Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BRA2 (TXD17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TXNDC17
Synonyms:TXNL5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length123 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6

Subunit structure

Interacts with TRXR1 and DYNLL1/DNCL1. Ref.6

Subcellular location

Cytoplasm Ref.5.

Tissue specificity

Ubiquitously expressed in cell lines. Ref.5

Post-translational modification

The oxidized protein is reduced by TRXR1.

Sequence similarities

Belongs to the thioredoxin family.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 123122Thioredoxin domain-containing protein 17
PRO_0000120022

Regions

Domain41 – 12383Thioredoxin

Sites

Active site431Nucleophile
Active site461Nucleophile
Site441Contributes to redox potential value
Site451Contributes to redox potential value

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Disulfide bond43 ↔ 46Redox-active Ref.9

Experimental info

Mutagenesis431C → S: Loss of peroxidase activity. Ref.5
Mutagenesis461C → S: Loss of peroxidase activity. Ref.5

Secondary structure

...................... 123
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BRA2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 887ADB4704946B86

FASTA12313,941
        10         20         30         40         50         60 
MARYEEVSVS GFEEFHRAVE QHNGKTIFAY FTGSKDAGGK SWCPDCVQAE PVVREGLKHI 

        70         80         90        100        110        120 
SEGCVFIYCQ VGEKPYWKDP NNDFRKNLKV TAVPTLLKYG TPQKLVESEC LQANLVEMLF 


SED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ344101 mRNA. Translation: CAC51435.1.
AK291963 mRNA. Translation: BAF84652.1.
CH471108 Genomic DNA. Translation: EAW90302.1.
BC006405 mRNA. Translation: AAH06405.1.
RefSeqNP_116120.1. NM_032731.3.
UniGeneHs.408236.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WOUX-ray1.80A1-123[»]
ProteinModelPortalQ9BRA2.
SMRQ9BRA2. Positions 4-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124277. 25 interactions.
STRING9606.ENSP00000250101.

PTM databases

PhosphoSiteQ9BRA2.

Polymorphism databases

DMDM74732856.

2D gel databases

REPRODUCTION-2DPAGEIPI00646689.

Proteomic databases

PaxDbQ9BRA2.
PRIDEQ9BRA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250101; ENSP00000250101; ENSG00000129235.
GeneID84817.
KEGGhsa:84817.
UCSCuc002gdf.4. human.

Organism-specific databases

CTD84817.
GeneCardsGC17P006486.
HGNCHGNC:28218. TXNDC17.
HPAHPA022931.
neXtProtNX_Q9BRA2.
PharmGKBPA162407489.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285127.
HOGENOMHOG000241811.
HOVERGENHBG079628.
InParanoidQ9BRA2.
OMASGFEEFN.
OrthoDBEOG70CR8Q.
PhylomeDBQ9BRA2.
TreeFamTF313854.

Gene expression databases

ArrayExpressQ9BRA2.
BgeeQ9BRA2.
CleanExHS_TXNDC17.
GenevestigatorQ9BRA2.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR010357. DUF953_thioredox.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR12452. PTHR12452. 1 hit.
PfamPF06110. DUF953. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9BRA2.
GenomeRNAi84817.
NextBio75010.
PROQ9BRA2.

Entry information

Entry nameTXD17_HUMAN
AccessionPrimary (citable) accession number: Q9BRA2
Secondary accession number(s): A8K7E8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM