GenomeNet

Database: UniProt
Entry: P39940
LinkDB: P39940
Original site: P39940 
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   29-SEP-2021, entry version 213.
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RL   Unpublished observations (FEB-1993).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}.
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   SMR; P39940; -.
DR   BioGRID; 36869; 1257.
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; RAHQSRM; -.
DR   BRENDA; 2.3.2.26; 984.
DR   Reactome; R-SCE-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-SCE-9013406; RHOQ 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: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:0006333; P:chromatin assembly or disassembly; 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:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
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: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:0042493; P:response to drug; 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
//
DBGET integrated database retrieval system