P23202 (URE2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein URE2

Gene names

Name:	URE2
Ordered Locus Names:	YNL229C
ORF Names:	N1165

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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 structure	Homodimer. Interacts with NNK1. Ref.8
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. Present with 7060 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the GST superfamily. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Nitrate assimilation
Cellular component	Amyloid
Molecular function	Prion
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cytoplasmic sequestering of transcription factor Inferred from mutant phenotype. Source: SGD nitrate assimilation Inferred from electronic annotation. Source: UniProtKB-KW protein urmylation Inferred from mutant phenotype. Source: SGD regulation of nitrogen utilization Inferred from mutant phenotype. Source: SGD response to aluminum ion Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD soluble fraction Inferred from direct assay. Source: SGD
Molecular function	glutathione peroxidase activity Inferred from direct assay. Source: SGD phosphoprotein binding Inferred from direct assay. Source: SGD transcription corepressor activity Inferred from physical interaction. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NNK1	P36003	3	EBI-20138,EBI-9796

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 354

354

Protein URE2

PRO_0000186013

Regions

Domain

112 – 196

85

GST N-terminal

Domain

205 – 354

150

GST C-terminal

Amino acid modifications

Modified residue

282

1

Phosphotyrosine Ref.7

Modified residue

283

1

Phosphoserine Ref.7

Modified residue

287

1

Phosphothreonine Ref.7

Experimental info

Mutagenesis

313

1

F → S: Destroys protein function.

Secondary structure

1

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354

Helix Strand Turn

Details...

Helix

101 – 105

5

Beta strand

111 – 118

8

Helix

123 – 135

13

Beta strand

139 – 143

5

Turn

146 – 151

6

Helix

154 – 159

6

Beta strand

167 – 170

4

Helix

171 – 173

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P23202 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 2C628976034B0F1C	FASTA	354	40,271
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1990286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 12177423] [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: 8896273] [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: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-282; SER-283 AND THR-287, MASS SPECTROMETRY.
[8]	"A global protein kinase and phosphatase interaction network in yeast." Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B., Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D., Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C., Nesvizhskii A.I., Tyers M. Science 328:1043-1046(2010) [PubMed: 20489023] [Abstract] Cited for: INTERACTION WITH NNK1.
[9]	"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: 11342133] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-353.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Mad yeast disease - Issue 47 of June 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A39609.

RefSeq

NP_014170.1. NM_001183067.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P23202.

SMR

P23202. Positions 96-354.

DisProt

DP00353.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1308N.

IntAct

P23202. 25 interactions.

MINT

MINT-393865.

STRING

P23202.

Proteomic databases

PeptideAtlas

P23202.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL229C; YNL229C; YNL229C.

GeneID

855492.

KEGG

sce:YNL229C.

NMPDR

fig|4932.3.peg.5235.

Organism-specific databases

CYGD

YNL229c.

SGD

S000005173. URE2.

Phylogenomic databases

eggNOG

fuNOG04827.

HOGENOM

HBG753188.

OMA

KWTKHMM.

OrthoDB

EOG4X0R27.

Gene expression databases

ArrayExpress

P23202.

Genevestigator

P23202.

GermOnline

YNL229C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR017298. Prion_URE2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

KO

K00799.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PIRSF

PIRSF037861. Prion_URE2. 1 hit.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

979478.

Entry information

Entry name

URE2_YEAST

Accession

Primary (citable) accession number: P23202
Secondary accession number(s): D6W0W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program