UniProt ID: G8JL17 |
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000256|RuleBase:RU201113}. 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:RU201113}; PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU201113}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity. {ECO:0000256|RuleBase:RU201113}. DOMAIN: The SBD domain (substrate-binding domain) mediates the interaction with substrate proteins. It is related to the TRAF family. {ECO:0000256|RuleBase:RU201113}. SIMILARITY: Belongs to the SINA (Seven in absentia) family. {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}. |
UniProt ID: Q7SYL3 |
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. Induces cellular growth arrest by inhibiting the G2/M transition (PubMed:15055544). May play a role in the regulation of the cellular clock function (By similarity). {ECO:0000250|UniProtKB:O43255, ECO:0000269|PubMed:15055544}. 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; PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43255}. TISSUE SPECIFICITY: In embryos it is expressed in all blastomeres starting at the mid-blastulla. After 20 somite stage, it is expressed mainly in the posterior part. Expressed in brain, including the eye, the cranial cavity, otic vesicle, optic chiasm and in the gut. {ECO:0000269|PubMed:12915316}. DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. {ECO:0000269|PubMed:12915316}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity. {ECO:0000250}. DOMAIN: The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family. {ECO:0000269|PubMed:15055544}. SIMILARITY: Belongs to the SINA (Seven in absentia) family. {ECO:0000305}. |
UniProt ID: A0A8M2BHM7 |
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. {ECO:0000256|RuleBase:RU201113}. 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:RU201113}; PATHWAY: Protein modification; protein ubiquitination. {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU201113}. DOMAIN: The RING-type zinc finger domain is essential for ubiquitin ligase activity. {ECO:0000256|RuleBase:RU201113}. DOMAIN: The SBD domain (substrate-binding domain) mediates the interaction with substrate proteins. It is related to the TRAF family. {ECO:0000256|RuleBase:RU201113}. SIMILARITY: Belongs to the SINA (Seven in absentia) family. {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |