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YEAST:TRX2

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) TRX2 (synonyms: TRX1)
Protein Name(s) Thioredoxin-2

Thioredoxin II TR-II Thioredoxin-1

External Links
UniProt P22803
EMBL M59168
M62648
U40843
Z49133
Z72994
AY557817
BK006941
PIR S15049
RefSeq NP_011725.3
PDB 2FA4
2HSY
3PIN
4DSS
PDBsum 2FA4
2HSY
3PIN
4DSS
ProteinModelPortal P22803
SMR P22803
BioGrid 33462
DIP DIP-5552N
IntAct P22803
MINT MINT-474704
STRING 4932.YGR209C
MaxQB P22803
PaxDb P22803
PeptideAtlas P22803
EnsemblFungi [example_ID YGR209C]
GeneID 853123
KEGG sce:YGR209C
SGD S000003441
eggNOG COG0526
GeneTree ENSGT00530000063008
HOGENOM HOG000292977
InParanoid P22803
KO K03671
OMA CKMISPH
OrthoDB EOG71CFZN
BioCyc YEAST:G3O-30891-MONOMER
Reactome REACT_188484
REACT_189238
REACT_191152
REACT_238684
EvolutionaryTrace P22803
NextBio 973163
Proteomes UP000002311
Genevestigator P22803
GO GO:0005829
GO:0000324
GO:0000139
GO:0005634
GO:0015036
GO:0015035
GO:0045454
GO:0009263
GO:0006888
GO:0006749
GO:0006662
GO:0080058
GO:0015031
GO:0006890
GO:0000103
GO:0042144
GO:0000011
Gene3D 3.40.30.10
InterPro IPR005746
IPR012336
IPR017937
IPR013766
PANTHER PTHR10438
Pfam PF00085
PIRSF PIRSF000077
SUPFAM SSF52833
TIGRFAMs TIGR01068
PROSITE PS00194
PS51352

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0045454

cell redox homeostasis

PMID:22561702[1]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004033

P

Seeded From UniProt

complete

involved_in

GO:0080058

protein deglutathionylation

PMID:27708136[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_input:(UniProtKB:Q12324)

Seeded From UniProt

complete

involved_in

GO:0006749

glutathione metabolic process

PMID:23242256[3]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000006012

P

Seeded From UniProt

complete

involved_in

GO:0080058

protein deglutathionylation

PMID:20074363[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004033

P

Seeded From UniProt

complete

involved_in

GO:0080058

protein deglutathionylation

PMID:20074363[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042144

vacuole fusion, non-autophagic

PMID:9657146[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0015036

disulfide oxidoreductase activity

PMID:1988444[6]

ECO:0000250

sequence similarity evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

involved_in

GO:0006890

retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum

PMID:9813082[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006888

endoplasmic reticulum to Golgi vesicle-mediated transport

PMID:9813082[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

GO:0000011

vacuole inheritance

PMID:8603912[8]

ECO:0000315

P

complete

part_of

GO:0005829

cytosol

PMID:8603912[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0000324

fungal-type vacuole

PMID:9657146[5]

ECO:0000353

physical interaction evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0000103

sulfate assimilation

PMID:2026619[9]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004033

P

Seeded From UniProt

complete

involved_in

GO:0000011

vacuole inheritance

PMID:8603912[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0000011

vacuole inheritance

PMID:9015301[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006662

glycerol ether metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005746

P

Seeded From UniProt

complete

enables

GO:0015035

protein disulfide oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005746

F

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005746
InterPro:IPR013766
InterPro:IPR017937

P

Seeded From UniProt

complete

involved_in

GO:0009263

deoxyribonucleotide biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0215

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

involved_in

GO:0015031

protein transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0653

P

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:0005794

Golgi apparatus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0333

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

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-0249

P

Seeded From UniProt

complete

part_of

GO:0000139

Golgi membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0134

C

Seeded From UniProt

complete

Notes

References

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

  1. Dardalhon, M et al. () Redox-sensitive YFP sensors monitor dynamic nuclear and cytosolic glutathione redox changes. Free Radic. Biol. Med. 52 2254-65 PubMed GONUTS page
  2. Chandel, A et al. (2016) Glutathione depletion activates the yeast vacuolar transient receptor potential channel, Yvc1p, by reversible glutathionylation of specific cysteines. Mol. Biol. Cell 27 3913-3925 PubMed GONUTS page
  3. Morgan, B et al. (2013) Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat. Chem. Biol. 9 119-25 PubMed GONUTS page
  4. 4.0 4.1 Greetham, D et al. (2010) Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae. BMC Biochem. 11 3 PubMed GONUTS page
  5. 5.0 5.1 Xu, Z et al. (1998) LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell 93 1125-34 PubMed GONUTS page
  6. Gan, ZR (1991) Yeast thioredoxin genes. J. Biol. Chem. 266 1692-6 PubMed GONUTS page
  7. 7.0 7.1 Spang, A & Schekman, R (1998) Reconstitution of retrograde transport from the Golgi to the ER in vitro. J. Cell Biol. 143 589-99 PubMed GONUTS page
  8. 8.0 8.1 8.2 Xu, Z & Wickner, W (1996) Thioredoxin is required for vacuole inheritance in Saccharomyces cerevisiae. J. Cell Biol. 132 787-94 PubMed GONUTS page
  9. Muller, EG (1991) Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. J. Biol. Chem. 266 9194-202 PubMed GONUTS page
  10. Xu, Z et al. (1997) A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to promote yeast vacuole inheritance. J. Cell Biol. 136 299-306 PubMed GONUTS page