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Q9NNW7

- TRXR2_HUMAN

UniProt

Q9NNW7 - TRXR2_HUMAN

Protein

Thioredoxin reductase 2, mitochondrial

Gene

TXNRD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.

    Catalytic activityi

    Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

    Cofactori

    FAD.CuratedUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei497 – 4971Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi41 – 7030FADBy similarityAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. heart development Source: Ensembl
    3. hemopoiesis Source: Ensembl
    4. response to oxygen radical Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_172715. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin reductase 2, mitochondrial (EC:1.8.1.9)
    Alternative name(s):
    Selenoprotein Z
    Short name:
    SelZ
    TR-beta
    Thioredoxin reductase TR3
    Gene namesi
    Name:TXNRD2
    Synonyms:KIAA1652, TRXR2
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:18155. TXNRD2.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti154. Familial isolated dilated cardiomyopathy.
    PharmGKBiPA38302.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
    BLAST
    Chaini37 – 524488Thioredoxin reductase 2, mitochondrialPRO_0000030288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi86 ↔ 91Redox-activeBy similarity
    Modified residuei175 – 1751N6-succinyllysineBy similarity
    Modified residuei329 – 3291N6-succinyllysineBy similarity
    Cross-linki522 ↔ 523Cysteinyl-selenocysteine (Cys-Sec)By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ9NNW7.
    PaxDbiQ9NNW7.
    PRIDEiQ9NNW7.

    PTM databases

    PhosphoSiteiQ9NNW7.

    Expressioni

    Tissue specificityi

    Highly expressed in the prostate, ovary, liver, testis, uterus, colon and small intestine. Intermediate levels in brain, skeletal muscle, heart and spleen. Low levels in placenta, pancreas, thymus and peripheral blood leukocytes. According to PubMed:10608886, high levels in kidney, whereas according to PubMed:9923614, levels are low.3 Publications

    Gene expression databases

    ArrayExpressiQ9NNW7.
    BgeeiQ9NNW7.
    GenevestigatoriQ9NNW7.

    Organism-specific databases

    HPAiCAB002007.
    HPA003323.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi115836. 8 interactions.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W1Emodel-A/B36-524[»]
    ProteinModelPortaliQ9NNW7.
    SMRiQ9NNW7. Positions 37-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1249.
    HOVERGENiHBG004959.
    InParanoidiQ9NNW7.
    KOiK00384.
    OMAiHFTGPNA.
    PhylomeDBiQ9NNW7.
    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 (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NNW7-1) [UniParc]FASTAAdd to Basket

    Also known as: AlphaCurated

    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

    MAAMAVALRG LGGRFRWRTQ AVAGGVRGAA RGAAAGQRDY DLLVVGGGSG    50
    GLACAKEAAQ LGRKVAVVDY VEPSPQGTRW GLGGTCVNVG CIPKKLMHQA 100
    ALLGGLIQDA PNYGWEVAQP VPHDWRKMAE AVQNHVKSLN WGHRVQLQDR 150
    KVKYFNIKAS FVDEHTVCGV AKGGKEILLS ADHIIIATGG RPRYPTHIEG 200
    ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI GLDTTIMMRS 250
    IPLRGFDQQM SSMVIEHMAS HGTRFLRGCA PSRVRRLPDG QLQVTWEDST 300
    TGKEDTGTFD TVLWAIGRVP DTRSLNLEKA GVDTSPDTQK ILVDSREATS 350
    VPHIYAIGDV VEGRPELTPI AIMAGRLLVQ RLFGGSSDLM DYDNVPTTVF 400
    TPLEYGCVGL SEEEAVARHG QEHVEVYHAH YKPLEFTVAG RDASQCYVKM 450
    VCLREPPQLV LGLHFLGPNA GEVTQGFALG IKCGASYAQV MRTVGIHPTC 500
    SEEVVKLRIS KRSGLDPTVT GCUG 524
    Length:524
    Mass (Da):56,507
    Last modified:February 26, 2008 - v3
    Checksum:iB575A185A2183DAC
    GO
    Isoform 2 (identifier: Q9NNW7-2) [UniParc]FASTAAdd to Basket

    Also known as: BetaCurated

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: MAAMAVALRGLGGRFRWRTQAVAGGVRGAA → MEDQ

    Show »
    Length:498
    Mass (Da):53,970
    Checksum:i7B255499E2F1881E
    GO
    Isoform 3 (identifier: Q9NNW7-3) [UniParc]FASTAAdd to Basket

    Also known as: SelZf2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-96: Missing.

    Show »
    Length:428
    Mass (Da):46,841
    Checksum:iCA7963D57A19ADAB
    GO
    Isoform 4 (identifier: Q9NNW7-4) [UniParc]FASTAAdd to Basket

    Also known as: SelZf1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-247: Missing.

    Show »
    Length:277
    Mass (Da):30,291
    Checksum:i80F3E412BF2738F3
    GO

    Sequence cautioni

    The sequence AAD25167.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAG47635.1 differs from that shown. Reason: Erroneous termination at position 523. Translated as Sec.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331Missing in AAG47635. 1 PublicationCurated
    Sequence conflicti285 – 2851R → K in AAG47635. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141R → L.
    Corresponds to variant rs45593642 [ dbSNP | Ensembl ].
    VAR_051777
    Natural varianti66 – 661A → S.3 Publications
    Corresponds to variant rs5748469 [ dbSNP | Ensembl ].
    VAR_051778
    Natural varianti299 – 2991S → R.
    Corresponds to variant rs5992495 [ dbSNP | Ensembl ].
    VAR_051779
    Natural varianti370 – 3701I → T.3 Publications
    Corresponds to variant rs1139793 [ dbSNP | Ensembl ].
    VAR_051780

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 247247Missing in isoform 4. 1 PublicationVSP_008306Add
    BLAST
    Alternative sequencei1 – 9696Missing in isoform 3. 1 PublicationVSP_008305Add
    BLAST
    Alternative sequencei1 – 3030MAAMA…VRGAA → MEDQ in isoform 2. CuratedVSP_008304Add
    BLAST

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei523 – 5231Selenocysteine

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171054 mRNA. Translation: AAD51324.1.
    AF106697 mRNA. Translation: AAD19597.1.
    AF044212 mRNA. Translation: AAD25167.1. Different initiation.
    AB019694 mRNA. Translation: BAA77601.2.
    AB019695 mRNA. Translation: BAA77602.2.
    AF166126 mRNA. Translation: AAF21431.1.
    AF166127 mRNA. Translation: AAF21432.1.
    AF201385 mRNA. Translation: AAG47635.1. Sequence problems.
    AC000078 Genomic DNA. No translation available.
    AC000080 Genomic DNA. No translation available.
    AC000090 Genomic DNA. No translation available.
    BC007489 mRNA. Translation: AAH07489.3.
    CCDSiCCDS42981.1. [Q9NNW7-1]
    RefSeqiNP_001269441.1. NM_001282512.1.
    NP_006431.2. NM_006440.4. [Q9NNW7-1]
    UniGeneiHs.443430.

    Genome annotation databases

    EnsembliENST00000400521; ENSP00000383365; ENSG00000184470. [Q9NNW7-1]
    GeneIDi10587.
    KEGGihsa:10587.
    UCSCiuc002zqq.1. human. [Q9NNW7-4]
    uc021wlj.1. human. [Q9NNW7-1]

    Polymorphism databases

    DMDMi182705230.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, Selenocysteine

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171054 mRNA. Translation: AAD51324.1 .
    AF106697 mRNA. Translation: AAD19597.1 .
    AF044212 mRNA. Translation: AAD25167.1 . Different initiation.
    AB019694 mRNA. Translation: BAA77601.2 .
    AB019695 mRNA. Translation: BAA77602.2 .
    AF166126 mRNA. Translation: AAF21431.1 .
    AF166127 mRNA. Translation: AAF21432.1 .
    AF201385 mRNA. Translation: AAG47635.1 . Sequence problems.
    AC000078 Genomic DNA. No translation available.
    AC000080 Genomic DNA. No translation available.
    AC000090 Genomic DNA. No translation available.
    BC007489 mRNA. Translation: AAH07489.3 .
    CCDSi CCDS42981.1. [Q9NNW7-1 ]
    RefSeqi NP_001269441.1. NM_001282512.1.
    NP_006431.2. NM_006440.4. [Q9NNW7-1 ]
    UniGenei Hs.443430.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W1E model - A/B 36-524 [» ]
    ProteinModelPortali Q9NNW7.
    SMRi Q9NNW7. Positions 37-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115836. 8 interactions.

    Chemistry

    BindingDBi Q9NNW7.
    ChEMBLi CHEMBL2403.

    PTM databases

    PhosphoSitei Q9NNW7.

    Polymorphism databases

    DMDMi 182705230.

    Proteomic databases

    MaxQBi Q9NNW7.
    PaxDbi Q9NNW7.
    PRIDEi Q9NNW7.

    Protocols and materials databases

    DNASUi 10587.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000400521 ; ENSP00000383365 ; ENSG00000184470 . [Q9NNW7-1 ]
    GeneIDi 10587.
    KEGGi hsa:10587.
    UCSCi uc002zqq.1. human. [Q9NNW7-4 ]
    uc021wlj.1. human. [Q9NNW7-1 ]

    Organism-specific databases

    CTDi 10587.
    GeneCardsi GC22M019863.
    H-InvDB HIX0016244.
    HGNCi HGNC:18155. TXNRD2.
    HPAi CAB002007.
    HPA003323.
    MIMi 606448. gene.
    neXtProti NX_Q9NNW7.
    Orphaneti 154. Familial isolated dilated cardiomyopathy.
    PharmGKBi PA38302.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1249.
    HOVERGENi HBG004959.
    InParanoidi Q9NNW7.
    KOi K00384.
    OMAi HFTGPNA.
    PhylomeDBi Q9NNW7.
    TreeFami TF314782.

    Enzyme and pathway databases

    Reactomei REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi TXNRD2. human.
    GenomeRNAii 10587.
    NextBioi 40203.
    PROi Q9NNW7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NNW7.
    Bgeei Q9NNW7.
    Genevestigatori Q9NNW7.

    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

    1. "Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases."
      Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 274:24522-24530(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning, sequencing and functional expression of a novel human thioredoxin reductase."
      Gasdaska P.Y., Berggren M.M., Berry M.J., Powis G.
      FEBS Lett. 442:105-111(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-66.
      Tissue: Fetal heart and Placenta.
    3. "Human mitochondrial thioredoxin reductase: cDNA cloning, expression and genomic organization."
      Miranda-Vizuete A., Damdimopoulos A.E., Pedrajas J.R., Gustafsson J.-A., Spyrou G.
      Eur. J. Biochem. 261:405-412(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Adrenal gland and Testis.
    4. Toji S., Yano M., Tamai K.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), VARIANT THR-370.
    5. "Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif."
      Lescure A., Gautheret D., Carbon P., Krol A.
      J. Biol. Chem. 274:38147-38154(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, VARIANT THR-370.
      Tissue: Cervix carcinoma.
    6. Kim J.-R., Lee Y.H., Lee S.-R., Kim B.H., Rhee S.G., Kim J.H.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), VARIANTS SER-66 AND THR-370.
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] OF 40-524, VARIANT SER-66.
      Tissue: Skin.
    9. "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: ALTERNATIVE SPLICING.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTRXR2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NNW7
    Secondary accession number(s): O95840
    , Q96IJ2, Q9H2Z5, Q9NZV3, Q9NZV4, Q9P2Y0, Q9P2Y1, Q9UQU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3