Q9BRA2 (TXD17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TXNDC17
Synonyms:	TXNL5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	123 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	tumor necrosis factor-mediated signaling pathway Inferred from mutant phenotype Ref.5. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	electron carrier activity Inferred from direct assay Ref.10. Source: UniProtKB peroxidase activity Inferred from direct assay Ref.5. Source: UniProtKB protein binding Inferred from physical interaction Ref.5. Source: UniProtKB protein-disulfide reductase activity Inferred from direct assay Ref.5Ref.10. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 123

122

Thioredoxin domain-containing protein 17

PRO_0000120022

Regions

Domain

41 – 123

83

Thioredoxin

Sites

Active site

43

1

Nucleophile

Active site

46

1

Nucleophile

Site

44

1

Contributes to redox potential value

Site

45

1

Contributes to redox potential value

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

78

1

N6-acetyllysine Ref.8

Disulfide bond

43 ↔ 46

Redox-active Ref.10

Experimental info

Mutagenesis

43

1

C → S: Loss of peroxidase activity. Ref.5

Mutagenesis

46

1

C → S: Loss of peroxidase activity. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

123

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Helix

12 – 20

9

Turn

21 – 24

4

Beta strand

25 – 32

8

Helix

44 – 56

13

Helix

57 – 59

3

Beta strand

64 – 70

7

Helix

74 – 78

5

Helix

83 – 88

6

Beta strand

92 – 98

7

Beta strand

104 – 106

3

Helix

107 – 111

5

Helix

113 – 121

9

Sequences

	Sequence		Length	Mass (Da)
	Q9BRA2 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 887ADB4704946B86	FASTA	123	13,941
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 14702039] [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. , 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: 15489334] [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: 14607844] [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: 14607843] [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78, MASS SPECTROMETRY.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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: 15355959] [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.

IPI

IPI00646689.

RefSeq

NP_116120.1. NM_032731.3.

UniGene

Hs.408236.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WOU	X-ray	1.80	A	1-123	[»]

ProteinModelPortal

Q9BRA2.

SMR

Q9BRA2. Positions 4-122.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9BRA2.

PTM databases

PhosphoSite

Q9BRA2.

Polymorphism databases

DMDM

74732856.

2D gel databases

REPRODUCTION-2DPAGE

IPI00646689.

Proteomic databases

PRIDE

Q9BRA2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000250101; ENSP00000250101; ENSG00000129235.

GeneID

84817.

KEGG

hsa:84817.

UCSC

uc002gdf.2. human.

Organism-specific databases

CTD

84817.

GeneCards

GC17P006486.

H-InvDB

HIX0013479.

HGNC

HGNC:28218. TXNDC17.

HPA

HPA022931.

neXtProt

NX_Q9BRA2.

PharmGKB

PA162407489.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000012195.

HOGENOM

HBG381944.

HOVERGEN

HBG079628.

InParanoid

Q9BRA2.

OMA

SGFEEFN.

OrthoDB

EOG44F6BG.

PhylomeDB

Q9BRA2.

Gene expression databases

ArrayExpress

Q9BRA2.

Bgee

Q9BRA2.

CleanEx

HS_TXNDC17.

Genevestigator

Q9BRA2.

GermOnline

ENSG00000129235. Homo sapiens.

Family and domain databases

InterPro

IPR010357. DUF953_thioredox.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR12452. DUF953_thioredox. 1 hit.

Pfam

PF06110. DUF953. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00194. THIOREDOXIN_1. False negative.
PS51352. THIOREDOXIN_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

75010.

Entry information

Entry name

TXD17_HUMAN

Accession

Primary (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:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.