ID RSP5_YEAST Reviewed; 809 AA. AC P39940; D3DM31; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 225. DE RecName: Full=E3 ubiquitin-protein ligase RSP5; DE EC=2.3.2.26 {ECO:0000305|PubMed:19920177, ECO:0000305|PubMed:30893611}; DE AltName: Full=HECT-type E3 ubiquitin transferase RSP5; DE AltName: Full=Reverses SPT-phenotype protein 5; GN Name=RSP5; Synonyms=MDP1, NPI1; OrderedLocusNames=YER125W; GN ORFNames=SYGP-ORF41; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP IDENTIFICATION. RA Winston F.; RL Unpublished observations (FEB-1993). RN [4] RP FUNCTION. RC STRAIN=Sigma 1278B; RX PubMed=8596462; DOI=10.1111/j.1365-2958.1995.mmi_18010077.x; RA Hein C., Springael J.-Y., Volland C., Haguenauer-Tsapis R., Andre B.; RT "NPI1, an essential yeast gene involved in induced degradation of Gap1 and RT Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase."; RL Mol. Microbiol. 18:77-87(1995). RN [5] RP FUNCTION. RX PubMed=7708685; DOI=10.1073/pnas.92.7.2563; RA Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.; RT "A family of proteins structurally and functionally related to the E6-AP RT ubiquitin-protein ligase."; RL Proc. Natl. Acad. Sci. U.S.A. 92:2563-2567(1995). RN [6] RP ERRATUM OF PUBMED:7708685. RX PubMed=7761480; DOI=10.1073/pnas.92.11.5249-b; RA Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.; RL Proc. Natl. Acad. Sci. U.S.A. 92:5249-5249(1995). RN [7] RP INTERACTION WITH BUL1. RX PubMed=8668140; DOI=10.1128/mcb.16.7.3255; RA Yashiroda H., Oguchi T., Yasuda Y., Toh-e A., Kikuchi Y.; RT "Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in RT Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 16:3255-3263(1996). RN [8] RP FUNCTION, AND INTERACTION WITH BUL1 AND BUL2. RX PubMed=9931424; DOI=10.1016/s0378-1119(98)00535-6; RA Yashiroda H., Kaida D., Toh-e A., Kikuchi Y.; RT "The PY-motif of Bul1 protein is essential for growth of Saccharomyces RT cerevisiae under various stress conditions."; RL Gene 225:39-46(1998). RN [9] RP FUNCTION, AND MUTAGENESIS OF LEU-733 AND CYS-777. RC STRAIN=S288c / FY56; RX PubMed=9858558; DOI=10.1128/mcb.19.1.342; RA Wang G., Yang J., Huibregtse J.M.; RT "Functional domains of the rsp5 ubiquitin-protein ligase."; RL Mol. Cell. Biol. 19:342-352(1999). RN [10] RP FUNCTION, AND INTERACTION WITH ROD1 AND ROG3. RX PubMed=12163175; DOI=10.1016/s0014-5793(02)03104-6; RA Andoh T., Hirata Y., Kikuchi A.; RT "PY motifs of Rod1 are required for binding to Rsp5 and for drug RT resistance."; RL FEBS Lett. 525:131-134(2002). RN [11] RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX. RX PubMed=12821147; DOI=10.1016/s0006-291x(03)01090-8; RA Kaida D., Toh-e A., Kikuchi Y.; RT "Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in RT budding yeast."; RL Biochem. Biophys. Res. Commun. 306:1037-1041(2003). RN [12] RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX. RX PubMed=14560004; DOI=10.1128/mcb.23.21.7566-7584.2003; RA Abe F., Iida H.; RT "Pressure-induced differential regulation of the two tryptophan permeases RT Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and RT Bul2."; RL Mol. Cell. Biol. 23:7566-7584(2003). RN [13] RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX. RX PubMed=15247235; DOI=10.1074/jbc.m407372200; RA Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B., RA Primig M., Hall M.N.; RT "NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent RT transcription in Saccharomyces cerevisiae."; RL J. Biol. Chem. 279:37512-37517(2004). RN [14] RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX. RX PubMed=15020711; DOI=10.1091/mbc.e03-10-0727; RA Pizzirusso M., Chang A.; RT "Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, RT to the endosomal/vacuolar system in yeast."; RL Mol. Biol. Cell 15:2401-2409(2004). RN [15] RP INTERACTION WITH HSE1. RX PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x; RA Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., RA Stevens T.H.; RT "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces RT cerevisiae."; RL Traffic 5:194-210(2004). RN [16] RP FUNCTION, AND INTERACTION WITH RUP1 AND UBP2. RX PubMed=15933713; DOI=10.1038/sj.emboj.7600710; RA Kee Y., Lyon N., Huibregtse J.M.; RT "The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 RT deubiquitinating enzyme."; RL EMBO J. 24:2414-2424(2005). RN [17] RP FUNCTION OF THE RSP5-BUL1/2 COMPLEX. RX PubMed=16864574; DOI=10.1074/jbc.m605551200; RA Feller A., Boeckstaens M., Marini A.-M., Dubois E.; RT "Transduction of the nitrogen signal activating Gln3-mediated transcription RT is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in RT Saccharomyces cerevisiae."; RL J. Biol. Chem. 281:28546-28554(2006). RN [18] RP INTERACTION WITH RCR1. RX PubMed=17213653; DOI=10.1271/bbb.60446; RA Imai K., Noda Y., Adachi H., Yoda K.; RT "Peculiar protein-protein interactions of the novel endoplasmic reticulum RT membrane protein Rcr1 and ubiquitin ligase Rsp5."; RL Biosci. Biotechnol. Biochem. 71:249-252(2007). RN [19] RP FUNCTION, AND INTERACTION WITH HSE1. RX PubMed=17079730; DOI=10.1091/mbc.e06-06-0557; RA Ren J., Kee Y., Huibregtse J.M., Piper R.C.; RT "Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, RT associates with ubiquitin peptidases and a ligase to control sorting RT efficiency into multivesicular bodies."; RL Mol. Biol. Cell 18:324-335(2007). RN [20] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE RSP5-UBA1-UBC5 RP UBIQUITIN LIGASE COMPLEX, AND INTERACTION WITH UBP2. RX PubMed=19920177; DOI=10.1073/pnas.0907052106; RA Harreman M., Taschner M., Sigurdsson S., Anindya R., Reid J., Somesh B., RA Kong S.E., Banks C.A., Conaway R.C., Conaway J.W., Svejstrup J.Q.; RT "Distinct ubiquitin ligases act sequentially for RNA polymerase II RT polyubiquitylation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:20705-20710(2009). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [22] RP FUNCTION, INTERACTION WITH LAS17; LSB1; LSB2 AND RVS167, AND SUBCELLULAR RP LOCATION. RX PubMed=22000681; DOI=10.1016/j.ejcb.2011.08.002; RA Kaminska J., Spiess M., Stawiecka-Mirota M., Monkaityte R., RA Haguenauer-Tsapis R., Urban-Grimal D., Winsor B., Zoladek T.; RT "Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo and in RT vitro."; RL Eur. J. Cell Biol. 90:1016-1028(2011). RN [23] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [24] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=30893611; DOI=10.1016/j.celrep.2019.02.067; RA Sugiyama T., Li S., Kato M., Ikeuchi K., Ichimura A., Matsuo Y., Inada T.; RT "Sequential ubiquitination of ribosomal protein uS3 triggers the RT degradation of non-functional 18S rRNA."; RL Cell Rep. 26:3400-3415(2019). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 384-809 IN COMPLEX WITH RP UBIQUITIN. RX PubMed=21399621; DOI=10.1038/embor.2011.23; RA Kim H.C., Steffen A.M., Oldham M.L., Chen J., Huibregtse J.M.; RT "Structure and function of a HECT domain ubiquitin-binding site."; RL EMBO Rep. 12:334-341(2011). CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then CC directly transfers the ubiquitin to targeted substrates CC (PubMed:19920177, PubMed:7708685, PubMed:15933713, PubMed:30893611). CC Component of a RSP5 ubiquitin ligase complex which specifies CC polyubiquitination and intracellular trafficking of the general amino CC acid permease GAP1 as well as other cell surface proteins like GAP1, CC FUR4, MAL61, PMA1 and STE2 (PubMed:8596462). The RSP5-BUL1/2 complex is CC also necessary for the heat-shock element (HSE)-mediated gene CC expression, nitrogen starvation GLN3-dependent transcription, pressure- CC induced differential regulation of the two tryptophan permeases TAT1 CC and TAT2 and sorting efficiency into multivesicular bodies CC (PubMed:15247235, PubMed:16864574, PubMed:17079730, PubMed:14560004, CC PubMed:12821147, PubMed:15020711, PubMed:9931424). The RSP5-UBA1-UBC5 CC ubiquitin ligase complex ubiquitinates RPO21 forming 'Lys-63'-linked CC polyubiquitin chains (PubMed:19920177, PubMed:9858558). Plays a role in CC tolerance to o-dinitrobenzene (PubMed:12163175). Involved in actin CC cytoskeleton organization and dynamics (PubMed:22000681). Ubiquitinates CC the LAS17-binding proteins LSB1 and PIN3/LSB2 without directing them CC for degradation and affects LAS17 levels in a SLA1-dependent and CC LSB1/2-independent manner (PubMed:22000681). Also involved in the CC degradation of non-functional 18S rRNAs in response to stalled CC ribosomes by mediating polyubiquitination of monoubiquitinated CC RPS3/uS3: mediates formation of 'Lys-63'-linked polyubiquitin chains on CC monoubiquitined RPS3/uS3, promoting the degradation of non-functional CC 18S rRNAs (PubMed:30893611). {ECO:0000269|PubMed:12163175, CC ECO:0000269|PubMed:12821147, ECO:0000269|PubMed:14560004, CC ECO:0000269|PubMed:15020711, ECO:0000269|PubMed:15247235, CC ECO:0000269|PubMed:15933713, ECO:0000269|PubMed:16864574, CC ECO:0000269|PubMed:17079730, ECO:0000269|PubMed:19920177, CC ECO:0000269|PubMed:22000681, ECO:0000269|PubMed:30893611, CC ECO:0000269|PubMed:7708685, ECO:0000269|PubMed:8596462, CC ECO:0000269|PubMed:9858558, ECO:0000269|PubMed:9931424}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.26; Evidence={ECO:0000305|PubMed:19920177, CC ECO:0000305|PubMed:30893611}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:30893611}. CC -!- SUBUNIT: Component of the RSP5-BUL1/2 ubiquitin ligase complex composed CC of at least RSP5 and BUL1 or BUL2 (PubMed:8668140, PubMed:9931424). CC Component of the RSP5-UBA1-UBC5 ubiquitin ligase complex composed of E3 CC RSP5, E1 UBA1 and E2 UBC5 (Probable). Forms also a ternary complex with CC RUP1 and UBP2 (PubMed:15933713). Interacts (via WW domains) with LSB1 CC (PubMed:22000681). Interacts (via WW domains) with PIN3/LSB2 CC (PubMed:22000681). Interacts (via WW domains) with RCR1 (via PY motifs) CC (PubMed:17213653). Interacts with UBP2; the interaction is direct CC (PubMed:19920177). Interacts with HSE1 (PubMed:15086794, CC PubMed:17079730). Interacts with LAS17 (PubMed:22000681). Interacts CC with ROG3 (PubMed:12163175). Interacts with ROD1 (PubMed:12163175). CC Interacts with RVS167 (PubMed:22000681). Interacts with ubiquitin CC (PubMed:21399621). {ECO:0000269|PubMed:12163175, CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:15933713, CC ECO:0000269|PubMed:17079730, ECO:0000269|PubMed:17213653, CC ECO:0000269|PubMed:19920177, ECO:0000269|PubMed:21399621, CC ECO:0000269|PubMed:22000681, ECO:0000269|PubMed:8668140, CC ECO:0000269|PubMed:9931424, ECO:0000305|PubMed:19920177}. CC -!- INTERACTION: CC P39940; Q07622: ACK1; NbExp=3; IntAct=EBI-16219, EBI-38674; CC P39940; P80210: ADE12; NbExp=2; IntAct=EBI-16219, EBI-14267; CC P39940; P36117: ALY1; NbExp=4; IntAct=EBI-16219, EBI-26358; CC P39940; P47029: ALY2; NbExp=5; IntAct=EBI-16219, EBI-25974; CC P39940; P18634: ART10; NbExp=5; IntAct=EBI-16219, EBI-27197; CC P39940; P53244: ART5; NbExp=4; IntAct=EBI-16219, EBI-23201; CC P39940; Q05979: BNA5; NbExp=2; IntAct=EBI-16219, EBI-10016; CC P39940; P48524: BUL1; NbExp=4; IntAct=EBI-16219, EBI-3881; CC P39940; Q00684: CDC14; NbExp=2; IntAct=EBI-16219, EBI-4192; CC P39940; Q12734: CSR2; NbExp=2; IntAct=EBI-16219, EBI-32379; CC P39940; P15202: CTA1; NbExp=2; IntAct=EBI-16219, EBI-4061; CC P39940; Q08412: CUE5; NbExp=3; IntAct=EBI-16219, EBI-37580; CC P39940; P54005: DIA1; NbExp=3; IntAct=EBI-16219, EBI-27668; CC P39940; P53759: DUS1; NbExp=2; IntAct=EBI-16219, EBI-27885; CC P39940; P38167: ECM21; NbExp=2; IntAct=EBI-16219, EBI-21359; CC P39940; P00925: ENO2; NbExp=2; IntAct=EBI-16219, EBI-6475; CC P39940; P36141: FMP46; NbExp=2; IntAct=EBI-16219, EBI-26445; CC P39940; P06738: GPH1; NbExp=2; IntAct=EBI-16219, EBI-13389; CC P39940; P32347: HEM12; NbExp=2; IntAct=EBI-16219, EBI-5711; CC P39940; P53051: IMA1; NbExp=2; IntAct=EBI-16219, EBI-10464; CC P39940; P00817: IPP1; NbExp=2; IntAct=EBI-16219, EBI-9338; CC P39940; Q12502: LDB19; NbExp=3; IntAct=EBI-16219, EBI-2113927; CC P39940; P53281: LSB1; NbExp=2; IntAct=EBI-16219, EBI-23329; CC P39940; P38998: LYS1; NbExp=3; IntAct=EBI-16219, EBI-10264; CC P39940; P49367: LYS4; NbExp=2; IntAct=EBI-16219, EBI-10276; CC P39940; P36060: MCR1; NbExp=2; IntAct=EBI-16219, EBI-10565; CC P39940; P30952: MLS1; NbExp=3; IntAct=EBI-16219, EBI-10428; CC P39940; Q01560: NPL3; NbExp=2; IntAct=EBI-16219, EBI-12114; CC P39940; P39683: NPT1; NbExp=2; IntAct=EBI-16219, EBI-12218; CC P39940; P10963: PCK1; NbExp=2; IntAct=EBI-16219, EBI-13770; CC P39940; P16862: PFK2; NbExp=3; IntAct=EBI-16219, EBI-9435; CC P39940; P36069: PMU1; NbExp=2; IntAct=EBI-16219, EBI-26862; CC P39940; P25044: PTP1; NbExp=2; IntAct=EBI-16219, EBI-14183; CC P39940; P11154: PYC1; NbExp=2; IntAct=EBI-16219, EBI-14358; CC P39940; P38212: RCR1; NbExp=3; IntAct=EBI-16219, EBI-21381; CC P39940; Q03446: RCR2; NbExp=2; IntAct=EBI-16219, EBI-18180; CC P39940; Q00453: RGM1; NbExp=2; IntAct=EBI-16219, EBI-15073; CC P39940; Q02805: ROD1; NbExp=3; IntAct=EBI-16219, EBI-15679; CC P39940; P43602: ROG3; NbExp=3; IntAct=EBI-16219, EBI-22976; CC P39940; P20436: RPB8; NbExp=3; IntAct=EBI-16219, EBI-15794; CC P39940; P14359: SNA3; NbExp=2; IntAct=EBI-16219, EBI-26122; CC P39940; Q07549: SNA4; NbExp=2; IntAct=EBI-16219, EBI-22078; CC P39940; P39015: STM1; NbExp=3; IntAct=EBI-16219, EBI-11238; CC P39940; Q07748: THI13; NbExp=2; IntAct=EBI-16219, EBI-36080; CC P39940; Q08975: THI21; NbExp=3; IntAct=EBI-16219, EBI-30327; CC P39940; P43534: THI5; NbExp=2; IntAct=EBI-16219, EBI-19221; CC P39940; P23254: TKL1; NbExp=2; IntAct=EBI-16219, EBI-19291; CC P39940; Q08919: TRE1; NbExp=3; IntAct=EBI-16219, EBI-31915; CC P39940; Q12162: TY1A-PL; NbExp=2; IntAct=EBI-16219, EBI-36658; CC P39940; Q12472: TY2B-DR1; NbExp=2; IntAct=EBI-16219, EBI-35737; CC P39940; P33296: UBC6; NbExp=2; IntAct=EBI-16219, EBI-19745; CC P39940; P38081: YBR056W; NbExp=3; IntAct=EBI-16219, EBI-21453; CC P39940; P25561: YCL021W; NbExp=3; IntAct=EBI-16219, EBI-21696; CC P39940; P38835: YHR131C; NbExp=3; IntAct=EBI-16219, EBI-24724; CC P39940; P53108: YIP5; NbExp=2; IntAct=EBI-16219, EBI-24051; CC P39940; P40892: YJL218W; NbExp=2; IntAct=EBI-16219, EBI-26263; CC P39940; P47137: YJR096W; NbExp=3; IntAct=EBI-16219, EBI-25572; CC P39940; P36140: YKR047W; NbExp=2; IntAct=EBI-16219, EBI-26441; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22000681}. Nucleus CC {ECO:0000305}. Cytoplasm, cytoskeleton, actin patch CC {ECO:0000269|PubMed:22000681}. CC -!- PTM: The ubiquitination appears to be the result of an intramolecular CC transfer of ubiquitin. CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester CC formation. CC -!- SIMILARITY: Belongs to the RSP5/NEDD4 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U18916; AAC03223.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07785.1; -; Genomic_DNA. DR PIR; S43217; S43217. DR RefSeq; NP_011051.3; NM_001179015.3. DR PDB; 3OLM; X-ray; 2.50 A; A=384-809. DR PDB; 4LCD; X-ray; 3.10 A; A/B=383-809. DR PDB; 5HPL; X-ray; 2.31 A; A/B=430-809. DR PDBsum; 3OLM; -. DR PDBsum; 4LCD; -. DR PDBsum; 5HPL; -. DR AlphaFoldDB; P39940; -. DR SMR; P39940; -. DR BioGRID; 36869; 1268. DR ComplexPortal; CPX-2921; RSP5-BUL1 ubiquitin ligase complex. DR ComplexPortal; CPX-2923; RSP5-BUL2 ubiquitin ligase complex. DR DIP; DIP-2238N; -. DR ELM; P39940; -. DR IntAct; P39940; 189. DR MINT; P39940; -. DR STRING; 4932.YER125W; -. DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family. DR TCDB; 8.A.30.1.4; the nedd4-family interacting protein-2 (nedd4) family. DR GlyGen; P39940; 13 sites, 1 O-linked glycan (13 sites). DR iPTMnet; P39940; -. DR MaxQB; P39940; -. DR PaxDb; 4932-YER125W; -. DR PeptideAtlas; P39940; -. DR EnsemblFungi; YER125W_mRNA; YER125W; YER125W. DR GeneID; 856862; -. DR KEGG; sce:YER125W; -. DR AGR; SGD:S000000927; -. DR SGD; S000000927; RSP5. DR VEuPathDB; FungiDB:YER125W; -. DR eggNOG; KOG0940; Eukaryota. DR HOGENOM; CLU_002173_0_0_1; -. DR InParanoid; P39940; -. DR OMA; DNYTIQI; -. DR OrthoDB; 5480520at2759; -. DR BioCyc; YEAST:G3O-30288-MONOMER; -. DR BRENDA; 2.3.2.26; 984. DR Reactome; R-SCE-9013406; RHOQ GTPase cycle. DR Reactome; R-SCE-9013420; RHOU GTPase cycle. DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 856862; 7 hits in 10 CRISPR screens. DR EvolutionaryTrace; P39940; -. DR PRO; PR:P39940; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P39940; Protein. DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell. DR GO; GO:0005934; C:cellular bud tip; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:0010008; C:endosome membrane; IDA:SGD. DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0005886; C:plasma membrane; HDA:SGD. DR GO; GO:1990306; C:RSP5-BUL ubiquitin ligase complex; IPI:ComplexPortal. DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI. DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:SGD. DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD. DR GO; GO:0006325; P:chromatin organization; IMP:SGD. DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD. DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD. DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD. DR GO; GO:0070651; P:nonfunctional rRNA decay; IDA:UniProt. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD. DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD. DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:SGD. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD. DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; NAS:ComplexPortal. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IPI:SGD. DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:SGD. DR GO; GO:0010794; P:regulation of dolichol biosynthetic process; IMP:SGD. DR GO; GO:0032443; P:regulation of ergosterol biosynthetic process; IMP:SGD. DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:SGD. DR GO; GO:0010796; P:regulation of multivesicular body size; IMP:SGD. DR GO; GO:0006808; P:regulation of nitrogen utilization; IGI:SGD. DR GO; GO:0019220; P:regulation of phosphate metabolic process; IGI:SGD. DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD. DR GO; GO:2000203; P:regulation of ribosomal large subunit export from nucleus; IMP:SGD. DR GO; GO:2000232; P:regulation of rRNA processing; IMP:SGD. DR GO; GO:2000238; P:regulation of tRNA export from nucleus; IMP:SGD. DR GO; GO:2000235; P:regulation of tRNA processing; IMP:SGD. DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IMP:SGD. DR GO; GO:0034517; P:ribophagy; IGI:SGD. DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:SGD. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD. DR CDD; cd00078; HECTc; 1. DR CDD; cd00201; WW; 3. DR Gene3D; 2.20.70.10; -; 2. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1. DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR024928; E3_ub_ligase_SMURF1. DR InterPro; IPR000569; HECT_dom. DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1. DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00632; HECT; 1. DR Pfam; PF00397; WW; 3. DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00456; WW; 3. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1. DR SUPFAM; SSF51045; WW domain; 3. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50237; HECT; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 3. DR PROSITE; PS50020; WW_DOMAIN_2; 3. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Cytoskeleton; Isopeptide bond; Nucleus; KW Reference proteome; Repeat; Transferase; Ubl conjugation; KW Ubl conjugation pathway. FT CHAIN 1..809 FT /note="E3 ubiquitin-protein ligase RSP5" FT /id="PRO_0000120335" FT DOMAIN 1..105 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 229..262 FT /note="WW 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 331..364 FT /note="WW 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 387..420 FT /note="WW 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 705..809 FT /note="HECT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104" FT REGION 99..122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 139..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 257..298 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 103..119 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 139..225 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 257..277 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 777 FT /note="Glycyl thioester intermediate" FT CROSSLNK 258 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT MUTAGEN 516 FT /note="Y->A: Has subtle defects on both initial FT ubiquitination and chain elongation of substrate proteins." FT MUTAGEN 521 FT /note="Y->A: Has defects on both initial ubiquitination and FT chain elongation of substrate proteins." FT MUTAGEN 537 FT /note="I->D: Has defects on both initial ubiquitination and FT chain elongation of substrate proteins." FT MUTAGEN 618 FT /note="F->D: Has defects on both initial ubiquitination and FT chain elongation of substrate proteins." FT MUTAGEN 733 FT /note="L->S: In RSP5-1; impairs ubiquitin-thioester FT formation and catalysis of substrate ubiquitination." FT /evidence="ECO:0000269|PubMed:9858558" FT MUTAGEN 777 FT /note="C->A: Loss of ubiquitination." FT /evidence="ECO:0000269|PubMed:9858558" FT STRAND 393..396 FT /evidence="ECO:0007829|PDB:4LCD" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:3OLM" FT TURN 408..411 FT /evidence="ECO:0007829|PDB:3OLM" FT STRAND 412..416 FT /evidence="ECO:0007829|PDB:3OLM" FT HELIX 435..443 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 451..459 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 461..463 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 464..473 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 479..481 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 482..488 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 496..511 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 514..516 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 517..521 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 526..531 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 535..537 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 541..557 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 568..574 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 581..586 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 589..600 FT /evidence="ECO:0007829|PDB:5HPL" FT TURN 604..606 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 610..617 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 620..627 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 630..632 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 633..635 FT /evidence="ECO:0007829|PDB:4LCD" FT TURN 637..639 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 640..652 FT /evidence="ECO:0007829|PDB:5HPL" FT TURN 653..656 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 657..668 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 673..676 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 681..689 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 696..701 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 703..708 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 713..724 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 727..738 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 748..750 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 754..757 FT /evidence="ECO:0007829|PDB:4LCD" FT STRAND 760..763 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 773..775 FT /evidence="ECO:0007829|PDB:5HPL" FT TURN 776..779 FT /evidence="ECO:0007829|PDB:5HPL" FT STRAND 780..782 FT /evidence="ECO:0007829|PDB:5HPL" FT HELIX 789..801 FT /evidence="ECO:0007829|PDB:5HPL" SQ SEQUENCE 809 AA; 91816 MW; 6F1836384479E70F CRC64; MPSSISVKLV AAESLYKRDV FRSPDPFAVL TIDGYQTKST SAAKKTLNPY WNETFKFDDI NENSILTIQV FDQKKFKKKD QGFLGVVNVR VGDVLGHLDE DTATSSGRPR EETITRDLKK SNDGMAVSGR LIVVLSKLPS SSPHSQAPSG HTASSSTNTS STTRTNGHST SSTRNHSTSH PSRGTAQAVE STLQSGTTAA TNTATTSHRS TNSTSSATRQ YSSFEDQYGR LPPGWERRTD NFGRTYYVDH NTRTTTWKRP TLDQTEAERG NQLNANTELE RRQHRGRTLP GGSSDNSSVT VQVGGGSNIP PVNGAAAAAF AATGGTTSGL GELPSGWEQR FTPEGRAYFV DHNTRTTTWV DPRRQQYIRT YGPTNTTIQQ QPVSQLGPLP SGWEMRLTNT ARVYFVDHNT KTTTWDDPRL PSSLDQNVPQ YKRDFRRKVI YFRSQPALRI LPGQCHIKVR RKNIFEDAYQ EIMRQTPEDL KKRLMIKFDG EEGLDYGGVS REFFFLLSHE MFNPFYCLFE YSAYDNYTIQ INPNSGINPE HLNYFKFIGR VVGLGVFHRR FLDAFFVGAL YKMMLRKKVV LQDMEGVDAE VYNSLNWMLE NSIDGVLDLT FSADDERFGE VVTVDLKPDG RNIEVTDGNK KEYVELYTQW RIVDRVQEQF KAFMDGFNEL IPEDLVTVFD ERELELLIGG IAEIDIEDWK KHTDYRGYQE SDEVIQWFWK CVSEWDNEQR ARLLQFTTGT SRIPVNGFKD LQGSDGPRRF TIEKAGEVQQ LPKSHTCFNR VDLPQYVDYD SMKQKLTLAV EETIGFGQE //