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Q9BRA2

- TXD17_HUMAN

UniProt

Q9BRA2 - TXD17_HUMAN

Protein

Thioredoxin domain-containing protein 17

Gene

TXNDC17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei43 – 431Nucleophile
    Sitei44 – 441Contributes to redox potential value
    Sitei45 – 451Contributes to redox potential value
    Active sitei46 – 461Nucleophile

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. peroxidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein-disulfide reductase activity Source: UniProtKB

    GO - Biological processi

    1. oxidation-reduction process Source: GOC
    2. tumor necrosis factor-mediated signaling pathway Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin domain-containing protein 17
    Alternative name(s):
    14 kDa thioredoxin-related protein
    Short name:
    TRP14
    Protein 42-9-9
    Thioredoxin-like protein 5
    Gene namesi
    Name:TXNDC17
    Synonyms:TXNL5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:28218. TXNDC17.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431C → S: Loss of peroxidase activity. 1 Publication
    Mutagenesisi46 – 461C → S: Loss of peroxidase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162407489.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 123122Thioredoxin domain-containing protein 17PRO_0000120022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Disulfide bondi43 ↔ 46Redox-active1 Publication

    Post-translational modificationi

    The oxidized protein is reduced by TRXR1.

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiQ9BRA2.
    PaxDbiQ9BRA2.
    PRIDEiQ9BRA2.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00646689.

    PTM databases

    PhosphoSiteiQ9BRA2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in cell lines.1 Publication

    Gene expression databases

    ArrayExpressiQ9BRA2.
    BgeeiQ9BRA2.
    CleanExiHS_TXNDC17.
    GenevestigatoriQ9BRA2.

    Organism-specific databases

    HPAiHPA022931.

    Interactioni

    Subunit structurei

    Interacts with TRXR1 and DYNLL1/DNCL1.1 Publication

    Protein-protein interaction databases

    BioGridi124277. 25 interactions.
    STRINGi9606.ENSP00000250101.

    Structurei

    Secondary structure

    1
    123
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Helixi12 – 209
    Turni21 – 244
    Beta strandi25 – 328
    Helixi44 – 5613
    Helixi57 – 593
    Beta strandi64 – 707
    Helixi74 – 785
    Helixi83 – 886
    Beta strandi92 – 987
    Beta strandi104 – 1063
    Helixi107 – 1115
    Helixi113 – 1219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WOUX-ray1.80A1-123[»]
    ProteinModelPortaliQ9BRA2.
    SMRiQ9BRA2. Positions 4-122.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BRA2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 12383ThioredoxinAdd
    BLAST

    Sequence similaritiesi

    Belongs to the thioredoxin family.Curated
    Contains 1 thioredoxin domain.Curated

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiNOG285127.
    HOGENOMiHOG000241811.
    HOVERGENiHBG079628.
    InParanoidiQ9BRA2.
    OMAiSGFEEFN.
    OrthoDBiEOG70CR8Q.
    PhylomeDBiQ9BRA2.
    TreeFamiTF313854.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR010357. DUF953_thioredox.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PANTHERiPTHR12452. PTHR12452. 1 hit.
    PfamiPF06110. DUF953. 1 hit.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9BRA2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE    50
    PVVREGLKHI SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG 100
    TPQKLVESEC LQANLVEMLF SED 123
    Length:123
    Mass (Da):13,941
    Last modified:June 1, 2001 - v1
    Checksum:i887ADB4704946B86
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ344101 mRNA. Translation: CAC51435.1.
    AK291963 mRNA. Translation: BAF84652.1.
    CH471108 Genomic DNA. Translation: EAW90302.1.
    BC006405 mRNA. Translation: AAH06405.1.
    CCDSiCCDS11077.1.
    RefSeqiNP_116120.1. NM_032731.3.
    UniGeneiHs.408236.

    Genome annotation databases

    EnsembliENST00000250101; ENSP00000250101; ENSG00000129235.
    GeneIDi84817.
    KEGGihsa:84817.
    UCSCiuc002gdf.4. human.

    Polymorphism databases

    DMDMi74732856.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ344101 mRNA. Translation: CAC51435.1 .
    AK291963 mRNA. Translation: BAF84652.1 .
    CH471108 Genomic DNA. Translation: EAW90302.1 .
    BC006405 mRNA. Translation: AAH06405.1 .
    CCDSi CCDS11077.1.
    RefSeqi NP_116120.1. NM_032731.3.
    UniGenei Hs.408236.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WOU X-ray 1.80 A 1-123 [» ]
    ProteinModelPortali Q9BRA2.
    SMRi Q9BRA2. Positions 4-122.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124277. 25 interactions.
    STRINGi 9606.ENSP00000250101.

    PTM databases

    PhosphoSitei Q9BRA2.

    Polymorphism databases

    DMDMi 74732856.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00646689.

    Proteomic databases

    MaxQBi Q9BRA2.
    PaxDbi Q9BRA2.
    PRIDEi Q9BRA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250101 ; ENSP00000250101 ; ENSG00000129235 .
    GeneIDi 84817.
    KEGGi hsa:84817.
    UCSCi uc002gdf.4. human.

    Organism-specific databases

    CTDi 84817.
    GeneCardsi GC17P006486.
    HGNCi HGNC:28218. TXNDC17.
    HPAi HPA022931.
    neXtProti NX_Q9BRA2.
    PharmGKBi PA162407489.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285127.
    HOGENOMi HOG000241811.
    HOVERGENi HBG079628.
    InParanoidi Q9BRA2.
    OMAi SGFEEFN.
    OrthoDBi EOG70CR8Q.
    PhylomeDBi Q9BRA2.
    TreeFami TF313854.

    Miscellaneous databases

    EvolutionaryTracei Q9BRA2.
    GenomeRNAii 84817.
    NextBioi 75010.
    PROi Q9BRA2.

    Gene expression databases

    ArrayExpressi Q9BRA2.
    Bgeei Q9BRA2.
    CleanExi HS_TXNDC17.
    Genevestigatori Q9BRA2.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR010357. DUF953_thioredox.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    PANTHERi PTHR12452. PTHR12452. 1 hit.
    Pfami PF06110. DUF953. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Schmidt T.
      Thesis (2001), University of Goettingen, Germany
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Umbilical vein endothelial cell.
    2. "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].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Skin.
    5. "Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function."
      Jeong W., Yoon H.W., Lee S.-R., Rhee S.G.
      J. Biol. Chem. 279:3142-3150(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-58, FUNCTION, MUTAGENESIS OF CYS-43 AND CYS-46, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways."
      Jeong W., Chang T.-S., Boja E.S., Fales H.M., Rhee S.G.
      J. Biol. Chem. 279:3151-3159(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DYNLL1.
    7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Structural basis of cellular redox regulation by human TRP14."
      Woo J.R., Kim S.J., Jeong W., Cho Y.H., Lee S.C., Chung Y.J., Rhee S.G., Ryu S.E.
      J. Biol. Chem. 279:48120-48125(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BOND.

    Entry informationi

    Entry nameiTXD17_HUMAN
    AccessioniPrimary (citable) accession number: Q9BRA2
    Secondary accession number(s): A8K7E8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3