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P10599

- THIO_HUMAN

UniProt

P10599 - THIO_HUMAN

Protein

Thioredoxin

Gene

TXN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
    ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei26 – 261Deprotonates C-terminal active site Cys
    Active sitei32 – 321Nucleophile
    Sitei33 – 331Contributes to redox potential value
    Sitei34 – 341Contributes to redox potential value
    Active sitei35 – 351Nucleophile

    GO - Molecular functioni

    1. peptide disulfide oxidoreductase activity Source: Ensembl
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. cell proliferation Source: ProtInc
    3. cell redox homeostasis Source: Ensembl
    4. cellular component movement Source: ProtInc
    5. glycerol ether metabolic process Source: InterPro
    6. innate immune response Source: Reactome
    7. negative regulation of protein export from nucleus Source: Ensembl
    8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. nucleobase-containing small molecule interconversion Source: Reactome
    10. nucleobase-containing small molecule metabolic process Source: Reactome
    11. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    12. oxidation-reduction process Source: UniProtKB
    13. positive regulation of DNA binding Source: UniProtKB
    14. regulation of protein import into nucleus, translocation Source: UniProtKB
    15. response to radiation Source: UniProtKB
    16. signal transduction Source: ProtInc
    17. small molecule metabolic process Source: Reactome
    18. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Electron transport, Transcription, Transcription regulation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
    REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    REACT_75808. The NLRP3 inflammasome.
    SignaLinkiP10599.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin
    Short name:
    Trx
    Alternative name(s):
    ATL-derived factor
    Short name:
    ADF
    Surface-associated sulphydryl protein
    Short name:
    SASP
    Gene namesi
    Name:TXN
    Synonyms:TRDX, TRX, TRX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12435. TXN.

    Subcellular locationi

    Nucleus. Cytoplasm. Secreted
    Note: Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrion Source: Ensembl
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-35. 1 Publication
    Mutagenesisi35 – 351C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-32. 1 Publication
    Mutagenesisi60 – 601D → N: Loss of pH-dependence of dimerization.
    Mutagenesisi62 – 621C → S: Retains its reducing activity. Retains interaction with APEX1 and transcription activation; when associated with S-69 and S-73. 1 Publication
    Mutagenesisi69 – 691C → S: No effect on reducing activity, interaction with APEX1 and on S-nitrosylation of C-73. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-73. 2 Publications
    Mutagenesisi70 – 701E → A: Strongly reduced interaction with CASP3; when associated with A-72. 1 Publication
    Mutagenesisi72 – 721K → A: Strongly reduced interaction with CASP3; when associated with A-70. 1 Publication
    Mutagenesisi73 – 731C → D: Strongly reduced S-nitrosylation of CASP3. 3 Publications
    Mutagenesisi73 – 731C → S: Loss of nitrosylation, and loss of S-nitrosylating activity towards CASP3. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-69. 3 Publications
    Mutagenesisi73 – 731C → S: Retains its reducing activity. 3 Publications

    Organism-specific databases

    PharmGKBiPA37091.

    Protein family/group databases

    Allergomei3543. Hom s Trx.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 105104ThioredoxinPRO_0000120005Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei8 – 81N6-succinyllysineBy similarity
    Disulfide bondi32 ↔ 35Redox-active2 PublicationsPROSITE-ProRule annotation
    Modified residuei39 – 391N6-acetyllysine1 Publication
    Modified residuei62 – 621S-nitrosocysteine2 Publications
    Modified residuei69 – 691S-nitrosocysteine2 Publications
    Modified residuei73 – 731S-nitrosocysteine; alternate3 Publications
    Disulfide bondi73 – 73Interchain; alternate1 Publication
    Modified residuei94 – 941N6-acetyllysine; alternateBy similarity
    Modified residuei94 – 941N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins.4 Publications
    In case of infection, ubiquitinated by S.typhimurium protein slrP, leading to its degradation.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP10599.
    PaxDbiP10599.
    PeptideAtlasiP10599.
    PRIDEiP10599.

    2D gel databases

    DOSAC-COBS-2DPAGEP10599.
    REPRODUCTION-2DPAGEIPI00216298.
    SWISS-2DPAGEP10599.

    PTM databases

    PhosphoSiteiP10599.

    Expressioni

    Inductioni

    Up-regulated by ionizing radiation.1 Publication

    Gene expression databases

    ArrayExpressiP10599.
    BgeeiP10599.
    CleanExiHS_TXN.
    GenevestigatoriP10599.

    Organism-specific databases

    HPAiCAB008678.
    HPA047478.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. In case of infection, interacts with S.typhimurium protein slrP. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COPS5Q929058EBI-594644,EBI-594661
    MAP3K5Q996832EBI-594644,EBI-476263
    MYD88Q998364EBI-594644,EBI-447677
    PTPN1P180312EBI-594644,EBI-968788

    Protein-protein interaction databases

    BioGridi113146. 60 interactions.
    DIPiDIP-6129N.
    IntActiP10599. 29 interactions.
    MINTiMINT-1522967.
    STRINGi9606.ENSP00000363641.

    Structurei

    Secondary structure

    1
    105
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi8 – 1710
    Turni18 – 203
    Beta strandi23 – 286
    Beta strandi30 – 323
    Helixi33 – 4816
    Turni49 – 513
    Beta strandi52 – 587
    Turni59 – 624
    Helixi63 – 697
    Beta strandi73 – 819
    Beta strandi84 – 918
    Helixi94 – 10411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AIUX-ray2.00A1-105[»]
    1AUCX-ray2.10A1-105[»]
    1CQGNMR-A1-105[»]
    1CQHNMR-A1-105[»]
    1ERTX-ray1.70A1-105[»]
    1ERUX-ray2.10A1-105[»]
    1ERVX-ray1.65A1-105[»]
    1ERWX-ray1.80A1-105[»]
    1M7TNMR-A1-66[»]
    1MDINMR-A1-105[»]
    1MDJNMR-A1-105[»]
    1MDKNMR-A1-105[»]
    1TRSNMR-A1-105[»]
    1TRUNMR-A1-105[»]
    1TRVNMR-A1-105[»]
    1TRWNMR-A1-105[»]
    1W1Cmodel-C1-105[»]
    1W1Emodel-C1-105[»]
    2HSHX-ray1.35A1-105[»]
    2HXKX-ray1.65A/B/C1-105[»]
    2IFQX-ray1.20A/B/C1-105[»]
    2IIYX-ray1.70A1-105[»]
    3E3EX-ray2.01A/B1-105[»]
    3KD0X-ray1.70A1-105[»]
    3M9JX-ray1.10A/B1-105[»]
    3M9KX-ray1.50A/B1-105[»]
    3QFAX-ray2.20C/D2-105[»]
    3QFBX-ray2.60C/D2-105[»]
    3TRXNMR-A1-105[»]
    4LL1X-ray2.00B/D1-105[»]
    4LL4X-ray2.70B/D1-105[»]
    4OO4X-ray0.97A/B1-105[»]
    4OO5X-ray1.54A1-105[»]
    4TRXNMR-A1-105[»]
    ProteinModelPortaliP10599.
    SMRiP10599. Positions 1-105.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10599.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 105104ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the thioredoxin family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000292977.
    HOVERGENiHBG009243.
    InParanoidiP10599.
    KOiK03671.
    OMAiCRVISPI.
    OrthoDBiEOG7H4DX9.
    PhylomeDBiP10599.
    TreeFamiTF318932.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PANTHERiPTHR10438. PTHR10438. 1 hit.
    PfamiPF00085. Thioredoxin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000077. Thioredoxin. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P10599-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS    50
    NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT 100
    INELV 105
    Length:105
    Mass (Da):11,737
    Last modified:January 23, 2007 - v3
    Checksum:i256F4E3C8A187693
    GO
    Isoform 2 (identifier: P10599-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         44-63: Missing.

    Show »
    Length:85
    Mass (Da):9,452
    Checksum:i3CC6254BD6A1D66F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391K → N in AAA74596. (PubMed:3170595)Curated
    Sequence conflicti39 – 391K → N in AAF86466. 1 PublicationCurated
    Sequence conflicti74 – 741M → T in AAA74596. (PubMed:3170595)Curated
    Sequence conflicti74 – 741M → T in AAF86466. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei44 – 6320Missing in isoform 2. 1 PublicationVSP_045607Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04026 mRNA. Translation: AAA74596.1.
    X77584 mRNA. Translation: CAA54687.1.
    X54539, X54540, X54541 Genomic DNA. Translation: CAA38410.1.
    AF276919 mRNA. Translation: AAF86466.1.
    AY004872 mRNA. Translation: AAF87085.1.
    AF313911 mRNA. Translation: AAG34699.1.
    AK289508 mRNA. Translation: BAF82197.1.
    CR407665 mRNA. Translation: CAG28593.1.
    AF548001 Genomic DNA. Translation: AAN33187.1.
    AL158158 Genomic DNA. Translation: CAI14066.1.
    AL158158 Genomic DNA. Translation: CAI14067.1.
    CH471105 Genomic DNA. Translation: EAW59059.1.
    CH471105 Genomic DNA. Translation: EAW59060.1.
    BC003377 mRNA. Translation: AAH03377.1.
    BC054866 mRNA. Translation: AAH54866.1.
    AF065241 mRNA. Translation: AAC17430.1.
    CCDSiCCDS35103.1. [P10599-1]
    CCDS59139.1. [P10599-2]
    PIRiJH0568.
    RefSeqiNP_001231867.1. NM_001244938.1. [P10599-2]
    NP_003320.2. NM_003329.3. [P10599-1]
    UniGeneiHs.435136.

    Genome annotation databases

    EnsembliENST00000374515; ENSP00000363639; ENSG00000136810. [P10599-2]
    ENST00000374517; ENSP00000363641; ENSG00000136810. [P10599-1]
    GeneIDi7295.
    KEGGihsa:7295.
    UCSCiuc004bep.2. human. [P10599-1]
    uc004beq.2. human.

    Polymorphism databases

    DMDMi135773.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04026 mRNA. Translation: AAA74596.1 .
    X77584 mRNA. Translation: CAA54687.1 .
    X54539 , X54540 , X54541 Genomic DNA. Translation: CAA38410.1 .
    AF276919 mRNA. Translation: AAF86466.1 .
    AY004872 mRNA. Translation: AAF87085.1 .
    AF313911 mRNA. Translation: AAG34699.1 .
    AK289508 mRNA. Translation: BAF82197.1 .
    CR407665 mRNA. Translation: CAG28593.1 .
    AF548001 Genomic DNA. Translation: AAN33187.1 .
    AL158158 Genomic DNA. Translation: CAI14066.1 .
    AL158158 Genomic DNA. Translation: CAI14067.1 .
    CH471105 Genomic DNA. Translation: EAW59059.1 .
    CH471105 Genomic DNA. Translation: EAW59060.1 .
    BC003377 mRNA. Translation: AAH03377.1 .
    BC054866 mRNA. Translation: AAH54866.1 .
    AF065241 mRNA. Translation: AAC17430.1 .
    CCDSi CCDS35103.1. [P10599-1 ]
    CCDS59139.1. [P10599-2 ]
    PIRi JH0568.
    RefSeqi NP_001231867.1. NM_001244938.1. [P10599-2 ]
    NP_003320.2. NM_003329.3. [P10599-1 ]
    UniGenei Hs.435136.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AIU X-ray 2.00 A 1-105 [» ]
    1AUC X-ray 2.10 A 1-105 [» ]
    1CQG NMR - A 1-105 [» ]
    1CQH NMR - A 1-105 [» ]
    1ERT X-ray 1.70 A 1-105 [» ]
    1ERU X-ray 2.10 A 1-105 [» ]
    1ERV X-ray 1.65 A 1-105 [» ]
    1ERW X-ray 1.80 A 1-105 [» ]
    1M7T NMR - A 1-66 [» ]
    1MDI NMR - A 1-105 [» ]
    1MDJ NMR - A 1-105 [» ]
    1MDK NMR - A 1-105 [» ]
    1TRS NMR - A 1-105 [» ]
    1TRU NMR - A 1-105 [» ]
    1TRV NMR - A 1-105 [» ]
    1TRW NMR - A 1-105 [» ]
    1W1C model - C 1-105 [» ]
    1W1E model - C 1-105 [» ]
    2HSH X-ray 1.35 A 1-105 [» ]
    2HXK X-ray 1.65 A/B/C 1-105 [» ]
    2IFQ X-ray 1.20 A/B/C 1-105 [» ]
    2IIY X-ray 1.70 A 1-105 [» ]
    3E3E X-ray 2.01 A/B 1-105 [» ]
    3KD0 X-ray 1.70 A 1-105 [» ]
    3M9J X-ray 1.10 A/B 1-105 [» ]
    3M9K X-ray 1.50 A/B 1-105 [» ]
    3QFA X-ray 2.20 C/D 2-105 [» ]
    3QFB X-ray 2.60 C/D 2-105 [» ]
    3TRX NMR - A 1-105 [» ]
    4LL1 X-ray 2.00 B/D 1-105 [» ]
    4LL4 X-ray 2.70 B/D 1-105 [» ]
    4OO4 X-ray 0.97 A/B 1-105 [» ]
    4OO5 X-ray 1.54 A 1-105 [» ]
    4TRX NMR - A 1-105 [» ]
    ProteinModelPortali P10599.
    SMRi P10599. Positions 1-105.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113146. 60 interactions.
    DIPi DIP-6129N.
    IntActi P10599. 29 interactions.
    MINTi MINT-1522967.
    STRINGi 9606.ENSP00000363641.

    Chemistry

    ChEMBLi CHEMBL2010624.

    Protein family/group databases

    Allergomei 3543. Hom s Trx.

    PTM databases

    PhosphoSitei P10599.

    Polymorphism databases

    DMDMi 135773.

    2D gel databases

    DOSAC-COBS-2DPAGE P10599.
    REPRODUCTION-2DPAGE IPI00216298.
    SWISS-2DPAGE P10599.

    Proteomic databases

    MaxQBi P10599.
    PaxDbi P10599.
    PeptideAtlasi P10599.
    PRIDEi P10599.

    Protocols and materials databases

    DNASUi 7295.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374515 ; ENSP00000363639 ; ENSG00000136810 . [P10599-2 ]
    ENST00000374517 ; ENSP00000363641 ; ENSG00000136810 . [P10599-1 ]
    GeneIDi 7295.
    KEGGi hsa:7295.
    UCSCi uc004bep.2. human. [P10599-1 ]
    uc004beq.2. human.

    Organism-specific databases

    CTDi 7295.
    GeneCardsi GC09M113006.
    HGNCi HGNC:12435. TXN.
    HPAi CAB008678.
    HPA047478.
    MIMi 187700. gene.
    neXtProti NX_P10599.
    PharmGKBi PA37091.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000292977.
    HOVERGENi HBG009243.
    InParanoidi P10599.
    KOi K03671.
    OMAi CRVISPI.
    OrthoDBi EOG7H4DX9.
    PhylomeDBi P10599.
    TreeFami TF318932.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    REACT_75808. The NLRP3 inflammasome.
    SignaLinki P10599.

    Miscellaneous databases

    ChiTaRSi TXN. human.
    EvolutionaryTracei P10599.
    GeneWikii Thioredoxin.
    GenomeRNAii 7295.
    NextBioi 28523.
    PROi P10599.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10599.
    Bgeei P10599.
    CleanExi HS_TXN.
    Genevestigatori P10599.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    PANTHERi PTHR10438. PTHR10438. 1 hit.
    Pfami PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000077. Thioredoxin. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a cDNA for human thioredoxin."
      Wollman E.E., D'Auriol L., Rimsky L., Shaw A., Jacquot J.-P., Wingfield P., Graber P., Dessarps F.
      J. Biol. Chem. 263:15506-15512(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction."
      Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J.
      EMBO J. 8:757-764(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Isolation and characterization of human thioredoxin-encoding genes."
      Tonissen K.F., Wells J.R.E.
      Gene 102:221-228(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Reddy P.G., Bhuyan D.K., Bhuyan K.C.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lens.
    5. "Cloning, purification and characterization of human lens thioredoxin."
      Liu A., Lou M.F.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lens.
    6. "Cloning and sequencing of thioredoxin cDNA from human brain."
      Xu J.Y., Xu L., Li K.S., Dai R.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cerebellum.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. NIEHS SNPs program
      Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    10. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cervix.
    13. "An alternative splice variant of human thioredoxin."
      Wang Y., Wang Y.G., Zhang Y., Yuan Y., Ma D.
      Chin. Sci. Bull. 43:292-295(1998)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-85 (ISOFORM 2), ALTERNATIVE SPLICING.
      Tissue: Liver.
    14. "Characterization of a thioredoxin-related surface protein."
      Dean M.F., Martin H., Sansom P.A.
      Biochem. J. 304:861-867(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21 AND 38-57.
      Tissue: Monocyte.
    15. "Identification of a thioredoxin-related protein associated with plasma membranes."
      Martin H., Dean M.
      Biochem. Biophys. Res. Commun. 175:123-128(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-15.
    16. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 9-48; 73-81 AND 95-105, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    17. Cited for: FUNCTION.
    18. "Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway."
      Rubartelli A., Bajetto A., Allavena G., Wollman E., Sitia R.
      J. Biol. Chem. 267:24161-24164(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    19. "AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1."
      Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., Yodoi J.
      Proc. Natl. Acad. Sci. U.S.A. 94:3633-3638(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH APEX1, MUTAGENESIS OF CYS-32; CYS-35; CYS-62; CYS-69 AND CYS-73, SUBCELLULAR LOCATION.
    20. "Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation."
      Wei S.J., Botero A., Hirota K., Bradbury C.M., Markovina S., Laszlo A., Spitz D.R., Goswami P.C., Yodoi J., Gius D.
      Cancer Res. 60:6688-6695(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION.
    21. "S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1."
      Yasinska I.M., Kozhukhar A.V., Sumbayev V.V.
      Arch. Biochem. Biophys. 428:198-203(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-NITROSYLATION, INTERACTION WITH MAP3K5.
    22. "Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine."
      Mitchell D.A., Marletta M.A.
      Nat. Chem. Biol. 1:154-158(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-73, S-NITROSYLATION AT CYS-73.
    23. "Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells."
      Mitchell D.A., Morton S.U., Fernhoff N.B., Marletta M.A.
      Proc. Natl. Acad. Sci. U.S.A. 104:11609-11614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-69; GLU-70; LYS-72 AND CYS-73, S-NITROSYLATION AT CYS-73 IN RESPONSE TO NITRIC OXIDE.
    24. "Abnormal proteins in primary breast cancer tissues from 25 Sudanese patients."
      Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M., Harbi S.O., Stansalas J., Mohamed A.O.
      Eur. J. Inflamm. 6:115-121(2008)
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    25. "Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase for mammalian thioredoxin."
      Bernal-Bayard J., Ramos-Morales F.
      J. Biol. Chem. 284:27587-27595(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH S.TYPHIMURIUM SLRP, UBIQUITINATION.
    26. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin."
      Forman-Kay J.D., Clore G.M., Dricoll P.C., Wingfield P., Richards F.M., Gronenborn A.M.
      Biochemistry 28:7088-7097(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    29. "High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution."
      Forman-Kay J.D., Clore G.M., Wingfield P., Gronenborn A.M.
      Biochemistry 30:2685-2698(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    30. "The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin."
      Qin J., Clore G.M., Gronenborn A.M.
      Structure 2:503-522(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    31. "Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B."
      Qin J., Clore G.M., Kennedy W.M., Huth J.R., Gronenborn A.M.
      Structure 3:289-297(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    32. "The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal."
      Qin J., Clore G.M., Kennedy W.P., Kuszewski J., Gronenborn A.M.
      Structure 4:613-620(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    33. "Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer."
      Weichsel A., Gasdaska J.R., Powis G., Montfort W.R.
      Structure 4:735-751(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
    34. "Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant."
      Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G., Montfort W.R.
      Biochemistry 36:13979-13988(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-60, SUBUNIT.
    35. "Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin."
      Weichsel A., Brailey J.L., Montfort W.R.
      Biochemistry 46:1219-1227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, DISULFIDE BONDS, S-NITROSYLATION AT CYS-62 AND CYS-69.

    Entry informationi

    Entry nameiTHIO_HUMAN
    AccessioniPrimary (citable) accession number: P10599
    Secondary accession number(s): B1ALW1
    , O60744, Q53X69, Q96KI3, Q9UDG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 178 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3