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P10599 (THIO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin

Short name=Trx
Alternative name(s):
ATL-derived factor
Short name=ADF
Surface-associated sulphydryl protein
Short name=SASP
Gene names
Name:TXN
Synonyms:TRDX, TRX, TRX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.17 Ref.19 Ref.20 Ref.22 Ref.23

ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55). Ref.17 Ref.19 Ref.20 Ref.22 Ref.23

Subunit structure

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. Ref.19 Ref.21 Ref.25 Ref.34 Ref.35

Subcellular location

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. Ref.18 Ref.19 Ref.20

Induction

Up-regulated by ionizing radiation. Ref.20

Post-translational modification

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.

In case of infection, ubiquitinated by S.typhimurium protein slrP, leading to its degradation.

Sequence similarities

Belongs to the thioredoxin family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Biological processElectron transport
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
   DomainRedox-active center
   Molecular functionActivator
   PTMAcetylation
Disulfide bond
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Traceable author statement Ref.1. Source: ProtInc

cell redox homeostasis

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Traceable author statement PubMed 10947064. Source: ProtInc

cellular component movement

Traceable author statement PubMed 10947064. Source: ProtInc

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

innate immune response

Traceable author statement. Source: Reactome

negative regulation of protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

oxidation-reduction process

Inferred from direct assay Ref.20. Source: UniProtKB

positive regulation of DNA binding

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of protein import into nucleus, translocation

Inferred from direct assay Ref.20. Source: UniProtKB

response to radiation

Inferred from direct assay Ref.20. Source: UniProtKB

signal transduction

Traceable author statement PubMed 10947064. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpeptide disulfide oxidoreductase activity

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10599-1)

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.
Isoform 2 (identifier: P10599-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14 Ref.15
Chain2 – 105104Thioredoxin
PRO_0000120005

Regions

Domain2 – 105104Thioredoxin

Sites

Active site321Nucleophile
Active site351Nucleophile
Site261Deprotonates C-terminal active site Cys
Site331Contributes to redox potential value
Site341Contributes to redox potential value

Amino acid modifications

Modified residue31N6-acetyllysine Ref.26
Modified residue81N6-succinyllysine By similarity
Modified residue391N6-acetyllysine Ref.26
Modified residue621S-nitrosocysteine Ref.35
Modified residue691S-nitrosocysteine Ref.35
Modified residue731S-nitrosocysteine; alternate Ref.22 Ref.23
Modified residue941N6-acetyllysine; alternate By similarity
Modified residue941N6-succinyllysine; alternate By similarity
Disulfide bond32 ↔ 35Redox-active Ref.29 Ref.35
Disulfide bond73Interchain; alternate Ref.35

Natural variations

Alternative sequence44 – 6320Missing in isoform 2.
VSP_045607

Experimental info

Mutagenesis321C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-35. Ref.19
Mutagenesis351C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-32. Ref.19
Mutagenesis601D → N: Loss of pH-dependence of dimerization.
Mutagenesis621C → S: Retains its reducing activity. Retains interaction with APEX1 and transcription activation; when associated with S-69 and S-73. Ref.19
Mutagenesis691C → 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. Ref.19 Ref.23
Mutagenesis701E → A: Strongly reduced interaction with CASP3; when associated with A-72. Ref.23
Mutagenesis721K → A: Strongly reduced interaction with CASP3; when associated with A-70. Ref.23
Mutagenesis731C → D: Strongly reduced S-nitrosylation of CASP3. Ref.19 Ref.22 Ref.23
Mutagenesis731C → 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. Ref.19 Ref.22 Ref.23
Mutagenesis731C → S: Retains its reducing activity. Ref.19 Ref.22 Ref.23
Sequence conflict391K → N in AAA74596. Ref.1
Sequence conflict391K → N in AAF86466. Ref.4
Sequence conflict741M → T in AAA74596. Ref.1
Sequence conflict741M → T in AAF86466. Ref.4

Secondary structure

...................... 105
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 256F4E3C8A187693

FASTA10511,737
        10         20         30         40         50         60 
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD 

        70         80         90        100 
DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV 

« Hide

Isoform 2 [UniParc].

Checksum: 3CC6254BD6A1D66F
Show »

FASTA859,452

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Human thioredoxin reactivity-structure/function relationship."
Jacquot J.-P., de Lamotte F., Fontecav M., Schuermann P., Decottignies P., Miginiac-Maslow M., Wollman E.
Biochem. Biophys. Res. Commun. 173:1375-1381(1990) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJH0568.
RefSeqNP_001231867.1. NM_001244938.1.
NP_003320.2. NM_003329.3.
UniGeneHs.435136.

3D structure databases

PDBe
RCSB PDB
PDBj
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-A1-65[»]
1MDINMR-A2-104[»]
1MDJNMR-A2-104[»]
1MDKNMR-A2-104[»]
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[»]
ProteinModelPortalP10599.
SMRP10599. Positions 1-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113146. 65 interactions.
DIPDIP-6129N.
IntActP10599. 28 interactions.
MINTMINT-1522967.
STRING9606.ENSP00000363641.

Chemistry

ChEMBLCHEMBL2010624.

Protein family/group databases

Allergome3543. Hom s Trx.

PTM databases

PhosphoSiteP10599.

Polymorphism databases

DMDM135773.

2D gel databases

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

Proteomic databases

PaxDbP10599.
PeptideAtlasP10599.
PRIDEP10599.

Protocols and materials databases

DNASU7295.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374515; ENSP00000363639; ENSG00000136810. [P10599-2]
ENST00000374517; ENSP00000363641; ENSG00000136810. [P10599-1]
GeneID7295.
KEGGhsa:7295.
UCSCuc004bep.2. human. [P10599-1]

Organism-specific databases

CTD7295.
GeneCardsGC09M113006.
HGNCHGNC:12435. TXN.
HPACAB008678.
HPA047478.
MIM187700. gene.
neXtProtNX_P10599.
PharmGKBPA37091.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000292977.
HOVERGENHBG009243.
InParanoidP10599.
KOK03671.
OMASKYAFQE.
OrthoDBEOG7H4DX9.
PhylomeDBP10599.
TreeFamTF318932.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_120956. Cellular responses to stress.
REACT_6900. Immune System.
SignaLinkP10599.

Gene expression databases

ArrayExpressP10599.
BgeeP10599.
CleanExHS_TXN.
GenevestigatorP10599.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERPTHR10438. PTHR10438. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFPIRSF000077. Thioredoxin. 1 hit.
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTXN. human.
EvolutionaryTraceP10599.
GeneWikiThioredoxin.
GenomeRNAi7295.
NextBio28523.
PROP10599.
SOURCESearch...

Entry information

Entry nameTHIO_HUMAN
AccessionPrimary (citable) accession number: P10599
Secondary accession number(s): B1ALW1 expand/collapse secondary AC list , O60744, Q53X69, Q96KI3, Q9UDG5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM