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P23202

- URE2_YEAST

UniProt

P23202 - URE2_YEAST

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Protein
Transcriptional regulator URE2
Gene
URE2, YNL229C, N1165
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 – 1241Glutathione
Binding sitei151 – 1511Glutathione

GO - Molecular functioni

  1. glutathione peroxidase activity Source: SGD
  2. phosphoprotein binding Source: SGD
  3. protein binding Source: IntAct
  4. transcription corepressor activity Source: SGD

GO - Biological processi

  1. cytoplasmic sequestering of transcription factor Source: SGD
  2. nitrate assimilation Source: UniProtKB-KW
  3. protein urmylation Source: SGD
  4. regulation of RNA biosynthetic process Source: GOC
  5. regulation of nitrogen utilization Source: SGD
  6. 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: Chromosome XIV

Organism-specific databases

CYGDiYNL229c.
SGDiS000005173. URE2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. 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 URE2
PRO_0000186013Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP23202.
PaxDbiP23202.
PeptideAtlasiP23202.

Expressioni

Gene expression databases

GenevestigatoriP23202.

Interactioni

Subunit structurei

Homodimer. Interacts with NNK1.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi35609. 291 interactions.
DIPiDIP-1308N.
IntActiP23202. 29 interactions.
MINTiMINT-393865.
STRINGi4932.YNL229C.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi103 – 1075
Beta strandi111 – 1188
Helixi123 – 13412
Beta strandi139 – 1435
Turni146 – 1494
Helixi150 – 1523
Helixi154 – 1574
Beta strandi167 – 1704
Turni171 – 1755
Beta strandi176 – 1805
Helixi181 – 19616
Helixi206 – 22217
Helixi224 – 23512
Beta strandi237 – 2393
Helixi242 – 27130
Helixi279 – 2846
Beta strandi285 – 2873
Helixi289 – 2913
Beta strandi295 – 2973
Helixi308 – 3114
Helixi314 – 3174
Helixi320 – 3234
Helixi327 – 3304
Helixi332 – 34211
Helixi345 – 3506

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP23202.

Family & Domainsi

Domains and Repeats

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

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125742.
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.
IPR017298. Prion_URE2.
IPR012336. Thioredoxin-like_fold.
[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

MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN    50
SSSNNNNVQN NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS 100
RITKFFQEQP LEGYTLFSHR SAPNGFKVAI VLSELGFHYN TIFLDFNLGE 150
HRAPEFVSVN PNARVPALID HGMDNLSIWE SGAILLHLVN KYYKETGNPL 200
LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK IASAVERYTD 250
EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW 300
LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA 350
LRGE 354
Length:354
Mass (Da):40,271
Last modified:November 1, 1991 - v1
Checksum:i2C628976034B0F1C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A39609.
RefSeqi NP_014170.1. NM_001183067.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G6W X-ray 2.50 A/B/C/D 94-354 [» ]
1G6Y X-ray 2.80 A/B 94-354 [» ]
1HQO X-ray 2.30 A/B 97-354 [» ]
1JZR X-ray 2.90 A/B/C/D 95-354 [» ]
1K0A X-ray 2.50 A/B 95-354 [» ]
1K0B X-ray 2.50 A/B/C/D 95-354 [» ]
1K0C X-ray 2.50 A/B/C/D 95-354 [» ]
1K0D X-ray 2.20 A/B/C/D 95-354 [» ]
DisProti DP00353.
ProteinModelPortali P23202.
SMRi P23202. Positions 96-354.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35609. 291 interactions.
DIPi DIP-1308N.
IntActi P23202. 29 interactions.
MINTi MINT-393865.
STRINGi 4932.YNL229C.

Proteomic databases

MaxQBi P23202.
PaxDbi P23202.
PeptideAtlasi P23202.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YNL229C ; YNL229C ; YNL229C .
GeneIDi 855492.
KEGGi sce:YNL229C.

Organism-specific databases

CYGDi YNL229c.
SGDi S000005173. URE2.

Phylogenomic databases

eggNOGi COG0625.
HOGENOMi HOG000125742.
KOi K00799.
OMAi VYKWTKH.
OrthoDBi EOG7KWSWX.

Enzyme and pathway databases

BioCyci YEAST:YNL229C-MONOMER.

Miscellaneous databases

EvolutionaryTracei P23202.
NextBioi 979478.

Gene expression databases

Genevestigatori P23202.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR017298. Prion_URE2.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF037861. Prion_URE2. 1 hit.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 142 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 (1 Publication). [URE3] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [URE3] propagation (1 Publication).
Present with 7060 molecules/cell in log phase SD medium.

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