UniProt ID: Q1L8L6 |
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death. {ECO:0000250|UniProtKB:Q6ZMZ0}. 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:O60260}; PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Interacts with UBE2L3, UBE2L6 and UCKL1. {ECO:0000250|UniProtKB:Q6ZMZ0}. SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. DOMAIN: The first IBR-type zinc finger is the most crucial for interaction with UBE2L3, UBE2L6 and UCKL1. {ECO:0000250|UniProtKB:Q6ZMZ0}. 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 domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain. {ECO:0000250|UniProtKB:O60260}. SIMILARITY: Belongs to the RBR family. RNF19 subfamily. {ECO:0000305}. SEQUENCE CAUTION: Sequence=CAK11317.1; Type=Erroneous initiation; Evidence={ECO:0000305}; |
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