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Q16881

- TRXR1_HUMAN

UniProt

Q16881 - TRXR1_HUMAN

Protein

Thioredoxin reductase 1, cytoplasmic

Gene

TXNRD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei622 – 6221Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi192 – 20918FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. electron carrier activity Source: InterPro
    2. flavin adenine dinucleotide binding Source: InterPro
    3. NADP binding Source: InterPro
    4. protein binding Source: IntAct
    5. protein disulfide oxidoreductase activity Source: InterPro
    6. thioredoxin-disulfide reductase activity Source: Reactome

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. cell redox homeostasis Source: InterPro
    3. cellular lipid metabolic process Source: Reactome
    4. mesoderm formation Source: Ensembl
    5. nucleobase-containing small molecule interconversion Source: Reactome
    6. nucleobase-containing small molecule metabolic process Source: Reactome
    7. signal transduction Source: ProtInc
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin reductase 1, cytoplasmic (EC:1.8.1.9)
    Short name:
    TR
    Alternative name(s):
    Gene associated with retinoic and interferon-induced mortality 12 protein
    Short name:
    GRIM-12
    Short name:
    Gene associated with retinoic and IFN-induced mortality 12 protein
    KM-102-derived reductase-like factor
    Thioredoxin reductase TR1
    Gene namesi
    Name:TXNRD1
    Synonyms:GRIM12, KDRF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12437. TXNRD1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl
    3. nucleolus Source: HPA
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37093.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 649649Thioredoxin reductase 1, cytoplasmicPRO_0000030286Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi209 ↔ 214Redox-activeBy similarity
    Modified residuei218 – 2181N6-succinyllysineBy similarity
    Modified residuei281 – 2811Phosphotyrosine1 Publication
    Cross-linki647 ↔ 648Cysteinyl-selenocysteine (Cys-Sec)By similarity

    Post-translational modificationi

    The N-terminus of isoform 5 is blocked.
    ISGylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ16881.
    PaxDbiQ16881.
    PRIDEiQ16881.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00554786.

    PTM databases

    PhosphoSiteiQ16881.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Inductioni

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ16881.
    BgeeiQ16881.
    GenevestigatoriQ16881.

    Organism-specific databases

    HPAiCAB004607.
    CAB015834.
    HPA001395.
    HPA043871.

    Interactioni

    Subunit structurei

    Homodimer. Isoform 4 interacts with ESR1 and ESR2. Interacts with HERC5.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAV1Q031354EBI-716617,EBI-603614
    ESR1P033724EBI-9080335,EBI-78473
    ESR2Q927313EBI-9080335,EBI-78505

    Protein-protein interaction databases

    BioGridi113147. 31 interactions.
    IntActiQ16881. 9 interactions.
    MINTiMINT-1525880.

    Structurei

    Secondary structure

    1
    649
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi162 – 1687
    Helixi172 – 18312
    Beta strandi188 – 1914
    Helixi208 – 2125
    Helixi214 – 23320
    Turni234 – 2374
    Helixi248 – 27225
    Beta strandi276 – 2783
    Beta strandi280 – 2867
    Beta strandi289 – 2935
    Beta strandi295 – 2973
    Beta strandi301 – 3099
    Beta strandi313 – 3153
    Helixi323 – 3264
    Helixi330 – 3334
    Beta strandi342 – 3465
    Helixi350 – 36112
    Beta strandi366 – 3727
    Turni374 – 3774
    Helixi380 – 39213
    Beta strandi396 – 41015
    Beta strandi412 – 4143
    Beta strandi416 – 42712
    Beta strandi429 – 43911
    Beta strandi443 – 4464
    Beta strandi448 – 4503
    Turni453 – 4564
    Turni461 – 4633
    Beta strandi479 – 4813
    Helixi483 – 4853
    Beta strandi486 – 4894
    Helixi493 – 50816
    Beta strandi522 – 5243
    Beta strandi526 – 5283
    Beta strandi530 – 5345
    Helixi537 – 5448
    Helixi546 – 5483
    Beta strandi549 – 5568
    Helixi559 – 5624
    Turni563 – 5653
    Turni568 – 5703
    Beta strandi571 – 5788
    Turni579 – 5824
    Beta strandi584 – 5929
    Helixi595 – 60713
    Helixi612 – 6176
    Helixi625 – 6317
    Turni636 – 6394

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W1Cmodel-A/B161-649[»]
    2CFYX-ray2.70A/B/C/D/E/F151-647[»]
    2J3NX-ray2.80A/B/C/D/E/F151-647[»]
    2ZZ0X-ray2.80A/B/C/D150-647[»]
    2ZZBX-ray3.20A/B/C/D150-647[»]
    2ZZCX-ray2.60A/B/C/D150-647[»]
    3QFAX-ray2.20A/B151-649[»]
    3QFBX-ray2.60A/B151-649[»]
    ProteinModelPortaliQ16881.
    SMRiQ16881. Positions 59-644.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16881.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 156101GlutaredoxinPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    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.1 Publication

    Sequence similaritiesi

    Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOVERGENiHBG004959.
    InParanoidiQ16881.
    KOiK00384.
    OMAiILQAGCX.
    OrthoDBiEOG779NXG.
    PhylomeDBiQ16881.
    TreeFamiTF314782.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR002109. Glutaredoxin.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR012336. Thioredoxin-like_fold.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view]
    PfamiPF00462. Glutaredoxin. 1 hit.
    PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01438. TGR. 1 hit.
    PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
    PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16881-1) [UniParc]FASTAAdd to Basket

    Also known as: V, TXNRD1_v3

    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

    MGCAEGKAVA AAAPTELQTK GKNGDGRRRS AKDHHPGKTL PENPAGFTST    50
    ATADSRALLQ AYIDGHSVVI FSRSTCTRCT EVKKLFKSLC VPYFVLELDQ 100
    TEDGRALEGT LSELAAETDL PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK 150
    MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE AAQYGKKVMV LDFVTPTPLG 200
    TRWGLGGTCV NVGCIPKKLM HQAALLGQAL QDSRNYGWKV EETVKHDWDR 250
    MIEAVQNHIG SLNWGYRVAL REKKVVYENA YGQFIGPHRI KATNNKGKEK 300
    IYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY 350
    VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ 400
    FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVMLA IGRDACTRKI 450
    GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG 500
    RLLAQRLYAG STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE 550
    VYHSYFWPLE WTIPSRDNNK CYAKIICNTK DNERVVGFHV LGPNAGEVTQ 600
    GFAAALKCGL TKKQLDSTIG IHPVCAEVFT TLSVTKRSGA SILQAGCUG 649

    Note: Minor isoform.

    Length:649
    Mass (Da):70,906
    Last modified:February 26, 2008 - v3
    Checksum:i5A51C3F77EB03EFE
    GO
    Isoform 2 (identifier: Q16881-2) [UniParc]FASTAAdd to Basket

    Also known as: II, TXNRD1_v4

    The sequence of this isoform differs from the canonical sequence as follows:
         1-106: Missing.
         107-138: LEGTLSELAAETDLPVVFVKQRKIGGHGPTLK → MLSRLVLNSWAQAIIRPRPPKVLGLQVTTFSE

    Show »
    Length:543
    Mass (Da):59,787
    Checksum:i990DB8D334659B4D
    GO
    Isoform 3 (identifier: Q16881-3) [UniParc]FASTAAdd to Basket

    Also known as: III, TXNRD1_v5

    The sequence of this isoform differs from the canonical sequence as follows:
         1-51: Missing.
         52-100: TADSRALLQA...VPYFVLELDQ → MQQVMLTCKG...LTRSALLLCH

    Show »
    Length:598
    Mass (Da):65,567
    Checksum:i81F496F5BB85A49E
    GO
    Isoform 4 (identifier: Q16881-4) [UniParc]FASTAAdd to Basket

    Also known as: IV, TXNRD1_v2, TrxR1b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-98: Missing.
         99-101: DQT → MSC

    Show »
    Length:551
    Mass (Da):60,419
    Checksum:iF54B034AADF51E5B
    GO
    Isoform 5 (identifier: Q16881-5) [UniParc]FASTAAdd to Basket

    Also known as: I, TXNRD1_v1, TrxR1a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-150: Missing.

    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.

    Show »
    Length:499
    Mass (Da):54,754
    Checksum:iC24BAEB4A573EABE
    GO
    Isoform 6 (identifier: Q16881-6) [UniParc]FASTAAdd to Basket

    Also known as: VI

    The sequence of this isoform differs from the canonical sequence as follows:
         1-139: MGCAEGKAVA...IGGHGPTLKA → MPVDDYWLCL...QERNVQFGLA

    Show »
    Length:614
    Mass (Da):67,266
    Checksum:i9C635E1C6EA94934
    GO
    Isoform 7 (identifier: Q16881-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-188: Missing.

    Note: No experimental confirmation.

    Show »
    Length:461
    Mass (Da):50,873
    Checksum:i07D3A620A6BD82EA
    GO

    Sequence cautioni

    The sequence AAB35418.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence AAC69621.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence AAF15900.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence AAV38446.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence AAZ67916.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence BAA13674.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence BAH11490.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence BAH12374.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence BAH14140.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence CAA04503.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence CAA62629.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence CAG38744.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
    The sequence EAW97745.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531G → S in AAQ62473. (PubMed:14980707)Curated
    Sequence conflicti181 – 1811A → P in AAF15900. 1 PublicationCurated
    Sequence conflicti194 – 1941V → G in AAF15900. 1 PublicationCurated
    Sequence conflicti200 – 2001G → E in AAQ62469. (PubMed:14980707)Curated
    Sequence conflicti202 – 2021R → K in AAQ62463. (PubMed:14980707)Curated
    Sequence conflicti215 – 2151I → N in AAQ62463. (PubMed:14980707)Curated
    Sequence conflicti297 – 2971G → D in BAH11490. (PubMed:14702039)Curated
    Sequence conflicti306 – 3061R → S in AAB35418. (PubMed:7589432)Curated
    Sequence conflicti306 – 3061R → S in CAA62629. (PubMed:7589432)Curated
    Sequence conflicti306 – 3061R → S in AAL15432. (PubMed:14980707)Curated
    Sequence conflicti365 – 3651D → N in AAC69621. (PubMed:9774665)Curated
    Sequence conflicti437 – 4371V → A in BAH12374. (PubMed:14702039)Curated
    Sequence conflicti441 – 4411I → M in BAH12374. (PubMed:14702039)Curated
    Sequence conflicti449 – 4491K → R in CAG38744. 1 PublicationCurated
    Sequence conflicti641 – 6411S → R in AAC69621. (PubMed:9774665)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti365 – 3651D → G.2 Publications
    Corresponds to variant rs1127954 [ dbSNP | Ensembl ].
    VAR_051776

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 188188Missing in isoform 7. 1 PublicationVSP_053819Add
    BLAST
    Alternative sequencei1 – 150150Missing in isoform 5. 7 PublicationsVSP_031558Add
    BLAST
    Alternative sequencei1 – 139139MGCAE…PTLKA → MPVDDYWLCLPASCARPFVQ TVRVVQSCPHCCWFPGVLPS VPEPLRMPAMLPTGSHSAVL PPSHCSTAPPSTSQEPSSSA DPKLCLSPPTSDSRQERNVQ FGLA in isoform 6. CuratedVSP_031559Add
    BLAST
    Alternative sequencei1 – 106106Missing in isoform 2. CuratedVSP_031560Add
    BLAST
    Alternative sequencei1 – 9898Missing in isoform 4. 1 PublicationVSP_031561Add
    BLAST
    Alternative sequencei1 – 5151Missing in isoform 3. CuratedVSP_031562Add
    BLAST
    Alternative sequencei52 – 10049TADSR…LELDQ → MQQVMLTCKGVNRGHAVPAG PGRKPRPRRSSRLLAGEKHL TRSALLLCH in isoform 3. CuratedVSP_031563Add
    BLAST
    Alternative sequencei99 – 1013DQT → MSC in isoform 4. 1 PublicationVSP_031564
    Alternative sequencei107 – 13832LEGTL…GPTLK → MLSRLVLNSWAQAIIRPRPP KVLGLQVTTFSE in isoform 2. CuratedVSP_031565Add
    BLAST

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei648 – 6481Selenocysteine1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91247 mRNA. Translation: CAA62629.1. Sequence problems.
    S79851 mRNA. Translation: AAB35418.1. Sequence problems.
    D88687 mRNA. Translation: BAA13674.1. Sequence problems.
    AF077367 mRNA. Translation: AAC69621.1. Sequence problems.
    AY057105 mRNA. Translation: AAL15432.1.
    AY344081 mRNA. Translation: AAQ62461.1.
    AY344083 mRNA. Translation: AAQ62462.1.
    AY344084 mRNA. Translation: AAQ62463.1.
    AY344086 mRNA. Translation: AAQ62464.1.
    AY344087 mRNA. Translation: AAQ62465.1.
    AY344089 mRNA. Translation: AAQ62466.1.
    AY344092 mRNA. Translation: AAQ62467.1.
    AY344093 mRNA. Translation: AAQ62468.1.
    AY344095 mRNA. Translation: AAQ62469.1.
    AY344096 mRNA. Translation: AAQ62470.1.
    AY344670 mRNA. Translation: AAQ62471.1.
    AY344673 mRNA. Translation: AAQ62472.1.
    AY344679 mRNA. Translation: AAQ62473.1.
    AJ001050 mRNA. Translation: CAA04503.1. Sequence problems.
    AF208018 mRNA. Translation: AAF15900.1. Sequence problems.
    AK293322 mRNA. Translation: BAH11490.1. Sequence problems.
    AK296495 mRNA. Translation: BAH12374.1. Sequence problems.
    AK304241 mRNA. Translation: BAH14140.1. Sequence problems.
    CR536506 mRNA. Translation: CAG38744.1. Sequence problems.
    BT019640 mRNA. Translation: AAV38446.1. Sequence problems.
    DQ157758 Genomic DNA. Translation: AAZ67916.1. Sequence problems.
    AC089983 Genomic DNA. No translation available.
    AC090107 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97745.1. Sequence problems.
    BC018122 mRNA. Translation: AAH18122.2.
    CCDSiCCDS53820.1. [Q16881-1]
    CCDS53821.1. [Q16881-4]
    CCDS53823.1. [Q16881-5]
    CCDS58274.1. [Q16881-7]
    PIRiS66677.
    RefSeqiNP_001087240.1. NM_001093771.2. [Q16881-1]
    NP_001248374.1. NM_001261445.1.
    NP_001248375.1. NM_001261446.1. [Q16881-7]
    NP_003321.3. NM_003330.3. [Q16881-4]
    NP_877393.1. NM_182729.2. [Q16881-5]
    NP_877419.1. NM_182742.2. [Q16881-5]
    NP_877420.1. NM_182743.2. [Q16881-5]
    UniGeneiHs.654922.

    Genome annotation databases

    GeneIDi7296.
    KEGGihsa:7296.
    UCSCiuc010swp.3. human. [Q16881-1]
    uc021rcy.2. human. [Q16881-4]

    Polymorphism databases

    DMDMi172046253.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, Selenocysteine

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91247 mRNA. Translation: CAA62629.1 . Sequence problems.
    S79851 mRNA. Translation: AAB35418.1 . Sequence problems.
    D88687 mRNA. Translation: BAA13674.1 . Sequence problems.
    AF077367 mRNA. Translation: AAC69621.1 . Sequence problems.
    AY057105 mRNA. Translation: AAL15432.1 .
    AY344081 mRNA. Translation: AAQ62461.1 .
    AY344083 mRNA. Translation: AAQ62462.1 .
    AY344084 mRNA. Translation: AAQ62463.1 .
    AY344086 mRNA. Translation: AAQ62464.1 .
    AY344087 mRNA. Translation: AAQ62465.1 .
    AY344089 mRNA. Translation: AAQ62466.1 .
    AY344092 mRNA. Translation: AAQ62467.1 .
    AY344093 mRNA. Translation: AAQ62468.1 .
    AY344095 mRNA. Translation: AAQ62469.1 .
    AY344096 mRNA. Translation: AAQ62470.1 .
    AY344670 mRNA. Translation: AAQ62471.1 .
    AY344673 mRNA. Translation: AAQ62472.1 .
    AY344679 mRNA. Translation: AAQ62473.1 .
    AJ001050 mRNA. Translation: CAA04503.1 . Sequence problems.
    AF208018 mRNA. Translation: AAF15900.1 . Sequence problems.
    AK293322 mRNA. Translation: BAH11490.1 . Sequence problems.
    AK296495 mRNA. Translation: BAH12374.1 . Sequence problems.
    AK304241 mRNA. Translation: BAH14140.1 . Sequence problems.
    CR536506 mRNA. Translation: CAG38744.1 . Sequence problems.
    BT019640 mRNA. Translation: AAV38446.1 . Sequence problems.
    DQ157758 Genomic DNA. Translation: AAZ67916.1 . Sequence problems.
    AC089983 Genomic DNA. No translation available.
    AC090107 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97745.1 . Sequence problems.
    BC018122 mRNA. Translation: AAH18122.2 .
    CCDSi CCDS53820.1. [Q16881-1 ]
    CCDS53821.1. [Q16881-4 ]
    CCDS53823.1. [Q16881-5 ]
    CCDS58274.1. [Q16881-7 ]
    PIRi S66677.
    RefSeqi NP_001087240.1. NM_001093771.2. [Q16881-1 ]
    NP_001248374.1. NM_001261445.1.
    NP_001248375.1. NM_001261446.1. [Q16881-7 ]
    NP_003321.3. NM_003330.3. [Q16881-4 ]
    NP_877393.1. NM_182729.2. [Q16881-5 ]
    NP_877419.1. NM_182742.2. [Q16881-5 ]
    NP_877420.1. NM_182743.2. [Q16881-5 ]
    UniGenei Hs.654922.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W1C model - A/B 161-649 [» ]
    2CFY X-ray 2.70 A/B/C/D/E/F 151-647 [» ]
    2J3N X-ray 2.80 A/B/C/D/E/F 151-647 [» ]
    2ZZ0 X-ray 2.80 A/B/C/D 150-647 [» ]
    2ZZB X-ray 3.20 A/B/C/D 150-647 [» ]
    2ZZC X-ray 2.60 A/B/C/D 150-647 [» ]
    3QFA X-ray 2.20 A/B 151-649 [» ]
    3QFB X-ray 2.60 A/B 151-649 [» ]
    ProteinModelPortali Q16881.
    SMRi Q16881. Positions 59-644.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113147. 31 interactions.
    IntActi Q16881. 9 interactions.
    MINTi MINT-1525880.

    Chemistry

    BindingDBi Q16881.
    ChEMBLi CHEMBL2096978.

    PTM databases

    PhosphoSitei Q16881.

    Polymorphism databases

    DMDMi 172046253.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00554786.

    Proteomic databases

    MaxQBi Q16881.
    PaxDbi Q16881.
    PRIDEi Q16881.

    Protocols and materials databases

    DNASUi 7296.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 7296.
    KEGGi hsa:7296.
    UCSCi uc010swp.3. human. [Q16881-1 ]
    uc021rcy.2. human. [Q16881-4 ]

    Organism-specific databases

    CTDi 7296.
    GeneCardsi GC12P104609.
    H-InvDB HIX0010939.
    HGNCi HGNC:12437. TXNRD1.
    HPAi CAB004607.
    CAB015834.
    HPA001395.
    HPA043871.
    MIMi 601112. gene.
    neXtProti NX_Q16881.
    PharmGKBi PA37093.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1249.
    HOVERGENi HBG004959.
    InParanoidi Q16881.
    KOi K00384.
    OMAi ILQAGCX.
    OrthoDBi EOG779NXG.
    PhylomeDBi Q16881.
    TreeFami TF314782.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_172715. Detoxification of Reactive Oxygen Species.
    REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    ChiTaRSi TXNRD1. human.
    EvolutionaryTracei Q16881.
    GeneWikii TXNRD1.
    GenomeRNAii 7296.
    NextBioi 28527.
    PROi Q16881.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16881.
    Bgeei Q16881.
    Genevestigatori Q16881.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR002109. Glutaredoxin.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR012336. Thioredoxin-like_fold.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view ]
    Pfami PF00462. Glutaredoxin. 1 hit.
    PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01438. TGR. 1 hit.
    PROSITEi PS51354. GLUTAREDOXIN_2. 1 hit.
    PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a human thioredoxin reductase."
      Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G.
      FEBS Lett. 373:5-9(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PROTEIN SEQUENCE OF 153-161; 307-315 AND 585-607, VARIANT GLY-365.
      Tissue: Placenta.
    2. "Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102."
      Koishi R., Kawashima I., Yoshimura C., Sugawara M., Serizawa N.
      J. Biol. Chem. 272:2570-2577(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 122-127 AND 147-151, TISSUE SPECIFICITY.
      Tissue: Bone marrow stroma.
    3. "Thioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid."
      Hofman E.R., Boyanapalli M., Lindner D.J., Weihua X., Hassel B.A., Jagus R., Gutierrez P.L., Kalvakolanu D.V.
      Mol. Cell. Biol. 18:6493-6504(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INDUCTION.
      Tissue: Mammary carcinoma.
    4. "Evidence for intriguingly complex transcription of human thioredoxin reductase 1."
      Rundloef A.-K., Janard M., Miranda-Vizuete A., Arner E.S.
      Free Radic. Biol. Med. 36:641-656(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), VARIANT GLY-365.
      Tissue: Mammary gland, Ovary, Testis and Thymus.
    5. "Identification by ddPCR of thioredoxin reductase as a vitamin D regulated gene in human osteoblasts."
      Schuetze N., Bachthaler M., Lechner A., Koehrle J., Jakob F.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    6. "Cloning and sequencing of thioredoxin reductase gene from human brain."
      Xu L., Dai R., Xu J.Y.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Brain.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
      Tissue: Astrocyte, Thalamus and Trachea.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      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.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    10. NIEHS SNPs program
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    11. "The finished DNA sequence of human chromosome 12."
      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.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION.
      Tissue: Trachea.
    13. "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 5).
      Tissue: Lung.
    14. "Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene."
      Gladyshev V.N., Jeang K.-T., Stadtman T.C.
      Proc. Natl. Acad. Sci. U.S.A. 93:6146-6151(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 307-316; 449-456; 466-476 AND 638-649, BLOCKAGE OF N-TERMINUS, SELENOCYSTEINE AT SEC-648, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity."
      Tamura T., Stadtman T.C.
      Proc. Natl. Acad. Sci. U.S.A. 93:1006-1011(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, CHARACTERIZATION, PRESENCE OF SELENOCYSTEINE.
    16. "Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1."
      Su D., Gladyshev V.N.
      Biochemistry 43:12177-12188(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6), DOMAIN.
    17. "An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling."
      Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A., Spyrou G.
      J. Biol. Chem. 279:38721-38729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR1 AND ESR2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY (ISOFORM 4).
    18. "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-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
      Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
      Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HERC5, ISGYLATION.
    20. "Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1."
      Dammeyer P., Damdimopoulos A.E., Nordman T., Jimenez A., Miranda-Vizuete A., Arner E.S.J.
      J. Biol. Chem. 283:2814-2821(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION (ISOFORM 1).
    21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis."
      Fritz-Wolf K., Urig S., Becker K.
      J. Mol. Biol. 370:116-127(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) (ISOFORM 5).

    Entry informationi

    Entry nameiTRXR1_HUMAN
    AccessioniPrimary (citable) accession number: Q16881
    Secondary accession number(s): B7Z1F4
    , B7Z3Y8, B7Z904, E9PMY9, F5H780, Q6FI31, Q6VB40, Q6VB41, Q6VB42, Q6VBP2, Q6VBP3, Q6VBP4, Q6VBP5, Q6VBP9, Q6VBQ0, Q6YNQ1, Q76P53, Q7LA96, Q8WVC8, Q99475, Q9UES8, Q9UH79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 170 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 thioredoxin reductase active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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