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UniProtKB/Swiss-Prot entry P39940

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RSP5_YEAST
Primary accession number P39940
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 85)
Name and origin of the protein
Protein name E3 ubiquitin-protein ligase RSP5
Synonyms EC 6.3.2.-
Reverses SPT-phenotype protein 5
Gene name
Name: RSP5
Synonyms: MDP1, NPI1
OrderedLocusNames: YER125W
ORFNames: SYGP-ORF41
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan]
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]
 IDENTIFICATION.
Winston F.;
Unpublished observations (FEB-1993).
[3]
 CHARACTERIZATION.
STRAIN=Sigma 1278B;
PubMed=8596462 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
 FUNCTION.
PubMed=7708685 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
 ERRATUM.
PubMed=7761480 [NCBI, ExPASy, EBI, Israel, Japan]
Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.;
Proc. Natl. Acad. Sci. U.S.A. 92:5249-5249(1995).
[6]
 INTERACTION WITH BUL1.
PubMed=8668140 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
 FUNCTION, AND INTERACTION WITH BUL1 AND BUL2.
DOI=10.1016/S0378-1119(98)00535-6; PubMed=9931424 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
 FUNCTION, AND MUTAGENESIS OF LEU-733 AND CYS-777.
STRAIN=S288c / FY56;
PubMed=9858558 [NCBI, ExPASy, EBI, Israel, Japan]
Wang G., Yang J., Huibregtse J.M.;
"Functional domains of the rsp5 ubiquitin-protein ligase.";
Mol. Cell. Biol. 19:342-352(1999).
[9]
 FUNCTION, AND INTERACTION WITH ROD1 AND ROG3.
DOI=10.1016/S0014-5793(02)03104-6; PubMed=12163175 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
 FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
DOI=10.1016/S0006-291X(03)01090-8; PubMed=12821147 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
 FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
DOI=10.1128/MCB.23.21.7566-7584.2003; PubMed=14560004 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
 FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
DOI=10.1074/jbc.M407372200; PubMed=15247235 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
 FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
DOI=10.1091/mbc.E03-10-0727; PubMed=15020711 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
 INTERACTION WITH HSE1.
DOI=10.1111/j.1600-0854.2004.00169.x; PubMed=15086794 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
 FUNCTION, AND INTERACTION WITH RUP1 AND UBP2.
DOI=10.1038/sj.emboj.7600710; PubMed=15933713 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
 FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
DOI=10.1074/jbc.M605551200; PubMed=16864574 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
 INTERACTION WITH RCR1.
DOI=10.1271/bbb.60446; PubMed=17213653 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[18]
 FUNCTION, AND INTERACTION WITH HSE1.
DOI=10.1091/mbc.E06-06-0557; PubMed=17079730 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U18916; AAC03223.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S43217; S43217.
RefSeq NP_011051.1; -.
3D structure databases
HSSP Q62940; 1I5H. [HSSP ENTRY / PDB]
ModBase P39940.
Protein-protein interaction databases
DIP DIP:2238N; -.
IntAct P39940; -.
Organism-specific databases
CYGD YER125w; -.
SGD S000000927; RSP5.
Yeast-GFP YER125W.
Gene expression databases
ArrayExpress P39940; -.
GermOnline YER125W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0010008; Cellular component: endosome membrane (inferred from direct assay from SGD).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from SGD).
GO:0000151; Cellular component: ubiquitin ligase complex (inferred from direct assay from MGI).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from direct assay from MGI).
GO:0006333; Biological process: chromatin assembly or disassembly (inferred from mutant phenotype from SGD).
GO:0006897; Biological process: endocytosis (traceable author statement from SGD).
GO:0010142; Biological process: farnesyl diphosphate biosynthetic process, mevalonate pathway (inferred from mutant phenotype from SGD).
GO:0006406; Biological process: mRNA export from nucleus (inferred from mutant phenotype from SGD).
GO:0006513; Biological process: protein monoubiquitination (inferred from direct assay from SGD).
GO:0000209; Biological process: protein polyubiquitination (inferred from direct assay from SGD).
GO:0034517; Biological process: ribophagy (inferred from genetic interaction from SGD).
GO:0006350; Biological process: transcription (traceable author statement from SGD).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000008; C2_Ca-dep.
IPR000569; HECT.
IPR002349; WW.
IPR001202; WW_Rsp5_WWP.
Graphical view of domain structure.
Pfam PF00168; C2; 1.
PF00632; HECT; 1.
PF00397; WW; 3.
Pfam graphical view of domain structure.
PRINTS PR00403; WWDOMAIN.
SMART SM00239; C2; 1.
SM00119; HECTc; 1.
SM00456; WW; 3.
SMART graphical view of domain structure.
PROSITE PS50004; C2; 1.
PS50237; HECT; 1.
PS01159; WW_DOMAIN_1; 3.
PS50020; WW_DOMAIN_2; 3.
PROSITE graphical view of domain structure (profiles).
ProtoNet P39940.
Proteomic databases
PeptideAtlas P39940; -.
Genome annotation databases
Ensembl YER125W; Saccharomyces cerevisiae. [Contig view]
GeneID 856862; -.
GenomeReviews U00092_GR; YER125W.
KEGG sce:YER125W; -.
NMPDR fig|4932.3.peg.2127; -.
Phylogenomic databases
HOGENOM P39940; -.
Other
LinkHub P39940; -.
NextBio 983216; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Ligase; Nucleus; Repeat; Ubl conjugation; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   809  809     E3 ubiquitin-protein ligase RSP5. PRO_0000120335
DOMAIN   1    88  88     C2. 
DOMAIN   229   262  34     WW 1. 
DOMAIN   331   364  34     WW 2. 
DOMAIN   387   420  34     WW 3. 
DOMAIN   705   809  105     HECT. 
COMPBIAS   315   322  8     Poly-Ala. 
ACT_SITE   777   777        Glycyl thioester intermediate. 
MUTAGEN   733   733        L->S: In RSP5-1; impairs ubiquitin-thioester formation and catalysis of substrate ubiquitination. 
MUTAGEN   777   777        C->A: Loss of ubiquitination. 
Sequence information
Length: 809 AA [This is the length of the unprocessed precursor] Molecular weight: 91816 Da [This is the MW of the unprocessed precursor] CRC64: 6F1836384479E70F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPSSISVKLV AAESLYKRDV FRSPDPFAVL TIDGYQTKST SAAKKTLNPY WNETFKFDDI 

        70         80         90        100        110        120 
NENSILTIQV FDQKKFKKKD QGFLGVVNVR VGDVLGHLDE DTATSSGRPR EETITRDLKK 

       130        140        150        160        170        180 
SNDGMAVSGR LIVVLSKLPS SSPHSQAPSG HTASSSTNTS STTRTNGHST SSTRNHSTSH 

       190        200        210        220        230        240 
PSRGTAQAVE STLQSGTTAA TNTATTSHRS TNSTSSATRQ YSSFEDQYGR LPPGWERRTD 

       250        260        270        280        290        300 
NFGRTYYVDH NTRTTTWKRP TLDQTEAERG NQLNANTELE RRQHRGRTLP GGSSDNSSVT 

       310        320        330        340        350        360 
VQVGGGSNIP PVNGAAAAAF AATGGTTSGL GELPSGWEQR FTPEGRAYFV DHNTRTTTWV 

       370        380        390        400        410        420 
DPRRQQYIRT YGPTNTTIQQ QPVSQLGPLP SGWEMRLTNT ARVYFVDHNT KTTTWDDPRL 

       430        440        450        460        470        480 
PSSLDQNVPQ YKRDFRRKVI YFRSQPALRI LPGQCHIKVR RKNIFEDAYQ EIMRQTPEDL 

       490        500        510        520        530        540 
KKRLMIKFDG EEGLDYGGVS REFFFLLSHE MFNPFYCLFE YSAYDNYTIQ INPNSGINPE 

       550        560        570        580        590        600 
HLNYFKFIGR VVGLGVFHRR FLDAFFVGAL YKMMLRKKVV LQDMEGVDAE VYNSLNWMLE 

       610        620        630        640        650        660 
NSIDGVLDLT FSADDERFGE VVTVDLKPDG RNIEVTDGNK KEYVELYTQW RIVDRVQEQF 

       670        680        690        700        710        720 
KAFMDGFNEL IPEDLVTVFD ERELELLIGG IAEIDIEDWK KHTDYRGYQE SDEVIQWFWK 

       730        740        750        760        770        780 
CVSEWDNEQR ARLLQFTTGT SRIPVNGFKD LQGSDGPRRF TIEKAGEVQQ LPKSHTCFNR 

       790        800 
VDLPQYVDYD SMKQKLTLAV EETIGFGQE
P39940 in FASTA format

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