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YEAST:TRXB1
Contents
Species (Taxon ID) | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292) | |
Gene Name(s) | TRR1 | |
Protein Name(s) | Thioredoxin reductase 1 | |
External Links | ||
UniProt | P29509 | |
EMBL | U10274 U28372 X04273 AY557749 BK006938 | |
PIR | S61150 | |
RefSeq | NP_010640.1 | |
PDB | 3D8X 3ITJ | |
PDBsum | 3D8X 3ITJ | |
ProteinModelPortal | P29509 | |
SMR | P29509 | |
BioGrid | 32410 | |
DIP | DIP-4319N | |
IntAct | P29509 | |
MINT | MINT-488138 | |
STRING | 4932.YDR353W | |
MaxQB | P29509 | |
PaxDb | P29509 | |
PeptideAtlas | P29509 | |
PRIDE | P29509 | |
EnsemblFungi | [example_ID YDR353W] | |
GeneID | 851955 | |
KEGG | sce:YDR353W | |
SGD | S000002761 | |
eggNOG | COG0492 | |
GeneTree | ENSGT00390000011774 | |
HOGENOM | HOG000072912 | |
InParanoid | P29509 | |
KO | K00384 | |
OMA | NSMLCKC | |
OrthoDB | EOG7DC2FH | |
BioCyc | YEAST:YDR353W-MONOMER | |
EvolutionaryTrace | P29509 | |
NextBio | 970056 | |
Proteomes | UP000002311 | |
Genevestigator | P29509 | |
GO | GO:0005829 GO:0005758 GO:0008198 GO:0050660 GO:0004791 GO:0045454 GO:0034599 GO:0019430 | |
InterPro | IPR013027 IPR008255 IPR023753 IPR001327 IPR000103 IPR005982 | |
Pfam | PF00070 PF07992 | |
PRINTS | PR00368 PR00469 | |
TIGRFAMs | TIGR01292 | |
PROSITE | PS00573 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
part_of |
GO:0005739 |
mitochondrion |
ECO:0007005 |
high throughput direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0045454 |
cell redox homeostasis |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0045454 |
cell redox homeostasis |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0034599 |
cellular response to oxidative stress |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
SGD:S000000160 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0008198 |
ferrous iron binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005758 |
mitochondrial intermembrane space |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0019430 |
removal of superoxide radicals |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004791 |
thioredoxin-disulfide reductase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005739 |
mitochondrion |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005758 |
mitochondrial intermembrane space |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Renvoisé, M et al. (2014) Quantitative variations of the mitochondrial proteome and phosphoproteome during fermentative and respiratory growth in Saccharomyces cerevisiae. J Proteomics 106 140-50 PubMed GONUTS page
- ↑ 2.0 2.1 Luikenhuis, S et al. (1998) The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol. Biol. Cell 9 1081-91 PubMed GONUTS page
- ↑ Wong, CM et al. (2004) Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable. J. Biol. Chem. 279 23207-13 PubMed GONUTS page
- ↑ 4.0 4.1 Kang, HJ et al. (2008) A novel role for thioredoxin reductase in the iron metabolism of S. cerevisiae. Biochem. Biophys. Res. Commun. 371 63-8 PubMed GONUTS page
- ↑ Vögtle, FN et al. (2012) Intermembrane space proteome of yeast mitochondria. Mol. Cell Proteomics 11 1840-52 PubMed GONUTS page
- ↑ Chae, HZ et al. (1994) Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269 27670-8 PubMed GONUTS page