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E3 ubiquitin-protein ligase RSP5 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase RSP5) (Reverses SPT-phenotype protein 5)

 RSP5_YEAST              Reviewed;         809 AA.
P39940; D3DM31;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 183.
RecName: Full=E3 ubiquitin-protein ligase RSP5;
EC=2.3.2.26;
AltName: Full=HECT-type E3 ubiquitin transferase RSP5;
AltName: Full=Reverses SPT-phenotype protein 5;
Name=RSP5; Synonyms=MDP1, NPI1; OrderedLocusNames=YER125W;
ORFNames=SYGP-ORF41;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
IDENTIFICATION.
Winston F.;
Unpublished observations (FEB-1993).
[4]
CHARACTERIZATION.
STRAIN=Sigma 1278B;
PubMed=8596462; DOI=10.1111/j.1365-2958.1995.mmi_18010077.x;
Hein C., Springael J.-Y., Volland C., Haguenauer-Tsapis R., Andre B.;
"NPI1, an essential yeast gene involved in induced degradation of Gap1
and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase.";
Mol. Microbiol. 18:77-87(1995).
[5]
FUNCTION.
PubMed=7708685; DOI=10.1073/pnas.92.7.2563;
Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.;
"A family of proteins structurally and functionally related to the E6-
AP ubiquitin-protein ligase.";
Proc. Natl. Acad. Sci. U.S.A. 92:2563-2567(1995).
[6]
ERRATUM.
PubMed=7761480; DOI=10.1073/pnas.92.11.5249-b;
Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.;
Proc. Natl. Acad. Sci. U.S.A. 92:5249-5249(1995).
[7]
INTERACTION WITH BUL1.
PubMed=8668140; DOI=10.1128/MCB.16.7.3255;
Yashiroda H., Oguchi T., Yasuda Y., Toh-e A., Kikuchi Y.;
"Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 16:3255-3263(1996).
[8]
FUNCTION, AND INTERACTION WITH BUL1 AND BUL2.
PubMed=9931424; DOI=10.1016/S0378-1119(98)00535-6;
Yashiroda H., Kaida D., Toh-e A., Kikuchi Y.;
"The PY-motif of Bul1 protein is essential for growth of Saccharomyces
cerevisiae under various stress conditions.";
Gene 225:39-46(1998).
[9]
FUNCTION, AND MUTAGENESIS OF LEU-733 AND CYS-777.
STRAIN=S288c / FY56;
PubMed=9858558; DOI=10.1128/MCB.19.1.342;
Wang G., Yang J., Huibregtse J.M.;
"Functional domains of the rsp5 ubiquitin-protein ligase.";
Mol. Cell. Biol. 19:342-352(1999).
[10]
FUNCTION, AND INTERACTION WITH ROD1 AND ROG3.
PubMed=12163175; DOI=10.1016/S0014-5793(02)03104-6;
Andoh T., Hirata Y., Kikuchi A.;
"PY motifs of Rod1 are required for binding to Rsp5 and for drug
resistance.";
FEBS Lett. 525:131-134(2002).
[11]
FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
PubMed=12821147; DOI=10.1016/S0006-291X(03)01090-8;
Kaida D., Toh-e A., Kikuchi Y.;
"Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression
in budding yeast.";
Biochem. Biophys. Res. Commun. 306:1037-1041(2003).
[12]
FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
PubMed=14560004; DOI=10.1128/MCB.23.21.7566-7584.2003;
Abe F., Iida H.;
"Pressure-induced differential regulation of the two tryptophan
permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding
proteins, Bul1 and Bul2.";
Mol. Cell. Biol. 23:7566-7584(2003).
[13]
FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
PubMed=15247235; DOI=10.1074/jbc.M407372200;
Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B.,
Primig M., Hall M.N.;
"NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent
transcription in Saccharomyces cerevisiae.";
J. Biol. Chem. 279:37512-37517(2004).
[14]
FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
PubMed=15020711; DOI=10.1091/mbc.E03-10-0727;
Pizzirusso M., Chang A.;
"Ubiquitin-mediated targeting of a mutant plasma membrane ATPase,
Pma1-7, to the endosomal/vacuolar system in yeast.";
Mol. Biol. Cell 15:2401-2409(2004).
[15]
INTERACTION WITH HSE1.
PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x;
Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P.,
Stevens T.H.;
"Protein-protein interactions of ESCRT complexes in the yeast
Saccharomyces cerevisiae.";
Traffic 5:194-210(2004).
[16]
FUNCTION, AND INTERACTION WITH RUP1 AND UBP2.
PubMed=15933713; DOI=10.1038/sj.emboj.7600710;
Kee Y., Lyon N., Huibregtse J.M.;
"The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2
deubiquitinating enzyme.";
EMBO J. 24:2414-2424(2005).
[17]
FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
PubMed=16864574; DOI=10.1074/jbc.M605551200;
Feller A., Boeckstaens M., Marini A.-M., Dubois E.;
"Transduction of the nitrogen signal activating Gln3-mediated
transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin
ligase in Saccharomyces cerevisiae.";
J. Biol. Chem. 281:28546-28554(2006).
[18]
INTERACTION WITH RCR1.
PubMed=17213653; DOI=10.1271/bbb.60446;
Imai K., Noda Y., Adachi H., Yoda K.;
"Peculiar protein-protein interactions of the novel endoplasmic
reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5.";
Biosci. Biotechnol. Biochem. 71:249-252(2007).
[19]
FUNCTION, AND INTERACTION WITH HSE1.
PubMed=17079730; DOI=10.1091/mbc.E06-06-0557;
Ren J., Kee Y., Huibregtse J.M., Piper R.C.;
"Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex,
associates with ubiquitin peptidases and a ligase to control sorting
efficiency into multivesicular bodies.";
Mol. Biol. Cell 18:324-335(2007).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[21]
FUNCTION, INTERACTION WITH LAS17; LSB1; LSB2 AND RVS167, AND
SUBCELLULAR LOCATION.
PubMed=22000681; DOI=10.1016/j.ejcb.2011.08.002;
Kaminska J., Spiess M., Stawiecka-Mirota M., Monkaityte R.,
Haguenauer-Tsapis R., Urban-Grimal D., Winsor B., Zoladek T.;
"Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo
and in vitro.";
Eur. J. Cell Biol. 90:1016-1028(2011).
[22]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[23]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 384-809 IN COMPLEX WITH
UBIQUITIN.
PubMed=21399621; DOI=10.1038/embor.2011.23;
Kim H.C., Steffen A.M., Oldham M.L., Chen J., Huibregtse J.M.;
"Structure and function of a HECT domain ubiquitin-binding site.";
EMBO Rep. 12:334-341(2011).
-!- FUNCTION: 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.
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. 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. Also acts on RBP1. Plays a role in tolerance to o-
dinitrobenzene. Involved in actin cytoskeleton organization and
dynamics. 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.
{ECO:0000269|PubMed:12163175, ECO:0000269|PubMed:12821147,
ECO:0000269|PubMed:14560004, ECO:0000269|PubMed:15020711,
ECO:0000269|PubMed:15247235, ECO:0000269|PubMed:15933713,
ECO:0000269|PubMed:16864574, ECO:0000269|PubMed:17079730,
ECO:0000269|PubMed:22000681, ECO:0000269|PubMed:7708685,
ECO:0000269|PubMed:9858558, ECO:0000269|PubMed:9931424}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Component of the RSP5-BUL1/2 ubiquitin ligase complex
composed of at least RSP5 and BUL1 or BUL2. Forms also a ternary
complex with RUP1 and UBP2. Interacts (via WW domains) with LSB1,
PIN3/LSB2 and RCR1 (via PY motifs). Interacts with HSE1, LAS17,
ROG3, ROD1 and RVS167. {ECO:0000269|PubMed:12163175,
ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:15933713,
ECO:0000269|PubMed:17079730, ECO:0000269|PubMed:17213653,
ECO:0000269|PubMed:21399621, ECO:0000269|PubMed:22000681,
ECO:0000269|PubMed:8668140, ECO:0000269|PubMed:9931424}.
-!- INTERACTION:
Q07622:ACK1; NbExp=3; IntAct=EBI-16219, EBI-38674;
P80210:ADE12; NbExp=2; IntAct=EBI-16219, EBI-14267;
P36117:ALY1; NbExp=4; IntAct=EBI-16219, EBI-26358;
P47029:ALY2; NbExp=5; IntAct=EBI-16219, EBI-25974;
P18634:ART10; NbExp=5; IntAct=EBI-16219, EBI-27197;
P53244:ART5; NbExp=4; IntAct=EBI-16219, EBI-23201;
Q05979:BNA5; NbExp=2; IntAct=EBI-16219, EBI-10016;
P48524:BUL1; NbExp=4; IntAct=EBI-16219, EBI-3881;
Q00684:CDC14; NbExp=2; IntAct=EBI-16219, EBI-4192;
Q12734:CSR2; NbExp=2; IntAct=EBI-16219, EBI-32379;
P15202:CTA1; NbExp=2; IntAct=EBI-16219, EBI-4061;
Q08412:CUE5; NbExp=3; IntAct=EBI-16219, EBI-37580;
P54005:DIA1; NbExp=3; IntAct=EBI-16219, EBI-27668;
P53759:DUS1; NbExp=2; IntAct=EBI-16219, EBI-27885;
P38167:ECM21; NbExp=2; IntAct=EBI-16219, EBI-21359;
P00925:ENO2; NbExp=2; IntAct=EBI-16219, EBI-6475;
P36141:FMP46; NbExp=2; IntAct=EBI-16219, EBI-26445;
P06738:GPH1; NbExp=2; IntAct=EBI-16219, EBI-13389;
P32347:HEM12; NbExp=2; IntAct=EBI-16219, EBI-5711;
P53051:IMA1; NbExp=2; IntAct=EBI-16219, EBI-10464;
P00817:IPP1; NbExp=2; IntAct=EBI-16219, EBI-9338;
Q12502:LDB19; NbExp=3; IntAct=EBI-16219, EBI-2113927;
P53281:LSB1; NbExp=2; IntAct=EBI-16219, EBI-23329;
P38998:LYS1; NbExp=3; IntAct=EBI-16219, EBI-10264;
P49367:LYS4; NbExp=2; IntAct=EBI-16219, EBI-10276;
P36060:MCR1; NbExp=2; IntAct=EBI-16219, EBI-10565;
P30952:MLS1; NbExp=3; IntAct=EBI-16219, EBI-10428;
Q01560:NPL3; NbExp=2; IntAct=EBI-16219, EBI-12114;
P39683:NPT1; NbExp=2; IntAct=EBI-16219, EBI-12218;
P10963:PCK1; NbExp=2; IntAct=EBI-16219, EBI-13770;
P16862:PFK2; NbExp=3; IntAct=EBI-16219, EBI-9435;
P36069:PMU1; NbExp=2; IntAct=EBI-16219, EBI-26862;
P25044:PTP1; NbExp=2; IntAct=EBI-16219, EBI-14183;
P11154:PYC1; NbExp=2; IntAct=EBI-16219, EBI-14358;
P38212:RCR1; NbExp=3; IntAct=EBI-16219, EBI-21381;
Q03446:RCR2; NbExp=2; IntAct=EBI-16219, EBI-18180;
Q00453:RGM1; NbExp=2; IntAct=EBI-16219, EBI-15073;
Q02805:ROD1; NbExp=3; IntAct=EBI-16219, EBI-15679;
P43602:ROG3; NbExp=3; IntAct=EBI-16219, EBI-22976;
P20436:RPB8; NbExp=3; IntAct=EBI-16219, EBI-15794;
P14359:SNA3; NbExp=2; IntAct=EBI-16219, EBI-26122;
Q07549:SNA4; NbExp=2; IntAct=EBI-16219, EBI-22078;
P39015:STM1; NbExp=3; IntAct=EBI-16219, EBI-11238;
Q07748:THI13; NbExp=2; IntAct=EBI-16219, EBI-36080;
Q08975:THI21; NbExp=3; IntAct=EBI-16219, EBI-30327;
P43534:THI5; NbExp=2; IntAct=EBI-16219, EBI-19221;
P23254:TKL1; NbExp=2; IntAct=EBI-16219, EBI-19291;
Q08919:TRE1; NbExp=3; IntAct=EBI-16219, EBI-31915;
Q12162:TY1A-PL; NbExp=2; IntAct=EBI-16219, EBI-36658;
Q12472:TY2B-DR1; NbExp=2; IntAct=EBI-16219, EBI-35737;
P33296:UBC6; NbExp=2; IntAct=EBI-16219, EBI-19745;
P38081:YBR056W; NbExp=3; IntAct=EBI-16219, EBI-21453;
P25561:YCL021W; NbExp=3; IntAct=EBI-16219, EBI-21696;
P38835:YHR131C; NbExp=3; IntAct=EBI-16219, EBI-24724;
P53108:YIP5; NbExp=2; IntAct=EBI-16219, EBI-24051;
P40892:YJL218W; NbExp=2; IntAct=EBI-16219, EBI-26263;
P47137:YJR096W; NbExp=3; IntAct=EBI-16219, EBI-25572;
P36140:YKR047W; NbExp=2; IntAct=EBI-16219, EBI-26441;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22000681}.
Nucleus {ECO:0000305}. Cytoplasm, cytoskeleton, actin patch
{ECO:0000269|PubMed:22000681}.
-!- PTM: The ubiquitination appears to be the result of an
intramolecular transfer of ubiquitin.
-!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
thioester formation.
-!- SIMILARITY: Belongs to the RSP5/NEDD4 family. {ECO:0000305}.
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EMBL; U18916; AAC03223.1; -; Genomic_DNA.
EMBL; BK006939; DAA07785.1; -; Genomic_DNA.
PIR; S43217; S43217.
RefSeq; NP_011051.3; NM_001179015.3.
PDB; 3OLM; X-ray; 2.50 A; A=384-809.
PDB; 4LCD; X-ray; 3.10 A; A/B=383-809.
PDB; 5HPL; X-ray; 2.31 A; A/B=430-809.
PDBsum; 3OLM; -.
PDBsum; 4LCD; -.
PDBsum; 5HPL; -.
ProteinModelPortal; P39940; -.
SMR; P39940; -.
BioGrid; 36869; 1217.
DIP; DIP-2238N; -.
ELM; P39940; -.
IntAct; P39940; 189.
MINT; MINT-520379; -.
STRING; 4932.YER125W; -.
iPTMnet; P39940; -.
MaxQB; P39940; -.
PRIDE; P39940; -.
EnsemblFungi; YER125W; YER125W; YER125W.
GeneID; 856862; -.
KEGG; sce:YER125W; -.
EuPathDB; FungiDB:YER125W; -.
SGD; S000000927; RSP5.
GeneTree; ENSGT00760000118966; -.
HOGENOM; HOG000208451; -.
InParanoid; P39940; -.
KO; K10591; -.
OMA; PGWEIRK; -.
OrthoDB; EOG092C016J; -.
BioCyc; YEAST:G3O-30288-MONOMER; -.
BRENDA; 2.3.2.B9; 984.
Reactome; R-SCE-1169408; ISG15 antiviral mechanism.
Reactome; R-SCE-5632684; Hedgehog 'on' state.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
EvolutionaryTrace; P39940; -.
PRO; PR:P39940; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0010008; C:endosome membrane; IDA:SGD.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:SGD.
GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:SGD.
GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
GO; GO:0034644; P:cellular response to UV; IMP:SGD.
GO; GO:0006333; P:chromatin assembly or disassembly; IMP:SGD.
GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD.
GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:SGD.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IPI:SGD.
GO; GO:0051865; P:protein autoubiquitination; IGI:SGD.
GO; GO:0006513; P:protein monoubiquitination; IDA:SGD.
GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:SGD.
GO; GO:0010794; P:regulation of dolichol biosynthetic process; IMP:SGD.
GO; GO:0032443; P:regulation of ergosterol biosynthetic process; IMP:SGD.
GO; GO:0031384; P:regulation of initiation of mating projection growth; IMP:SGD.
GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:SGD.
GO; GO:0010796; P:regulation of multivesicular body size; IMP:SGD.
GO; GO:0006808; P:regulation of nitrogen utilization; IGI:SGD.
GO; GO:0019220; P:regulation of phosphate metabolic process; IGI:SGD.
GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
GO; GO:2000203; P:regulation of ribosomal large subunit export from nucleus; IMP:SGD.
GO; GO:2000232; P:regulation of rRNA processing; IMP:SGD.
GO; GO:2000238; P:regulation of tRNA export from nucleus; IMP:SGD.
GO; GO:2000235; P:regulation of tRNA processing; IMP:SGD.
GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IMP:SGD.
GO; GO:0042493; P:response to drug; IMP:SGD.
GO; GO:0034517; P:ribophagy; IGI:SGD.
GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:SGD.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 3.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR024928; E3_ub_ligase_SMURF1.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00168; C2; 1.
Pfam; PF00632; HECT; 1.
Pfam; PF00397; WW; 3.
PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
SMART; SM00239; C2; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00456; WW; 3.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF51045; SSF51045; 3.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS01159; WW_DOMAIN_1; 3.
PROSITE; PS50020; WW_DOMAIN_2; 3.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; Nucleus; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 809 E3 ubiquitin-protein ligase RSP5.
/FTId=PRO_0000120335.
DOMAIN 1 88 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 229 262 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 331 364 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 387 420 WW 3. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 705 809 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
COMPBIAS 315 322 Poly-Ala.
ACT_SITE 777 777 Glycyl thioester intermediate.
CROSSLNK 258 258 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 516 516 Y->A: Has subtle defects on both initial
ubiquitination and chain elongation of
substrate proteins.
MUTAGEN 521 521 Y->A: Has defects on both initial
ubiquitination and chain elongation of
substrate proteins.
MUTAGEN 537 537 I->D: Has defects on both initial
ubiquitination and chain elongation of
substrate proteins.
MUTAGEN 618 618 F->D: Has defects on both initial
ubiquitination and chain elongation of
substrate proteins.
MUTAGEN 733 733 L->S: In RSP5-1; impairs ubiquitin-
thioester formation and catalysis of
substrate ubiquitination.
{ECO:0000269|PubMed:9858558}.
MUTAGEN 777 777 C->A: Loss of ubiquitination.
{ECO:0000269|PubMed:9858558}.
STRAND 393 396 {ECO:0000244|PDB:4LCD}.
STRAND 405 407 {ECO:0000244|PDB:3OLM}.
TURN 408 411 {ECO:0000244|PDB:3OLM}.
STRAND 412 416 {ECO:0000244|PDB:3OLM}.
HELIX 435 443 {ECO:0000244|PDB:5HPL}.
HELIX 446 448 {ECO:0000244|PDB:5HPL}.
STRAND 451 459 {ECO:0000244|PDB:5HPL}.
HELIX 461 463 {ECO:0000244|PDB:5HPL}.
HELIX 464 473 {ECO:0000244|PDB:5HPL}.
HELIX 479 481 {ECO:0000244|PDB:5HPL}.
STRAND 482 488 {ECO:0000244|PDB:5HPL}.
HELIX 496 511 {ECO:0000244|PDB:5HPL}.
HELIX 514 516 {ECO:0000244|PDB:5HPL}.
STRAND 517 521 {ECO:0000244|PDB:5HPL}.
STRAND 526 531 {ECO:0000244|PDB:5HPL}.
HELIX 535 537 {ECO:0000244|PDB:5HPL}.
HELIX 541 557 {ECO:0000244|PDB:5HPL}.
HELIX 568 574 {ECO:0000244|PDB:5HPL}.
HELIX 581 586 {ECO:0000244|PDB:5HPL}.
HELIX 589 600 {ECO:0000244|PDB:5HPL}.
TURN 604 606 {ECO:0000244|PDB:5HPL}.
STRAND 610 617 {ECO:0000244|PDB:5HPL}.
STRAND 620 627 {ECO:0000244|PDB:5HPL}.
HELIX 630 632 {ECO:0000244|PDB:5HPL}.
STRAND 633 635 {ECO:0000244|PDB:4LCD}.
TURN 637 639 {ECO:0000244|PDB:5HPL}.
HELIX 640 652 {ECO:0000244|PDB:5HPL}.
TURN 653 656 {ECO:0000244|PDB:5HPL}.
HELIX 657 668 {ECO:0000244|PDB:5HPL}.
HELIX 673 676 {ECO:0000244|PDB:5HPL}.
HELIX 681 689 {ECO:0000244|PDB:5HPL}.
HELIX 696 701 {ECO:0000244|PDB:5HPL}.
STRAND 703 708 {ECO:0000244|PDB:5HPL}.
HELIX 713 724 {ECO:0000244|PDB:5HPL}.
HELIX 727 738 {ECO:0000244|PDB:5HPL}.
HELIX 748 750 {ECO:0000244|PDB:5HPL}.
STRAND 754 757 {ECO:0000244|PDB:4LCD}.
STRAND 760 763 {ECO:0000244|PDB:5HPL}.
STRAND 773 775 {ECO:0000244|PDB:5HPL}.
TURN 776 779 {ECO:0000244|PDB:5HPL}.
STRAND 780 782 {ECO:0000244|PDB:5HPL}.
HELIX 789 801 {ECO:0000244|PDB:5HPL}.
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


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