oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
protein binding
thioredoxin-disulfide reductase activity
protein-disulfide reductase (NAD(P)) activity
RNA binding
Cellular component
extracellular region
extracellular exosome
nucleus
cytoplasm
mitochondrion
cytosol
nucleoplasm
Biological process
activation of protein kinase B activity
positive regulation of protein kinase B signaling
nucleobase-containing small molecule interconversion
glycerol ether metabolic process
regulation of transcription, DNA-templated
cell-cell signaling
negative regulation of transcription by RNA polymerase II
cell redox homeostasis
transcription, DNA-templated
positive regulation of peptidyl-serine phosphorylation
negative regulation of protein export from nucleus
response to radiation
positive regulation of DNA binding
negative regulation of hydrogen peroxide-induced cell death
cell population proliferation
signal transduction
protein repair
cellular oxidant detoxification
cellular response to oxidative stress
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
7295
22166
Ensembl
ENSG00000136810
ENSMUSG00000028367
UniProt
P10599
P10639
RefSeq (mRNA)
NM_003329 NM_001244938
NM_011660
RefSeq (protein)
NP_001231867 NP_003320
NP_035790
Location (UCSC)
Chr 9: 110.24 – 110.26 Mb
Chr 4: 57.94 – 57.96 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Thioredoxin (TRX or TXN) is a class of small redox proteins known to be present in all organisms. It plays a role in many important biological processes, including redox signaling. In humans, thioredoxins are encoded by TXN and TXN2 genes.[5][6] Loss-of-function mutation of either of the two human thioredoxin genes is lethal at the four-cell stage of the developing embryo. Although not entirely understood, thioredoxin is linked to medicine through their response to reactive oxygen species (ROS). In plants, thioredoxins regulate a spectrum of critical functions, ranging from photosynthesis to growth, flowering and the development and germination of seeds. Thioredoxins play a role in cell-to-cell communication.[7]
^ abcGRCh38: Ensembl release 89: ENSG00000136810 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000028367 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Wollman EE, d'Auriol L, Rimsky L, Shaw A, Jacquot JP, Wingfield P, Graber P, Dessarps F, Robin P, Galibert F (October 1988). "Cloning and expression of a cDNA for human thioredoxin". The Journal of Biological Chemistry. 263 (30): 15506–12. doi:10.1016/S0021-9258(19)37617-3. PMID 3170595.
^"Entrez Gene: TXN2 thioredoxin 2".
^Meng L, Wong JH, Feldman LJ, Lemaux PG, Buchanan BB (February 2010). "A membrane-associated thioredoxin required for plant growth moves from cell to cell, suggestive of a role in intercellular communication". Proceedings of the National Academy of Sciences of the United States of America. 107 (8): 3900–5. Bibcode:2010PNAS..107.3900M. doi:10.1073/pnas.0913759107. PMC 2840455. PMID 20133584.
Thioredoxin (TRX or TXN) is a class of small redox proteins known to be present in all organisms. It plays a role in many important biological processes...
Thioredoxin reductases (TR, TrxR) (EC 1.8.1.9) are enzymes that reduce thioredoxin (Trx). Two classes of thioredoxin reductase have been identified: one...
chloroplasts. The thioredoxin system contains the 12-kDa protein thioredoxin and its companion thioredoxin reductase. Proteins related to thioredoxin are present...
Thioredoxins are small disulfide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general...
The thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical...
existing ones. The T7 DNA polymerase requires a host factor, E. coli thioredoxin, in order to carry out its function. This helps stabilize the binding...
Thioredoxin-interacting protein is a protein that in humans is encoded by the TXNIP gene. TXNIP has been shown to interact with Thioredoxin and ZBTB32...
is a component of the antioxidant enzymes glutathione peroxidase and thioredoxin reductase (which indirectly reduce certain oxidized molecules in animals...
December 2001). "Physiological functions of thioredoxin and thioredoxin reductase: Thioredoxin and thioredoxin reductase". European Journal of Biochemistry...
electrons donated from the dithiol groups of the protein thioredoxin. Regeneration of thioredoxin occurs when nicotinamide adenine dinucleotide phosphate...
potential Glutathione-ascorbate cycle Bacterial glutathione transferase Thioredoxin, a cysteine-containing small proteins with very similar functions as...
Thioredoxin reductase 1, cytoplasmic is an enzyme that in humans is encoded by the TXNRD1 gene. This gene encodes a member of the family of pyridine nucleotide...
regulation systems at work when the cycle must be turned on or off: the thioredoxin/ferredoxin activation system, which activates some of the cycle enzymes;...
reduction of this disulfide bond is mediated by the NADPH-thioredoxin reductase-thioredoxin system. The light chain of BoNT acts as a metalloprotease...
bond to separate thiols occurs, mainly by the enzyme NADPH-thioredoxin reductase-thioredoxin. The light chain is then free to cleave the Gln76-Phe77 bond...
selenium-containing enzyme in some plants and in animals (thioredoxin reductase) generates reduced thioredoxin, a dithiol that serves as an electron source for...