TXN | ENSG00000136810 | NCBI 7295

Details for: TXN

Gene ID: 7295

Symbol: TXN

Ensembl ID: ENSG00000136810

Description: thioredoxin

Associated with

Cell recruitment (pro-inflammatory response)
(R-HSA-9664424)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to chemical stress
(R-HSA-9711123)
Cellular senescence
(R-HSA-2559583)
Detoxification of reactive oxygen species
(R-HSA-3299685)
Disease
(R-HSA-1643685)
Foxo-mediated transcription
(R-HSA-9614085)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Inflammasomes
(R-HSA-622312)
Innate immune system
(R-HSA-168249)
Interconversion of nucleotide di- and triphosphates
(R-HSA-499943)
Keap1-nfe2l2 pathway
(R-HSA-9755511)
Leishmania infection
(R-HSA-9658195)
Metabolism
(R-HSA-1430728)
Metabolism of nucleotides
(R-HSA-15869)
Metabolism of proteins
(R-HSA-392499)
Nfe2l2 regulating anti-oxidant/detoxification enzymes
(R-HSA-9818027)
Nuclear events mediated by nfe2l2
(R-HSA-9759194)
Nucleotide-binding domain, leucine rich repeat containing receptor (nlr) signaling pathways
(R-HSA-168643)
Oxidative stress induced senescence
(R-HSA-2559580)
Parasitic infection pathways
(R-HSA-9824443)
Protein repair
(R-HSA-5676934)
Purinergic signaling in leishmaniasis infection
(R-HSA-9660826)
Regulation of foxo transcriptional activity by acetylation
(R-HSA-9617629)
Rna polymerase ii transcription
(R-HSA-73857)
The nlrp3 inflammasome
(R-HSA-844456)
Tp53 regulates metabolic genes
(R-HSA-5628897)
Transcriptional regulation by tp53
(R-HSA-3700989)
Cell redox homeostasis
(GO:0045454)
Cellular detoxification of hydrogen peroxide
(GO:0061692)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Extracellular exosome
(GO:0070062)
Extracellular region
(GO:0005576)
Negative regulation of protein export from nucleus
(GO:0046826)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Positive regulation of dna binding
(GO:0043388)
Positive regulation of peptidyl-cysteine s-nitrosylation
(GO:2000170)
Positive regulation of peptidyl-serine phosphorylation
(GO:0033138)
Positive regulation of phosphatidylinositol 3-kinase/protein kinase b signal transduction
(GO:0051897)
Protein-disulfide reductase (nad(p)h) activity
(GO:0047134)
Protein-disulfide reductase activity
(GO:0015035)
Protein binding
(GO:0005515)
Protein homodimerization activity
(GO:0042803)
Response to nitric oxide
(GO:0071731)
Response to radiation
(GO:0009314)
Rna binding
(GO:0003723)
Thioredoxin-disulfide reductase (nadph) activity
(GO:0004791)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 648.3645
Cell Significance Index: -100.8500
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 374.8964
Cell Significance Index: -95.0900
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 342.3372
Cell Significance Index: -141.0300
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 285.2437
Cell Significance Index: -134.6700
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 252.0387
Cell Significance Index: -129.6500
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 201.1111
Cell Significance Index: -134.9500
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 101.5040
Cell Significance Index: -125.1500
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 36.2710
Cell Significance Index: -97.1700
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 34.4028
Cell Significance Index: -135.7600
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 25.7891
Cell Significance Index: -79.2100
Cell Name: oral mucosa squamous cell (CL1001576)
Fold Change: 19.9965
Cell Significance Index: 171.8300
Cell Name: prostate gland microvascular endothelial cell (CL2000059)
Fold Change: 12.1040
Cell Significance Index: 86.9300
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 8.6900
Cell Significance Index: 249.1100
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: 6.8266
Cell Significance Index: 120.6400
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 6.5983
Cell Significance Index: 176.5000
Cell Name: monocyte-derived dendritic cell (CL0011031)
Fold Change: 6.1943
Cell Significance Index: 106.4200
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: 6.1365
Cell Significance Index: 37.7700
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 5.5838
Cell Significance Index: 262.4400
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 5.2466
Cell Significance Index: 109.8200
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 5.1419
Cell Significance Index: 363.6600
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 4.9201
Cell Significance Index: 366.6900
Cell Name: cell in vitro (CL0001034)
Fold Change: 4.6831
Cell Significance Index: 2557.5600
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 4.5065
Cell Significance Index: 812.3900
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 4.4322
Cell Significance Index: 40.8200
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 4.3189
Cell Significance Index: 126.8400
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 4.2805
Cell Significance Index: 526.3300
Cell Name: peg cell (CL4033014)
Fold Change: 4.1756
Cell Significance Index: 96.4700
Cell Name: lactocyte (CL0002325)
Fold Change: 4.1122
Cell Significance Index: 531.2700
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 3.7982
Cell Significance Index: 177.0900
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 3.7083
Cell Significance Index: 1639.5300
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 3.5606
Cell Significance Index: 40.4500
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 3.3271
Cell Significance Index: 456.9100
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 3.1891
Cell Significance Index: 34.6700
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 3.1011
Cell Significance Index: 84.4100
Cell Name: granulosa cell (CL0000501)
Fold Change: 2.4672
Cell Significance Index: 64.8800
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 2.3606
Cell Significance Index: 43.6300
Cell Name: kidney cell (CL1000497)
Fold Change: 2.2933
Cell Significance Index: 18.3100
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 1.9152
Cell Significance Index: 86.8100
Cell Name: odontoblast (CL0000060)
Fold Change: 1.8746
Cell Significance Index: 240.3100
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 1.5914
Cell Significance Index: 45.8500
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.5256
Cell Significance Index: 79.2500
Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.5248
Cell Significance Index: 98.3800
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 1.0347
Cell Significance Index: 35.9600
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.9445
Cell Significance Index: 187.4400
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 0.8538
Cell Significance Index: 245.6600
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.8051
Cell Significance Index: 22.5000
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.7254
Cell Significance Index: 549.0500
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.6279
Cell Significance Index: 16.7700
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.5889
Cell Significance Index: 100.5600
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.5020
Cell Significance Index: 81.6500
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.3039
Cell Significance Index: 60.9600
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.2442
Cell Significance Index: 16.8900
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.2359
Cell Significance Index: 44.8900
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.1907
Cell Significance Index: 172.1800
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.1900
Cell Significance Index: 22.4100
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.1849
Cell Significance Index: 9.7100
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.1430
Cell Significance Index: 104.8800
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.0986
Cell Significance Index: 35.3500
Cell Name: paneth cell of colon (CL0009009)
Fold Change: 0.0734
Cell Significance Index: 1.1000
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.0639
Cell Significance Index: 1.0700
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.0252
Cell Significance Index: 2.5000
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.0068
Cell Significance Index: 0.4200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.0127
Cell Significance Index: -0.4500
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0165
Cell Significance Index: -12.2400
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.0328
Cell Significance Index: -1.0500
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: -0.0445
Cell Significance Index: -83.8200
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0616
Cell Significance Index: -6.2900
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0809
Cell Significance Index: -149.2300
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0880
Cell Significance Index: -54.9600
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0982
Cell Significance Index: -151.2200
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.1173
Cell Significance Index: -159.4800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.1460
Cell Significance Index: -92.7400
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.1713
Cell Significance Index: -96.6200
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.2799
Cell Significance Index: -127.0500
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.3374
Cell Significance Index: -71.0700
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.4525
Cell Significance Index: -11.5600
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.5105
Cell Significance Index: -40.4300
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.5355
Cell Significance Index: -61.3500
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.5871
Cell Significance Index: -68.4200
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.7494
Cell Significance Index: -16.2400
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.8097
Cell Significance Index: -117.7000
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.8671
Cell Significance Index: -11.8300
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.9487
Cell Significance Index: -108.2900
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -1.2990
Cell Significance Index: -135.2600
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -1.3117
Cell Significance Index: -78.7500
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -1.6677
Cell Significance Index: -127.9800
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -1.6728
Cell Significance Index: -105.4300
Cell Name: extravillous trophoblast (CL0008036)
Fold Change: -1.6802
Cell Significance Index: -10.4400
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -1.7719
Cell Significance Index: -99.4300
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -1.8356
Cell Significance Index: -123.4300
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -1.9634
Cell Significance Index: -49.0800
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -2.0173
Cell Significance Index: -25.8400
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -2.1804
Cell Significance Index: -133.6800
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -2.2692
Cell Significance Index: -13.7100
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -2.2767
Cell Significance Index: -67.0600
Cell Name: melanocyte of skin (CL1000458)
Fold Change: -2.3472
Cell Significance Index: -32.9000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -2.6594
Cell Significance Index: -68.3600
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -2.7922
Cell Significance Index: -59.4700
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -2.9515
Cell Significance Index: -79.0900
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -3.0108
Cell Significance Index: -110.5300

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** TXN is a small, 12-kDa protein that belongs to the thioredoxin superfamily. Its structure consists of a single domain with a cysteine residue at its active site, which is essential for its redox activity. The protein exhibits high affinity for reduced glutathione (GSH), allowing it to efficiently reduce oxidized cysteine residues in target proteins. TXN is also capable of disulfide bond formation and reduction, enabling it to participate in protein disulfide reductase activity. **Pathways and Functions** TXN's functions are mediated through its interactions with various cellular pathways, including: 1. **Cellular Redox Homeostasis**: TXN's primary role is to maintain the balance of reduced and oxidized glutathione levels, ensuring that the cellular redox environment remains optimal for protein function. 2. **Protein Function Regulation**: TXN reduces oxidized cysteine residues in target proteins, thereby restoring their proper function and activity. 3. **Immune Response**: TXN modulates immune responses by regulating the activity of key immune molecules, such as inflammatory cytokines and transcription factors. 4. **Cellular Stress Response**: TXN participates in the cellular response to stress, including oxidative stress, heat shock, and radiation-induced damage. 5. **Detoxification of Reactive Oxygen Species**: TXN helps to neutralize reactive oxygen species (ROS) by reducing hydrogen peroxide and other oxidants. **Clinical Significance** TXN's dysregulation has been implicated in various diseases, including: 1. **Oxidative Stress-Related Disorders**: TXN's dysfunction has been linked to conditions such as atherosclerosis, cancer, and neurodegenerative diseases. 2. **Infectious Diseases**: TXN plays a crucial role in the immune response to infections, and its dysregulation has been implicated in diseases such as Leishmania infection. 3. **Metabolic Disorders**: TXN's role in regulating metabolic pathways, including glucose and lipid metabolism, makes it an important target for the treatment of metabolic disorders. 4. **Cancer**: TXN's expression and activity have been found to be altered in various types of cancer, suggesting its potential as a biomarker or therapeutic target. In conclusion, TXN is a multifunctional protein that plays a critical role in maintaining cellular redox homeostasis, regulating protein function, and modulating immune responses. Its dysregulation has been implicated in various diseases, highlighting its importance as a therapeutic target and potential biomarker.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Thioredoxin

Genular Protein ID: 1291118948

Symbol: THIO_HUMAN

Name: Thioredoxin

UniProtKB Accession Codes:

P10599 B1ALW1 O60744 Q53X69 Q96KI3 Q9UDG5

Database IDs:

Citations:

PubMed ID: 3170595

Title: Cloning and expression of a cDNA for human thioredoxin.

PubMed ID: 3170595

DOI: 10.1016/s0021-9258(19)37617-3

PubMed ID: 2785919

Title: ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction.

PubMed ID: 2785919

DOI: 10.1002/j.1460-2075.1989.tb03436.x

PubMed ID: 1874447

Title: Isolation and characterization of human thioredoxin-encoding genes.

PubMed ID: 1874447

DOI: 10.1016/0378-1119(91)90081-l

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15164053

Title: DNA sequence and analysis of human chromosome 9.

PubMed ID: 15164053

DOI: 10.1038/nature02465

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7818492

Title: Characterization of a thioredoxin-related surface protein.

PubMed ID: 7818492

DOI: 10.1042/bj3040861

PubMed ID: 1998498

Title: Identification of a thioredoxin-related protein associated with plasma membranes.

PubMed ID: 1998498

DOI: 10.1016/s0006-291x(05)81209-4

PubMed ID: 2176490

Title: Human thioredoxin reactivity-structure/function relationship.

PubMed ID: 2176490

DOI: 10.1016/s0006-291x(05)80940-4

PubMed ID: 1332947

Title: Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway.

PubMed ID: 1332947

DOI: 10.1016/s0021-9258(18)35742-9

PubMed ID: 9108029

Title: AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1.

PubMed ID: 9108029

DOI: 10.1073/pnas.94.8.3633

PubMed ID: 11118054

Title: Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation.

PubMed ID: 11118054

PubMed ID: 15246877

Title: S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1.

PubMed ID: 15246877

DOI: 10.1016/j.abb.2004.06.004

PubMed ID: 16408020

Title: Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine.

PubMed ID: 16408020

DOI: 10.1038/nchembio720

PubMed ID: 17182577

Title: Cross-reactivity and 1.4-A crystal structure of Malassezia sympodialis thioredoxin (Mala s 13), a member of a new pan-allergen family.

PubMed ID: 17182577

DOI: 10.4049/jimmunol.178.1.389

PubMed ID: 17606900

Title: Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells.

PubMed ID: 17606900

DOI: 10.1073/pnas.0704898104

PubMed ID: 19032234

Title: Auto- and cross-reactivity to thioredoxin allergens in allergic bronchopulmonary aspergillosis.

PubMed ID: 19032234

DOI: 10.1111/j.1398-9995.2008.01777.x

PubMed ID: 19690162

Title: Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxin.

PubMed ID: 19690162

DOI: 10.1074/jbc.m109.010363

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21489611

Title: Malassezia sympodialis thioredoxin-specific T cells are highly cross-reactive to human thioredoxin in atopic dermatitis.

PubMed ID: 21489611

DOI: 10.1016/j.jaci.2011.02.043

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 2684271

Title: A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin.

PubMed ID: 2684271

DOI: 10.1021/bi00443a045

PubMed ID: 2001356

Title: High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution.

PubMed ID: 2001356

DOI: 10.1021/bi00224a017

PubMed ID: 7922028

Title: The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin.

PubMed ID: 7922028

DOI: 10.1016/s0969-2126(00)00051-4

PubMed ID: 7788295

Title: Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.

PubMed ID: 7788295

DOI: 10.1016/s0969-2126(01)00159-9

PubMed ID: 8736558

Title: The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.

PubMed ID: 8736558

DOI: 10.1016/s0969-2126(96)00065-2

PubMed ID: 8805557

Title: Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.

PubMed ID: 8805557

DOI: 10.1016/s0969-2126(96)00079-2

PubMed ID: 9369469

Title: Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant.

PubMed ID: 9369469

DOI: 10.1021/bi971004s

PubMed ID: 17260951

Title: Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin.

PubMed ID: 17260951

DOI: 10.1021/bi061878r

Sequence Information:

Length: 105
Mass: 11737
Checksum: 256F4E3C8A187693
Sequence:

MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD 
DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: TXN

Associated with

Cells (max top 100)

Other Information

Cloning and expression of a cDNA for human thioredoxin. PubMed ID: 3170595

ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. PubMed ID: 2785919

Isolation and characterization of human thioredoxin-encoding genes. PubMed ID: 1874447

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

DNA sequence and analysis of human chromosome 9. PubMed ID: 15164053

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Characterization of a thioredoxin-related surface protein. PubMed ID: 7818492

Identification of a thioredoxin-related protein associated with plasma membranes. PubMed ID: 1998498

Human thioredoxin reactivity-structure/function relationship. PubMed ID: 2176490

Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. PubMed ID: 1332947

AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. PubMed ID: 9108029

Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation. PubMed ID: 11118054

S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1. PubMed ID: 15246877

Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. PubMed ID: 16408020

Cross-reactivity and 1.4-A crystal structure of Malassezia sympodialis thioredoxin (Mala s 13), a member of a new pan-allergen family. PubMed ID: 17182577

Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells. PubMed ID: 17606900

Auto- and cross-reactivity to thioredoxin allergens in allergic bronchopulmonary aspergillosis. PubMed ID: 19032234

Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxin. PubMed ID: 19690162

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Initial characterization of the human central proteome. PubMed ID: 21269460

Malassezia sympodialis thioredoxin-specific T cells are highly cross-reactive to human thioredoxin in atopic dermatitis. PubMed ID: 21489611

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin. PubMed ID: 2684271

High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. PubMed ID: 2001356

The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. PubMed ID: 7922028

Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B. PubMed ID: 7788295

The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. PubMed ID: 8736558

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. PubMed ID: 8805557

Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --&gt; asparagine mutant. PubMed ID: 9369469

Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin. PubMed ID: 17260951