSDDVEKALLAKLKTECGCQFTQKLENMFRDKELWLTLATSFRDWREAQPTKMSIDISLRVLTAGVWPTVQCNPVVLPQELSVAYEMFTQYYTEKHTGRKLTINTLLGNADVKATFYPPPKASMSNEENGPGPSSSGESMKERKPEHKILQVNTHQMIILLQFNHHNRISCQQLMDELKIPERELKRNLQSLALGKASQRILVRKNKGKDAIDMSDEFAVNDNFQSKLTRVKVQMVTGKVESEPEIRETRQKVEDDRKLEVEAAIVRIMKARKKLNHNNLVAEVTQQLRHRFMPSPIIIKQRIETLIEREYLARDEHDHRAYQYIA | ||||||
Cross-link | 721 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) | ||||
Sequence: K |
Post-translational modification
Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.
Keywords
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q17391 | bath-40 Q9NF14 | 2 | EBI-593075, EBI-313743 | |
BINARY | Q17391 | bath-41 P41886 | 2 | EBI-593075, EBI-314147 | |
BINARY | Q17391 | bath-42 P34371 | 3 | EBI-593075, EBI-315422 | |
BINARY | Q17391 | CELE_B0281.5 O16612 | 2 | EBI-593075, EBI-326132 | |
BINARY | Q17391 | CELE_D2045.8 Q18986 | 2 | EBI-593075, EBI-326795 | |
BINARY | Q17391 | inso-1 Q18776 | 3 | EBI-593075, EBI-312114 | |
BINARY | Q17391 | mel-26 Q94420 | 3 | EBI-593075, EBI-320790 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 568-596 | Disordered | ||||
Sequence: YPPPKASMSNEENGPGPSSSGESMKERKP |
Sequence similarities
Belongs to the cullin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length777
- Mass (Da)90,236
- Last updated2003-06-20 v2
- Checksum3D90A41092E540A7
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0K3ASX8 | A0A0K3ASX8_CAEEL | cul-3 | 240 | ||
A0A0K3AV81 | A0A0K3AV81_CAEEL | cul-3 | 113 | ||
A0A0K3AY70 | A0A0K3AY70_CAEEL | cul-3 | 717 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 586 | in Ref. 1; AAC47122 | ||||
Sequence: S → G | ||||||
Sequence conflict | 614 | in Ref. 1; AAC47122 | ||||
Sequence: F → L | ||||||
Sequence conflict | 623 | in Ref. 1; AAC47122 | ||||
Sequence: Q → QHEQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U58085 EMBL· GenBank· DDBJ | AAC47122.1 EMBL· GenBank· DDBJ | mRNA | ||
BX284605 EMBL· GenBank· DDBJ | CCD74336.1 EMBL· GenBank· DDBJ | Genomic DNA |