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Protein

Transcriptional regulator URE2

Gene

URE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in nitrogen catabolite repression. Down-regulates the expression of many genes involved in nitrogen utilization by inhibiting the GATA transcriptional activators GLN3 and GAT1. Under good nitrogen conditions, binds to the phosphorylated forms of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing transcription of genes expressed upon nitrogen limitation. Is also an atypical glutaredoxin without a catalytical cysteine residue. Has glutathione peroxidase and thiol:disulfide oxidoreductase activities in both native and fibrillar form. Also shows insulin disulfide reductase and dehydroascorbic acid reductase (DHAR) actvites.6 Publications

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.1 Publication

Kineticsi

kcat is 1.2 sec(-1) with bis-(2-hydroxyethyl) disulfide (HEDS) as substrate.

  1. KM=2.4 mM for bis-(2-hydroxyethyl) disulfide (HEDS)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei124 – 1241Glutathione1 Publication
    Binding sitei151 – 1511Glutathione1 Publication

    GO - Molecular functioni

    • glutathione peroxidase activity Source: SGD
    • phosphoprotein binding Source: SGD
    • transcription corepressor activity Source: SGD

    GO - Biological processi

    • cytoplasmic sequestering of protein Source: SGD
    • cytoplasmic sequestering of transcription factor Source: SGD
    • negative regulation of nucleic acid-templated transcription Source: GOC
    • nitrate assimilation Source: UniProtKB-KW
    • protein urmylation Source: SGD
    • regulation of nitrogen utilization Source: SGD
    • response to aluminum ion Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Prion

    Keywords - Biological processi

    Nitrate assimilation

    Enzyme and pathway databases

    BioCyciYEAST:YNL229C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional regulator URE2
    Alternative name(s):
    Disulfide reductase (EC:1.8.4.-)
    Glutathione peroxidase (EC:1.11.1.9)
    Gene namesi
    Name:URE2
    Ordered Locus Names:YNL229C
    ORF Names:N1165
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XIV

    Organism-specific databases

    CYGDiYNL229c.
    EuPathDBiFungiDB:YNL229C.
    SGDiS000005173. URE2.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Amyloid, Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1221A → S: Reduces glutaredoxin activity. 1 Publication
    Mutagenesisi124 – 1241N → A or V: Abolishes glutaredoxin activity. 1 Publication
    Mutagenesisi313 – 3131F → S: Destroys protein function.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 354353Transcriptional regulator URE2PRO_0000186013Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP23202.
    PaxDbiP23202.
    PeptideAtlasiP23202.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with NNK1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NNK1P360034EBI-20138,EBI-9796

    Protein-protein interaction databases

    BioGridi35609. 294 interactions.
    DIPiDIP-1308N.
    IntActiP23202. 29 interactions.
    MINTiMINT-393865.
    STRINGi4932.YNL229C.

    Structurei

    Secondary structure

    1
    354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi101 – 1055Combined sources
    Beta strandi111 – 1188Combined sources
    Helixi123 – 13412Combined sources
    Beta strandi139 – 1435Combined sources
    Turni146 – 1494Combined sources
    Helixi150 – 1523Combined sources
    Helixi154 – 1574Combined sources
    Beta strandi167 – 1704Combined sources
    Turni171 – 1755Combined sources
    Beta strandi176 – 1805Combined sources
    Helixi181 – 19616Combined sources
    Helixi206 – 22217Combined sources
    Helixi224 – 23512Combined sources
    Beta strandi237 – 2393Combined sources
    Helixi242 – 27130Combined sources
    Turni276 – 2783Combined sources
    Helixi279 – 2846Combined sources
    Beta strandi285 – 2873Combined sources
    Helixi289 – 2913Combined sources
    Helixi293 – 2953Combined sources
    Helixi308 – 3114Combined sources
    Helixi314 – 3174Combined sources
    Helixi320 – 3234Combined sources
    Helixi327 – 3304Combined sources
    Helixi332 – 34211Combined sources
    Helixi345 – 3506Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G6WX-ray2.50A/B/C/D94-354[»]
    1G6YX-ray2.80A/B94-354[»]
    1HQOX-ray2.30A/B97-354[»]
    1JZRX-ray2.90A/B/C/D95-354[»]
    1K0AX-ray2.50A/B95-354[»]
    1K0BX-ray2.50A/B/C/D95-354[»]
    1K0CX-ray2.50A/B/C/D95-354[»]
    1K0DX-ray2.20A/B/C/D95-354[»]
    DisProtiDP00353.
    ProteinModelPortaliP23202.
    SMRiP23202. Positions 96-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23202.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini112 – 19685GST N-terminalAdd
    BLAST
    Domaini205 – 354150GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8988Prion domain (PrD)Add
    BLAST
    Regioni164 – 1652Glutathione binding
    Regioni180 – 1812Glutathione binding

    Domaini

    The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.2 Publications

    Sequence similaritiesi

    Belongs to the GST superfamily.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125742.
    InParanoidiP23202.
    KOiK00799.
    OMAiVYKWTKH.
    OrthoDBiEOG7KWSWX.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    IPR017298. Ure2.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037861. Prion_URE2. 1 hit.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P23202-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN
    60 70 80 90 100
    SSSNNNNVQN NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS
    110 120 130 140 150
    RITKFFQEQP LEGYTLFSHR SAPNGFKVAI VLSELGFHYN TIFLDFNLGE
    160 170 180 190 200
    HRAPEFVSVN PNARVPALID HGMDNLSIWE SGAILLHLVN KYYKETGNPL
    210 220 230 240 250
    LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK IASAVERYTD
    260 270 280 290 300
    EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW
    310 320 330 340 350
    LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA

    LRGE
    Length:354
    Mass (Da):40,271
    Last modified:November 1, 1991 - v1
    Checksum:i2C628976034B0F1C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M35268 Genomic DNA. Translation: AAA35201.1.
    AF525174 Genomic DNA. Translation: AAM93167.1.
    AF525175 Genomic DNA. Translation: AAM93168.1.
    AF525176 Genomic DNA. Translation: AAM93169.1.
    AF525177 Genomic DNA. Translation: AAM93170.1.
    AF525178 Genomic DNA. Translation: AAM93171.1.
    AF525179 Genomic DNA. Translation: AAM93172.1.
    AF525180 Genomic DNA. Translation: AAM93173.1.
    AF525181 Genomic DNA. Translation: AAM93174.1.
    AF525182 Genomic DNA. Translation: AAM93175.1.
    AF525183 Genomic DNA. Translation: AAM93176.1.
    AF525184 Genomic DNA. Translation: AAM93177.1.
    AF525185 Genomic DNA. Translation: AAM93178.1.
    AF525186 Genomic DNA. Translation: AAM93179.1.
    AF525187 Genomic DNA. Translation: AAM93180.1.
    AF525188 Genomic DNA. Translation: AAM93181.1.
    AF525189 Genomic DNA. Translation: AAM93182.1.
    AF525190 Genomic DNA. Translation: AAM93183.1.
    AF525191 Genomic DNA. Translation: AAM93184.1.
    AF525192 Genomic DNA. Translation: AAM93185.1.
    Z69381 Genomic DNA. Translation: CAA93369.1.
    Z71505 Genomic DNA. Translation: CAA96134.1.
    BK006947 Genomic DNA. Translation: DAA10329.1.
    PIRiA39609.
    RefSeqiNP_014170.1. NM_001183067.1.

    Genome annotation databases

    EnsemblFungiiYNL229C; YNL229C; YNL229C.
    GeneIDi855492.
    KEGGisce:YNL229C.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Mad yeast disease - Issue 47 of June 2004

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M35268 Genomic DNA. Translation: AAA35201.1.
    AF525174 Genomic DNA. Translation: AAM93167.1.
    AF525175 Genomic DNA. Translation: AAM93168.1.
    AF525176 Genomic DNA. Translation: AAM93169.1.
    AF525177 Genomic DNA. Translation: AAM93170.1.
    AF525178 Genomic DNA. Translation: AAM93171.1.
    AF525179 Genomic DNA. Translation: AAM93172.1.
    AF525180 Genomic DNA. Translation: AAM93173.1.
    AF525181 Genomic DNA. Translation: AAM93174.1.
    AF525182 Genomic DNA. Translation: AAM93175.1.
    AF525183 Genomic DNA. Translation: AAM93176.1.
    AF525184 Genomic DNA. Translation: AAM93177.1.
    AF525185 Genomic DNA. Translation: AAM93178.1.
    AF525186 Genomic DNA. Translation: AAM93179.1.
    AF525187 Genomic DNA. Translation: AAM93180.1.
    AF525188 Genomic DNA. Translation: AAM93181.1.
    AF525189 Genomic DNA. Translation: AAM93182.1.
    AF525190 Genomic DNA. Translation: AAM93183.1.
    AF525191 Genomic DNA. Translation: AAM93184.1.
    AF525192 Genomic DNA. Translation: AAM93185.1.
    Z69381 Genomic DNA. Translation: CAA93369.1.
    Z71505 Genomic DNA. Translation: CAA96134.1.
    BK006947 Genomic DNA. Translation: DAA10329.1.
    PIRiA39609.
    RefSeqiNP_014170.1. NM_001183067.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G6WX-ray2.50A/B/C/D94-354[»]
    1G6YX-ray2.80A/B94-354[»]
    1HQOX-ray2.30A/B97-354[»]
    1JZRX-ray2.90A/B/C/D95-354[»]
    1K0AX-ray2.50A/B95-354[»]
    1K0BX-ray2.50A/B/C/D95-354[»]
    1K0CX-ray2.50A/B/C/D95-354[»]
    1K0DX-ray2.20A/B/C/D95-354[»]
    DisProtiDP00353.
    ProteinModelPortaliP23202.
    SMRiP23202. Positions 96-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35609. 294 interactions.
    DIPiDIP-1308N.
    IntActiP23202. 29 interactions.
    MINTiMINT-393865.
    STRINGi4932.YNL229C.

    Proteomic databases

    MaxQBiP23202.
    PaxDbiP23202.
    PeptideAtlasiP23202.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYNL229C; YNL229C; YNL229C.
    GeneIDi855492.
    KEGGisce:YNL229C.

    Organism-specific databases

    CYGDiYNL229c.
    EuPathDBiFungiDB:YNL229C.
    SGDiS000005173. URE2.

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125742.
    InParanoidiP23202.
    KOiK00799.
    OMAiVYKWTKH.
    OrthoDBiEOG7KWSWX.

    Enzyme and pathway databases

    BioCyciYEAST:YNL229C-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP23202.
    NextBioi979478.
    PROiP23202.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    IPR017298. Ure2.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037861. Prion_URE2. 1 hit.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases."
      Coschigano P.W., Magasanik B.
      Mol. Cell. Biol. 11:822-832(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein."
      Edskes H.K., Wickner R.B.
      Proc. Natl. Acad. Sci. U.S.A. 99:16384-16391(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 14085 / CBS 3093 / IFO 1997 / NRRL Y-12657, ATCC 9804 / CBS 400 / DSM 70478 / IFO 0210 / JCM 2220, Boots, CBS 2087, CBS 4734, CBS 5112, CBS 5287, CBS 7957, Chevalieri / ATCC 10604 / CBS 405 / IFO 0258 / NRRL Y-1546, Fleischmann, McPhie Sourdough, SAF, Sigma 1278B, Wyeast#1007, YJM 143, YJM 280, YJM 320, YJM 326 and YJM 415.
    3. "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain."
      Pandolfo D., de Antoni A., Lanfranchi G., Valle G.
      Yeast 12:1071-1076(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae."
      Wickner R.B.
      Science 264:566-569(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRION FORMATION.
    7. "Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells."
      Masison D.C., Wickner R.B.
      Science 270:93-95(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN PRION.
    8. "Interaction of the GATA factor Gln3p with the nitrogen regulator Ure2p in Saccharomyces cerevisiae."
      Blinder D., Coschigano P.W., Magasanik B.
      J. Bacteriol. 178:4734-4736(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors."
      Beck T., Hall M.N.
      Nature 402:689-692(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Nitrogen catabolite repression of DAL80 expression depends on the relative levels of Gat1p and Ure2p production in Saccharomyces cerevisiae."
      Cunningham T.S., Andhare R., Cooper T.G.
      J. Biol. Chem. 275:14408-14414(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p."
      Moriyama H., Edskes H.K., Wickner R.B.
      Mol. Cell. Biol. 20:8916-8922(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRION FORMATION, PRION CURING.
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. "The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms."
      Bai M., Zhou J.M., Perrett S.
      J. Biol. Chem. 279:50025-50030(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils."
      Zhang Z.R., Perrett S.
      J. Biol. Chem. 284:14058-14067(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-122 AND ASN-124.
    16. Cited for: INTERACTION WITH NNK1.
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. "Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds."
      Bousset L., Belrhali H., Melki R., Morera S.
      Biochemistry 40:13564-13573(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 95-354 IN COMPLEX WITH GLUTATHIONE AND INHIBITORS.
    19. "The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p."
      Umland T.C., Taylor K.L., Rhee S., Wickner R.B., Davies D.R.
      Proc. Natl. Acad. Sci. U.S.A. 98:1459-1464(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 97-354.
    20. "Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae."
      Bousset L., Belrhali H., Janin J., Melki R., Morera S.
      Structure 9:39-46(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-353.
    21. "Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p."
      Chan J.C., Oyler N.A., Yau W.M., Tycko R.
      Biochemistry 44:10669-10680(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 10-39.
    22. "Characterization of beta-sheet structure in Ure2p(1-89) yeast prion fibrils by solid-state nuclear magnetic resonance."
      Baxa U., Wickner R.B., Steven A.C., Anderson D.E., Marekov L.N., Yau W.M., Tycko R.
      Biochemistry 46:13149-13162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-89, DOMAIN PRION.

    Entry informationi

    Entry nameiURE2_YEAST
    AccessioniPrimary (citable) accession number: P23202
    Secondary accession number(s): D6W0W3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: June 24, 2015
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    [URE3] is the prion form of URE2. [URE3] is the result of a conformational change of the cellular URE2 protein that becomes self-propagating and infectious. This conformational change generates a form of URE2 that assembles into amyloid fibrils. [URE3]-aggregates sequester soluble URE2, which then fails to retain GLN3 in the cytoplasm, resulting in GLN3 activation and consequently derepression of genes that are required for utilization of poor nirogen sources (PubMed:7909170). [URE3] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [URE3] propagation (PubMed:11073991).2 Publications
    Present with 7060 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    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 XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.