UniProt ID: F1QJX5 |
FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues, leading to their ubiquitination and subsequent degradation (By similarity). Positively regulates hedgehog/shh-signaling pathways that function in eye development, neuronal specification and somite development (PubMed:27195754). Activation of shh up-regulates transcription of ubr3, which in turn promotes hedgehog/shh signaling possibly by controlling negative regulators such as Kif7 (PubMed:27195754). {ECO:0000250|UniProtKB:Q9W3M3, ECO:0000269|PubMed:27195754}. CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9W3M3}; PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q9W3M3}. DEVELOPMENTAL STAGE: Expressed in the embryonic retina, central nervous system and trunk (at the protein level). {ECO:0000269|PubMed:27195754}. DISRUPTION PHENOTYPE: Heterozygotes fail to form cohesive and stratified epithelium in their optic vesicles. Average somite angle is increased by 30% and the posterior central nervous system displays a gain of Rohon-Beard sensory neurons. Defects are the result of decreased Hh/shh-signaling demonstrated by the reduced expression of the Hh/shh target gene ptch2. {ECO:0000269|PubMed:27195754}. SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}. |
UniProt ID: A0A8M9Q4T2 |
FUNCTION: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. {ECO:0000256|RuleBase:RU366018}. CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900, ECO:0000256|RuleBase:RU366018}; PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|RuleBase:RU366018}. SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750, ECO:0000256|RuleBase:RU366018}. |
UniProt ID: A0A8M9QB29 |
FUNCTION: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. {ECO:0000256|RuleBase:RU366018}. CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900, ECO:0000256|RuleBase:RU366018}; PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|RuleBase:RU366018}. SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750, ECO:0000256|RuleBase:RU366018}. |
UniProt ID: A0A8M9QJY5 |
FUNCTION: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N- terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. {ECO:0000256|RuleBase:RU366018}. CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900, ECO:0000256|RuleBase:RU366018}; PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|RuleBase:RU366018}. SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750, ECO:0000256|RuleBase:RU366018}. |
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