RSP5_YEAST
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 03-AUG-2022, entry version 216.
DE RecName: Full=E3 ubiquitin-protein ligase RSP5;
DE EC=2.3.2.26;
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RL Unpublished observations (FEB-1993).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 CHARACTERIZATION.
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 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 [21]
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 [22]
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 [23]
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. Component of a
CC RSP5 ubiquitin ligase complex which specifies polyubiquitination and
CC intracellular trafficking of the general amino acid permease GAP1 as
CC well as other cell surface proteins like GAP1, FUR4, MAL61, PMA1 and
CC STE2. The RSP5-BUL1/2 complex is also necessary for the heat-shock
CC element (HSE)-mediated gene expression, nitrogen starvation GLN3-
CC dependent transcription, pressure-induced differential regulation of
CC the two tryptophan permeases TAT1 and TAT2 and sorting efficiency into
CC multivesicular bodies. Also acts on RBP1. Plays a role in tolerance to
CC o-dinitrobenzene. Involved in actin cytoskeleton organization and
CC dynamics. Ubiquitinates the LAS17-binding proteins LSB1 and PIN3/LSB2
CC without directing them for degradation and affects LAS17 levels in a
CC SLA1-dependent and LSB1/2-independent manner.
CC {ECO:0000269|PubMed:12163175, ECO:0000269|PubMed:12821147,
CC ECO:0000269|PubMed:14560004, ECO:0000269|PubMed:15020711,
CC ECO:0000269|PubMed:15247235, ECO:0000269|PubMed:15933713,
CC ECO:0000269|PubMed:16864574, ECO:0000269|PubMed:17079730,
CC ECO:0000269|PubMed:22000681, ECO:0000269|PubMed:7708685,
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the RSP5-BUL1/2 ubiquitin ligase complex composed
CC of at least RSP5 and BUL1 or BUL2. Forms also a ternary complex with
CC RUP1 and UBP2. Interacts (via WW domains) with LSB1, PIN3/LSB2 and RCR1
CC (via PY motifs). Interacts with HSE1, LAS17, ROG3, ROD1 and RVS167.
CC {ECO:0000269|PubMed:12163175, ECO:0000269|PubMed:15086794,
CC ECO:0000269|PubMed:15933713, ECO:0000269|PubMed:17079730,
CC ECO:0000269|PubMed:17213653, ECO:0000269|PubMed:21399621,
CC ECO:0000269|PubMed:22000681, ECO:0000269|PubMed:8668140,
CC ECO:0000269|PubMed:9931424}.
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}.
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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; 1261.
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 iPTMnet; P39940; -.
DR MaxQB; P39940; -.
DR PaxDb; P39940; -.
DR PRIDE; P39940; -.
DR EnsemblFungi; YER125W_mRNA; YER125W; YER125W.
DR GeneID; 856862; -.
DR KEGG; sce:YER125W; -.
DR SGD; S000000927; RSP5.
DR VEuPathDB; FungiDB:YER125W; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR InParanoid; P39940; -.
DR OMA; FNAFITG; -.
DR BioCyc; YEAST:G3O-30288-MON; -.
DR BRENDA; 2.3.2.26; 984.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
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:0010008; C:endosome membrane; IDA:SGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma 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:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0034644; P:cellular response to UV; IMP: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: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; IC:ComplexPortal.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IPI:SGD.
DR GO; GO:0051865; P:protein autoubiquitination; IGI:SGD.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
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:0031384; P:regulation of initiation of mating projection growth; 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:0009410; P:response to xenobiotic stimulus; 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; 2.60.40.150; -; 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 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; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 3.
DR SUPFAM; SSF56204; SSF56204; 1.
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
