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Reviewed, UniProtKB/Swiss-Prot P10599 (THIO_HUMAN)

Last modified February 9, 2010. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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) [Complete 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. Ref.16 Ref.18 Ref.21

ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55). Ref.16 Ref.18 Ref.21

Subunit structure

Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. Ref.17 Ref.31 Ref.32

Subcellular location

Cytoplasm.

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.

Sequence similarities

Belongs to the thioredoxin family.

Contains 1 thioredoxin domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COPS5Q929055EBI-594644,EBI-594661
TXNIPQ9H3M72EBI-594644,EBI-1369170

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
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.24
Modified residue391N6-acetyllysine Ref.24
Modified residue621S-nitrosocysteine Ref.32
Modified residue691S-nitrosocysteine Ref.32
Modified residue731S-nitrosocysteine; alternate Ref.18 Ref.21
Modified residue941N6-acetyllysine Ref.20
Modified residue1001Phosphothreonine Ref.19
Disulfide bond32 ↔ 35Redox-active Ref.32 Ref.26
Disulfide bond73Interchain; alternate Ref.32

Experimental info

Mutagenesis601D → N: Loss of pH-dependence of dimerization.
Mutagenesis691C → S: No effect on activity and on S-nitrosylation of C-73. Ref.21
Mutagenesis701E → A: Strongly reduced interaction with CASP3; when associated with A-72. Ref.21
Mutagenesis721K → A: Strongly reduced interaction with CASP3; when associated with A-70. Ref.21
Mutagenesis731C → D: Strongly reduced S-nitrosylation of CASP3. Ref.18 Ref.21
Mutagenesis731C → S: Loss of nitrosylation, and loss of S-nitrosylating activity towards CASP3. Ref.18 Ref.21
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
P10599-1 [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

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: 3170595] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2785919] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Isolation and characterization of human thioredoxin-encoding genes."
Tonissen K.F., Wells J.R.E.
Gene 102:221-228(1991) [PubMed: 1874447] [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].
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].
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].
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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
[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: 15164053] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix.
[13]"Characterization of a thioredoxin-related surface protein."
Dean M.F., Martin H., Sansom P.A.
Biochem. J. 304:861-867(1994) [PubMed: 7818492] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21 AND 38-57.
Tissue: Monocyte.
[14]"Identification of a thioredoxin-related protein associated with plasma membranes."
Martin H., Dean M.
Biochem. Biophys. Res. Commun. 175:123-128(1991) [PubMed: 1998498] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15.
[15]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, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]"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: 2176490] [Abstract]
Cited for: FUNCTION.
[17]"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: 15246877] [Abstract]
Cited for: S-NITROSYLATION, INTERACTION WITH MAP3K5.
[18]"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: 16408020] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-73, S-NITROSYLATION AT CYS-73.
[19]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, MASS SPECTROMETRY.
Tissue: Hepatocyte.
[20]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94, MASS SPECTROMETRY.
Tissue: Epithelium.
[21]"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: 17606900] [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.
[22]"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.
[23]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-39, MASS SPECTROMETRY.
[25]"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: 2684271] [Abstract]
Cited for: STRUCTURE BY NMR.
[26]"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: 2001356] [Abstract]
Cited for: STRUCTURE BY NMR.
[27]"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: 7922028] [Abstract]
Cited for: STRUCTURE BY NMR.
[28]"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: 7788295] [Abstract]
Cited for: STRUCTURE BY NMR.
[29]"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: 8736558] [Abstract]
Cited for: STRUCTURE BY NMR.
[30]"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: 8805557] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[31]"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: 9369469] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-60, SUBUNIT.
[32]"Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin."
Weichsel A., Brailey J.L., Montfort W.R.
Biochemistry 46:1219-1227(2007) [PubMed: 17260951] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, DISULFIDE BONDS, S-NITROSYLATION AT CYS-62 AND CYS-69.
+Additional computationally mapped references.

Web resources

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.
CH471105 Genomic DNA. Translation: EAW59059.1.
BC003377 mRNA. Translation: AAH03377.1.
BC054866 mRNA. Translation: AAH54866.1.
IPIIPI00216298.
PIRJH0568.
RefSeqNP_003320.2.
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[»]
3TRXNMR-A1-105[»]
4TRXNMR-A1-105[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-6129N.
IntActP10599. 3 interactions.
STRINGP10599.

PTM databases

PhosphoSiteP10599.

2-D gel databases

SWISS-2DPAGEP10599.
Aarhus/Ghent-2DPAGE8006. IEF.
Cornea-2DPAGEP10599.
DOSAC-COBS-2DPAGEP10599.
PHCI-2DPAGEP10599.
REPRODUCTION-2DPAGEIPI00216298.
Siena-2DPAGEP10599.

Proteomic databases

PeptideAtlasP10599.
PRIDEP10599.

Genome annotation databases

EnsemblENST00000374517; ENSP00000363641; ENSG00000136810; Homo sapiens. [Genome view]
GeneID7295.
KEGGhsa:7295.
UCSCuc004bep.1. human.

Organism-specific databases

CTD7295.
GeneCardsGC09M112045.
H-InvDBHIX0008275.
HGNCHGNC:12435. TXN.
HPACAB008678.
MIM187700. gene.
PharmGKBPA37091.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG493509.
HOVERGENP10599.
InParanoidP10599.
OMAIESKYAF.
OrthoDBEOG969TD7.
PhylomeDBP10599.

Enzyme and pathway databases

Pathway_Interaction_DBp38_mkk3_6pathway. p38 MAPK signaling pathway.
ptp1bpathway. Signaling events mediated by PTP1B.
tnfpathway. TNF receptor signaling pathway.
ReactomeREACT_1698. Metabolism of nucleotides.

Gene expression databases

ArrayExpressP10599.
BgeeP10599.
CleanExHS_TXN.
GenevestigatorP10599.
GermOnlineENSG00000136810. Homo sapiens.

Family and domain databases

InterProIPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR006662. Thioredoxin-like_subdom.
IPR015467. Thioredoxin_core.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR10438. Trx. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio28523.
SOURCESearch...

Entry information

Entry nameTHIO_HUMAN
AccessionPrimary (citable) accession number: P10599
Secondary accession number(s): Q53X69, Q96KI3, Q9UDG5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 9

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents