UniProt ID: Q6PFJ9
FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 ube2l3. Acts as an atypical E3 ubiquitin- protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets. The initial ubiquitin is then elongated. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes. {ECO:0000250|UniProtKB:Q9Y4X5}.
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L- cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)- ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5};
ACTIVITY REGULATION: Autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity. Inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1. {ECO:0000250|UniProtKB:Q9Y4X5}.
PATHWAY: Protein modification; protein ubiquitination.
SUBUNIT: Interacts (via the first RING-type zinc finger) with ube2l3. Associates with cullin-RING ubiquitin ligase (CRL) complexes containing neddylated cullin. {ECO:0000250|UniProtKB:Q9Y4X5}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus {ECO:0000250|UniProtKB:Q9Y4X5}.
DOMAIN: Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger. The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate. {ECO:0000250|UniProtKB:Q9Y4X5}.
DOMAIN: The Ariadne domain inhibits activity by masking the second RING-type zinc finger that contains the active site. {ECO:0000250|UniProtKB:Q9Y4X5}.
SIMILARITY: Belongs to the RBR family. Ariadne subfamily. {ECO:0000305}.
UniProt ID: B2GS68
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L- cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)- ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000256|SAAS:SAAS01116878};
SIMILARITY: Belongs to the RBR family. {ECO:0000256|SAAS:SAAS00692262}.
UniProt ID: A0A2R8QB49
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L- cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin- conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)- ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000256|SAAS:SAAS01116878};
SIMILARITY: Belongs to the RBR family. {ECO:0000256|SAAS:SAAS00692262}.
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