Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Gene associated with retinoic and interferon-induced mortality 12 protein) (GRIM-12) (Gene associated with retinoic and IFN-induced mortality 12 protein) (KM-102-derived reductase-like factor) (Thioredoxin reductase TR1)

 TRXR1_HUMAN             Reviewed;         649 AA.
Q16881; B7Z1F4; B7Z3Y8; B7Z904; E9PMY9; F5H780; Q6FI31; Q6VB40;
Q6VB41; Q6VB42; Q6VBP2; Q6VBP3; Q6VBP4; Q6VBP5; Q6VBP9; Q6VBQ0;
Q6YNQ1; Q76P53; Q7LA96; Q8WVC8; Q99475; Q9UES8; Q9UH79;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 3.
22-NOV-2017, entry version 203.
RecName: Full=Thioredoxin reductase 1, cytoplasmic;
Short=TR;
EC=1.8.1.9;
AltName: Full=Gene associated with retinoic and interferon-induced mortality 12 protein;
Short=GRIM-12;
Short=Gene associated with retinoic and IFN-induced mortality 12 protein;
AltName: Full=KM-102-derived reductase-like factor;
AltName: Full=Thioredoxin reductase TR1;
Name=TXNRD1; Synonyms=GRIM12, KDRF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PROTEIN SEQUENCE OF 153-161;
307-315 AND 585-607, AND VARIANT GLY-365.
TISSUE=Placenta;
PubMed=7589432; DOI=10.1016/0014-5793(95)01003-W;
Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G.;
"Cloning and sequencing of a human thioredoxin reductase.";
FEBS Lett. 373:5-9(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 122-127
AND 147-151, AND TISSUE SPECIFICITY.
TISSUE=Bone marrow stroma;
PubMed=8999974; DOI=10.1074/jbc.272.4.2570;
Koishi R., Kawashima I., Yoshimura C., Sugawara M., Serizawa N.;
"Cloning and characterization of a novel oxidoreductase KDRF from a
human bone marrow-derived stromal cell line KM-102.";
J. Biol. Chem. 272:2570-2577(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND INDUCTION.
TISSUE=Mammary carcinoma;
PubMed=9774665; DOI=10.1128/MCB.18.11.6493;
Hofman E.R., Boyanapalli M., Lindner D.J., Weihua X., Hassel B.A.,
Jagus R., Gutierrez P.L., Kalvakolanu D.V.;
"Thioredoxin reductase mediates cell death effects of the combination
of beta interferon and retinoic acid.";
Mol. Cell. Biol. 18:6493-6504(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE
[MRNA] (ISOFORMS 2; 3; 4 AND 5), AND VARIANT GLY-365.
TISSUE=Mammary gland, Ovary, Testis, and Thymus;
PubMed=14980707; DOI=10.1016/j.freeradbiomed.2003.12.004;
Rundloef A.-K., Janard M., Miranda-Vizuete A., Arner E.S.;
"Evidence for intriguingly complex transcription of human thioredoxin
reductase 1.";
Free Radic. Biol. Med. 36:641-656(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Schuetze N., Bachthaler M., Lechner A., Koehrle J., Jakob F.;
"Identification by ddPCR of thioredoxin reductase as a vitamin D
regulated gene in human osteoblasts.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Brain;
Xu L., Dai R., Xu J.Y.;
"Cloning and sequencing of thioredoxin reductase gene from human
brain.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Astrocyte, Thalamus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
TISSUE=Trachea;
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PROTEIN SEQUENCE OF 307-316; 449-456; 466-476 AND 638-649, BLOCKAGE OF
N-TERMINUS, SELENOCYSTEINE AT SEC-648, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=8650234; DOI=10.1073/pnas.93.12.6146;
Gladyshev V.N., Jeang K.-T., Stadtman T.C.;
"Selenocysteine, identified as the penultimate C-terminal residue in
human T-cell thioredoxin reductase, corresponds to TGA in the human
placental gene.";
Proc. Natl. Acad. Sci. U.S.A. 93:6146-6151(1996).
[15]
FUNCTION, HOMODIMERIZATION, CHARACTERIZATION, AND PRESENCE OF
SELENOCYSTEINE.
PubMed=8577704; DOI=10.1073/pnas.93.3.1006;
Tamura T., Stadtman T.C.;
"A new selenoprotein from human lung adenocarcinoma cells:
purification, properties, and thioredoxin reductase activity.";
Proc. Natl. Acad. Sci. U.S.A. 93:1006-1011(1996).
[16]
ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6), AND DOMAIN.
PubMed=15379556; DOI=10.1021/bi048478t;
Su D., Gladyshev V.N.;
"Alternative splicing involving the thioredoxin reductase module in
mammals: a glutaredoxin-containing thioredoxin reductase 1.";
Biochemistry 43:12177-12188(2004).
[17]
FUNCTION, INTERACTION WITH ESR1 AND ESR2, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY (ISOFORM 4).
PubMed=15199063; DOI=10.1074/jbc.M402753200;
Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A.,
Spyrou G.;
"An alternative splicing variant of the selenoprotein thioredoxin
reductase is a modulator of estrogen signaling.";
J. Biol. Chem. 279:38721-38729(2004).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[19]
INTERACTION WITH HERC5, AND ISGYLATION.
PubMed=16815975; DOI=10.1073/pnas.0600397103;
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
type I IFN-induced ISGylation of protein targets.";
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
[20]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION (ISOFORM 1).
PubMed=18042542; DOI=10.1074/jbc.M708939200;
Dammeyer P., Damdimopoulos A.E., Nordman T., Jimenez A.,
Miranda-Vizuete A., Arner E.S.J.;
"Induction of cell membrane protrusions by the N-terminal glutaredoxin
domain of a rare splice variant of human thioredoxin reductase 1.";
J. Biol. Chem. 283:2814-2821(2008).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 5), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 5), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[25]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) (ISOFORM 5).
PubMed=17512005; DOI=10.1016/j.jmb.2007.04.044;
Fritz-Wolf K., Urig S., Becker K.;
"The structure of human thioredoxin reductase 1 provides insights into
C-terminal rearrangements during catalysis.";
J. Mol. Biol. 370:116-127(2007).
-!- FUNCTION: Isoform 1 may possess glutaredoxin activity as well as
thioredoxin reductase activity and induces actin and tubulin
polymerization, leading to formation of cell membrane protrusions.
Isoform 4 enhances the transcriptional activity of estrogen
receptors alpha and beta while isoform 5 enhances the
transcriptional activity of the beta receptor only. Isoform 5 also
mediates cell death induced by a combination of interferon-beta
and retinoic acid. {ECO:0000269|PubMed:15199063,
ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8577704,
ECO:0000269|PubMed:9774665}.
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- SUBUNIT: Homodimer. Isoform 4 interacts with ESR1 and ESR2.
Interacts with HERC5. {ECO:0000269|PubMed:15199063,
ECO:0000269|PubMed:16815975}.
-!- INTERACTION:
Q03135:CAV1; NbExp=4; IntAct=EBI-716617, EBI-603614;
P03372:ESR1; NbExp=4; IntAct=EBI-9080335, EBI-78473;
Q92731:ESR2; NbExp=3; IntAct=EBI-9080335, EBI-78505;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=V, TXNRD1_v3;
IsoId=Q16881-1; Sequence=Displayed;
Note=Minor isoform.;
Name=2; Synonyms=II, TXNRD1_v4;
IsoId=Q16881-2; Sequence=VSP_031560, VSP_031565;
Name=3; Synonyms=III, TXNRD1_v5;
IsoId=Q16881-3; Sequence=VSP_031562, VSP_031563;
Name=4; Synonyms=IV, TXNRD1_v2, TrxR1b;
IsoId=Q16881-4; Sequence=VSP_031561, VSP_031564;
Name=5; Synonyms=I, TXNRD1_v1, TrxR1a;
IsoId=Q16881-5; Sequence=VSP_031558;
Note=Major isoform. The N-terminus of the sequence is processed
into a mature form that lacks residues Met-151 and Asn-152 at
the N-terminus. Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:22223895};
Name=6; Synonyms=VI;
IsoId=Q16881-6; Sequence=VSP_031559;
Name=7;
IsoId=Q16881-7; Sequence=VSP_053819;
Note=No experimental confirmation.;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed predominantly in Leydig
cells (at protein level). Also expressed in ovary, spleen, heart,
liver, kidney and pancreas and in a number of cancer cell lines.
Isoform 4 is widely expressed with highest levels in kidney,
testis, uterus, ovary, prostate, placenta and fetal liver.
{ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8999974}.
-!- INDUCTION: Isoform 5 is induced by a combination of interferon-
beta and retinoic acid (at protein level). Isoform 1 is induced by
estradiol or testosterone in HeLa cells.
{ECO:0000269|PubMed:9774665}.
-!- DOMAIN: The N-terminal glutaredoxin domain found in isoform 1 does
not contain the C-P-Y-C redox-active motif normally found in
glutaredoxins and has been found to be inactive in classical
glutaredoxin assays. {ECO:0000269|PubMed:15379556}.
-!- PTM: The N-terminus of isoform 5 is blocked.
-!- PTM: ISGylated. {ECO:0000305|PubMed:16815975}.
-!- MISCELLANEOUS: The thioredoxin reductase active site is a redox-
active disulfide bond. The selenocysteine residue is also
essential for catalytic activity.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB35418.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAC69621.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAF15900.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAV38446.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAZ67916.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=BAA13674.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=BAH11490.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=BAH12374.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=BAH14140.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=CAA04503.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=CAA62629.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=CAG38744.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=EAW97745.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/txnrd1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X91247; CAA62629.1; ALT_SEQ; mRNA.
EMBL; S79851; AAB35418.1; ALT_SEQ; mRNA.
EMBL; D88687; BAA13674.1; ALT_SEQ; mRNA.
EMBL; AF077367; AAC69621.1; ALT_SEQ; mRNA.
EMBL; AY057105; AAL15432.1; -; mRNA.
EMBL; AY344081; AAQ62461.1; -; mRNA.
EMBL; AY344083; AAQ62462.1; -; mRNA.
EMBL; AY344084; AAQ62463.1; -; mRNA.
EMBL; AY344086; AAQ62464.1; -; mRNA.
EMBL; AY344087; AAQ62465.1; -; mRNA.
EMBL; AY344089; AAQ62466.1; -; mRNA.
EMBL; AY344092; AAQ62467.1; -; mRNA.
EMBL; AY344093; AAQ62468.1; -; mRNA.
EMBL; AY344095; AAQ62469.1; -; mRNA.
EMBL; AY344096; AAQ62470.1; -; mRNA.
EMBL; AY344670; AAQ62471.1; -; mRNA.
EMBL; AY344673; AAQ62472.1; -; mRNA.
EMBL; AY344679; AAQ62473.1; -; mRNA.
EMBL; AJ001050; CAA04503.1; ALT_SEQ; mRNA.
EMBL; AF208018; AAF15900.1; ALT_SEQ; mRNA.
EMBL; AK293322; BAH11490.1; ALT_SEQ; mRNA.
EMBL; AK296495; BAH12374.1; ALT_SEQ; mRNA.
EMBL; AK304241; BAH14140.1; ALT_SEQ; mRNA.
EMBL; CR536506; CAG38744.1; ALT_SEQ; mRNA.
EMBL; BT019640; AAV38446.1; ALT_SEQ; mRNA.
EMBL; DQ157758; AAZ67916.1; ALT_SEQ; Genomic_DNA.
EMBL; AC089983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97745.1; ALT_SEQ; Genomic_DNA.
EMBL; BC018122; AAH18122.2; -; mRNA.
CCDS; CCDS53820.1; -. [Q16881-1]
CCDS; CCDS53821.1; -. [Q16881-4]
CCDS; CCDS53823.1; -. [Q16881-5]
CCDS; CCDS58274.1; -. [Q16881-7]
PIR; S66677; S66677.
RefSeq; NP_001087240.1; NM_001093771.2. [Q16881-1]
RefSeq; NP_001248374.1; NM_001261445.1.
RefSeq; NP_001248375.1; NM_001261446.1. [Q16881-7]
RefSeq; NP_003321.3; NM_003330.3. [Q16881-4]
RefSeq; NP_877393.1; NM_182729.2. [Q16881-5]
RefSeq; NP_877419.1; NM_182742.2. [Q16881-5]
RefSeq; NP_877420.1; NM_182743.2. [Q16881-5]
UniGene; Hs.654922; -.
UniGene; Hs.690011; -.
PDB; 1W1C; Model; -; A/B=161-649.
PDB; 2CFY; X-ray; 2.70 A; A/B/C/D/E/F=151-647.
PDB; 2J3N; X-ray; 2.80 A; A/B/C/D/E/F=151-647.
PDB; 2ZZ0; X-ray; 2.80 A; A/B/C/D=150-647.
PDB; 2ZZB; X-ray; 3.20 A; A/B/C/D=150-647.
PDB; 2ZZC; X-ray; 2.60 A; A/B/C/D=150-647.
PDB; 3QFA; X-ray; 2.20 A; A/B=151-649.
PDB; 3QFB; X-ray; 2.60 A; A/B=151-649.
PDBsum; 1W1C; -.
PDBsum; 2CFY; -.
PDBsum; 2J3N; -.
PDBsum; 2ZZ0; -.
PDBsum; 2ZZB; -.
PDBsum; 2ZZC; -.
PDBsum; 3QFA; -.
PDBsum; 3QFB; -.
ProteinModelPortal; Q16881; -.
SMR; Q16881; -.
BioGrid; 113147; 40.
IntAct; Q16881; 9.
MINT; MINT-1525880; -.
STRING; 9606.ENSP00000434516; -.
BindingDB; Q16881; -.
ChEMBL; CHEMBL1927; -.
DrugBank; DB01169; Arsenic trioxide.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB04106; Fotemustine.
DrugBank; DB05428; motexafin gadolinium.
DrugBank; DB02338; Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate.
DrugBank; DB05448; PX-12.
DrugBank; DB03566; Spermidine.
iPTMnet; Q16881; -.
PhosphoSitePlus; Q16881; -.
SwissPalm; Q16881; -.
BioMuta; TXNRD1; -.
DMDM; 172046253; -.
REPRODUCTION-2DPAGE; IPI00554786; -.
EPD; Q16881; -.
MaxQB; Q16881; -.
PaxDb; Q16881; -.
PeptideAtlas; Q16881; -.
PRIDE; Q16881; -.
DNASU; 7296; -.
Ensembl; ENST00000503506; ENSP00000421934; ENSG00000198431. [Q16881-5]
Ensembl; ENST00000524698; ENSP00000433425; ENSG00000198431. [Q16881-5]
Ensembl; ENST00000525566; ENSP00000434516; ENSG00000198431. [Q16881-1]
Ensembl; ENST00000526390; ENSP00000435123; ENSG00000198431. [Q16881-2]
Ensembl; ENST00000526691; ENSP00000435929; ENSG00000198431. [Q16881-4]
Ensembl; ENST00000529546; ENSP00000434919; ENSG00000198431. [Q16881-7]
GeneID; 7296; -.
KEGG; hsa:7296; -.
UCSC; uc010swp.4; human. [Q16881-1]
CTD; 7296; -.
DisGeNET; 7296; -.
EuPathDB; HostDB:ENSG00000198431.15; -.
GeneCards; TXNRD1; -.
H-InvDB; HIX0010939; -.
HGNC; HGNC:12437; TXNRD1.
HPA; CAB004607; -.
HPA; CAB015834; -.
HPA; HPA001395; -.
HPA; HPA043871; -.
MIM; 601112; gene.
neXtProt; NX_Q16881; -.
OpenTargets; ENSG00000198431; -.
PharmGKB; PA37093; -.
eggNOG; KOG1752; Eukaryota.
eggNOG; KOG4716; Eukaryota.
eggNOG; COG1249; LUCA.
GeneTree; ENSGT00390000007578; -.
HOVERGEN; HBG004959; -.
InParanoid; Q16881; -.
KO; K22182; -.
OrthoDB; EOG091G03IU; -.
PhylomeDB; Q16881; -.
TreeFam; TF314782; -.
BRENDA; 1.8.1.9; 2681.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2408550; Metabolism of ingested H2SeO4 and H2SeO3 into H2Se.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
Reactome; R-HSA-5263617; Metabolism of ingested MeSeO2H into MeSeH.
Reactome; R-HSA-5336415; Uptake and function of diphtheria toxin.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
ChiTaRS; TXNRD1; human.
EvolutionaryTrace; Q16881; -.
GeneWiki; TXNRD1; -.
GenomeRNAi; 7296; -.
PRO; PR:Q16881; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000198431; -.
ExpressionAtlas; Q16881; baseline and differential.
Genevisible; Q16881; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0098626; F:methylseleninic acid reductase activity; TAS:Reactome.
GO; GO:0098625; F:methylselenol reductase activity; TAS:Reactome.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; EXP:Reactome.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0000305; P:response to oxygen radical; IBA:GO_Central.
GO; GO:0001887; P:selenium compound metabolic process; TAS:Reactome.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
Pfam; PF00462; Glutaredoxin; 1.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01438; TGR; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond;
Electron transport; FAD; Flavoprotein; NADP; Nucleus; Oxidoreductase;
Phosphoprotein; Polymorphism; Redox-active center; Reference proteome;
Selenocysteine; Transport; Ubl conjugation.
CHAIN 1 649 Thioredoxin reductase 1, cytoplasmic.
/FTId=PRO_0000030286.
DOMAIN 56 156 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
NP_BIND 192 209 FAD. {ECO:0000250}.
ACT_SITE 622 622 Proton acceptor. {ECO:0000250}.
NON_STD 648 648 Selenocysteine.
{ECO:0000269|PubMed:8650234}.
MOD_RES 218 218 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9JMH6}.
MOD_RES 281 281 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
DISULFID 209 214 Redox-active. {ECO:0000250}.
CROSSLNK 647 648 Cysteinyl-selenocysteine (Cys-Sec).
{ECO:0000250}.
VAR_SEQ 1 188 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053819.
VAR_SEQ 1 150 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7589432,
ECO:0000303|PubMed:9774665,
ECO:0000303|Ref.5, ECO:0000303|Ref.6,
ECO:0000303|Ref.8, ECO:0000303|Ref.9}.
/FTId=VSP_031558.
VAR_SEQ 1 139 MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLP
ENPAGFTSTATADSRALLQAYIDGHSVVIFSRSTCTRCTEV
KKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDLPVV
FVKQRKIGGHGPTLKA -> MPVDDYWLCLPASCARPFVQT
VRVVQSCPHCCWFPGVLPSVPEPLRMPAMLPTGSHSAVLPP
SHCSTAPPSTSQEPSSSADPKLCLSPPTSDSRQERNVQFGL
A (in isoform 6). {ECO:0000305}.
/FTId=VSP_031559.
VAR_SEQ 1 106 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_031560.
VAR_SEQ 1 98 Missing (in isoform 4).
{ECO:0000303|PubMed:8999974}.
/FTId=VSP_031561.
VAR_SEQ 1 51 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_031562.
VAR_SEQ 52 100 TADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVP
YFVLELDQ -> MQQVMLTCKGVNRGHAVPAGPGRKPRPRR
SSRLLAGEKHLTRSALLLCH (in isoform 3).
{ECO:0000305}.
/FTId=VSP_031563.
VAR_SEQ 99 101 DQT -> MSC (in isoform 4).
{ECO:0000303|PubMed:8999974}.
/FTId=VSP_031564.
VAR_SEQ 107 138 LEGTLSELAAETDLPVVFVKQRKIGGHGPTLK -> MLSRL
VLNSWAQAIIRPRPPKVLGLQVTTFSE (in isoform
2). {ECO:0000305}.
/FTId=VSP_031565.
VARIANT 365 365 D -> G (in dbSNP:rs1127954).
{ECO:0000269|PubMed:14980707,
ECO:0000269|PubMed:7589432}.
/FTId=VAR_051776.
CONFLICT 153 153 G -> S (in Ref. 4; AAQ62473).
{ECO:0000305}.
CONFLICT 181 181 A -> P (in Ref. 6; AAF15900).
{ECO:0000305}.
CONFLICT 194 194 V -> G (in Ref. 6; AAF15900).
{ECO:0000305}.
CONFLICT 200 200 G -> E (in Ref. 4; AAQ62469).
{ECO:0000305}.
CONFLICT 202 202 R -> K (in Ref. 4; AAQ62463).
{ECO:0000305}.
CONFLICT 215 215 I -> N (in Ref. 4; AAQ62463).
{ECO:0000305}.
CONFLICT 297 297 G -> D (in Ref. 7; BAH11490).
{ECO:0000305}.
CONFLICT 306 306 R -> S (in Ref. 1; AAB35418/CAA62629 and
4; AAL15432). {ECO:0000305}.
CONFLICT 365 365 D -> N (in Ref. 3; AAC69621).
{ECO:0000305}.
CONFLICT 437 437 V -> A (in Ref. 7; BAH12374).
{ECO:0000305}.
CONFLICT 441 441 I -> M (in Ref. 7; BAH12374).
{ECO:0000305}.
CONFLICT 449 449 K -> R (in Ref. 8; CAG38744).
{ECO:0000305}.
CONFLICT 641 641 S -> R (in Ref. 3; AAC69621).
{ECO:0000305}.
STRAND 162 168 {ECO:0000244|PDB:3QFA}.
HELIX 172 183 {ECO:0000244|PDB:3QFA}.
STRAND 188 191 {ECO:0000244|PDB:3QFA}.
HELIX 208 212 {ECO:0000244|PDB:3QFA}.
HELIX 214 233 {ECO:0000244|PDB:3QFA}.
TURN 234 237 {ECO:0000244|PDB:3QFA}.
HELIX 248 272 {ECO:0000244|PDB:3QFA}.
STRAND 276 278 {ECO:0000244|PDB:3QFA}.
STRAND 280 286 {ECO:0000244|PDB:3QFA}.
STRAND 289 293 {ECO:0000244|PDB:3QFA}.
STRAND 295 297 {ECO:0000244|PDB:2ZZ0}.
STRAND 301 309 {ECO:0000244|PDB:3QFA}.
STRAND 313 315 {ECO:0000244|PDB:3QFA}.
HELIX 323 326 {ECO:0000244|PDB:3QFA}.
HELIX 330 333 {ECO:0000244|PDB:3QFA}.
STRAND 342 346 {ECO:0000244|PDB:3QFA}.
HELIX 350 361 {ECO:0000244|PDB:3QFA}.
STRAND 366 372 {ECO:0000244|PDB:3QFA}.
TURN 374 377 {ECO:0000244|PDB:2ZZ0}.
HELIX 380 392 {ECO:0000244|PDB:3QFA}.
STRAND 396 410 {ECO:0000244|PDB:3QFA}.
STRAND 412 414 {ECO:0000244|PDB:2J3N}.
STRAND 416 427 {ECO:0000244|PDB:3QFA}.
STRAND 429 439 {ECO:0000244|PDB:3QFA}.
STRAND 443 446 {ECO:0000244|PDB:3QFA}.
STRAND 448 450 {ECO:0000244|PDB:3QFA}.
TURN 453 456 {ECO:0000244|PDB:3QFA}.
TURN 461 463 {ECO:0000244|PDB:3QFA}.
STRAND 479 481 {ECO:0000244|PDB:3QFA}.
HELIX 483 485 {ECO:0000244|PDB:3QFA}.
STRAND 486 489 {ECO:0000244|PDB:3QFA}.
HELIX 493 508 {ECO:0000244|PDB:3QFA}.
STRAND 522 524 {ECO:0000244|PDB:3QFA}.
STRAND 526 528 {ECO:0000244|PDB:3QFA}.
STRAND 530 534 {ECO:0000244|PDB:3QFA}.
HELIX 537 544 {ECO:0000244|PDB:3QFA}.
HELIX 546 548 {ECO:0000244|PDB:3QFA}.
STRAND 549 556 {ECO:0000244|PDB:3QFA}.
HELIX 559 562 {ECO:0000244|PDB:3QFA}.
TURN 563 565 {ECO:0000244|PDB:3QFA}.
TURN 568 570 {ECO:0000244|PDB:3QFA}.
STRAND 571 578 {ECO:0000244|PDB:3QFA}.
TURN 579 582 {ECO:0000244|PDB:3QFA}.
STRAND 584 592 {ECO:0000244|PDB:3QFA}.
HELIX 595 607 {ECO:0000244|PDB:3QFA}.
HELIX 612 617 {ECO:0000244|PDB:3QFA}.
HELIX 625 631 {ECO:0000244|PDB:3QFA}.
TURN 636 639 {ECO:0000244|PDB:3QFA}.
SEQUENCE 649 AA; 70906 MW; 5A51C3F77EB03EFE CRC64;
MGCAEGKAVA AAAPTELQTK GKNGDGRRRS AKDHHPGKTL PENPAGFTST ATADSRALLQ
AYIDGHSVVI FSRSTCTRCT EVKKLFKSLC VPYFVLELDQ TEDGRALEGT LSELAAETDL
PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE
AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV NVGCIPKKLM HQAALLGQAL QDSRNYGWKV
EETVKHDWDR MIEAVQNHIG SLNWGYRVAL REKKVVYENA YGQFIGPHRI KATNNKGKEK
IYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY VALECAGFLA
GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV
AQSTNSEEII EGEYNTVMLA IGRDACTRKI GLETVGVKIN EKTGKIPVTD EEQTNVPYIY
AIGDILEDKV ELTPVAIQAG RLLAQRLYAG STVKCDYENV PTTVFTPLEY GACGLSEEKA
VEKFGEENIE VYHSYFWPLE WTIPSRDNNK CYAKIICNTK DNERVVGFHV LGPNAGEVTQ
GFAAALKCGL TKKQLDSTIG IHPVCAEVFT TLSVTKRSGA SILQAGCUG


Related products :

Catalog number Product name Quantity
EIAAB44148 Gene associated with retinoic and IFN-induced mortality 12 protein,Gene associated with retinoic and interferon-induced mortality 12 protein,GRIM12,GRIM-12,Homo sapiens,Human,KDRF,KM-102-derived reduc
EIAAB26732 Cell death regulatory protein GRIM-19,CI-B16.6,Complex I-B16.6,Gene associated with retinoic and IFN-induced mortality 19 protein,Gene associated with retinoic and interferon-induced mortality 19 prot
EIAAB26734 CDA016,Cell death regulatory protein GRIM-19,CGI-39,CI-B16.6,Complex I-B16.6,Gene associated with retinoic and IFN-induced mortality 19 protein,Gene associated with retinoic and interferon-induced mor
EIAAB26733 Bos taurus,Bovine,Cell death regulatory protein GRIM-19,CI-B16.6,Complex I-B16.6,Gene associated with retinoic-interferon-induced mortality 19 protein,GRIM19,GRIM-19,NADH dehydrogenase [ubiquinone] 1
EIAAB43736 Homo sapiens,Human,Protein TXNRD3NB,Thioredoxin reductase 2 intronic transcript 1,Thioredoxin reductase 3 intronic transcript 1,Thioredoxin reductase 3 neighbor gene protein,Thioredoxin reductase 3 ne
EIAAB44144 NADPH-dependent thioredoxin reductase,Rat,Rattus norvegicus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1
EIAAB44153 Homo sapiens,Human,TGR,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,TRXR3,TXNRD3
EIAAB44154 Mouse,Mus musculus,Tgr,Thioredoxin and glutathione reductase,Thioredoxin reductase 3,Thioredoxin reductase TR2,Trxr3,Txnrd3
EIAAB44146 Mouse,Mus musculus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1
orb90288 Yeast Thioredoxin Reductase protein Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin R 5
EIAAB44145 Bos taurus,Bovine,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,TXNRD1
EIAAB44147 Pig,Sus scrofa,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,TXNRD1
EIAAB33712 Gprc5a,G-protein coupled receptor family C group 5 member A,Mouse,Mus musculus,Rai3,Raig1,RAIG-1,Retinoic acid-induced gene 1 protein,Retinoic acid-induced protein 3
18-461-10472 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10473 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10669 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10670 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-003-44260 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein-coupling receptor PEIG-1 Polyclonal 0.05 mg Aff Pur
18-461-10751 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10340 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
EIAAB44150 Homo sapiens,Human,KIAA1652,Selenoprotein Z,SelZ,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,TR-beta,TRXR2,TXNRD2
EIAAB44151 Bos taurus,Bovine,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,TRXR2,TXNRD2
EIAAB44149 Mouse,Mus musculus,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,Trxr2,Txnrd2
EIAAB44152 Rat,Rattus norvegicus,Thioredoxin reductase 2, mitochondrial,Thioredoxin reductase TR3,Trxr2,Txnrd2
E1507r ELISA Kit FOR Thioredoxin reductase 1, cytoplasmic; organism: Rat; gene name: Txnrd1 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur