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UniProtKB/Swiss-Prot entry P23202


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

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Entry information
Entry name URE2_YEAST
Primary accession number P23202
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 88)
Name and origin of the protein
Protein name Protein URE2
Synonyms None
Gene name
Name: URE2
OrderedLocusNames: YNL229C
ORFNames: N1165
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 [GENOMIC DNA].
PubMed=1990286 [NCBI, ExPASy, EBI, Israel, Japan]
Coschigano P.W., Magasanik B.;
"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.";
Mol. Cell. Biol. 11:822-832(1991).
[2]
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;
DOI=10.1073/pnas.162349599; PubMed=12177423 [NCBI, ExPASy, EBI, Israel, Japan]
Edskes H.K., Wickner R.B.;
"Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.";
Proc. Natl. Acad. Sci. U.S.A. 99:16384-16391(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1071::AID-YEA4>3.3.CO;2-J; PubMed=8896273 [NCBI, ExPASy, EBI, Israel, Japan]
Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
"The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain.";
Yeast 12:1071-1076(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-282; SER-283 AND THR-287, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-353.
DOI=10.1016/S0969-2126(00)00553-0; PubMed=11342133 [NCBI, ExPASy, EBI, Israel, Japan]
Bousset L., Belrhali H., Janin J., Melki R., Morera S.;
"Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae.";
Structure 9:39-46(2001).
Comments
  • FUNCTION: Plays an important role in the cellular response to the nitrogen source. URE2 gene plays a major part in the repression of GLN1 and GDH2 genes by glutamine, and is required for the inactivation of glutamine synthetase. URE2 gene product may catalytically inactivate GLN3 in response to an increase in the intracellular concentration of glutamine.
  • SUBUNIT: Homodimer.
  • MISCELLANEOUS: Can provoque the non-Mendelian trait [URE3]. The [URE3] element of S.cerevisiae is due to the propagation of a transmissible form of the protein URE2. The infectivity of URE2 is thought to originate from a conformational change of the normal form of the prion protein. This conformational change generates a form of URE2 that assembles into amyloid fibrils.
  • MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the GST superfamily.
  • SIMILARITY: Contains 1 GST C-terminal domain.
  • SIMILARITY: Contains 1 GST N-terminal domain.
  • WEB RESOURCE: Name=Protein Spotlight; Note=Mad yeast disease -Issue 47 of June 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt047.shtml";.
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
M35268; AAA35201.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525174; AAM93167.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525175; AAM93168.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525176; AAM93169.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525177; AAM93170.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525178; AAM93171.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525179; AAM93172.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525180; AAM93173.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525181; AAM93174.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525182; AAM93175.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525183; AAM93176.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525184; AAM93177.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525185; AAM93178.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525186; AAM93179.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525187; AAM93180.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525188; AAM93181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525189; AAM93182.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525190; AAM93183.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525191; AAM93184.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525192; AAM93185.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z69381; CAA93369.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71505; CAA96134.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39609; A39609.
RefSeq NP_014170.1; -.
3D structure databases
PDB
1G6W; X-ray; 2.50 A; A/B/C/D=94-354.[ExPASy / RCSB / EBI]
1G6Y; X-ray; 2.80 A; A/B=94-354.[ExPASy / RCSB / EBI]
1HQO; X-ray; 2.30 A; A/B=97-354.[ExPASy / RCSB / EBI]
1JZR; X-ray; 2.90 A; A/B/C/D=95-354.[ExPASy / RCSB / EBI]
1K0A; X-ray; 2.50 A; A/B=95-354.[ExPASy / RCSB / EBI]
1K0B; X-ray; 2.50 A; A/B/C/D=95-354.[ExPASy / RCSB / EBI]
1K0C; X-ray; 2.50 A; A/B/C/D=95-354.[ExPASy / RCSB / EBI]
1K0D; X-ray; 2.20 A; A/B/C/D=95-354.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1G6W; -.
1G6Y; -.
1HQO; -.
1JZR; -.
1K0A; -.
1K0B; -.
1K0C; -.
1K0D; -.
DisProt DP00353; -.
ModBase P23202.
Protein-protein interaction databases
DIP DIP:1308N; -.
IntAct P23202; -.
Organism-specific databases
CYGD YNL229c; -.
SGD S000005173; URE2.
Yeast-GFP YNL229C.
Gene expression databases
GermOnline YNL229C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0005625; Cellular component: soluble fraction (inferred from direct assay from SGD).
GO:0051219; Molecular function: phosphoprotein binding (inferred from direct assay from SGD).
GO:0003714; Molecular function: transcription corepressor activity (inferred from genetic interaction from SGD).
GO:0042994; Biological process: cytoplasmic sequestering of transcription factor (inferred from mutant phenotype from SGD).
GO:0032447; Biological process: protein urmylation (inferred from mutant phenotype from SGD).
GO:0006808; Biological process: regulation of nitrogen utilization (inferred from mutant phenotype from SGD).
GO:0010044; Biological process: response to aluminum ion (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR010987; Glutathione-S-Trfase_C-like.
IPR004046; GST_C.
IPR004045; GST_N.
IPR017298; Prion_URE2.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1050.10; GST_C_like; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00043; GST_C; 1.
PF02798; GST_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037861; Prion_URE2; 1.
PROSITE PS50405; GST_CTER; 1.
PS50404; GST_NTER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P23202.
Proteomic databases
PeptideAtlas P23202; -.
Genome annotation databases
Ensembl YNL229C; Saccharomyces cerevisiae. [Contig view]
GeneID 855492; -.
GenomeReviews Y13139_GR; YNL229C.
KEGG sce:YNL229C; -.
NMPDR fig|4932.3.peg.5235; -.
Phylogenomic databases
HOGENOM P23202; -.
Other
LinkHub P23202; -.
ProtoNet P23202.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Nitrate assimilation; Phosphoprotein; Prion.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   354  354     Protein URE2. PRO_0000186013
DOMAIN   112   196  85     GST N-terminal. 
DOMAIN   205   354  150     GST C-terminal. 
MOD_RES   282   282        Phosphotyrosine. 
MOD_RES   283   283        Phosphoserine. 
MOD_RES   287   287        Phosphothreonine. 
MUTAGEN   313   313        F->S: Destroys protein function. 
STRAND   111   118  8      
HELIX   123   135  13      
STRAND   139   143  5      
TURN   146   151  6      
HELIX   154   159  6      
STRAND   167   170  4      
HELIX   171   173  3      
STRAND   175   178  4      
HELIX   181   196  16      
HELIX   206   222  17      
HELIX   224   235  12      
HELIX   242   268  27      
HELIX   308   317  10      
HELIX   320   323  4      
HELIX   327   330  4      
HELIX   332   343  12      
HELIX   345   352  8      
Sequence information
Length: 354 AA [This is the length of the unprocessed precursor] Molecular weight: 40271 Da [This is the MW of the unprocessed precursor] CRC64: 2C628976034B0F1C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN SSSNNNNVQN 

        70         80         90        100        110        120 
NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS RITKFFQEQP LEGYTLFSHR 

       130        140        150        160        170        180 
SAPNGFKVAI VLSELGFHYN TIFLDFNLGE HRAPEFVSVN PNARVPALID HGMDNLSIWE 

       190        200        210        220        230        240 
SGAILLHLVN KYYKETGNPL LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK 

       250        260        270        280        290        300 
IASAVERYTD EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW 

       310        320        330        340        350 
LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA LRGE 

P23202 in FASTA format

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View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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