O35445 · RNF5_MOUSE
- ProteinE3 ubiquitin-protein ligase RNF5
- GeneRnf5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids180 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination of target proteins (PubMed:23093945).
May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4 (By similarity).
Mediates ubiquitination of PXN/paxillin,thereby regulating cell motility and localization of PXN/paxillin (By similarity).
Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N (By similarity).
Mediates the 'Lys-48'-linked polyubiquitination of STING1 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses (By similarity).
Catalyzes ubiquitination and subsequent degradation of ATG4B, thereby inhibiting autophagy (PubMed:23093945).
May function together with E2 ubiquitin-conjugating enzymes UBE2D1/UBCH5A and UBE2D2/UBC4 (By similarity).
Mediates ubiquitination of PXN/paxillin,thereby regulating cell motility and localization of PXN/paxillin (By similarity).
Mediates the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD; the ubiquitination appears to involve E2 ubiquitin-conjugating enzyme UBE2N (By similarity).
Mediates the 'Lys-48'-linked polyubiquitination of STING1 at 'Lys-150' leading to its proteasomal degradation; the ubiquitination occurs in mitochondria after viral transfection and regulates antiviral responses (By similarity).
Catalyzes ubiquitination and subsequent degradation of ATG4B, thereby inhibiting autophagy (PubMed:23093945).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | mitochondrial membrane | |
Cellular Component | plasma membrane | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | protein-containing complex binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-like protein conjugating enzyme binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | ERAD pathway | |
Biological Process | negative regulation of autophagy | |
Biological Process | protein destabilization | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | protein K63-linked ubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of autophagosome assembly | |
Biological Process | response to bacterium | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase RNF5
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO35445
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Mitochondrion membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Predominantly located in the plasma membrane, with some localization occurring within cytoplasmic organelles.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 118-138 | Helical | ||||
Sequence: GGFHFSFGVGAFPFGFFTTVF | ||||||
Transmembrane | 160-180 | Helical | ||||
Sequence: SWQDSLFLFLAIFFFFWLLSI |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice are more resistant to lethal infections by group A Streptococcus due to increased autophagy (PubMed:23093945).
Macrophages show increased autophagosomes and more efficient bacterial clearance (PubMed:23093945).
Macrophages show increased autophagosomes and more efficient bacterial clearance (PubMed:23093945).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000240394 | 2-180 | E3 ubiquitin-protein ligase RNF5 | |||
Sequence: AAAEEEDGGPEGPNRERGGASATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPDRQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDAGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGAGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI | ||||||
Modified residue | 84 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 94 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 107 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for zinc finger, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 27-68 | RING-type | ||||
Sequence: CNICLETAREAVVSVCGHLYCWPCLHQWLETRPDRQECPVCK | ||||||
Region | 79-110 | Disordered | ||||
Sequence: LYGRGSQKPQDPRLKTPPRPQGQRPAPESRGG |
Sequence similarities
Belongs to the RNF5 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length180
- Mass (Da)19,837
- Last updated1998-01-01 v1
- Checksum3C00A30201F590CB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF030001 EMBL· GenBank· DDBJ | AAB82008.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC016449 EMBL· GenBank· DDBJ | AAH16449.1 EMBL· GenBank· DDBJ | mRNA |