Search results for TXN

Showing 20 results out of 47

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Species

Types

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Reaction types

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Protein (4 results from a total of 17)

TXN

Identifier: R-HSA-66000
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: TXN: P10599

TXN

Identifier: R-HSA-9617732
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: TXN: P10599
Identifier: R-HSA-73668
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P10599
Identifier: R-HSA-9617733
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: P10599

Reaction (4 results from a total of 17)

Identifier: R-HSA-9617735
Species: Homo sapiens
Compartment: nucleoplasm
Thioredoxin (TXN) reduces oxidized FOXO4 and disrupts interaction between FOXO4 and EP300 (p300). TXN-mediated disruption of FOXO4:EP300 complexes is negatively regulated by TXNIP (TBP-2), a TXN binding protein (Dansen et al. 2009).
Identifier: R-NUL-9617742
Species: Homo sapiens, Mus musculus
Compartment: nucleoplasm
Recombinant human thioredoxin (TXN) reduces oxidized recombinant mouse Foxo4 and disrupts interaction between Foxo4 and recombinant human EP300. TXN-mediated disruption of Foxo4:EP300 complexes is negatively regulated by recombinant human TXNIP (TBP-2), a TXN binding protein (Dansen et al. 2009).
Identifier: R-HSA-3697882
Species: Homo sapiens
Compartment: cytosol
Peroxiredoxin 5 (PRDX5) very efficiently reduces peroxynitrite using thioredoxin to yield nitrite (NO2-), water, and oxidized thioredoxin (Dubuisson et al. 2004). The N-terminal cysteine (Cys 47) of PRDX5 attacks the O-O peroxide bond of peroxynitrite.
Identifier: R-HSA-3341343
Species: Homo sapiens
Compartment: cytosol
Peroxiredoxin 1 (PRDX1), PRDX2, and PRDX5 in the cytosol reduce hydrogen peroxide (H2O2) with thioredoxin yielding oxidized thioredoxin and water (Yamashita et al. 1999, Lee et al. 2007, Nagy et al. 2011).

Complex (4 results from a total of 4)

Identifier: R-HSA-3225859
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-1250285
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3323058
Species: Homo sapiens
Compartment: mitochondrial matrix
Identifier: R-HSA-3323006
Species: Homo sapiens
Compartment: mitochondrial matrix

Chemical Compound (2 results from a total of 2)

Identifier: R-ALL-2142833
Compartment: cytosol
Primary external reference: ChEBI: thioredoxin disulfide: 18191
Identifier: R-ALL-2142774
Compartment: cytosol
Primary external reference: ChEBI: thioredoxin dithiol: 15967

Interactor (4 results from a total of 5)

Identifier: Q9NX01
Species: Homo sapiens
Primary external reference: UniProt: Q9NX01
Identifier: O14530
Species: Homo sapiens
Primary external reference: UniProt: O14530
Identifier: Q8N427
Species: Homo sapiens
Primary external reference: UniProt: Q8N427
Identifier: Q86VQ3
Species: Homo sapiens
Primary external reference: UniProt: Q86VQ3

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-5649944
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000198431

Pathway (1 results from a total of 1)

Identifier: R-HSA-2559580
Species: Homo sapiens
Oxidative stress, caused by increased concentration of reactive oxygen species (ROS) in the cell, can happen as a consequence of mitochondrial dysfunction induced by the oncogenic RAS (Moiseeva et al. 2009) or independent of oncogenic signaling. Prolonged exposure to interferon-beta (IFNB, IFN-beta) also results in ROS increase (Moiseeva et al. 2006). ROS oxidize thioredoxin (TXN), which causes TXN to dissociate from the N-terminus of MAP3K5 (ASK1), enabling MAP3K5 to become catalytically active (Saitoh et al. 1998). ROS also stimulate expression of Ste20 family kinases MINK1 (MINK) and TNIK through an unknown mechanism, and MINK1 and TNIK positively regulate MAP3K5 activation (Nicke et al. 2005).


MAP3K5 phosphorylates and activates MAP2K3 (MKK3) and MAP2K6 (MKK6) (Ichijo et al. 1997, Takekawa et al. 2005), which act as p38 MAPK kinases, as well as MAP2K4 (SEK1) (Ichijo et al. 1997, Matsuura et al. 2002), which, together with MAP2K7 (MKK7), acts as a JNK kinase.


MKK3 and MKK6 phosphorylate and activate p38 MAPK alpha (MAPK14) and beta (MAPK11) (Raingeaud et al. 1996), enabling p38 MAPKs to phosphorylate and activate MAPKAPK2 (MK2) and MAPKAPK3 (MK3) (Ben-Levy et al. 1995, Clifton et al. 1996, McLaughlin et al. 1996, Sithanandam et al. 1996, Meng et al. 2002, Lukas et al. 2004, White et al. 2007), as well as MAPKAPK5 (PRAK) (New et al. 1998 and 2003, Sun et al. 2007).


Phosphorylation of JNKs (MAPK8, MAPK9 and MAPK10) by MAP3K5-activated MAP2K4 (Deacon and Blank 1997, Fleming et al. 2000) allows JNKs to migrate to the nucleus (Mizukami et al. 1997) where they phosphorylate JUN. Phosphorylated JUN binds FOS phosphorylated by ERK1 or ERK2, downstream of activated RAS (Okazaki and Sagata 1995, Murphy et al. 2002), forming the activated protein 1 (AP-1) complex (FOS:JUN heterodimer) (Glover and Harrison 1995, Ainbinder et al. 1997).


Activation of p38 MAPKs and JNKs downstream of MAP3K5 (ASK1) ultimately converges on transcriptional regulation of CDKN2A locus. In dividing cells, nucleosomes bound to the CDKN2A locus are trimethylated on lysine residue 28 of histone H3 (HIST1H3A) by the Polycomb repressor complex 2 (PRC2), creating the H3K27Me3 (Me3K-28-HIST1H3A) mark (Bracken et al. 2007, Kotake et al. 2007). The expression of Polycomb constituents of PRC2 (Kuzmichev et al. 2002) - EZH2, EED and SUZ12 - and thereby formation of the PRC2, is positively regulated in growing cells by E2F1, E2F2 and E2F3 (Weinmann et al. 2001, Bracken et al. 2003). H3K27Me3 mark serves as a docking site for the Polycomb repressor complex 1 (PRC1) that contains BMI1 (PCGF4) and is therefore named PRC1.4, leading to the repression of transcription of p16INK4A and p14ARF from the CDKN2A locus, where PCR1.4 mediated repression of p14ARF transcription in humans may be context dependent (Voncken et al. 2005, Dietrich et al. 2007, Agherbi et al. 2009, Gao et al. 2012). MAPKAPK2 and MAPKAPK3, activated downstream of the MAP3K5-p38 MAPK cascade, phosphorylate BMI1 of the PRC1.4 complex, leading to dissociation of PRC1.4 complex from the CDKN2A locus and upregulation of p14ARF transcription (Voncken et al. 2005). AP-1 transcription factor, formed as a result of MAP3K5-JNK signaling, as well as RAS signaling, binds the promoter of KDM6B (JMJD3) gene and stimulates KDM6B expression. KDM6B is a histone demethylase that removes H3K27Me3 mark i.e. demethylates lysine K28 of HIST1H3A, thereby preventing PRC1.4 binding to the CDKN2A locus and allowing transcription of p16INK4A (Agger et al. 2009, Barradas et al. 2009, Lin et al. 2012).


p16INK4A inhibits phosphorylation-mediated inactivation of RB family members by CDK4 and CDK6, leading to cell cycle arrest (Serrano et al. 1993). p14ARF inhibits MDM2-mediated degradation of TP53 (p53) (Zhang et al. 1998), which also contributes to cell cycle arrest in cells undergoing oxidative stress. In addition, phosphorylation of TP53 by MAPKAPK5 (PRAK) activated downstream of MAP3K5-p38 MAPK signaling, activates TP53 and contributes to cellular senescence (Sun et al. 2007).

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