E3 ubiquitin-protein ligase RSP5

UniProtKB accession:  P39940

Grouped By:  Matching UniProtKB accession

UniProtKB description:  E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:19920177, PubMed:7708685, PubMed:15933713, PubMed:30893611). Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other cell surface proteins like GAP1, FUR4, MAL61, PMA1 and STE2 (PubMed:8596462). The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription, pressure-induced differential regulation of the two tryptophan permeases TAT1 and TAT2 and sorting efficiency into multivesicular bodies (PubMed:15247235, PubMed:16864574, PubMed:17079730, PubMed:14560004, PubMed:12821147, PubMed:15020711, PubMed:9931424). The RSP5-UBA1-UBC5 ubiquitin ligase complex ubiquitinates RPO21 forming 'Lys-63'-linked polyubiquitin chains (PubMed:19920177, PubMed:9858558). Plays a role in tolerance to o-dinitrobenzene (PubMed:12163175). Involved in actin cytoskeleton organization and dynamics (PubMed:22000681). Ubiquitinates the LAS17-binding proteins LSB1 and PIN3/LSB2 without directing them for degradation and affects LAS17 levels in a SLA1-dependent and LSB1/2-independent manner (PubMed:22000681). Also involved in the degradation of non-functional 18S rRNAs in response to stalled ribosomes by mediating polyubiquitination of monoubiquitinated RPS3/uS3: mediates formation of 'Lys-63'-linked polyubiquitin chains on monoubiquitined RPS3/uS3, promoting the degradation of non-functional 18S rRNAs (PubMed:30893611).