Q8CHG5 · AREL1_MOUSE
- ProteinApoptosis-resistant E3 ubiquitin protein ligase 1
- GeneArel1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids823 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase that catalyzes 'Lys-11'- or 'Lys-33'-linked polyubiquitin chains, with some preference for 'Lys-33' linkages (By similarity).
E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity).
Ubiquitinates SEPTIN4, DIABLO/SMAC and HTRA2 in vitro (By similarity).
Modulates pulmonary inflammation by targeting SOCS2 for ubiquitination and subsequent degradation by the proteasome (PubMed:31578312).
E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity).
Ubiquitinates SEPTIN4, DIABLO/SMAC and HTRA2 in vitro (By similarity).
Modulates pulmonary inflammation by targeting SOCS2 for ubiquitination and subsequent degradation by the proteasome (PubMed:31578312).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 790 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | apoptotic process | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | protein K11-linked ubiquitination | |
Biological Process | protein K33-linked ubiquitination | |
Biological Process | protein polyubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of inflammatory response | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameApoptosis-resistant E3 ubiquitin protein ligase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8CHG5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Mice show significant and stepwise decreases in indicators of inflammatory injury, such as bronchoalveolar lavage fluid protein concentration and cell count, as well as decreases in pro-inflammatory cytokine release.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 36 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000120350 | 1-823 | Apoptosis-resistant E3 ubiquitin protein ligase 1 | |||
Sequence: MFYVIGGIIVSVVAFFFTIKFLFELAARVVSFLQNEDRERRGDRTIYDYVRGNYLDPRSCKVSWDWKDPYEVGHSMAFRVHLFYKNGQPFPAHRPVGLRVHISHVELAVDIPVTQEVLQEPNSNVVKVAFTVRKAGRYEITVKLGGLNVAYSPYYKIFQPGMVVPSKTKIVCHFSTLVLTCGQPHTLQIVPRDEYDNPTNNSMSLRDEHSYSLAIHELGPQEEENNEVSFEKSVTSNRQTCQVFLRLTLHSRGCFHACISYQNQPINNGEFDIIVLSENEKNIVERNVSTSGVSIYFEAYLYNANNCTSTPWHLPPMHMSSSQRRPSTAIEEDDEDSPSECHTPEKVKKPKKVYCYVSPKQFSVKEFYLKIIPWRLYTFRVCPGTKFSYLGPDPVHKLLTLVVDDGIQPPVELSCKERNILAATFIRSLHKNIGGSETFQDKVNFFQRELRQVHMKRPHSKVTLKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTSQLFARFTDSNQALVHPNPNRPAHLRLKMYEFAGRLVGKCLYESSLGGAYKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSEMELVFAEEKYNKSGQLDKIVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDINVSDFKAHAVVVGGSWHFREKVMRWFWAVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTHSTLPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGCEGFGML |
Post-translational modification
Autoubiquitinated in vitro in the presence of E2 enzyme UBE2D1/UBCH5A.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in brain, testis, heart, liver, lung and kidney with very low levels in skeletal muscle and spleen.
Gene expression databases
Structure
Family & Domains
Features
Showing features for repeat, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 64-158 | Filamin | ||||
Sequence: WDWKDPYEVGHSMAFRVHLFYKNGQPFPAHRPVGLRVHISHVELAVDIPVTQEVLQEPNSNVVKVAFTVRKAGRYEITVKLGGLNVAYSPYYKIF | ||||||
Region | 315-345 | Disordered | ||||
Sequence: PPMHMSSSQRRPSTAIEEDDEDSPSECHTPE | ||||||
Region | 483-789 | Interaction with SOCS2 | ||||
Sequence: SISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTSQLFARFTDSNQALVHPNPNRPAHLRLKMYEFAGRLVGKCLYESSLGGAYKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSEMELVFAEEKYNKSGQLDKIVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDINVSDFKAHAVVVGGSWHFREKVMRWFWAVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTHSTLPTAHT | ||||||
Domain | 483-823 | HECT | ||||
Sequence: SISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTSQLFARFTDSNQALVHPNPNRPAHLRLKMYEFAGRLVGKCLYESSLGGAYKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSEMELVFAEEKYNKSGQLDKIVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDINVSDFKAHAVVVGGSWHFREKVMRWFWAVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTHSTLPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGCEGFGML |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length823
- Mass (Da)94,199
- Last updated2005-03-29 v2
- ChecksumE74AAE76555A20D4
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 424 | in Ref. 3; AAH60658 | ||||
Sequence: T → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB093230 EMBL· GenBank· DDBJ | BAC41414.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK077015 EMBL· GenBank· DDBJ | BAC36566.1 EMBL· GenBank· DDBJ | mRNA | ||
BC049900 EMBL· GenBank· DDBJ | AAH49900.1 EMBL· GenBank· DDBJ | mRNA | ||
BC060658 EMBL· GenBank· DDBJ | AAH60658.1 EMBL· GenBank· DDBJ | mRNA |