Q8QG64 · RBX1_SALSA
- ProteinE3 ubiquitin-protein ligase RBX1
- Generbx1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids108 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
E3 ubiquitin ligase component of multiple cullin-RING-based E3 ubiquitin-protein ligase (CRLs) complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins, including proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. CRLs complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins, ARIH1 mediating addition of the first ubiquitin on CRLs targets. The functional specificity of the E3 ubiquitin-protein ligase complexes depends on the variable substrate recognition components. Promotes the neddylation of CUL1, CUL2, CUL4 and CUL4 via its interaction with UBE2M.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Protein modification; protein neddylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 42 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 45 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 53 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 56 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 68 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 75 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 77 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 80 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 82 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 94 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 97 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Cul3-RING ubiquitin ligase complex | |
Cellular Component | Cul4A-RING E3 ubiquitin ligase complex | |
Cellular Component | Cul4B-RING E3 ubiquitin ligase complex | |
Cellular Component | Cul7-RING ubiquitin ligase complex | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | SCF ubiquitin ligase complex | |
Molecular Function | cullin family protein binding | |
Molecular Function | NEDD8 ligase activity | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein monoubiquitination | |
Biological Process | protein neddylation | |
Biological Process | protein ubiquitination | |
Biological Process | SCF-dependent proteasomal ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase RBX1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Protacanthopterygii > Salmoniformes > Salmonidae > Salmoninae > Salmo
Accessions
- Primary accessionQ8QG64
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056015 | 1-108 | E3 ubiquitin-protein ligase RBX1 | |||
Sequence: MAAAMDVDTPSATNSGASKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH |
Proteomic databases
Expression
Tissue specificity
Expressed in heart and kidney.
Induction
During hyperosmotic stress and thermal stress.
Gene expression databases
Interaction
Subunit
Part of SCF complexes, which consist of skp1, cul1, rbx1 and a F-box protein. Interacts with ube2m (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 53-98 | RING-type | ||||
Sequence: CIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDN |
Domain
The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.
Sequence similarities
Belongs to the RING-box family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length108
- Mass (Da)12,318
- Last updated2003-10-03 v2
- Checksum44C3EA712CEDC7BB
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY027936 EMBL· GenBank· DDBJ | AAK29182.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |