Full text data of TXN
TXN
(TRDX, TRX, TRX1)
[Confidence: high (present in two of the MS resources)]
Thioredoxin; Trx (ATL-derived factor; ADF; Surface-associated sulphydryl protein; SASP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Thioredoxin; Trx (ATL-derived factor; ADF; Surface-associated sulphydryl protein; SASP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00216298
IPI00216298 thioredoxin thioredoxin membrane n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00216298 thioredoxin thioredoxin membrane n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
P10599
ID THIO_HUMAN Reviewed; 105 AA.
AC P10599; B1ALW1; O60744; Q53X69; Q96KI3; Q9UDG5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 170.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
DE AltName: Full=ATL-derived factor;
DE Short=ADF;
DE AltName: Full=Surface-associated sulphydryl protein;
DE Short=SASP;
GN Name=TXN; Synonyms=TRDX, TRX, TRX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3170595;
RA Wollman E.E., D'Auriol L., Rimsky L., Shaw A., Jacquot J.-P.,
RA Wingfield P., Graber P., Dessarps F.;
RT "Cloning and expression of a cDNA for human thioredoxin.";
RL J. Biol. Chem. 263:15506-15512(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2785919;
RA Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J.,
RA Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J.;
RT "ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to
RT thioredoxin; possible involvement of dithiol-reduction in the IL-2
RT receptor induction.";
RL EMBO J. 8:757-764(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1874447; DOI=10.1016/0378-1119(91)90081-L;
RA Tonissen K.F., Wells J.R.E.;
RT "Isolation and characterization of human thioredoxin-encoding genes.";
RL Gene 102:221-228(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lens;
RA Reddy P.G., Bhuyan D.K., Bhuyan K.C.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lens;
RA Liu A., Lou M.F.;
RT "Cloning, purification and characterization of human lens
RT thioredoxin.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Xu J.Y., Xu L., Li K.S., Dai R.;
RT "Cloning and sequencing of thioredoxin cDNA from human brain.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-85 (ISOFORM 2), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Liver;
RA Wang Y., Wang Y.G., Zhang Y., Yuan Y., Ma D.;
RT "An alternative splice variant of human thioredoxin.";
RL Chin. Sci. Bull. 43:292-295(1998).
RN [14]
RP PROTEIN SEQUENCE OF 2-21 AND 38-57.
RC TISSUE=Monocyte;
RX PubMed=7818492;
RA Dean M.F., Martin H., Sansom P.A.;
RT "Characterization of a thioredoxin-related surface protein.";
RL Biochem. J. 304:861-867(1994).
RN [15]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=1998498; DOI=10.1016/S0006-291X(05)81209-4;
RA Martin H., Dean M.;
RT "Identification of a thioredoxin-related protein associated with
RT plasma membranes.";
RL Biochem. Biophys. Res. Commun. 175:123-128(1991).
RN [16]
RP PROTEIN SEQUENCE OF 9-48; 73-81 AND 95-105, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [17]
RP FUNCTION.
RX PubMed=2176490; DOI=10.1016/S0006-291X(05)80940-4;
RA Jacquot J.-P., de Lamotte F., Fontecav M., Schuermann P.,
RA Decottignies P., Miginiac-Maslow M., Wollman E.;
RT "Human thioredoxin reactivity-structure/function relationship.";
RL Biochem. Biophys. Res. Commun. 173:1375-1381(1990).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=1332947;
RA Rubartelli A., Bajetto A., Allavena G., Wollman E., Sitia R.;
RT "Secretion of thioredoxin by normal and neoplastic cells through a
RT leaderless secretory pathway.";
RL J. Biol. Chem. 267:24161-24164(1992).
RN [19]
RP FUNCTION, SUBUNIT, INTERACTION WITH APEX1, MUTAGENESIS OF CYS-32;
RP CYS-35; CYS-62; CYS-69 AND CYS-73, AND SUBCELLULAR LOCATION.
RX PubMed=9108029; DOI=10.1073/pnas.94.8.3633;
RA Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., Yodoi J.;
RT "AP-1 transcriptional activity is regulated by a direct association
RT between thioredoxin and Ref-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3633-3638(1997).
RN [20]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11118054;
RA Wei S.J., Botero A., Hirota K., Bradbury C.M., Markovina S.,
RA Laszlo A., Spitz D.R., Goswami P.C., Yodoi J., Gius D.;
RT "Thioredoxin nuclear translocation and interaction with redox factor-1
RT activates the activator protein-1 transcription factor in response to
RT ionizing radiation.";
RL Cancer Res. 60:6688-6695(2000).
RN [21]
RP S-NITROSYLATION, AND INTERACTION WITH MAP3K5.
RX PubMed=15246877; DOI=10.1016/j.abb.2004.06.004;
RA Yasinska I.M., Kozhukhar A.V., Sumbayev V.V.;
RT "S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide
RT system activates apoptosis signal-regulating kinase 1.";
RL Arch. Biochem. Biophys. 428:198-203(2004).
RN [22]
RP FUNCTION, MUTAGENESIS OF CYS-73, AND S-NITROSYLATION AT CYS-73.
RX PubMed=16408020; DOI=10.1038/nchembio720;
RA Mitchell D.A., Marletta M.A.;
RT "Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site
RT cysteine.";
RL Nat. Chem. Biol. 1:154-158(2005).
RN [23]
RP FUNCTION, MUTAGENESIS OF CYS-69; GLU-70; LYS-72 AND CYS-73, AND
RP S-NITROSYLATION AT CYS-73 IN RESPONSE TO NITRIC OXIDE.
RX PubMed=17606900; DOI=10.1073/pnas.0704898104;
RA Mitchell D.A., Morton S.U., Fernhoff N.B., Marletta M.A.;
RT "Thioredoxin is required for S-nitrosation of procaspase-3 and the
RT inhibition of apoptosis in Jurkat cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11609-11614(2007).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RA Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M.,
RA Harbi S.O., Stansalas J., Mohamed A.O.;
RT "Abnormal proteins in primary breast cancer tissues from 25 Sudanese
RT patients.";
RL Eur. J. Inflamm. 6:115-121(2008).
RN [25]
RP INTERACTION WITH S.TYPHIMURIUM SLRP, AND UBIQUITINATION.
RX PubMed=19690162; DOI=10.1074/jbc.M109.010363;
RA Bernal-Bayard J., Ramos-Morales F.;
RT "Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase
RT for mammalian thioredoxin.";
RL J. Biol. Chem. 284:27587-27595(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-39, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP STRUCTURE BY NMR.
RX PubMed=2684271; DOI=10.1021/bi00443a045;
RA Forman-Kay J.D., Clore G.M., Dricoll P.C., Wingfield P.,
RA Richards F.M., Gronenborn A.M.;
RT "A proton nuclear magnetic resonance assignment and secondary
RT structure determination of recombinant human thioredoxin.";
RL Biochemistry 28:7088-7097(1989).
RN [29]
RP STRUCTURE BY NMR.
RX PubMed=2001356; DOI=10.1021/bi00224a017;
RA Forman-Kay J.D., Clore G.M., Wingfield P., Gronenborn A.M.;
RT "High-resolution three-dimensional structure of reduced recombinant
RT human thioredoxin in solution.";
RL Biochemistry 30:2685-2698(1991).
RN [30]
RP STRUCTURE BY NMR.
RX PubMed=7922028; DOI=10.1016/S0969-2126(00)00051-4;
RA Qin J., Clore G.M., Gronenborn A.M.;
RT "The high-resolution three-dimensional solution structures of the
RT oxidized and reduced states of human thioredoxin.";
RL Structure 2:503-522(1994).
RN [31]
RP STRUCTURE BY NMR.
RX PubMed=7788295; DOI=10.1016/S0969-2126(01)00159-9;
RA Qin J., Clore G.M., Kennedy W.M., Huth J.R., Gronenborn A.M.;
RT "Solution structure of human thioredoxin in a mixed disulfide
RT intermediate complex with its target peptide from the transcription
RT factor NF kappa B.";
RL Structure 3:289-297(1995).
RN [32]
RP STRUCTURE BY NMR.
RX PubMed=8736558; DOI=10.1016/S0969-2126(96)00065-2;
RA Qin J., Clore G.M., Kennedy W.P., Kuszewski J., Gronenborn A.M.;
RT "The solution structure of human thioredoxin complexed with its target
RT from Ref-1 reveals peptide chain reversal.";
RL Structure 4:613-620(1996).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=8805557; DOI=10.1016/S0969-2126(96)00079-2;
RA Weichsel A., Gasdaska J.R., Powis G., Montfort W.R.;
RT "Crystal structures of reduced, oxidized, and mutated human
RT thioredoxins: evidence for a regulatory homodimer.";
RL Structure 4:735-751(1996).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-60, AND SUBUNIT.
RX PubMed=9369469; DOI=10.1021/bi971004s;
RA Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G.,
RA Montfort W.R.;
RT "Human thioredoxin homodimers: regulation by pH, role of aspartate 60,
RT and crystal structure of the aspartate 60 --> asparagine mutant.";
RL Biochemistry 36:13979-13988(1997).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, DISULFIDE BONDS, AND
RP S-NITROSYLATION AT CYS-62 AND CYS-69.
RX PubMed=17260951; DOI=10.1021/bi061878r;
RA Weichsel A., Brailey J.L., Montfort W.R.;
RT "Buried S-nitrosocysteine revealed in crystal structures of human
RT thioredoxin.";
RL Biochemistry 46:1219-1227(2007).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide
CC and catalyzes dithiol-disulfide exchange reactions. Plays a role
CC in the reversible S-nitrosylation of cysteine residues in target
CC proteins, and thereby contributes to the response to intracellular
CC nitric oxide. Nitrosylates the active site Cys of CASP3 in
CC response to nitric oxide (NO), and thereby inhibits caspase-3
CC activity. Induces the FOS/JUN AP-1 DNA-binding activity in
CC ionizing radiation (IR) cells through its oxidation/reduction
CC status and stimulates AP-1 transcriptional activity.
CC -!- FUNCTION: ADF augments the expression of the interleukin-2
CC receptor TAC (IL2R/P55).
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TXNIP through
CC the redox-active site. Interacts with MAP3K5 and CASP3. In case of
CC infection, interacts with S.typhimurium protein slrP. Interacts
CC with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-
CC binding activity in a redox-dependent manner.
CC -!- INTERACTION:
CC Q92905:COPS5; NbExp=8; IntAct=EBI-594644, EBI-594661;
CC Q99683:MAP3K5; NbExp=2; IntAct=EBI-594644, EBI-476263;
CC Q99836:MYD88; NbExp=4; IntAct=EBI-594644, EBI-447677;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Secreted. Note=Secreted
CC by a leaderless secretory pathway. Predominantly in the cytoplasm
CC in non irradiated cells. Radiation induces translocation of TRX
CC from the cytoplasm to the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10599-2; Sequence=VSP_045607;
CC -!- INDUCTION: Up-regulated by ionizing radiation.
CC -!- PTM: In the fully reduced protein, both Cys-69 and Cys-73 are
CC nitrosylated in response to nitric oxide (NO). When two disulfide
CC bonds are present in the protein, only Cys-73 is nitrosylated.
CC Cys-73 can serve as donor for nitrosylation of target proteins.
CC -!- PTM: In case of infection, ubiquitinated by S.typhimurium protein
CC slrP, leading to its degradation.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/txn/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TXNID44354ch9q31.html";
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DR EMBL; J04026; AAA74596.1; -; mRNA.
DR EMBL; X77584; CAA54687.1; -; mRNA.
DR EMBL; X54539; CAA38410.1; -; Genomic_DNA.
DR EMBL; X54540; CAA38410.1; JOINED; Genomic_DNA.
DR EMBL; X54541; CAA38410.1; JOINED; Genomic_DNA.
DR EMBL; AF276919; AAF86466.1; -; mRNA.
DR EMBL; AY004872; AAF87085.1; -; mRNA.
DR EMBL; AF313911; AAG34699.1; -; mRNA.
DR EMBL; AK289508; BAF82197.1; -; mRNA.
DR EMBL; CR407665; CAG28593.1; -; mRNA.
DR EMBL; AF548001; AAN33187.1; -; Genomic_DNA.
DR EMBL; AL158158; CAI14066.1; -; Genomic_DNA.
DR EMBL; AL158158; CAI14067.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW59059.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW59060.1; -; Genomic_DNA.
DR EMBL; BC003377; AAH03377.1; -; mRNA.
DR EMBL; BC054866; AAH54866.1; -; mRNA.
DR EMBL; AF065241; AAC17430.1; -; mRNA.
DR PIR; JH0568; JH0568.
DR RefSeq; NP_001231867.1; NM_001244938.1.
DR RefSeq; NP_003320.2; NM_003329.3.
DR UniGene; Hs.435136; -.
DR PDB; 1AIU; X-ray; 2.00 A; A=1-105.
DR PDB; 1AUC; X-ray; 2.10 A; A=1-105.
DR PDB; 1CQG; NMR; -; A=1-105.
DR PDB; 1CQH; NMR; -; A=1-105.
DR PDB; 1ERT; X-ray; 1.70 A; A=1-105.
DR PDB; 1ERU; X-ray; 2.10 A; A=1-105.
DR PDB; 1ERV; X-ray; 1.65 A; A=1-105.
DR PDB; 1ERW; X-ray; 1.80 A; A=1-105.
DR PDB; 1M7T; NMR; -; A=1-65.
DR PDB; 1MDI; NMR; -; A=2-104.
DR PDB; 1MDJ; NMR; -; A=2-104.
DR PDB; 1MDK; NMR; -; A=2-104.
DR PDB; 1TRS; NMR; -; A=1-105.
DR PDB; 1TRU; NMR; -; A=1-105.
DR PDB; 1TRV; NMR; -; A=1-105.
DR PDB; 1TRW; NMR; -; A=1-105.
DR PDB; 1W1C; Model; -; C=1-105.
DR PDB; 1W1E; Model; -; C=1-105.
DR PDB; 2HSH; X-ray; 1.35 A; A=1-105.
DR PDB; 2HXK; X-ray; 1.65 A; A/B/C=1-105.
DR PDB; 2IFQ; X-ray; 1.20 A; A/B/C=1-105.
DR PDB; 2IIY; X-ray; 1.70 A; A=1-105.
DR PDB; 3E3E; X-ray; 2.01 A; A/B=1-105.
DR PDB; 3KD0; X-ray; 1.70 A; A=1-105.
DR PDB; 3M9J; X-ray; 1.10 A; A/B=1-105.
DR PDB; 3M9K; X-ray; 1.50 A; A/B=1-105.
DR PDB; 3QFA; X-ray; 2.20 A; C/D=2-105.
DR PDB; 3QFB; X-ray; 2.60 A; C/D=2-105.
DR PDB; 3TRX; NMR; -; A=1-105.
DR PDB; 4TRX; NMR; -; A=1-105.
DR PDBsum; 1AIU; -.
DR PDBsum; 1AUC; -.
DR PDBsum; 1CQG; -.
DR PDBsum; 1CQH; -.
DR PDBsum; 1ERT; -.
DR PDBsum; 1ERU; -.
DR PDBsum; 1ERV; -.
DR PDBsum; 1ERW; -.
DR PDBsum; 1M7T; -.
DR PDBsum; 1MDI; -.
DR PDBsum; 1MDJ; -.
DR PDBsum; 1MDK; -.
DR PDBsum; 1TRS; -.
DR PDBsum; 1TRU; -.
DR PDBsum; 1TRV; -.
DR PDBsum; 1TRW; -.
DR PDBsum; 1W1C; -.
DR PDBsum; 1W1E; -.
DR PDBsum; 2HSH; -.
DR PDBsum; 2HXK; -.
DR PDBsum; 2IFQ; -.
DR PDBsum; 2IIY; -.
DR PDBsum; 3E3E; -.
DR PDBsum; 3KD0; -.
DR PDBsum; 3M9J; -.
DR PDBsum; 3M9K; -.
DR PDBsum; 3QFA; -.
DR PDBsum; 3QFB; -.
DR PDBsum; 3TRX; -.
DR PDBsum; 4TRX; -.
DR ProteinModelPortal; P10599; -.
DR SMR; P10599; 1-105.
DR DIP; DIP-6129N; -.
DR IntAct; P10599; 28.
DR MINT; MINT-1522967; -.
DR STRING; 9606.ENSP00000363641; -.
DR ChEMBL; CHEMBL2010624; -.
DR Allergome; 3543; Hom s Trx.
DR PhosphoSite; P10599; -.
DR DMDM; 135773; -.
DR DOSAC-COBS-2DPAGE; P10599; -.
DR REPRODUCTION-2DPAGE; IPI00216298; -.
DR SWISS-2DPAGE; P10599; -.
DR PaxDb; P10599; -.
DR PeptideAtlas; P10599; -.
DR PRIDE; P10599; -.
DR DNASU; 7295; -.
DR Ensembl; ENST00000374515; ENSP00000363639; ENSG00000136810.
DR Ensembl; ENST00000374517; ENSP00000363641; ENSG00000136810.
DR GeneID; 7295; -.
DR KEGG; hsa:7295; -.
DR UCSC; uc004beq.2; human.
DR CTD; 7295; -.
DR GeneCards; GC09M113006; -.
DR HGNC; HGNC:12435; TXN.
DR HPA; CAB008678; -.
DR MIM; 187700; gene.
DR neXtProt; NX_P10599; -.
DR PharmGKB; PA37091; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000292977; -.
DR HOVERGEN; HBG009243; -.
DR InParanoid; P10599; -.
DR KO; K03671; -.
DR OMA; SKYAFQE; -.
DR OrthoDB; EOG7H4DX9; -.
DR PhylomeDB; P10599; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P10599; -.
DR ChiTaRS; TXN; human.
DR EvolutionaryTrace; P10599; -.
DR GeneWiki; Thioredoxin; -.
DR GenomeRNAi; 7295; -.
DR NextBio; 28523; -.
DR PRO; PR:P10599; -.
DR ArrayExpress; P10599; -.
DR Bgee; P10599; -.
DR CleanEx; HS_TXN; -.
DR Genevestigator; P10599; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IEA:Ensembl.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016999; P:antibiotic metabolic process; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0033158; P:regulation of protein import into nucleus, translocation; IDA:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0071548; P:response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0097068; P:response to thyroxine stimulus; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10438; PTHR10438; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Nucleus; Redox-active center;
KW Reference proteome; S-nitrosylation; Secreted; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 105 Thioredoxin.
FT /FTId=PRO_0000120005.
FT DOMAIN 2 105 Thioredoxin.
FT ACT_SITE 32 32 Nucleophile.
FT ACT_SITE 35 35 Nucleophile.
FT SITE 26 26 Deprotonates C-terminal active site Cys.
FT SITE 33 33 Contributes to redox potential value.
FT SITE 34 34 Contributes to redox potential value.
FT MOD_RES 3 3 N6-acetyllysine.
FT MOD_RES 39 39 N6-acetyllysine.
FT MOD_RES 62 62 S-nitrosocysteine.
FT MOD_RES 69 69 S-nitrosocysteine.
FT MOD_RES 73 73 S-nitrosocysteine; alternate.
FT DISULFID 32 35 Redox-active.
FT DISULFID 73 73 Interchain; alternate.
FT VAR_SEQ 44 63 Missing (in isoform 2).
FT /FTId=VSP_045607.
FT MUTAGEN 32 32 C->S: Loses its reducing activity,
FT interaction with APEX1 and transcription
FT activation; when associated with S-35.
FT MUTAGEN 35 35 C->S: Loses its reducing activity,
FT interaction with APEX1 and transcription
FT activation; when associated with S-32.
FT MUTAGEN 60 60 D->N: Loss of pH-dependence of
FT dimerization.
FT MUTAGEN 62 62 C->S: Retains its reducing activity.
FT Retains interaction with APEX1 and
FT transcription activation; when associated
FT with S-69 and S-73.
FT MUTAGEN 69 69 C->S: No effect on reducing activity,
FT interaction with APEX1 and on S-
FT nitrosylation of C-73. Retains
FT interaction with APEX1 and transcription
FT activation; when associated with S-62 and
FT S-73.
FT MUTAGEN 70 70 E->A: Strongly reduced interaction with
FT CASP3; when associated with A-72.
FT MUTAGEN 72 72 K->A: Strongly reduced interaction with
FT CASP3; when associated with A-70.
FT MUTAGEN 73 73 C->D: Strongly reduced S-nitrosylation of
FT CASP3.
FT MUTAGEN 73 73 C->S: Loss of nitrosylation, and loss of
FT S-nitrosylating activity towards CASP3.
FT Retains interaction with APEX1 and
FT transcription activation; when associated
FT with S-62 and S-69.
FT MUTAGEN 73 73 C->S: Retains its reducing activity.
FT CONFLICT 39 39 K -> N (in Ref. 1; AAA74596 and 4;
FT AAF86466).
FT CONFLICT 74 74 M -> T (in Ref. 1; AAA74596 and 4;
FT AAF86466).
FT STRAND 3 5
FT HELIX 8 17
FT TURN 18 20
FT STRAND 23 28
FT STRAND 30 32
FT HELIX 33 48
FT TURN 49 51
FT STRAND 52 58
FT TURN 59 61
FT HELIX 63 68
FT STRAND 73 81
FT STRAND 84 92
FT HELIX 94 104
SQ SEQUENCE 105 AA; 11737 MW; 256F4E3C8A187693 CRC64;
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD
DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV
//
ID THIO_HUMAN Reviewed; 105 AA.
AC P10599; B1ALW1; O60744; Q53X69; Q96KI3; Q9UDG5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 170.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
DE AltName: Full=ATL-derived factor;
DE Short=ADF;
DE AltName: Full=Surface-associated sulphydryl protein;
DE Short=SASP;
GN Name=TXN; Synonyms=TRDX, TRX, TRX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3170595;
RA Wollman E.E., D'Auriol L., Rimsky L., Shaw A., Jacquot J.-P.,
RA Wingfield P., Graber P., Dessarps F.;
RT "Cloning and expression of a cDNA for human thioredoxin.";
RL J. Biol. Chem. 263:15506-15512(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2785919;
RA Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J.,
RA Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J.;
RT "ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to
RT thioredoxin; possible involvement of dithiol-reduction in the IL-2
RT receptor induction.";
RL EMBO J. 8:757-764(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1874447; DOI=10.1016/0378-1119(91)90081-L;
RA Tonissen K.F., Wells J.R.E.;
RT "Isolation and characterization of human thioredoxin-encoding genes.";
RL Gene 102:221-228(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lens;
RA Reddy P.G., Bhuyan D.K., Bhuyan K.C.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lens;
RA Liu A., Lou M.F.;
RT "Cloning, purification and characterization of human lens
RT thioredoxin.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Xu J.Y., Xu L., Li K.S., Dai R.;
RT "Cloning and sequencing of thioredoxin cDNA from human brain.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-85 (ISOFORM 2), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Liver;
RA Wang Y., Wang Y.G., Zhang Y., Yuan Y., Ma D.;
RT "An alternative splice variant of human thioredoxin.";
RL Chin. Sci. Bull. 43:292-295(1998).
RN [14]
RP PROTEIN SEQUENCE OF 2-21 AND 38-57.
RC TISSUE=Monocyte;
RX PubMed=7818492;
RA Dean M.F., Martin H., Sansom P.A.;
RT "Characterization of a thioredoxin-related surface protein.";
RL Biochem. J. 304:861-867(1994).
RN [15]
RP PROTEIN SEQUENCE OF 2-15.
RX PubMed=1998498; DOI=10.1016/S0006-291X(05)81209-4;
RA Martin H., Dean M.;
RT "Identification of a thioredoxin-related protein associated with
RT plasma membranes.";
RL Biochem. Biophys. Res. Commun. 175:123-128(1991).
RN [16]
RP PROTEIN SEQUENCE OF 9-48; 73-81 AND 95-105, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [17]
RP FUNCTION.
RX PubMed=2176490; DOI=10.1016/S0006-291X(05)80940-4;
RA Jacquot J.-P., de Lamotte F., Fontecav M., Schuermann P.,
RA Decottignies P., Miginiac-Maslow M., Wollman E.;
RT "Human thioredoxin reactivity-structure/function relationship.";
RL Biochem. Biophys. Res. Commun. 173:1375-1381(1990).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=1332947;
RA Rubartelli A., Bajetto A., Allavena G., Wollman E., Sitia R.;
RT "Secretion of thioredoxin by normal and neoplastic cells through a
RT leaderless secretory pathway.";
RL J. Biol. Chem. 267:24161-24164(1992).
RN [19]
RP FUNCTION, SUBUNIT, INTERACTION WITH APEX1, MUTAGENESIS OF CYS-32;
RP CYS-35; CYS-62; CYS-69 AND CYS-73, AND SUBCELLULAR LOCATION.
RX PubMed=9108029; DOI=10.1073/pnas.94.8.3633;
RA Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., Yodoi J.;
RT "AP-1 transcriptional activity is regulated by a direct association
RT between thioredoxin and Ref-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3633-3638(1997).
RN [20]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11118054;
RA Wei S.J., Botero A., Hirota K., Bradbury C.M., Markovina S.,
RA Laszlo A., Spitz D.R., Goswami P.C., Yodoi J., Gius D.;
RT "Thioredoxin nuclear translocation and interaction with redox factor-1
RT activates the activator protein-1 transcription factor in response to
RT ionizing radiation.";
RL Cancer Res. 60:6688-6695(2000).
RN [21]
RP S-NITROSYLATION, AND INTERACTION WITH MAP3K5.
RX PubMed=15246877; DOI=10.1016/j.abb.2004.06.004;
RA Yasinska I.M., Kozhukhar A.V., Sumbayev V.V.;
RT "S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide
RT system activates apoptosis signal-regulating kinase 1.";
RL Arch. Biochem. Biophys. 428:198-203(2004).
RN [22]
RP FUNCTION, MUTAGENESIS OF CYS-73, AND S-NITROSYLATION AT CYS-73.
RX PubMed=16408020; DOI=10.1038/nchembio720;
RA Mitchell D.A., Marletta M.A.;
RT "Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site
RT cysteine.";
RL Nat. Chem. Biol. 1:154-158(2005).
RN [23]
RP FUNCTION, MUTAGENESIS OF CYS-69; GLU-70; LYS-72 AND CYS-73, AND
RP S-NITROSYLATION AT CYS-73 IN RESPONSE TO NITRIC OXIDE.
RX PubMed=17606900; DOI=10.1073/pnas.0704898104;
RA Mitchell D.A., Morton S.U., Fernhoff N.B., Marletta M.A.;
RT "Thioredoxin is required for S-nitrosation of procaspase-3 and the
RT inhibition of apoptosis in Jurkat cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11609-11614(2007).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RA Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M.,
RA Harbi S.O., Stansalas J., Mohamed A.O.;
RT "Abnormal proteins in primary breast cancer tissues from 25 Sudanese
RT patients.";
RL Eur. J. Inflamm. 6:115-121(2008).
RN [25]
RP INTERACTION WITH S.TYPHIMURIUM SLRP, AND UBIQUITINATION.
RX PubMed=19690162; DOI=10.1074/jbc.M109.010363;
RA Bernal-Bayard J., Ramos-Morales F.;
RT "Salmonella type III secretion effector SlrP is an E3 ubiquitin ligase
RT for mammalian thioredoxin.";
RL J. Biol. Chem. 284:27587-27595(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-39, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP STRUCTURE BY NMR.
RX PubMed=2684271; DOI=10.1021/bi00443a045;
RA Forman-Kay J.D., Clore G.M., Dricoll P.C., Wingfield P.,
RA Richards F.M., Gronenborn A.M.;
RT "A proton nuclear magnetic resonance assignment and secondary
RT structure determination of recombinant human thioredoxin.";
RL Biochemistry 28:7088-7097(1989).
RN [29]
RP STRUCTURE BY NMR.
RX PubMed=2001356; DOI=10.1021/bi00224a017;
RA Forman-Kay J.D., Clore G.M., Wingfield P., Gronenborn A.M.;
RT "High-resolution three-dimensional structure of reduced recombinant
RT human thioredoxin in solution.";
RL Biochemistry 30:2685-2698(1991).
RN [30]
RP STRUCTURE BY NMR.
RX PubMed=7922028; DOI=10.1016/S0969-2126(00)00051-4;
RA Qin J., Clore G.M., Gronenborn A.M.;
RT "The high-resolution three-dimensional solution structures of the
RT oxidized and reduced states of human thioredoxin.";
RL Structure 2:503-522(1994).
RN [31]
RP STRUCTURE BY NMR.
RX PubMed=7788295; DOI=10.1016/S0969-2126(01)00159-9;
RA Qin J., Clore G.M., Kennedy W.M., Huth J.R., Gronenborn A.M.;
RT "Solution structure of human thioredoxin in a mixed disulfide
RT intermediate complex with its target peptide from the transcription
RT factor NF kappa B.";
RL Structure 3:289-297(1995).
RN [32]
RP STRUCTURE BY NMR.
RX PubMed=8736558; DOI=10.1016/S0969-2126(96)00065-2;
RA Qin J., Clore G.M., Kennedy W.P., Kuszewski J., Gronenborn A.M.;
RT "The solution structure of human thioredoxin complexed with its target
RT from Ref-1 reveals peptide chain reversal.";
RL Structure 4:613-620(1996).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=8805557; DOI=10.1016/S0969-2126(96)00079-2;
RA Weichsel A., Gasdaska J.R., Powis G., Montfort W.R.;
RT "Crystal structures of reduced, oxidized, and mutated human
RT thioredoxins: evidence for a regulatory homodimer.";
RL Structure 4:735-751(1996).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-60, AND SUBUNIT.
RX PubMed=9369469; DOI=10.1021/bi971004s;
RA Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G.,
RA Montfort W.R.;
RT "Human thioredoxin homodimers: regulation by pH, role of aspartate 60,
RT and crystal structure of the aspartate 60 --> asparagine mutant.";
RL Biochemistry 36:13979-13988(1997).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, DISULFIDE BONDS, AND
RP S-NITROSYLATION AT CYS-62 AND CYS-69.
RX PubMed=17260951; DOI=10.1021/bi061878r;
RA Weichsel A., Brailey J.L., Montfort W.R.;
RT "Buried S-nitrosocysteine revealed in crystal structures of human
RT thioredoxin.";
RL Biochemistry 46:1219-1227(2007).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide
CC and catalyzes dithiol-disulfide exchange reactions. Plays a role
CC in the reversible S-nitrosylation of cysteine residues in target
CC proteins, and thereby contributes to the response to intracellular
CC nitric oxide. Nitrosylates the active site Cys of CASP3 in
CC response to nitric oxide (NO), and thereby inhibits caspase-3
CC activity. Induces the FOS/JUN AP-1 DNA-binding activity in
CC ionizing radiation (IR) cells through its oxidation/reduction
CC status and stimulates AP-1 transcriptional activity.
CC -!- FUNCTION: ADF augments the expression of the interleukin-2
CC receptor TAC (IL2R/P55).
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TXNIP through
CC the redox-active site. Interacts with MAP3K5 and CASP3. In case of
CC infection, interacts with S.typhimurium protein slrP. Interacts
CC with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-
CC binding activity in a redox-dependent manner.
CC -!- INTERACTION:
CC Q92905:COPS5; NbExp=8; IntAct=EBI-594644, EBI-594661;
CC Q99683:MAP3K5; NbExp=2; IntAct=EBI-594644, EBI-476263;
CC Q99836:MYD88; NbExp=4; IntAct=EBI-594644, EBI-447677;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Secreted. Note=Secreted
CC by a leaderless secretory pathway. Predominantly in the cytoplasm
CC in non irradiated cells. Radiation induces translocation of TRX
CC from the cytoplasm to the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10599-2; Sequence=VSP_045607;
CC -!- INDUCTION: Up-regulated by ionizing radiation.
CC -!- PTM: In the fully reduced protein, both Cys-69 and Cys-73 are
CC nitrosylated in response to nitric oxide (NO). When two disulfide
CC bonds are present in the protein, only Cys-73 is nitrosylated.
CC Cys-73 can serve as donor for nitrosylation of target proteins.
CC -!- PTM: In case of infection, ubiquitinated by S.typhimurium protein
CC slrP, leading to its degradation.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/txn/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TXNID44354ch9q31.html";
CC -----------------------------------------------------------------------
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DR EMBL; J04026; AAA74596.1; -; mRNA.
DR EMBL; X77584; CAA54687.1; -; mRNA.
DR EMBL; X54539; CAA38410.1; -; Genomic_DNA.
DR EMBL; X54540; CAA38410.1; JOINED; Genomic_DNA.
DR EMBL; X54541; CAA38410.1; JOINED; Genomic_DNA.
DR EMBL; AF276919; AAF86466.1; -; mRNA.
DR EMBL; AY004872; AAF87085.1; -; mRNA.
DR EMBL; AF313911; AAG34699.1; -; mRNA.
DR EMBL; AK289508; BAF82197.1; -; mRNA.
DR EMBL; CR407665; CAG28593.1; -; mRNA.
DR EMBL; AF548001; AAN33187.1; -; Genomic_DNA.
DR EMBL; AL158158; CAI14066.1; -; Genomic_DNA.
DR EMBL; AL158158; CAI14067.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW59059.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW59060.1; -; Genomic_DNA.
DR EMBL; BC003377; AAH03377.1; -; mRNA.
DR EMBL; BC054866; AAH54866.1; -; mRNA.
DR EMBL; AF065241; AAC17430.1; -; mRNA.
DR PIR; JH0568; JH0568.
DR RefSeq; NP_001231867.1; NM_001244938.1.
DR RefSeq; NP_003320.2; NM_003329.3.
DR UniGene; Hs.435136; -.
DR PDB; 1AIU; X-ray; 2.00 A; A=1-105.
DR PDB; 1AUC; X-ray; 2.10 A; A=1-105.
DR PDB; 1CQG; NMR; -; A=1-105.
DR PDB; 1CQH; NMR; -; A=1-105.
DR PDB; 1ERT; X-ray; 1.70 A; A=1-105.
DR PDB; 1ERU; X-ray; 2.10 A; A=1-105.
DR PDB; 1ERV; X-ray; 1.65 A; A=1-105.
DR PDB; 1ERW; X-ray; 1.80 A; A=1-105.
DR PDB; 1M7T; NMR; -; A=1-65.
DR PDB; 1MDI; NMR; -; A=2-104.
DR PDB; 1MDJ; NMR; -; A=2-104.
DR PDB; 1MDK; NMR; -; A=2-104.
DR PDB; 1TRS; NMR; -; A=1-105.
DR PDB; 1TRU; NMR; -; A=1-105.
DR PDB; 1TRV; NMR; -; A=1-105.
DR PDB; 1TRW; NMR; -; A=1-105.
DR PDB; 1W1C; Model; -; C=1-105.
DR PDB; 1W1E; Model; -; C=1-105.
DR PDB; 2HSH; X-ray; 1.35 A; A=1-105.
DR PDB; 2HXK; X-ray; 1.65 A; A/B/C=1-105.
DR PDB; 2IFQ; X-ray; 1.20 A; A/B/C=1-105.
DR PDB; 2IIY; X-ray; 1.70 A; A=1-105.
DR PDB; 3E3E; X-ray; 2.01 A; A/B=1-105.
DR PDB; 3KD0; X-ray; 1.70 A; A=1-105.
DR PDB; 3M9J; X-ray; 1.10 A; A/B=1-105.
DR PDB; 3M9K; X-ray; 1.50 A; A/B=1-105.
DR PDB; 3QFA; X-ray; 2.20 A; C/D=2-105.
DR PDB; 3QFB; X-ray; 2.60 A; C/D=2-105.
DR PDB; 3TRX; NMR; -; A=1-105.
DR PDB; 4TRX; NMR; -; A=1-105.
DR PDBsum; 1AIU; -.
DR PDBsum; 1AUC; -.
DR PDBsum; 1CQG; -.
DR PDBsum; 1CQH; -.
DR PDBsum; 1ERT; -.
DR PDBsum; 1ERU; -.
DR PDBsum; 1ERV; -.
DR PDBsum; 1ERW; -.
DR PDBsum; 1M7T; -.
DR PDBsum; 1MDI; -.
DR PDBsum; 1MDJ; -.
DR PDBsum; 1MDK; -.
DR PDBsum; 1TRS; -.
DR PDBsum; 1TRU; -.
DR PDBsum; 1TRV; -.
DR PDBsum; 1TRW; -.
DR PDBsum; 1W1C; -.
DR PDBsum; 1W1E; -.
DR PDBsum; 2HSH; -.
DR PDBsum; 2HXK; -.
DR PDBsum; 2IFQ; -.
DR PDBsum; 2IIY; -.
DR PDBsum; 3E3E; -.
DR PDBsum; 3KD0; -.
DR PDBsum; 3M9J; -.
DR PDBsum; 3M9K; -.
DR PDBsum; 3QFA; -.
DR PDBsum; 3QFB; -.
DR PDBsum; 3TRX; -.
DR PDBsum; 4TRX; -.
DR ProteinModelPortal; P10599; -.
DR SMR; P10599; 1-105.
DR DIP; DIP-6129N; -.
DR IntAct; P10599; 28.
DR MINT; MINT-1522967; -.
DR STRING; 9606.ENSP00000363641; -.
DR ChEMBL; CHEMBL2010624; -.
DR Allergome; 3543; Hom s Trx.
DR PhosphoSite; P10599; -.
DR DMDM; 135773; -.
DR DOSAC-COBS-2DPAGE; P10599; -.
DR REPRODUCTION-2DPAGE; IPI00216298; -.
DR SWISS-2DPAGE; P10599; -.
DR PaxDb; P10599; -.
DR PeptideAtlas; P10599; -.
DR PRIDE; P10599; -.
DR DNASU; 7295; -.
DR Ensembl; ENST00000374515; ENSP00000363639; ENSG00000136810.
DR Ensembl; ENST00000374517; ENSP00000363641; ENSG00000136810.
DR GeneID; 7295; -.
DR KEGG; hsa:7295; -.
DR UCSC; uc004beq.2; human.
DR CTD; 7295; -.
DR GeneCards; GC09M113006; -.
DR HGNC; HGNC:12435; TXN.
DR HPA; CAB008678; -.
DR MIM; 187700; gene.
DR neXtProt; NX_P10599; -.
DR PharmGKB; PA37091; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000292977; -.
DR HOVERGEN; HBG009243; -.
DR InParanoid; P10599; -.
DR KO; K03671; -.
DR OMA; SKYAFQE; -.
DR OrthoDB; EOG7H4DX9; -.
DR PhylomeDB; P10599; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_120956; Cellular responses to stress.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P10599; -.
DR ChiTaRS; TXN; human.
DR EvolutionaryTrace; P10599; -.
DR GeneWiki; Thioredoxin; -.
DR GenomeRNAi; 7295; -.
DR NextBio; 28523; -.
DR PRO; PR:P10599; -.
DR ArrayExpress; P10599; -.
DR Bgee; P10599; -.
DR CleanEx; HS_TXN; -.
DR Genevestigator; P10599; -.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IEA:Ensembl.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016999; P:antibiotic metabolic process; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl.
DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome.
DR GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0033158; P:regulation of protein import into nucleus, translocation; IDA:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0071548; P:response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0097068; P:response to thyroxine stimulus; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10438; PTHR10438; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Electron transport; Nucleus; Redox-active center;
KW Reference proteome; S-nitrosylation; Secreted; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 105 Thioredoxin.
FT /FTId=PRO_0000120005.
FT DOMAIN 2 105 Thioredoxin.
FT ACT_SITE 32 32 Nucleophile.
FT ACT_SITE 35 35 Nucleophile.
FT SITE 26 26 Deprotonates C-terminal active site Cys.
FT SITE 33 33 Contributes to redox potential value.
FT SITE 34 34 Contributes to redox potential value.
FT MOD_RES 3 3 N6-acetyllysine.
FT MOD_RES 39 39 N6-acetyllysine.
FT MOD_RES 62 62 S-nitrosocysteine.
FT MOD_RES 69 69 S-nitrosocysteine.
FT MOD_RES 73 73 S-nitrosocysteine; alternate.
FT DISULFID 32 35 Redox-active.
FT DISULFID 73 73 Interchain; alternate.
FT VAR_SEQ 44 63 Missing (in isoform 2).
FT /FTId=VSP_045607.
FT MUTAGEN 32 32 C->S: Loses its reducing activity,
FT interaction with APEX1 and transcription
FT activation; when associated with S-35.
FT MUTAGEN 35 35 C->S: Loses its reducing activity,
FT interaction with APEX1 and transcription
FT activation; when associated with S-32.
FT MUTAGEN 60 60 D->N: Loss of pH-dependence of
FT dimerization.
FT MUTAGEN 62 62 C->S: Retains its reducing activity.
FT Retains interaction with APEX1 and
FT transcription activation; when associated
FT with S-69 and S-73.
FT MUTAGEN 69 69 C->S: No effect on reducing activity,
FT interaction with APEX1 and on S-
FT nitrosylation of C-73. Retains
FT interaction with APEX1 and transcription
FT activation; when associated with S-62 and
FT S-73.
FT MUTAGEN 70 70 E->A: Strongly reduced interaction with
FT CASP3; when associated with A-72.
FT MUTAGEN 72 72 K->A: Strongly reduced interaction with
FT CASP3; when associated with A-70.
FT MUTAGEN 73 73 C->D: Strongly reduced S-nitrosylation of
FT CASP3.
FT MUTAGEN 73 73 C->S: Loss of nitrosylation, and loss of
FT S-nitrosylating activity towards CASP3.
FT Retains interaction with APEX1 and
FT transcription activation; when associated
FT with S-62 and S-69.
FT MUTAGEN 73 73 C->S: Retains its reducing activity.
FT CONFLICT 39 39 K -> N (in Ref. 1; AAA74596 and 4;
FT AAF86466).
FT CONFLICT 74 74 M -> T (in Ref. 1; AAA74596 and 4;
FT AAF86466).
FT STRAND 3 5
FT HELIX 8 17
FT TURN 18 20
FT STRAND 23 28
FT STRAND 30 32
FT HELIX 33 48
FT TURN 49 51
FT STRAND 52 58
FT TURN 59 61
FT HELIX 63 68
FT STRAND 73 81
FT STRAND 84 92
FT HELIX 94 104
SQ SEQUENCE 105 AA; 11737 MW; 256F4E3C8A187693 CRC64;
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD
DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV
//
MIM
187700
*RECORD*
*FIELD* NO
187700
*FIELD* TI
*187700 THIOREDOXIN; TXN
;;TRX;;
TRX1
*FIELD* TX
DESCRIPTION
Thioredoxin is a 12-kD oxidoreductase enzyme containing a
read moredithiol-disulfide active site. It is ubiquitous and found in many
organisms from plants and bacteria to mammals. Multiple in vitro
substrates for thioredoxin have been identified, including ribonuclease,
choriogonadotropins, coagulation factors, glucocorticoid receptor, and
insulin. Reduction of insulin is classically used as an activity test.
CLONING
Wollman et al. (1988) identified a full-length cDNA clone encoding human
thioredoxin. The open reading frame codes for a protein of 104 amino
acids, excluding the initial methionine. This protein possesses the
highly conserved enzymatic active site common to plant and bacterial
thioredoxins: trp-cys-gly-pro-cys (amino acids 30 to 34).
GENE FUNCTION
By yeast 2-hybrid analysis of a human brain cDNA library, Saitoh et al.
(1998) identified TRX and ASK1 (MAP3K5; 602448) as interacting partners.
TRX associated with the N-terminal portion of ASK1 in vitro and in vivo,
and the interaction between TRX and ASK1 was highly dependent on the
redox status of TRX. Expression of TRX inhibited ASK1 kinase activity
and ASK1-dependent apoptosis. Inhibition of TRX resulted in activation
of endogenous ASK1 activity. Saitoh et al. (1998) concluded that TRX is
a physiologic inhibitor of ASK1 and may be involved in redox regulation
of the apoptosis signal transduction pathway.
Junn et al. (2000) found that the C-terminal half of mouse Vdup1 (TXNIP;
606599) interacted with the redox-active center of Trx. Mutation of 2
critical cysteines in the Trx active center abrogated the interaction
with Vdup1. Transfection of mouse Vdup1 into human embryonic kidney
cells reduced the endogenous reducing activity of TRX or the activity of
cotransfected TRX. Overexpression of Vdup1 inhibited interaction between
Trx and a thiol-specific antioxidant, Pag (PRDX1; 176763), and it
inhibited interaction between Trx and Ask1. Treatment of mouse
fibroblasts and T-cell hybridoma cells with various stress stimuli, such
as hydrogen peroxide or heat shock, induced Vdup1 expression. Exposure
of mouse fibroblasts overexpressing Vdup1 to stress resulted in reduced
cell proliferation and elevated apoptotic cell death. Junn et al. (2000)
concluded that VDUP1 functions as an oxidative stress mediator by
inhibiting TRX activity.
Wang et al. (2002) found that biomechanical strain or hydrogen peroxide
downregulated expression of Vdup1, but not Trx, in rat cardiomyocytes.
The rapid response occurred through transcriptional control and led to
increased Trx activity. Adenovirus-mediated overexpression of Vdup1
suppressed Trx activity and induced cardiomyocyte apoptosis.
Furthermore, Vdup1 overexpression sensitized cells to hydrogen
peroxide-induced apoptosis, whereas Trx overexpression protected cells
against injury. Wang et al. (2002) concluded that VDUP1 is a key
stress-responsive inhibitor of thioredoxin activity in cardiomyocytes.
Adriamycin (ADR) is an anticancer drug that causes severe cardiac
toxicity by generating free radicals. Shioji et al. (2002) found that
Trx1 was dose-dependently increased concomitant with formation of
hydroxyl radicals in ADR-treated neonatal rat cardiomyocytes. Treatment
with recombinant human TRX1 suppressed cardiomyocyte injury in
ADR-treated cells. Electron microscopy revealed better maintenance of
cardiac mitochondria and cellular architecture in ADR-treated
TRX1-expressing transgenic mice than in ADR-treated wildtype mice.
Formation of hydroxyl radicals following ADR treatment was reduced in
transgenic mice compared with wildtype mice, and transgenic mice showed
significantly increased survival.
Yoshioka et al. (2004) overexpressed thioredoxin in rat cardiomyocytes
and observed the induction of protein synthesis; overexpression of TXNIP
reduced protein synthesis in response to mechanical strain,
phenylephrine, and angiotensin II (see 106150). In vivo, myocardial TXN
activity increased 3.5-fold compared to sham controls after transverse
aortic constriction; however, aortic constriction did not increase TXN
expression but reduced TXNIP expression by 40%. Gene transfer studies
revealed that cells overexpressing TXNIP developed less hypertrophy
after aortic constriction than control cells in the same animals.
Yoshioka et al. (2004) concluded that TXN has a dual function as both an
antioxidant and a signaling protein involved in the development of
pressure-overload cardiac hypertrophy, and suggested that TXNIP is a
critical regulator of biomechanical signaling.
Nitric oxide (see 163731) acts substantially in cellular signal
transduction through stimulus-coupled S-nitrosylation of cysteine
residues. Benhar et al. (2008) searched for denitrosylase activities,
and focused on caspase-3 (600636), an exemplar of stimulus-dependent
denitrosylation, and identified thioredoxin and thioredoxin reductase
(see 601112) in a biochemical screen. In resting human lymphocytes,
thioredoxin-1 actively denitrosylated cytosolic caspase-3 and thereby
maintained a low steady-state amount of S-nitrosylation. Upon
stimulation of Fas, thioredoxin-2 (609063) mediated denitrosylation of
mitochondria-associated caspase-3, a process required for caspase-3
activation, and promoted apoptosis. Inhibition of
thioredoxin-thioredoxin reductases enabled identification of additional
substrates subject to endogenous S-nitrosylation. These substrates
included caspase-9 (602234) and protein tyrosine phosphatase-1B
(176885). Thus, Benhar et al. (2008) concluded that specific enzymatic
mechanisms may regulate basal and stimulus-induced denitrosylation in
mammalian cells.
GENE STRUCTURE
Tonissen and Wells (1991) determined that the TRX gene extends over 13
kb and consists of 5 exons.
Kaghad et al. (1994) also cloned the TXN gene and demonstrated that the
5 exons are separated by 4 introns. They determined the +1 transcription
start point by primer extension. The +1 site is located 22 bp downstream
from a TATAA box and defines a 5-prime untranslated region of 74 bp.
MAPPING
Using in situ chromosomal hybridization with a human TXN cDNA probe,
Lafage-Pochitaloff-Huvale et al. (1989) localized the gene to chromosome
3p12-p11. Southern analysis by Tonissen and Wells (1991) demonstrated
the presence of several TXN genes in the human genome. At least 1 of
these is inactive, i.e., a pseudogene. By Southern hybridization of
genomic DNAs from several donors, Kaghad et al. (1994) detected only 1
active TXN gene.
Taketo et al. (1994) found that the homologous gene in mouse is located
on chromosome 4 and that there is a processed Txn pseudogene in the
proximal region of mouse chromosome 1.
Heppell-Parton et al. (1995) concluded that the correct chromosomal
localization of the transcribed thioredoxin gene is 9q31. They
discovered this both by analysis of a somatic cell hybrid panel and by
fluorescence in situ hybridization of a YAC encoding the transcribed
gene. The localization to chromosome 9 was confirmed by PCR
amplification from a human/hamster somatic cell hybrid containing
chromosome 9 as its only human chromosome. No amplification signals were
detected in any of the other monochromosome hybrid cells. The location
of the mouse thioredoxin gene on chromosome 4 is noteworthy because part
of that chromosome shares homology with human chromosome 9.
*FIELD* RF
1. Benhar, M.; Forrester, M. T.; Hess, D. T.; Stamler, J. S.: Regulated
protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320:
1050-1054, 2008.
2. Heppell-Parton, A.; Cahn, A.; Bench, A.; Lowe, N.; Lehrach, H.;
Zehetner, G.; Rabbitts, P.: Thioredoxin, a mediator of growth inhibition,
maps to 9q31. Genomics 26: 379-381, 1995.
3. Junn, E.; Han, S. H.; Im, J. Y.; Yang, Y.; Cho, E. W.; Um, H. D.;
Kim, D. K.; Lee, K. W.; Han, P. L.; Rhee, S. G.; Choi, I.: Vitamin
D3 up-regulated protein 1 mediates oxidative stress via suppressing
the thioredoxin function. J. Immun. 164: 6287-6295, 2000.
4. Kaghad, M.; Dessarps, F.; Jacquemin-Sablon, H.; Caput, D.; Fradelizi,
D.; Wollman, E. E.: Genomic cloning of human thioredoxin-encoding
gene: mapping of the transcription start point and analysis of the
promoter. Gene 140: 273-278, 1994.
5. Lafage-Pochitaloff-Huvale, M.; Shaw, A.; Dessarps, F.; Mannoni,
P.; Fradelizi, D.; Wollman, E. E.: The gene for human thioredoxin
maps on the short arm of chromosome 3 at bands 3p11-p12. FEBS Lett. 255:
89-91, 1989.
6. Saitoh, M.; Nishitoh, H.; Fujii, M.; Takeda, K.; Tobiume, K.; Sawada,
Y.; Kawabata, M.; Miyazono, K.; Ichijo, H.: Mammalian thioredoxin
is a direct inhibitor of apoptosis signal-regulating kinase (ASK)
1. EMBO J. 17: 2596-2606, 1998.
7. Shioji, K.; Kishimoto, C.; Nakamura, H.; Masutani, H.; Yuan, Z.;
Oka, S.; Yodoi, J.: Overexpression of thioredoxin-1 in transgenic
mice attenuates adriamycin-induced cardiotoxicity. Circulation 106:
1403-1409, 2002.
8. Taketo, M.; Matsui, M.; Rochelle, J. M.; Yodoi, J.; Seldin, M.
F.: Mouse thioredoxin gene maps on chromosome 4, whereas its pseudogene
maps on chromosome 1. Genomics 21: 251-253, 1994.
9. Tonissen, K. F.; Wells, J. R. E.: Isolation and characterization
of human thioredoxin-encoding genes. Gene 102: 221-228, 1991.
10. Wang, Y.; De Keulenaer, G. W.; Lee, R. T.: Vitamin D3-up-regulated
protein-1 is a stress-responsive gene that regulates cardiomyocyte
viability through interaction with thioredoxin. J. Biol. Chem. 277:
26496-26500, 2002.
11. Wollman, E. E.; d'Auriol, L.; Rimsky, L.; Shaw, A.; Jacquot, J.-P.;
Wingfield, P.; Graber, P.; Dessarps, F.; Robin, P.; Galibert, F.;
Bertoglio, J.; Fradelizi, D.: Cloning and expression of a cDNA for
human thioredoxin. J. Biol. Chem. 263: 15506-15512, 1988.
12. Yoshioka, J.; Schulze, P. C.; Cupesi, M.; Sylvan, J. D.; MacGillivray,
C.; Gannon, J.; Huang, H.; Lee, R. T.: Thioredoxin-interacting protein
controls cardiac hypertrophy through regulation of thioredoxin activity. Circulation 109:
2581-2586, 2004.
*FIELD* CN
Ada Hamosh - updated: 6/10/2008
Patricia A. Hartz - updated: 2/23/2006
Marla J. F. O'Neill - updated: 2/7/2006
*FIELD* CD
Victor A. McKusick: 12/1/1988
*FIELD* ED
alopez: 06/11/2008
alopez: 6/11/2008
terry: 6/10/2008
mgross: 3/6/2006
terry: 2/23/2006
wwang: 2/7/2006
psherman: 9/21/1998
dholmes: 9/15/1997
terry: 7/7/1997
terry: 4/18/1995
jason: 6/7/1994
supermim: 3/16/1992
carol: 10/3/1991
carol: 6/27/1990
carol: 6/13/1990
*RECORD*
*FIELD* NO
187700
*FIELD* TI
*187700 THIOREDOXIN; TXN
;;TRX;;
TRX1
*FIELD* TX
DESCRIPTION
Thioredoxin is a 12-kD oxidoreductase enzyme containing a
read moredithiol-disulfide active site. It is ubiquitous and found in many
organisms from plants and bacteria to mammals. Multiple in vitro
substrates for thioredoxin have been identified, including ribonuclease,
choriogonadotropins, coagulation factors, glucocorticoid receptor, and
insulin. Reduction of insulin is classically used as an activity test.
CLONING
Wollman et al. (1988) identified a full-length cDNA clone encoding human
thioredoxin. The open reading frame codes for a protein of 104 amino
acids, excluding the initial methionine. This protein possesses the
highly conserved enzymatic active site common to plant and bacterial
thioredoxins: trp-cys-gly-pro-cys (amino acids 30 to 34).
GENE FUNCTION
By yeast 2-hybrid analysis of a human brain cDNA library, Saitoh et al.
(1998) identified TRX and ASK1 (MAP3K5; 602448) as interacting partners.
TRX associated with the N-terminal portion of ASK1 in vitro and in vivo,
and the interaction between TRX and ASK1 was highly dependent on the
redox status of TRX. Expression of TRX inhibited ASK1 kinase activity
and ASK1-dependent apoptosis. Inhibition of TRX resulted in activation
of endogenous ASK1 activity. Saitoh et al. (1998) concluded that TRX is
a physiologic inhibitor of ASK1 and may be involved in redox regulation
of the apoptosis signal transduction pathway.
Junn et al. (2000) found that the C-terminal half of mouse Vdup1 (TXNIP;
606599) interacted with the redox-active center of Trx. Mutation of 2
critical cysteines in the Trx active center abrogated the interaction
with Vdup1. Transfection of mouse Vdup1 into human embryonic kidney
cells reduced the endogenous reducing activity of TRX or the activity of
cotransfected TRX. Overexpression of Vdup1 inhibited interaction between
Trx and a thiol-specific antioxidant, Pag (PRDX1; 176763), and it
inhibited interaction between Trx and Ask1. Treatment of mouse
fibroblasts and T-cell hybridoma cells with various stress stimuli, such
as hydrogen peroxide or heat shock, induced Vdup1 expression. Exposure
of mouse fibroblasts overexpressing Vdup1 to stress resulted in reduced
cell proliferation and elevated apoptotic cell death. Junn et al. (2000)
concluded that VDUP1 functions as an oxidative stress mediator by
inhibiting TRX activity.
Wang et al. (2002) found that biomechanical strain or hydrogen peroxide
downregulated expression of Vdup1, but not Trx, in rat cardiomyocytes.
The rapid response occurred through transcriptional control and led to
increased Trx activity. Adenovirus-mediated overexpression of Vdup1
suppressed Trx activity and induced cardiomyocyte apoptosis.
Furthermore, Vdup1 overexpression sensitized cells to hydrogen
peroxide-induced apoptosis, whereas Trx overexpression protected cells
against injury. Wang et al. (2002) concluded that VDUP1 is a key
stress-responsive inhibitor of thioredoxin activity in cardiomyocytes.
Adriamycin (ADR) is an anticancer drug that causes severe cardiac
toxicity by generating free radicals. Shioji et al. (2002) found that
Trx1 was dose-dependently increased concomitant with formation of
hydroxyl radicals in ADR-treated neonatal rat cardiomyocytes. Treatment
with recombinant human TRX1 suppressed cardiomyocyte injury in
ADR-treated cells. Electron microscopy revealed better maintenance of
cardiac mitochondria and cellular architecture in ADR-treated
TRX1-expressing transgenic mice than in ADR-treated wildtype mice.
Formation of hydroxyl radicals following ADR treatment was reduced in
transgenic mice compared with wildtype mice, and transgenic mice showed
significantly increased survival.
Yoshioka et al. (2004) overexpressed thioredoxin in rat cardiomyocytes
and observed the induction of protein synthesis; overexpression of TXNIP
reduced protein synthesis in response to mechanical strain,
phenylephrine, and angiotensin II (see 106150). In vivo, myocardial TXN
activity increased 3.5-fold compared to sham controls after transverse
aortic constriction; however, aortic constriction did not increase TXN
expression but reduced TXNIP expression by 40%. Gene transfer studies
revealed that cells overexpressing TXNIP developed less hypertrophy
after aortic constriction than control cells in the same animals.
Yoshioka et al. (2004) concluded that TXN has a dual function as both an
antioxidant and a signaling protein involved in the development of
pressure-overload cardiac hypertrophy, and suggested that TXNIP is a
critical regulator of biomechanical signaling.
Nitric oxide (see 163731) acts substantially in cellular signal
transduction through stimulus-coupled S-nitrosylation of cysteine
residues. Benhar et al. (2008) searched for denitrosylase activities,
and focused on caspase-3 (600636), an exemplar of stimulus-dependent
denitrosylation, and identified thioredoxin and thioredoxin reductase
(see 601112) in a biochemical screen. In resting human lymphocytes,
thioredoxin-1 actively denitrosylated cytosolic caspase-3 and thereby
maintained a low steady-state amount of S-nitrosylation. Upon
stimulation of Fas, thioredoxin-2 (609063) mediated denitrosylation of
mitochondria-associated caspase-3, a process required for caspase-3
activation, and promoted apoptosis. Inhibition of
thioredoxin-thioredoxin reductases enabled identification of additional
substrates subject to endogenous S-nitrosylation. These substrates
included caspase-9 (602234) and protein tyrosine phosphatase-1B
(176885). Thus, Benhar et al. (2008) concluded that specific enzymatic
mechanisms may regulate basal and stimulus-induced denitrosylation in
mammalian cells.
GENE STRUCTURE
Tonissen and Wells (1991) determined that the TRX gene extends over 13
kb and consists of 5 exons.
Kaghad et al. (1994) also cloned the TXN gene and demonstrated that the
5 exons are separated by 4 introns. They determined the +1 transcription
start point by primer extension. The +1 site is located 22 bp downstream
from a TATAA box and defines a 5-prime untranslated region of 74 bp.
MAPPING
Using in situ chromosomal hybridization with a human TXN cDNA probe,
Lafage-Pochitaloff-Huvale et al. (1989) localized the gene to chromosome
3p12-p11. Southern analysis by Tonissen and Wells (1991) demonstrated
the presence of several TXN genes in the human genome. At least 1 of
these is inactive, i.e., a pseudogene. By Southern hybridization of
genomic DNAs from several donors, Kaghad et al. (1994) detected only 1
active TXN gene.
Taketo et al. (1994) found that the homologous gene in mouse is located
on chromosome 4 and that there is a processed Txn pseudogene in the
proximal region of mouse chromosome 1.
Heppell-Parton et al. (1995) concluded that the correct chromosomal
localization of the transcribed thioredoxin gene is 9q31. They
discovered this both by analysis of a somatic cell hybrid panel and by
fluorescence in situ hybridization of a YAC encoding the transcribed
gene. The localization to chromosome 9 was confirmed by PCR
amplification from a human/hamster somatic cell hybrid containing
chromosome 9 as its only human chromosome. No amplification signals were
detected in any of the other monochromosome hybrid cells. The location
of the mouse thioredoxin gene on chromosome 4 is noteworthy because part
of that chromosome shares homology with human chromosome 9.
*FIELD* RF
1. Benhar, M.; Forrester, M. T.; Hess, D. T.; Stamler, J. S.: Regulated
protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320:
1050-1054, 2008.
2. Heppell-Parton, A.; Cahn, A.; Bench, A.; Lowe, N.; Lehrach, H.;
Zehetner, G.; Rabbitts, P.: Thioredoxin, a mediator of growth inhibition,
maps to 9q31. Genomics 26: 379-381, 1995.
3. Junn, E.; Han, S. H.; Im, J. Y.; Yang, Y.; Cho, E. W.; Um, H. D.;
Kim, D. K.; Lee, K. W.; Han, P. L.; Rhee, S. G.; Choi, I.: Vitamin
D3 up-regulated protein 1 mediates oxidative stress via suppressing
the thioredoxin function. J. Immun. 164: 6287-6295, 2000.
4. Kaghad, M.; Dessarps, F.; Jacquemin-Sablon, H.; Caput, D.; Fradelizi,
D.; Wollman, E. E.: Genomic cloning of human thioredoxin-encoding
gene: mapping of the transcription start point and analysis of the
promoter. Gene 140: 273-278, 1994.
5. Lafage-Pochitaloff-Huvale, M.; Shaw, A.; Dessarps, F.; Mannoni,
P.; Fradelizi, D.; Wollman, E. E.: The gene for human thioredoxin
maps on the short arm of chromosome 3 at bands 3p11-p12. FEBS Lett. 255:
89-91, 1989.
6. Saitoh, M.; Nishitoh, H.; Fujii, M.; Takeda, K.; Tobiume, K.; Sawada,
Y.; Kawabata, M.; Miyazono, K.; Ichijo, H.: Mammalian thioredoxin
is a direct inhibitor of apoptosis signal-regulating kinase (ASK)
1. EMBO J. 17: 2596-2606, 1998.
7. Shioji, K.; Kishimoto, C.; Nakamura, H.; Masutani, H.; Yuan, Z.;
Oka, S.; Yodoi, J.: Overexpression of thioredoxin-1 in transgenic
mice attenuates adriamycin-induced cardiotoxicity. Circulation 106:
1403-1409, 2002.
8. Taketo, M.; Matsui, M.; Rochelle, J. M.; Yodoi, J.; Seldin, M.
F.: Mouse thioredoxin gene maps on chromosome 4, whereas its pseudogene
maps on chromosome 1. Genomics 21: 251-253, 1994.
9. Tonissen, K. F.; Wells, J. R. E.: Isolation and characterization
of human thioredoxin-encoding genes. Gene 102: 221-228, 1991.
10. Wang, Y.; De Keulenaer, G. W.; Lee, R. T.: Vitamin D3-up-regulated
protein-1 is a stress-responsive gene that regulates cardiomyocyte
viability through interaction with thioredoxin. J. Biol. Chem. 277:
26496-26500, 2002.
11. Wollman, E. E.; d'Auriol, L.; Rimsky, L.; Shaw, A.; Jacquot, J.-P.;
Wingfield, P.; Graber, P.; Dessarps, F.; Robin, P.; Galibert, F.;
Bertoglio, J.; Fradelizi, D.: Cloning and expression of a cDNA for
human thioredoxin. J. Biol. Chem. 263: 15506-15512, 1988.
12. Yoshioka, J.; Schulze, P. C.; Cupesi, M.; Sylvan, J. D.; MacGillivray,
C.; Gannon, J.; Huang, H.; Lee, R. T.: Thioredoxin-interacting protein
controls cardiac hypertrophy through regulation of thioredoxin activity. Circulation 109:
2581-2586, 2004.
*FIELD* CN
Ada Hamosh - updated: 6/10/2008
Patricia A. Hartz - updated: 2/23/2006
Marla J. F. O'Neill - updated: 2/7/2006
*FIELD* CD
Victor A. McKusick: 12/1/1988
*FIELD* ED
alopez: 06/11/2008
alopez: 6/11/2008
terry: 6/10/2008
mgross: 3/6/2006
terry: 2/23/2006
wwang: 2/7/2006
psherman: 9/21/1998
dholmes: 9/15/1997
terry: 7/7/1997
terry: 4/18/1995
jason: 6/7/1994
supermim: 3/16/1992
carol: 10/3/1991
carol: 6/27/1990
carol: 6/13/1990