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Protein

Thioredoxin domain-containing protein 17

Gene

TXNDC17

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

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-disulfide reductase activity Source: UniProtKB

GO - Biological processi

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

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: UniProtKB
Complete GO annotation...

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

BgeeiQ9BRA2.
CleanExiHS_TXNDC17.
ExpressionAtlasiQ9BRA2. baseline and differential.
GenevestigatoriQ9BRA2.

Organism-specific databases

HPAiHPA022931.

Interactioni

Subunit structurei

Interacts with TRXR1 and DYNLL1/DNCL1.1 Publication

Protein-protein interaction databases

BioGridi124277. 27 interactions.
STRINGi9606.ENSP00000250101.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000012195.
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

        10         20         30         40         50
MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE
60 70 80 90 100
PVVREGLKHI SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG
110 120
TPQKLVESEC LQANLVEMLF SED
Length:123
Mass (Da):13,941
Last modified:June 1, 2001 - v1
Checksum:i887ADB4704946B86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi124277. 27 interactions.
STRINGi9606.ENSP00000250101.

PTM databases

PhosphoSiteiQ9BRA2.

Polymorphism databases

DMDMi74732856.

2D gel databases

REPRODUCTION-2DPAGEIPI00646689.

Proteomic databases

MaxQBiQ9BRA2.
PaxDbiQ9BRA2.
PRIDEiQ9BRA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi84817.
GeneCardsiGC17P006486.
HGNCiHGNC:28218. TXNDC17.
HPAiHPA022931.
neXtProtiNX_Q9BRA2.
PharmGKBiPA162407489.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285127.
GeneTreeiENSGT00390000012195.
HOGENOMiHOG000241811.
HOVERGENiHBG079628.
InParanoidiQ9BRA2.
OMAiSGFEEFN.
OrthoDBiEOG70CR8Q.
PhylomeDBiQ9BRA2.
TreeFamiTF313854.

Miscellaneous databases

EvolutionaryTraceiQ9BRA2.
GenomeRNAii84817.
NextBioi75010.
PROiQ9BRA2.

Gene expression databases

BgeeiQ9BRA2.
CleanExiHS_TXNDC17.
ExpressionAtlasiQ9BRA2. baseline and differential.
GenevestigatoriQ9BRA2.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.