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YEAST:TRXB1

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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

PMID:24769239[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

PMID:9571241[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

PMID:9571241[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034599

cellular response to oxidative stress

PMID:15051715[3]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000000160
SGD:S000001272
SGD:S000002861
SGD:S000004099
SGD:S000004490

P

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:18406344[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18406344[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005758

mitochondrial intermembrane space

PMID:22984289[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004791

thioredoxin-disulfide reductase activity

PMID:7961686[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004791

thioredoxin-disulfide reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008255
InterPro:IPR023753

F

Seeded From UniProt

complete

involved_in

GO:0019430

removal of superoxide radicals

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005982
InterPro:IPR008255
InterPro:IPR023753

P

Seeded From UniProt

complete

enables

GO:0004791

thioredoxin-disulfide reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.8.1.9

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

part_of

GO:0005758

mitochondrial intermembrane space

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0169

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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. 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
  3. 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. 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
  5. Vögtle, FN et al. (2012) Intermembrane space proteome of yeast mitochondria. Mol. Cell Proteomics 11 1840-52 PubMed GONUTS page
  6. Chae, HZ et al. (1994) Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269 27670-8 PubMed GONUTS page