P23202 · URE2_YEAST
- ProteinTranscriptional regulator URE2
- GeneURE2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids354 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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) activities.
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).
[URE3] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [URE3] propagation (PubMed:11073991).
Present with 7060 molecules/cell in log phase SD medium.
Catalytic activity
- 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.4 mM | bis-(2-hydroxyethyl) disulfide (HEDS) |
kcat is 1.2 sec-1 with bis-(2-hydroxyethyl) disulfide (HEDS) as substrate.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | glutathione peroxidase activity | |
Molecular Function | phosphoprotein binding | |
Molecular Function | transcription corepressor activity | |
Biological Process | negative regulation of transcription by transcription factor localization | |
Biological Process | nitrate assimilation | |
Biological Process | protein urmylation | |
Biological Process | regulation of nitrogen utilization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTranscriptional regulator URE2
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP23202
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 122 | Reduces glutaredoxin activity. | ||||
Sequence: A → S | ||||||
Mutagenesis | 124 | Abolishes glutaredoxin activity. | ||||
Sequence: N → A or V | ||||||
Mutagenesis | 313 | Destroys protein function. | ||||
Sequence: F → S |
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000186013 | 2-354 | Transcriptional regulator URE2 | |||
Sequence: MNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQNNNSGRNGSQNNDNENNIKNTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYTLFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWESGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer. Interacts with NNK1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P23202 | GLN3 P18494 | 2 | EBI-20138, EBI-7657 | |
BINARY | P23202 | NNK1 P36003 | 4 | EBI-20138, EBI-9796 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-89 | Prion domain (PrD) | ||||
Sequence: MNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQNNNSGRNGSQNNDNENNIKNTLEQHRQQQQ | ||||||
Region | 22-76 | Disordered | ||||
Sequence: GNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQNNNSGRNGSQNNDNENN | ||||||
Domain | 112-196 | GST N-terminal | ||||
Sequence: EGYTLFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWESGAILLHLVNKYYKET | ||||||
Domain | 205-354 | GST C-terminal | ||||
Sequence: DLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE |
Domain
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.
Sequence similarities
Belongs to the GST superfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length354
- Mass (Da)40,271
- Last updated1991-11-01 v1
- Checksum2C628976034B0F1C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M35268 EMBL· GenBank· DDBJ | AAA35201.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525174 EMBL· GenBank· DDBJ | AAM93167.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525175 EMBL· GenBank· DDBJ | AAM93168.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525176 EMBL· GenBank· DDBJ | AAM93169.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525177 EMBL· GenBank· DDBJ | AAM93170.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525178 EMBL· GenBank· DDBJ | AAM93171.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525179 EMBL· GenBank· DDBJ | AAM93172.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525180 EMBL· GenBank· DDBJ | AAM93173.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525181 EMBL· GenBank· DDBJ | AAM93174.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525182 EMBL· GenBank· DDBJ | AAM93175.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525183 EMBL· GenBank· DDBJ | AAM93176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525184 EMBL· GenBank· DDBJ | AAM93177.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525185 EMBL· GenBank· DDBJ | AAM93178.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525186 EMBL· GenBank· DDBJ | AAM93179.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525187 EMBL· GenBank· DDBJ | AAM93180.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525188 EMBL· GenBank· DDBJ | AAM93181.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525189 EMBL· GenBank· DDBJ | AAM93182.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525190 EMBL· GenBank· DDBJ | AAM93183.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525191 EMBL· GenBank· DDBJ | AAM93184.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF525192 EMBL· GenBank· DDBJ | AAM93185.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z69381 EMBL· GenBank· DDBJ | CAA93369.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z71505 EMBL· GenBank· DDBJ | CAA96134.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006947 EMBL· GenBank· DDBJ | DAA10329.1 EMBL· GenBank· DDBJ | Genomic DNA |