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Q9JMH6

- TRXR1_MOUSE

UniProt

Q9JMH6 - TRXR1_MOUSE

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Protein

Thioredoxin reductase 1, cytoplasmic

Gene

Txnrd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei586 – 5861Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 17318FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. NADP binding Source: InterPro
  3. thioredoxin-disulfide reductase activity Source: MGI

GO - Biological processi

  1. cell proliferation Source: MGI
  2. cell redox homeostasis Source: InterPro
  3. gastrulation Source: MGI
  4. mesoderm formation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.8.1.9. 3474.
ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
REACT_198602. PPARA activates gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 1, cytoplasmic (EC:1.8.1.9)
Short name:
TR
Alternative name(s):
Thioredoxin reductase TR1
Gene namesi
Name:Txnrd1
Synonyms:Trxr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1354175. Txnrd1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: MGI
  3. mitochondrion Source: MGI
  4. nucleolus Source: Ensembl
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 613613Thioredoxin reductase 1, cytoplasmicPRO_0000067982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi173 ↔ 178Redox-activeBy similarity
Modified residuei182 – 1821N6-succinyllysine1 Publication
Modified residuei245 – 2451Phosphotyrosine1 Publication
Cross-linki611 ↔ 612Cysteinyl-selenocysteine (Cys-Sec)By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9JMH6.
PaxDbiQ9JMH6.
PRIDEiQ9JMH6.

2D gel databases

REPRODUCTION-2DPAGEQ9JMH6.

PTM databases

PhosphoSiteiQ9JMH6.

Expressioni

Gene expression databases

BgeeiQ9JMH6.
CleanExiMM_TXNRD1.
ExpressionAtlasiQ9JMH6. baseline and differential.
GenevestigatoriQ9JMH6.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9JMH6. 3 interactions.
MINTiMINT-1869051.

Structurei

3D structure databases

ProteinModelPortaliQ9JMH6.
SMRiQ9JMH6. Positions 124-611.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 9065Pro-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
GeneTreeiENSGT00390000007578.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiQ9JMH6.
KOiK00384.
OMAiVCAEIFT.
OrthoDBiEOG779NXG.
PhylomeDBiQ9JMH6.
TreeFamiTF314782.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JMH6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPVDDCWLYF PASRGRTFVQ TVWVAPTCPN CCWFPGFLPP VPRPPHVPRV
60 70 80 90 100
LLRGPRGAVL PASRPSKTLP SSSQTPCPTD PCICPPPSTP DSRQEKNTQS
110 120 130 140 150
ELPNKKGQLQ KLPTMNGSKD PPGSYDFDLI IIGGGSGGLA AAKEAAKFDK
160 170 180 190 200
KVLVLDFVTP TPLGTRWGLG GTCVNVGCIP KKLMHQAALL GQALKDSRNY
210 220 230 240 250
GWKVEDTVKH DWEKMTESVQ SHIGSLNWGY RVALREKKVV YENAYGRFIG
260 270 280 290 300
PHRIVATNNK GKEKIYSAER FLIATGERPR YLGIPGDKEY CISSDDLFSL
310 320 330 340 350
PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMANKI
360 370 380 390 400
GEHMEEHGIK FIRQFVPTKI EQIEAGTPGR LRVTAQSTNS EETIEGEFNT
410 420 430 440 450
VLLAVGRDSC TRTIGLETVG VKINEKTGKI PVTDEEQTNV PYIYAIGDIL
460 470 480 490 500
EGKLELTPVA IQAGRLLAQR LYGGSNVKCD YDNVPTTVFT PLEYGCCGLS
510 520 530 540 550
EEKAVEKFGE ENIEVYHSFF WPLEWTVPSR DNNKCYAKII CNLKDDERVV
560 570 580 590 600
GFHVLGPNAG EVTQGFAAAL KCGLTKQQLD STIGIHPVCA EIFTTLSVTK
610
RSGGDILQSG CUG
Length:613
Mass (Da):67,084
Last modified:February 26, 2008 - v3
Checksum:iC9FD2E2E8C55118C
GO
Isoform 2 (identifier: Q9JMH6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.

Show »
Length:499
Mass (Da):54,544
Checksum:iFEBB478D8B22429E
GO

Sequence cautioni

The sequence AAH37643.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec.
The sequence BAE26918.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec.
The sequence BAE40292.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381K → E in BAE28994. (PubMed:16141072)Curated
Sequence conflicti372 – 3721Q → R in BAE26918. (PubMed:16141072)Curated
Sequence conflicti607 – 6071L → V in BAE26918. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 114114Missing in isoform 2. 3 PublicationsVSP_031566Add
BLAST

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei612 – 6121SelenocysteineBy similarity

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB027565 mRNA. Translation: BAA86985.2.
AF333036 mRNA. Translation: AAK01140.1.
AK011902 mRNA. Translation: BAB27905.1.
AK146125 mRNA. Translation: BAE26918.1. Sequence problems.
AK149625 mRNA. Translation: BAE28994.1.
AK168356 mRNA. Translation: BAE40292.1. Sequence problems.
BC037643 mRNA. Translation: AAH37643.1. Sequence problems.
CCDSiCCDS24072.1. [Q9JMH6-2]
RefSeqiNP_001035978.1. NM_001042513.1. [Q9JMH6-2]
NP_001035979.1. NM_001042514.1. [Q9JMH6-2]
NP_001035988.1. NM_001042523.1. [Q9JMH6-1]
NP_056577.2. NM_015762.2. [Q9JMH6-2]
UniGeneiMm.210155.
Mm.471159.

Genome annotation databases

EnsembliENSMUST00000020484; ENSMUSP00000020484; ENSMUSG00000020250. [Q9JMH6-2]
GeneIDi50493.
KEGGimmu:50493.
UCSCiuc007gjy.1. mouse. [Q9JMH6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB027565 mRNA. Translation: BAA86985.2 .
AF333036 mRNA. Translation: AAK01140.1 .
AK011902 mRNA. Translation: BAB27905.1 .
AK146125 mRNA. Translation: BAE26918.1 . Sequence problems.
AK149625 mRNA. Translation: BAE28994.1 .
AK168356 mRNA. Translation: BAE40292.1 . Sequence problems.
BC037643 mRNA. Translation: AAH37643.1 . Sequence problems.
CCDSi CCDS24072.1. [Q9JMH6-2 ]
RefSeqi NP_001035978.1. NM_001042513.1. [Q9JMH6-2 ]
NP_001035979.1. NM_001042514.1. [Q9JMH6-2 ]
NP_001035988.1. NM_001042523.1. [Q9JMH6-1 ]
NP_056577.2. NM_015762.2. [Q9JMH6-2 ]
UniGenei Mm.210155.
Mm.471159.

3D structure databases

ProteinModelPortali Q9JMH6.
SMRi Q9JMH6. Positions 124-611.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9JMH6. 3 interactions.
MINTi MINT-1869051.

PTM databases

PhosphoSitei Q9JMH6.

2D gel databases

REPRODUCTION-2DPAGE Q9JMH6.

Proteomic databases

MaxQBi Q9JMH6.
PaxDbi Q9JMH6.
PRIDEi Q9JMH6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020484 ; ENSMUSP00000020484 ; ENSMUSG00000020250 . [Q9JMH6-2 ]
GeneIDi 50493.
KEGGi mmu:50493.
UCSCi uc007gjy.1. mouse. [Q9JMH6-1 ]

Organism-specific databases

CTDi 7296.
MGIi MGI:1354175. Txnrd1.

Phylogenomic databases

eggNOGi COG1249.
GeneTreei ENSGT00390000007578.
HOGENOMi HOG000276712.
HOVERGENi HBG004959.
InParanoidi Q9JMH6.
KOi K00384.
OMAi VCAEIFT.
OrthoDBi EOG779NXG.
PhylomeDBi Q9JMH6.
TreeFami TF314782.

Enzyme and pathway databases

BRENDAi 1.8.1.9. 3474.
Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
REACT_198602. PPARA activates gene expression.

Miscellaneous databases

ChiTaRSi TXNRD1. mouse.
NextBioi 307476.
PROi Q9JMH6.
SOURCEi Search...

Gene expression databases

Bgeei Q9JMH6.
CleanExi MM_TXNRD1.
ExpressionAtlasi Q9JMH6. baseline and differential.
Genevestigatori Q9JMH6.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view ]
Pfami PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01438. TGR. 1 hit.
PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of mouse thioredoxin reductases."
    Kawai H., Ota T., Suzuki F., Tatsuka M.
    Gene 242:321-330(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
    Tissue: Thymus.
  2. "Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing."
    Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 276:3106-3114(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J and DBA/2.
    Tissue: Embryo.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  5. "Genomic organisation and alternative splicing of mouse and human thioredoxin reductase 1 genes."
    Osborne S.A., Tonissen K.F.
    BMC Genomics 2:10-10(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    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.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTRXR1_MOUSE
AccessioniPrimary (citable) accession number: Q9JMH6
Secondary accession number(s): Q3UEB7
, Q3UK84, Q8CI31, Q99P49, Q9CSV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: February 26, 2008
Last modified: October 29, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3