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P39940

- RSP5_YEAST

UniProt

P39940 - RSP5_YEAST

Protein

E3 ubiquitin-protein ligase RSP5

Gene

RSP5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    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.12 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei777 – 7771Glycyl thioester intermediate

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. phosphatidylinositol binding Source: SGD
    3. protein binding Source: IntAct
    4. ubiquitin binding Source: SGD
    5. ubiquitin-protein transferase activity Source: SGD

    GO - Biological processi

    1. cellular response to UV Source: SGD
    2. chromatin assembly or disassembly Source: SGD
    3. late endosome to vacuole transport via multivesicular body sorting pathway Source: SGD
    4. mitochondrion organization Source: SGD
    5. positive regulation of endocytosis Source: SGD
    6. positive regulation of fatty acid biosynthetic process Source: SGD
    7. positive regulation of receptor-mediated endocytosis Source: SGD
    8. positive regulation of transcription from RNA polymerase II promoter Source: SGD
    9. proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
    10. protein autoubiquitination Source: SGD
    11. protein monoubiquitination Source: SGD
    12. protein polyubiquitination Source: SGD
    13. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
    14. regulation of actin cytoskeleton organization Source: SGD
    15. regulation of dolichol biosynthetic process Source: SGD
    16. regulation of ergosterol biosynthetic process Source: SGD
    17. regulation of initiation of mating projection growth Source: SGD
    18. regulation of mRNA export from nucleus Source: SGD
    19. regulation of multivesicular body size Source: SGD
    20. regulation of nitrogen utilization Source: SGD
    21. regulation of phosphate metabolic process Source: SGD
    22. regulation of protein localization Source: SGD
    23. regulation of ribosomal large subunit export from nucleus Source: SGD
    24. regulation of rRNA processing Source: SGD
    25. regulation of tRNA export from nucleus Source: SGD
    26. regulation of tRNA processing Source: SGD
    27. regulation of ubiquinone biosynthetic process Source: SGD
    28. response to drug Source: SGD
    29. ribophagy Source: SGD
    30. ubiquitin-dependent endocytosis Source: SGD
    31. ubiquitin-dependent protein catabolic process Source: MGI
    32. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30288-MONOMER.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RSP5 (EC:6.3.2.-)
    Alternative name(s):
    Reverses SPT-phenotype protein 5
    Gene namesi
    Name:RSP5
    Synonyms:MDP1, NPI1
    Ordered Locus Names:YER125W
    ORF Names:SYGP-ORF41
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER125w.
    SGDiS000000927. RSP5.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus Curated. Cytoplasmcytoskeletonactin patch 1 Publication

    GO - Cellular componenti

    1. actin cortical patch Source: UniProtKB-SubCell
    2. cellular bud tip Source: SGD
    3. cytoplasm Source: SGD
    4. endosome membrane Source: SGD
    5. extrinsic component of cytoplasmic side of plasma membrane Source: SGD
    6. Golgi apparatus Source: SGD
    7. nucleus Source: SGD
    8. ubiquitin ligase complex Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi516 – 5161Y → A: Has subtle defects on both initial ubiquitination and chain elongation of substrate proteins.
    Mutagenesisi521 – 5211Y → A: Has defects on both initial ubiquitination and chain elongation of substrate proteins.
    Mutagenesisi537 – 5371I → D: Has defects on both initial ubiquitination and chain elongation of substrate proteins.
    Mutagenesisi618 – 6181F → D: Has defects on both initial ubiquitination and chain elongation of substrate proteins.
    Mutagenesisi733 – 7331L → S in RSP5-1; impairs ubiquitin-thioester formation and catalysis of substrate ubiquitination. 1 Publication
    Mutagenesisi777 – 7771C → A: Loss of ubiquitination. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 809809E3 ubiquitin-protein ligase RSP5PRO_0000120335Add
    BLAST

    Post-translational modificationi

    The ubiquitination appears to be the result of an intramolecular transfer of ubiquitin.

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP39940.
    PaxDbiP39940.
    PeptideAtlasiP39940.

    Expressioni

    Gene expression databases

    GenevestigatoriP39940.

    Interactioni

    Subunit structurei

    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 RVS167.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACK1Q076222EBI-16219,EBI-38674
    ADE12P802102EBI-16219,EBI-14267
    ALY1P361174EBI-16219,EBI-26358
    ALY2P470295EBI-16219,EBI-25974
    ART10P186344EBI-16219,EBI-27197
    ART5P532444EBI-16219,EBI-23201
    BNA5Q059792EBI-16219,EBI-10016
    CDC14Q006842EBI-16219,EBI-4192
    CSR2Q127342EBI-16219,EBI-32379
    CTA1P152022EBI-16219,EBI-4061
    DIA1P540054EBI-16219,EBI-27668
    DUS1P537592EBI-16219,EBI-27885
    ECM21P381672EBI-16219,EBI-21359
    ENO2P009252EBI-16219,EBI-6475
    FMP46P361412EBI-16219,EBI-26445
    GPH1P067382EBI-16219,EBI-13389
    HEM12P323472EBI-16219,EBI-5711
    IMA1P530512EBI-16219,EBI-10464
    IPP1P008172EBI-16219,EBI-9338
    LDB19Q125023EBI-16219,EBI-2113927
    LYS1P389983EBI-16219,EBI-10264
    LYS4P493672EBI-16219,EBI-10276
    MCR1P360602EBI-16219,EBI-10565
    MLS1P309523EBI-16219,EBI-10428
    NPL3Q015602EBI-16219,EBI-12114
    NPT1P396832EBI-16219,EBI-12218
    PCK1P109632EBI-16219,EBI-13770
    PFK2P168623EBI-16219,EBI-9435
    PMU1P360692EBI-16219,EBI-26862
    PTP1P250442EBI-16219,EBI-14183
    PYC1P111542EBI-16219,EBI-14358
    RCR1P382123EBI-16219,EBI-21381
    RCR2Q034462EBI-16219,EBI-18180
    RGM1Q004532EBI-16219,EBI-15073
    ROD1Q028053EBI-16219,EBI-15679
    ROG3P436023EBI-16219,EBI-22976
    RPB8P204363EBI-16219,EBI-15794
    SNA3P143592EBI-16219,EBI-26122
    SNA4Q075492EBI-16219,EBI-22078
    STM1P390153EBI-16219,EBI-11238
    THI13Q077482EBI-16219,EBI-36080
    THI5P435342EBI-16219,EBI-19221
    TKL1P232542EBI-16219,EBI-19291
    TRE1Q089193EBI-16219,EBI-31915
    TY1A-PLQ121622EBI-16219,EBI-36658
    TY2B-DR1Q124722EBI-16219,EBI-35737
    UBC6P332962EBI-16219,EBI-19745
    YBR056WP380813EBI-16219,EBI-21453
    YCL021WP255613EBI-16219,EBI-21696
    YHR131CP388353EBI-16219,EBI-24724
    YIP5P531082EBI-16219,EBI-24051
    YJL218WP408922EBI-16219,EBI-26263
    YJR096WP471373EBI-16219,EBI-25572
    YKR047WP361402EBI-16219,EBI-26441

    Protein-protein interaction databases

    BioGridi36869. 399 interactions.
    DIPiDIP-2238N.
    IntActiP39940. 172 interactions.
    MINTiMINT-520379.
    STRINGi4932.YER125W.

    Structurei

    Secondary structure

    1
    809
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi393 – 3964
    Beta strandi405 – 4073
    Turni408 – 4114
    Beta strandi412 – 4165
    Helixi430 – 44314
    Helixi446 – 4483
    Beta strandi455 – 4606
    Helixi461 – 4633
    Helixi464 – 47411
    Helixi477 – 4804
    Beta strandi484 – 4896
    Helixi502 – 51110
    Helixi514 – 5163
    Beta strandi517 – 52610
    Beta strandi529 – 5313
    Helixi533 – 5375
    Helixi541 – 55717
    Helixi568 – 5747
    Helixi581 – 5877
    Helixi589 – 59810
    Turni604 – 6063
    Beta strandi610 – 6178
    Beta strandi620 – 6278
    Helixi630 – 6323
    Beta strandi633 – 6353
    Turni637 – 6393
    Helixi640 – 65213
    Turni653 – 6564
    Helixi657 – 66812
    Helixi673 – 6764
    Helixi681 – 6888
    Helixi696 – 7016
    Beta strandi703 – 7075
    Helixi713 – 72412
    Helixi727 – 73812
    Helixi748 – 7503
    Beta strandi754 – 7574
    Beta strandi760 – 7634
    Beta strandi773 – 7753
    Helixi776 – 7783
    Beta strandi780 – 7823
    Helixi789 – 80214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OLMX-ray2.50A384-809[»]
    4LCDX-ray3.10A/B383-809[»]
    ProteinModelPortaliP39940.
    SMRiP39940. Positions 3-135, 227-291, 329-806.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39940.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8888C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini229 – 26234WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini331 – 36434WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini387 – 42034WW 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini705 – 809105HECTPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi315 – 3228Poly-Ala

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 3 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5021.
    GeneTreeiENSGT00570000078756.
    HOGENOMiHOG000208451.
    KOiK10591.
    OMAiMHTGATT.
    OrthoDBiEOG735453.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 3 hits.
    [Graphical view]
    PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTiSM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 3 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 3 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 3 hits.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39940-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSSISVKLV AAESLYKRDV FRSPDPFAVL TIDGYQTKST SAAKKTLNPY    50
    WNETFKFDDI NENSILTIQV FDQKKFKKKD QGFLGVVNVR VGDVLGHLDE 100
    DTATSSGRPR EETITRDLKK SNDGMAVSGR LIVVLSKLPS SSPHSQAPSG 150
    HTASSSTNTS STTRTNGHST SSTRNHSTSH PSRGTAQAVE STLQSGTTAA 200
    TNTATTSHRS TNSTSSATRQ YSSFEDQYGR LPPGWERRTD NFGRTYYVDH 250
    NTRTTTWKRP TLDQTEAERG NQLNANTELE RRQHRGRTLP GGSSDNSSVT 300
    VQVGGGSNIP PVNGAAAAAF AATGGTTSGL GELPSGWEQR FTPEGRAYFV 350
    DHNTRTTTWV DPRRQQYIRT YGPTNTTIQQ QPVSQLGPLP SGWEMRLTNT 400
    ARVYFVDHNT KTTTWDDPRL PSSLDQNVPQ YKRDFRRKVI YFRSQPALRI 450
    LPGQCHIKVR RKNIFEDAYQ EIMRQTPEDL KKRLMIKFDG EEGLDYGGVS 500
    REFFFLLSHE MFNPFYCLFE YSAYDNYTIQ INPNSGINPE HLNYFKFIGR 550
    VVGLGVFHRR FLDAFFVGAL YKMMLRKKVV LQDMEGVDAE VYNSLNWMLE 600
    NSIDGVLDLT FSADDERFGE VVTVDLKPDG RNIEVTDGNK KEYVELYTQW 650
    RIVDRVQEQF KAFMDGFNEL IPEDLVTVFD ERELELLIGG IAEIDIEDWK 700
    KHTDYRGYQE SDEVIQWFWK CVSEWDNEQR ARLLQFTTGT SRIPVNGFKD 750
    LQGSDGPRRF TIEKAGEVQQ LPKSHTCFNR VDLPQYVDYD SMKQKLTLAV 800
    EETIGFGQE 809
    Length:809
    Mass (Da):91,816
    Last modified:February 1, 1995 - v1
    Checksum:i6F1836384479E70F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18916 Genomic DNA. Translation: AAC03223.1.
    BK006939 Genomic DNA. Translation: DAA07785.1.
    PIRiS43217.
    RefSeqiNP_011051.3. NM_001179015.3.

    Genome annotation databases

    EnsemblFungiiYER125W; YER125W; YER125W.
    GeneIDi856862.
    KEGGisce:YER125W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18916 Genomic DNA. Translation: AAC03223.1 .
    BK006939 Genomic DNA. Translation: DAA07785.1 .
    PIRi S43217.
    RefSeqi NP_011051.3. NM_001179015.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OLM X-ray 2.50 A 384-809 [» ]
    4LCD X-ray 3.10 A/B 383-809 [» ]
    ProteinModelPortali P39940.
    SMRi P39940. Positions 3-135, 227-291, 329-806.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36869. 399 interactions.
    DIPi DIP-2238N.
    IntActi P39940. 172 interactions.
    MINTi MINT-520379.
    STRINGi 4932.YER125W.

    Proteomic databases

    MaxQBi P39940.
    PaxDbi P39940.
    PeptideAtlasi P39940.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER125W ; YER125W ; YER125W .
    GeneIDi 856862.
    KEGGi sce:YER125W.

    Organism-specific databases

    CYGDi YER125w.
    SGDi S000000927. RSP5.

    Phylogenomic databases

    eggNOGi COG5021.
    GeneTreei ENSGT00570000078756.
    HOGENOMi HOG000208451.
    KOi K10591.
    OMAi MHTGATT.
    OrthoDBi EOG735453.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BioCyci YEAST:G3O-30288-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39940.
    NextBioi 983216.
    PROi P39940.

    Gene expression databases

    Genevestigatori P39940.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTi SM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 3 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 3 hits.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Winston F.
      Unpublished observations (FEB-1993)
      Cited for: IDENTIFICATION.
    4. "NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase."
      Hein C., Springael J.-Y., Volland C., Haguenauer-Tsapis R., Andre B.
      Mol. Microbiol. 18:77-87(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: Sigma 1278B.
    5. "A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase."
      Huibregtse J.M., Scheffner M., Beaudenon S., Howley P.M.
      Proc. Natl. Acad. Sci. U.S.A. 92:2563-2567(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Bul1, a new protein that binds to the Rsp5 ubiquitin ligase in Saccharomyces cerevisiae."
      Yashiroda H., Oguchi T., Yasuda Y., Toh-e A., Kikuchi Y.
      Mol. Cell. Biol. 16:3255-3263(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BUL1.
    7. "The PY-motif of Bul1 protein is essential for growth of Saccharomyces cerevisiae under various stress conditions."
      Yashiroda H., Kaida D., Toh-e A., Kikuchi Y.
      Gene 225:39-46(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BUL1 AND BUL2.
    8. "Functional domains of the rsp5 ubiquitin-protein ligase."
      Wang G., Yang J., Huibregtse J.M.
      Mol. Cell. Biol. 19:342-352(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LEU-733 AND CYS-777.
      Strain: S288c / FY56.
    9. "PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance."
      Andoh T., Hirata Y., Kikuchi A.
      FEBS Lett. 525:131-134(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ROD1 AND ROG3.
    10. "Rsp5-Bul1/2 complex is necessary for the HSE-mediated gene expression in budding yeast."
      Kaida D., Toh-e A., Kikuchi Y.
      Biochem. Biophys. Res. Commun. 306:1037-1041(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
    11. "Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2."
      Abe F., Iida H.
      Mol. Cell. Biol. 23:7566-7584(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
    12. "NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae."
      Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B., Primig M., Hall M.N.
      J. Biol. Chem. 279:37512-37517(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
    13. "Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast."
      Pizzirusso M., Chang A.
      Mol. Biol. Cell 15:2401-2409(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
    14. "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
      Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
      Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSE1.
    15. "The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme."
      Kee Y., Lyon N., Huibregtse J.M.
      EMBO J. 24:2414-2424(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RUP1 AND UBP2.
    16. "Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae."
      Feller A., Boeckstaens M., Marini A.-M., Dubois E.
      J. Biol. Chem. 281:28546-28554(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE RSP5-BUL1/2 COMPLEX.
    17. "Peculiar protein-protein interactions of the novel endoplasmic reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5."
      Imai K., Noda Y., Adachi H., Yoda K.
      Biosci. Biotechnol. Biochem. 71:249-252(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RCR1.
    18. "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."
      Ren J., Kee Y., Huibregtse J.M., Piper R.C.
      Mol. Biol. Cell 18:324-335(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSE1.
    19. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: FUNCTION, INTERACTION WITH LAS17; LSB1; LSB2 AND RVS167, SUBCELLULAR LOCATION.
    21. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Structure and function of a HECT domain ubiquitin-binding site."
      Kim H.C., Steffen A.M., Oldham M.L., Chen J., Huibregtse J.M.
      EMBO Rep. 12:334-341(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 384-809 IN COMPLEX WITH UBIQUITIN.

    Entry informationi

    Entry nameiRSP5_YEAST
    AccessioniPrimary (citable) accession number: P39940
    Secondary accession number(s): D3DM31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    A cysteine residue is required for ubiquitin-thioester formation.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3