THIO_HUMAN
ID THIO_HUMAN Reviewed; 105 AA.
AC P10599; B1ALW1; O60744; Q53X69; Q96KI3; Q9UDG5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 242.
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;
DE AltName: Allergen=Hom s Trx {ECO:0000305};
GN Name=TXN; Synonyms=TRDX, TRX, TRX1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3170595; DOI=10.1016/s0021-9258(19)37617-3;
RA Wollman E.E., D'Auriol L., Rimsky L., Shaw A., Jacquot J.-P., Wingfield P.,
RA 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; DOI=10.1002/j.1460-2075.1989.tb03436.x;
RA Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N.,
RA 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 receptor
RT 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 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; DOI=10.1042/bj3040861;
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 plasma
RT membranes.";
RL Biochem. Biophys. Res. Commun. 175:123-128(1991).
RN [16]
RP PROTEIN SEQUENCE OF 9-48; 73-81 AND 95-105, AND IDENTIFICATION BY MASS
RP 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., Decottignies P.,
RA 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; DOI=10.1016/s0021-9258(18)35742-9;
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, SUBCELLULAR LOCATION, ACTIVE
RP SITES, AND MUTAGENESIS OF CYS-32; CYS-35; CYS-62; CYS-69 AND CYS-73.
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 between
RT 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., Laszlo A.,
RA 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 system
RT 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, AND ALLERGEN.
RX PubMed=17182577; DOI=10.4049/jimmunol.178.1.389;
RA Limacher A., Glaser A.G., Meier C., Schmid-Grendelmeier P., Zeller S.,
RA Scapozza L., Crameri R.;
RT "Cross-reactivity and 1.4-A crystal structure of Malassezia sympodialis
RT thioredoxin (Mala s 13), a member of a new pan-allergen family.";
RL J. Immunol. 178:389-396(2007).
RN [24]
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 [25]
RP FUNCTION, AND ALLERGEN.
RX PubMed=19032234; DOI=10.1111/j.1398-9995.2008.01777.x;
RA Glaser A.G., Menz G., Kirsch A.I., Zeller S., Crameri R., Rhyner C.;
RT "Auto- and cross-reactivity to thioredoxin allergens in allergic
RT bronchopulmonary aspergillosis.";
RL Allergy 63:1617-1623(2008).
RN [26]
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., Harbi S.O.,
RA 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 [27]
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 for
RT mammalian thioredoxin.";
RL J. Biol. Chem. 284:27587-27595(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-39, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [29]
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., Buerckstuemmer T.,
RA 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 [30]
RP ALLERGEN.
RX PubMed=21489611; DOI=10.1016/j.jaci.2011.02.043;
RA Balaji H., Heratizadeh A., Wichmann K., Niebuhr M., Crameri R.,
RA Scheynius A., Werfel T.;
RT "Malassezia sympodialis thioredoxin-specific T cells are highly cross-
RT reactive to human thioredoxin in atopic dermatitis.";
RL J. Allergy Clin. Immunol. 128:92-99(2011).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [33]
RP STRUCTURE BY NMR.
RX PubMed=2684271; DOI=10.1021/bi00443a045;
RA Forman-Kay J.D., Clore G.M., Dricoll P.C., Wingfield P., Richards F.M.,
RA Gronenborn A.M.;
RT "A proton nuclear magnetic resonance assignment and secondary structure
RT determination of recombinant human thioredoxin.";
RL Biochemistry 28:7088-7097(1989).
RN [34]
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 human
RT thioredoxin in solution.";
RL Biochemistry 30:2685-2698(1991).
RN [35]
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 oxidized
RT and reduced states of human thioredoxin.";
RL Structure 2:503-522(1994).
RN [36]
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 intermediate
RT complex with its target peptide from the transcription factor NF kappa B.";
RL Structure 3:289-297(1995).
RN [37]
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 from
RT Ref-1 reveals peptide chain reversal.";
RL Structure 4:613-620(1996).
RN [38]
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 thioredoxins:
RT evidence for a regulatory homodimer.";
RL Structure 4:735-751(1996).
RN [39]
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, and
RT crystal structure of the aspartate 60 --> asparagine mutant.";
RL Biochemistry 36:13979-13988(1997).
RN [40]
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 and
CC catalyzes dithiol-disulfide exchange reactions (PubMed:2176490,
CC PubMed:17182577, PubMed:19032234). Plays a role in the reversible S-
CC nitrosylation of cysteine residues in target proteins, and thereby
CC contributes to the response to intracellular nitric oxide. Nitrosylates
CC the active site Cys of CASP3 in response to nitric oxide (NO), and
CC thereby inhibits caspase-3 activity (PubMed:16408020, PubMed:17606900).
CC Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation
CC (IR) cells through its oxidation/reduction status and stimulates AP-1
CC transcriptional activity (PubMed:9108029, PubMed:11118054).
CC {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:16408020,
CC ECO:0000269|PubMed:17182577, ECO:0000269|PubMed:17606900,
CC ECO:0000269|PubMed:19032234, ECO:0000269|PubMed:2176490,
CC ECO:0000269|PubMed:9108029}.
CC -!- FUNCTION: ADF augments the expression of the interleukin-2 receptor TAC
CC (IL2R/P55).
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:9369469, PubMed:17260951).
CC Interacts with TXNIP through the redox-active site (PubMed:17260951).
CC Interacts with MAP3K5 and CASP3 (PubMed:15246877). In case of
CC infection, interacts with S.typhimurium protein slrP (PubMed:19690162).
CC Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-
CC binding activity in a redox-dependent manner (PubMed:9108029).
CC {ECO:0000269|PubMed:15246877, ECO:0000269|PubMed:17260951,
CC ECO:0000269|PubMed:19690162, ECO:0000269|PubMed:9108029,
CC ECO:0000269|PubMed:9369469}.
CC -!- INTERACTION:
CC P10599; P01023: A2M; NbExp=3; IntAct=EBI-594644, EBI-640741;
CC P10599; P12814: ACTN1; NbExp=3; IntAct=EBI-594644, EBI-351710;
CC P10599; P31749: AKT1; NbExp=3; IntAct=EBI-594644, EBI-296087;
CC P10599; X5D778: ANKRD11; NbExp=6; IntAct=EBI-594644, EBI-17183751;
CC P10599; P23560-2: BDNF; NbExp=3; IntAct=EBI-594644, EBI-12275524;
CC P10599; P42574: CASP3; NbExp=6; IntAct=EBI-594644, EBI-524064;
CC P10599; Q92905: COPS5; NbExp=9; IntAct=EBI-594644, EBI-594661;
CC P10599; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-594644, EBI-742054;
CC P10599; G5E9A7: DMWD; NbExp=3; IntAct=EBI-594644, EBI-10976677;
CC P10599; P50570-2: DNM2; NbExp=3; IntAct=EBI-594644, EBI-10968534;
CC P10599; P00533: EGFR; NbExp=5; IntAct=EBI-594644, EBI-297353;
CC P10599; P19883: FST; NbExp=3; IntAct=EBI-594644, EBI-1571188;
CC P10599; P04406: GAPDH; NbExp=3; IntAct=EBI-594644, EBI-354056;
CC P10599; P14136: GFAP; NbExp=3; IntAct=EBI-594644, EBI-744302;
CC P10599; P07900: HSP90AA1; NbExp=3; IntAct=EBI-594644, EBI-296047;
CC P10599; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-594644, EBI-1055254;
CC P10599; Q14114-3: LRP8; NbExp=3; IntAct=EBI-594644, EBI-25832196;
CC P10599; Q99683: MAP3K5; NbExp=4; IntAct=EBI-594644, EBI-476263;
CC P10599; P51608: MECP2; NbExp=3; IntAct=EBI-594644, EBI-1189067;
CC P10599; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-594644, EBI-995714;
CC P10599; Q99836: MYD88; NbExp=4; IntAct=EBI-594644, EBI-447677;
CC P10599; P19404: NDUFV2; NbExp=3; IntAct=EBI-594644, EBI-713665;
CC P10599; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-594644, EBI-740897;
CC P10599; P37198: NUP62; NbExp=3; IntAct=EBI-594644, EBI-347978;
CC P10599; P32119: PRDX2; NbExp=2; IntAct=EBI-594644, EBI-1266300;
CC P10599; P18031: PTPN1; NbExp=2; IntAct=EBI-594644, EBI-968788;
CC P10599; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-594644, EBI-748621;
CC P10599; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-594644, EBI-742688;
CC P10599; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-594644, EBI-5235340;
CC P10599; Q9BXU3: TEX13A; NbExp=3; IntAct=EBI-594644, EBI-10301068;
CC P10599; Q12933: TRAF2; NbExp=3; IntAct=EBI-594644, EBI-355744;
CC P10599; Q9H3M7: TXNIP; NbExp=8; IntAct=EBI-594644, EBI-1369170;
CC P10599; D0ZRB2: slrP; Xeno; NbExp=7; IntAct=EBI-594644, EBI-10762386;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11118054,
CC ECO:0000269|PubMed:9108029}. Cytoplasm {ECO:0000269|PubMed:11118054,
CC ECO:0000269|PubMed:9108029}. Secreted {ECO:0000269|PubMed:1332947}.
CC Note=Translocates from the cytoplasm into the nucleus after phorbol 12-
CC myristate 13-acetate induction (PMA) (PubMed:9108029). Predominantly in
CC the cytoplasm in non irradiated cells (PubMed:11118054). Radiation
CC induces translocation of TRX from the cytoplasm to the nucleus
CC (PubMed:11118054). Secreted by a leaderless secretory pathway
CC (PubMed:1332947). {ECO:0000269|PubMed:11118054,
CC ECO:0000269|PubMed:1332947, ECO:0000269|PubMed:9108029}.
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 {ECO:0000269|PubMed:11118054}.
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 bonds
CC are present in the protein, only Cys-73 is nitrosylated. Cys-73 can
CC serve as donor for nitrosylation of target proteins.
CC {ECO:0000269|PubMed:15246877, ECO:0000269|PubMed:16408020,
CC ECO:0000269|PubMed:17260951, ECO:0000269|PubMed:17606900}.
CC -!- PTM: In case of infection, ubiquitinated by S.typhimurium protein slrP,
CC leading to its degradation. {ECO:0000269|PubMed:19690162}.
CC -!- ALLERGEN: Causes an allergic reaction in human (PubMed:17182577,
CC PubMed:19032234, PubMed:21489611). Recombinant protein binds to IgE in
CC atopic eczema-suffering patients allergic to opportunistic skin-
CC colonizing yeast M.sympodialis. Intermediate cross-reactivity is
CC detected between the recombinant thioredoxin from M.sympodialis (Mala s
CC 13) and recombinant form of this protein. Skin-prick test (SPT) and
CC atopy patch test (APT) with 5 patients confirm cross-reactivity between
CC the two proteins (PubMed:17182577). Recombinant protein binds to IgE of
CC patients suffering from allergic bronchopulmonary aspergillosis (ABPA)
CC and cross-reacts extensively with recombinant thioredoxin proteins from
CC A.fumigatus (Asp f 28 and Asp f 29) and Mala s 13. Causes a positive
CC skin reaction and induces proliferation of the human peripheral blood
CC mononuclear cells in ABPA patients allergic to this protein. Acts as an
CC IgE-binding self-antigen in ABPA patients allergic to fungal
CC thioredoxin (PubMed:19032234). In atopic dermatitis (AD)-suffering
CC patients allergic to M.sympodialis, a cross-reactivity between Mala s
CC 13 and this protein can be detected in T-cells of the peripheral blood
CC and skin. Keratinocytes stimulated by interferon (IFN)-alpha and tumor
CC necrosis factor (TNF)-alpha release thioredoxin, which then becomes
CC available for cross-reactivity with Mala s 13-specific T cells. The
CC autoreactive T cells identified include T-helper 1 (Th1), T-helper 2
CC (Th2), T-helper 17 (Th17) and T-helper 22 (Th22) phenotypes. Skinhoming
CC T cells autoreactive to this protein may be relevant for cutaneous
CC inflammation in patients with AD (PubMed:21489611).
CC {ECO:0000269|PubMed:17182577, ECO:0000269|PubMed:19032234,
CC ECO:0000269|PubMed:21489611}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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 and
CC 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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS35103.1; -. [P10599-1]
DR CCDS; CCDS59139.1; -. [P10599-2]
DR PIR; JH0568; JH0568.
DR RefSeq; NP_001231867.1; NM_001244938.1. [P10599-2]
DR RefSeq; NP_003320.2; NM_003329.3. [P10599-1]
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=1-66.
DR PDB; 1MDI; NMR; -; A=1-105.
DR PDB; 1MDJ; NMR; -; A=1-105.
DR PDB; 1MDK; NMR; -; A=1-105.
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; 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; 4LL1; X-ray; 2.00 A; B/D=1-105.
DR PDB; 4LL4; X-ray; 2.70 A; B/D=1-105.
DR PDB; 4OO4; X-ray; 0.97 A; A/B=1-105.
DR PDB; 4OO5; X-ray; 1.54 A; A=1-105.
DR PDB; 4POK; X-ray; 2.52 A; A/B/C/D=1-105.
DR PDB; 4POL; X-ray; 2.80 A; A/B/C/D=1-105.
DR PDB; 4POM; X-ray; 1.85 A; A/B/C/D=1-105.
DR PDB; 4PUF; X-ray; 3.30 A; C/D=1-105.
DR PDB; 4TRX; NMR; -; A=1-105.
DR PDB; 5DQY; X-ray; 1.40 A; 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; 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; 4LL1; -.
DR PDBsum; 4LL4; -.
DR PDBsum; 4OO4; -.
DR PDBsum; 4OO5; -.
DR PDBsum; 4POK; -.
DR PDBsum; 4POL; -.
DR PDBsum; 4POM; -.
DR PDBsum; 4PUF; -.
DR PDBsum; 4TRX; -.
DR PDBsum; 5DQY; -.
DR AlphaFoldDB; P10599; -.
DR BMRB; P10599; -.
DR SMR; P10599; -.
DR BioGRID; 113146; 235.
DR DIP; DIP-6129N; -.
DR IntAct; P10599; 103.
DR MINT; P10599; -.
DR STRING; 9606.ENSP00000363641; -.
DR BindingDB; P10599; -.
DR ChEMBL; CHEMBL2010624; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR Allergome; 3543; Hom s Trx.
DR CarbonylDB; P10599; -.
DR GlyGen; P10599; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P10599; -.
DR MetOSite; P10599; -.
DR PhosphoSitePlus; P10599; -.
DR SwissPalm; P10599; -.
DR BioMuta; TXN; -.
DR DMDM; 135773; -.
DR DOSAC-COBS-2DPAGE; P10599; -.
DR REPRODUCTION-2DPAGE; IPI00216298; -.
DR SWISS-2DPAGE; P10599; -.
DR EPD; P10599; -.
DR jPOST; P10599; -.
DR MassIVE; P10599; -.
DR MaxQB; P10599; -.
DR PaxDb; P10599; -.
DR PeptideAtlas; P10599; -.
DR PRIDE; P10599; -.
DR ProteomicsDB; 3175; -.
DR ProteomicsDB; 52616; -. [P10599-1]
DR TopDownProteomics; P10599-1; -. [P10599-1]
DR TopDownProteomics; P10599-2; -. [P10599-2]
DR Antibodypedia; 3281; 846 antibodies from 39 providers.
DR DNASU; 7295; -.
DR Ensembl; ENST00000374515.9; ENSP00000363639.5; ENSG00000136810.13. [P10599-2]
DR Ensembl; ENST00000374517.6; ENSP00000363641.5; ENSG00000136810.13. [P10599-1]
DR GeneID; 7295; -.
DR KEGG; hsa:7295; -.
DR MANE-Select; ENST00000374517.6; ENSP00000363641.5; NM_003329.4; NP_003320.2.
DR UCSC; uc004bep.3; human. [P10599-1]
DR CTD; 7295; -.
DR DisGeNET; 7295; -.
DR GeneCards; TXN; -.
DR HGNC; HGNC:12435; TXN.
DR HPA; ENSG00000136810; Tissue enhanced (esophagus).
DR MIM; 187700; gene.
DR neXtProt; NX_P10599; -.
DR OpenTargets; ENSG00000136810; -.
DR PharmGKB; PA37091; -.
DR VEuPathDB; HostDB:ENSG00000136810; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000154259; -.
DR HOGENOM; CLU_090389_14_6_1; -.
DR InParanoid; P10599; -.
DR OMA; MKEWIKQ; -.
DR OrthoDB; 1568661at2759; -.
DR PhylomeDB; P10599; -.
DR TreeFam; TF318932; -.
DR PathwayCommons; P10599; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-5676934; Protein repair.
DR Reactome; R-HSA-844456; The NLRP3 inflammasome.
DR Reactome; R-HSA-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SignaLink; P10599; -.
DR SIGNOR; P10599; -.
DR BioGRID-ORCS; 7295; 686 hits in 1023 CRISPR screens.
DR ChiTaRS; TXN; human.
DR EvolutionaryTrace; P10599; -.
DR GeneWiki; Thioredoxin; -.
DR GenomeRNAi; 7295; -.
DR Pharos; P10599; Tchem.
DR PRO; PR:P10599; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P10599; protein.
DR Bgee; ENSG00000136810; Expressed in gingival epithelium and 206 other tissues.
DR ExpressionAtlas; P10599; baseline and differential.
DR Genevisible; P10599; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; TAS:Reactome.
DR GO; GO:0032148; P:activation of protein kinase B activity; IC:ParkinsonsUK-UCL.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:ParkinsonsUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IC:ParkinsonsUK-UCL.
DR GO; GO:0071731; P:response to nitric oxide; IMP:UniProtKB.
DR GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
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; Allergen; Alternative splicing;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Electron transport;
KW Nucleus; Redox-active center; Reference proteome; S-nitrosylation;
KW Secreted; Transcription; Transcription regulation; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1998498,
FT ECO:0000269|PubMed:7818492"
FT CHAIN 2..105
FT /note="Thioredoxin"
FT /id="PRO_0000120005"
FT DOMAIN 2..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9108029"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9108029"
FT SITE 26
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000305"
FT SITE 33
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000305"
FT SITE 34
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000305"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 8
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10639"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 62
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:17260951"
FT MOD_RES 69
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:17260951"
FT MOD_RES 73
FT /note="S-nitrosocysteine; alternate"
FT /evidence="ECO:0000269|PubMed:16408020,
FT ECO:0000269|PubMed:17606900"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10639"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10639"
FT DISULFID 32..35
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:17260951, ECO:0000269|PubMed:2001356"
FT DISULFID 73
FT /note="Interchain; alternate"
FT /evidence="ECO:0000269|PubMed:17260951"
FT VAR_SEQ 44..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.13"
FT /id="VSP_045607"
FT MUTAGEN 32
FT /note="C->S: Loses its reducing activity, interaction with
FT APEX1 and transcription activation; when associated with S-
FT 35."
FT /evidence="ECO:0000269|PubMed:9108029"
FT MUTAGEN 35
FT /note="C->S: Loses its reducing activity, interaction with
FT APEX1 and transcription activation; when associated with S-
FT 32."
FT /evidence="ECO:0000269|PubMed:9108029"
FT MUTAGEN 60
FT /note="D->N: Loss of pH-dependence of dimerization."
FT MUTAGEN 62
FT /note="C->S: Retains its reducing activity. Retains
FT interaction with APEX1 and transcription activation; when
FT associated with S-69 and S-73."
FT /evidence="ECO:0000269|PubMed:9108029"
FT MUTAGEN 69
FT /note="C->S: No effect on reducing activity, interaction
FT with APEX1 and on S-nitrosylation of C-73. Retains
FT interaction with APEX1 and transcription activation; when
FT associated with S-62 and S-73."
FT /evidence="ECO:0000269|PubMed:17606900,
FT ECO:0000269|PubMed:9108029"
FT MUTAGEN 70
FT /note="E->A: Strongly reduced interaction with CASP3; when
FT associated with A-72."
FT /evidence="ECO:0000269|PubMed:17606900"
FT MUTAGEN 72
FT /note="K->A: Strongly reduced interaction with CASP3; when
FT associated with A-70."
FT /evidence="ECO:0000269|PubMed:17606900"
FT MUTAGEN 73
FT /note="C->D: Strongly reduced S-nitrosylation of CASP3."
FT /evidence="ECO:0000269|PubMed:16408020,
FT ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:9108029"
FT MUTAGEN 73
FT /note="C->S: Loss of nitrosylation, and loss of S-
FT nitrosylating activity towards CASP3. Retains interaction
FT with APEX1 and transcription activation; when associated
FT with S-62 and S-69."
FT /evidence="ECO:0000269|PubMed:16408020,
FT ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:9108029"
FT MUTAGEN 73
FT /note="C->S: Retains its reducing activity."
FT /evidence="ECO:0000269|PubMed:16408020,
FT ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:9108029"
FT CONFLICT 39
FT /note="K -> N (in Ref. 1; AAA74596 and 4; AAF86466)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="M -> T (in Ref. 1; AAA74596 and 4; AAF86466)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2IFQ"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:4OO4"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:4OO4"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:4OO4"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4TRX"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:4OO4"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3QFB"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4OO4"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:4OO4"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:4OO4"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:4OO4"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:4OO4"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:4OO4"
SQ SEQUENCE 105 AA; 11737 MW; 256F4E3C8A187693 CRC64;
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD
DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV
