Q8QG64 · RBX1_SALSA

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

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)
  • S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine + N6-[NEDD8-protein]-yl-[cullin]-L-lysine.
    EC:2.3.2.32 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.
Protein modification; protein neddylation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site42Zn2+ 1 (UniProtKB | ChEBI)
Binding site45Zn2+ 1 (UniProtKB | ChEBI)
Binding site53Zn2+ 2 (UniProtKB | ChEBI)
Binding site56Zn2+ 2 (UniProtKB | ChEBI)
Binding site68Zn2+ 2 (UniProtKB | ChEBI)
Binding site75Zn2+ 3 (UniProtKB | ChEBI)
Binding site77Zn2+ 3 (UniProtKB | ChEBI)
Binding site80Zn2+ 1 (UniProtKB | ChEBI)
Binding site82Zn2+ 2 (UniProtKB | ChEBI)
Binding site94Zn2+ 3 (UniProtKB | ChEBI)
Binding site97Zn2+ 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentCul3-RING ubiquitin ligase complex
Cellular ComponentCul4A-RING E3 ubiquitin ligase complex
Cellular ComponentCul4B-RING E3 ubiquitin ligase complex
Cellular ComponentCul7-RING ubiquitin ligase complex
Cellular Componentcytoplasm
Cellular Componentnucleus
Cellular ComponentSCF ubiquitin ligase complex
Molecular Functioncullin family protein binding
Molecular FunctionNEDD8 ligase activity
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processprotein monoubiquitination
Biological Processprotein neddylation
Biological Processprotein ubiquitination
Biological ProcessSCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase RBX1
  • EC number
  • Alternative names
    • Hyperosmotic protein 21 (sHOP21)
    • RING-box protein 1 (Rbx1)

Gene names

    • Name
      rbx1
    • Synonyms
      hop21

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Protacanthopterygii > Salmoniformes > Salmonidae > Salmoninae > Salmo

Accessions

  • Primary accession
    Q8QG64

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000560151-108E3 ubiquitin-protein ligase RBX1

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.

TypeIDPosition(s)Description
Zinc finger53-98RING-type

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    108
  • Mass (Da)
    12,318
  • Last updated
    2003-10-03 v2
  • Checksum
    44C3EA712CEDC7BB
MAAAMDVDTPSATNSGASKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH

Sequence caution

The sequence AAK29182.1 differs from that shown. Reason: Erroneous initiation

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY027936
EMBL· GenBank· DDBJ
AAK29182.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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