Reviewed, UniProtKB/Swiss-Prot P10599 (THIO_HUMAN)

Names and origin

Protein names

Recommended name:
    Thioredoxin
      Short name=Trx
Alternative name(s):
    ATL-derived factor
      Short name=ADF
    Surface-associated sulphydryl protein
      Short name=SASP

Gene names

Name:	TXN
Synonyms:	TRDX, TRX, TRX1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	105 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	Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Ref.16 Ref.18 Ref.21 ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55). Ref.16 Ref.18 Ref.21
Subunit structure	Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. Ref.17 Ref.31 Ref.32
Subcellular location	Cytoplasm.
Post-translational modification	In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins.
Sequence similarities	Belongs to the thioredoxin family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Acetylation Disulfide bond Phosphoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell proliferation Ref.1 Traceable author statement. Source: ProtInc cell redox homeostasis Inferred from electronic annotation. Source: InterPro cell-cell signaling Traceable author statement. Source: ProtInc cellular component movement Traceable author statement. Source: ProtInc electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Traceable author statement. Source: ProtInc transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COPS5	Q92905	5	EBI-594644,EBI-594661
TXNIP	Q9H3M7	2	EBI-594644,EBI-1369170

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.14

Chain

2 – 105

104

Thioredoxin

PRO_0000120005

Regions

Domain

2 – 105

104

Thioredoxin

Sites

Active site

32

1

Nucleophile

Active site

35

1

Nucleophile

Site

26

1

Deprotonates C-terminal active site Cys

Site

33

1

Contributes to redox potential value

Site

34

1

Contributes to redox potential value

Amino acid modifications

Modified residue

3

1

N6-acetyllysine Ref.24

Modified residue

39

1

N6-acetyllysine Ref.24

Modified residue

62

1

S-nitrosocysteine Ref.32

Modified residue

69

1

S-nitrosocysteine Ref.32

Modified residue

73

1

S-nitrosocysteine; alternate Ref.18 Ref.21

Modified residue

94

1

N6-acetyllysine Ref.20

Modified residue

100

1

Phosphothreonine Ref.19

Disulfide bond

32 ↔ 35

Redox-active Ref.32 Ref.26

Disulfide bond

73

Interchain; alternate Ref.32

Experimental info

Mutagenesis

60

1

D → N: Loss of pH-dependence of dimerization.

Mutagenesis

69

1

C → S: No effect on activity and on S-nitrosylation of C-73. Ref.21

Mutagenesis

70

1

E → A: Strongly reduced interaction with CASP3; when associated with A-72. Ref.21

Mutagenesis

72

1

K → A: Strongly reduced interaction with CASP3; when associated with A-70. Ref.21

Mutagenesis

73

1

C → D: Strongly reduced S-nitrosylation of CASP3. Ref.18 Ref.21

Mutagenesis

73

1

C → S: Loss of nitrosylation, and loss of S-nitrosylating activity towards CASP3. Ref.18 Ref.21

Sequence conflict

39

1

K → N in AAA74596. Ref.1

Sequence conflict

39

1

K → N in AAF86466. Ref.4

Sequence conflict

74

1

M → T in AAA74596. Ref.1

Sequence conflict

74

1

M → T in AAF86466. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

105

Helix Strand Turn

Details...

Beta strand

2 – 5

4

Helix

8 – 17

10

Turn

18 – 20

3

Beta strand

23 – 28

6

Helix

33 – 48

16

Beta strand

52 – 58

7

Turn

59 – 61

3

Helix

63 – 68

6

Beta strand

73 – 81

9

Beta strand

84 – 91

8

Helix

94 – 104

11

Sequences

	Sequence		Length	Mass (Da)
	P10599-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 256F4E3C8A187693	FASTA	105	11,737
	10 20 30 40 50 60 MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD 70 80 90 100 DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a cDNA for human thioredoxin." Wollman E.E., D'Auriol L., Rimsky L., Shaw A., Jacquot J.-P., Wingfield P., Graber P., Dessarps F. J. Biol. Chem. 263:15506-15512(1988) [PubMed: 3170595] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction." Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J. EMBO J. 8:757-764(1989) [PubMed: 2785919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Isolation and characterization of human thioredoxin-encoding genes." Tonissen K.F., Wells J.R.E. Gene 102:221-228(1991) [PubMed: 1874447] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	Reddy P.G., Bhuyan D.K., Bhuyan K.C. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.
[5]	"Cloning, purification and characterization of human lens thioredoxin." Liu A., Lou M.F. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.
[6]	"Cloning and sequencing of thioredoxin cDNA from human brain." Xu J.Y., Xu L., Li K.S., Dai R. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	NIEHS SNPs program Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"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: Cervix.
[13]	"Characterization of a thioredoxin-related surface protein." Dean M.F., Martin H., Sansom P.A. Biochem. J. 304:861-867(1994) [PubMed: 7818492] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21 AND 38-57. Tissue: Monocyte.
[14]	"Identification of a thioredoxin-related protein associated with plasma membranes." Martin H., Dean M. Biochem. Biophys. Res. Commun. 175:123-128(1991) [PubMed: 1998498] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-15.
[15]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 9-48; 73-81 AND 95-105, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]	"Human thioredoxin reactivity-structure/function relationship." Jacquot J.-P., de Lamotte F., Fontecav M., Schuermann P., Decottignies P., Miginiac-Maslow M., Wollman E. Biochem. Biophys. Res. Commun. 173:1375-1381(1990) [PubMed: 2176490] [Abstract] Cited for: FUNCTION.
[17]	"S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1." Yasinska I.M., Kozhukhar A.V., Sumbayev V.V. Arch. Biochem. Biophys. 428:198-203(2004) [PubMed: 15246877] [Abstract] Cited for: S-NITROSYLATION, INTERACTION WITH MAP3K5.
[18]	"Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine." Mitchell D.A., Marletta M.A. Nat. Chem. Biol. 1:154-158(2005) [PubMed: 16408020] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-73, S-NITROSYLATION AT CYS-73.
[19]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, MASS SPECTROMETRY. Tissue: Hepatocyte.
[20]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94, MASS SPECTROMETRY. Tissue: Epithelium.
[21]	"Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells." Mitchell D.A., Morton S.U., Fernhoff N.B., Marletta M.A. Proc. Natl. Acad. Sci. U.S.A. 104:11609-11614(2007) [PubMed: 17606900] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-69; GLU-70; LYS-72 AND CYS-73, S-NITROSYLATION AT CYS-73 IN RESPONSE TO NITRIC OXIDE.
[22]	"Abnormal proteins in primary breast cancer tissues from 25 Sudanese patients." Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M., Harbi S.O., Stansalas J., Mohamed A.O. Eur. J. Inflamm. 6:115-121(2008) Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Tissue: Mammary cancer.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[24]	"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-3 AND LYS-39, MASS SPECTROMETRY.
[25]	"A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin." Forman-Kay J.D., Clore G.M., Dricoll P.C., Wingfield P., Richards F.M., Gronenborn A.M. Biochemistry 28:7088-7097(1989) [PubMed: 2684271] [Abstract] Cited for: STRUCTURE BY NMR.
[26]	"High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution." Forman-Kay J.D., Clore G.M., Wingfield P., Gronenborn A.M. Biochemistry 30:2685-2698(1991) [PubMed: 2001356] [Abstract] Cited for: STRUCTURE BY NMR.
[27]	"The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin." Qin J., Clore G.M., Gronenborn A.M. Structure 2:503-522(1994) [PubMed: 7922028] [Abstract] Cited for: STRUCTURE BY NMR.
[28]	"Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B." Qin J., Clore G.M., Kennedy W.M., Huth J.R., Gronenborn A.M. Structure 3:289-297(1995) [PubMed: 7788295] [Abstract] Cited for: STRUCTURE BY NMR.
[29]	"The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal." Qin J., Clore G.M., Kennedy W.P., Kuszewski J., Gronenborn A.M. Structure 4:613-620(1996) [PubMed: 8736558] [Abstract] Cited for: STRUCTURE BY NMR.
[30]	"Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer." Weichsel A., Gasdaska J.R., Powis G., Montfort W.R. Structure 4:735-751(1996) [PubMed: 8805557] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[31]	"Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60 --> asparagine mutant." Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G., Montfort W.R. Biochemistry 36:13979-13988(1997) [PubMed: 9369469] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-60, SUBUNIT.
[32]	"Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin." Weichsel A., Brailey J.L., Montfort W.R. Biochemistry 46:1219-1227(2007) [PubMed: 17260951] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, DISULFIDE BONDS, S-NITROSYLATION AT CYS-62 AND CYS-69.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04026 mRNA. Translation: AAA74596.1.
X77584 mRNA. Translation: CAA54687.1.
X54539, X54540, X54541 Genomic DNA. Translation: CAA38410.1.
AF276919 mRNA. Translation: AAF86466.1.
AY004872 mRNA. Translation: AAF87085.1.
AF313911 mRNA. Translation: AAG34699.1.
AK289508 mRNA. Translation: BAF82197.1.
CR407665 mRNA. Translation: CAG28593.1.
AF548001 Genomic DNA. Translation: AAN33187.1.
AL158158 Genomic DNA. Translation: CAI14066.1.
CH471105 Genomic DNA. Translation: EAW59059.1.
BC003377 mRNA. Translation: AAH03377.1.
BC054866 mRNA. Translation: AAH54866.1.

IPI

IPI00216298.

PIR

JH0568.

RefSeq

NP_003320.2.

UniGene

Hs.435136

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AIU	X-ray	2.00	A	1-105	[»]
1AUC	X-ray	2.10	A	1-105	[»]
1CQG	NMR	-	A	1-105	[»]
1CQH	NMR	-	A	1-105	[»]
1ERT	X-ray	1.70	A	1-105	[»]
1ERU	X-ray	2.10	A	1-105	[»]
1ERV	X-ray	1.65	A	1-105	[»]
1ERW	X-ray	1.80	A	1-105	[»]
1M7T	NMR	-	A	1-65	[»]
1MDI	NMR	-	A	2-104	[»]
1MDJ	NMR	-	A	2-104	[»]
1MDK	NMR	-	A	2-104	[»]
1TRS	NMR	-	A	1-105	[»]
1TRU	NMR	-	A	1-105	[»]
1TRV	NMR	-	A	1-105	[»]
1TRW	NMR	-	A	1-105	[»]
1W1C	model	-	C	1-105	[»]
1W1E	model	-	C	1-105	[»]
2HSH	X-ray	1.35	A	1-105	[»]
2HXK	X-ray	1.65	A/B/C	1-105	[»]
2IFQ	X-ray	1.20	A/B/C	1-105	[»]
2IIY	X-ray	1.70	A	1-105	[»]
3TRX	NMR	-	A	1-105	[»]
4TRX	NMR	-	A	1-105	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6129N.

IntAct

P10599. 3 interactions.

STRING

P10599.

PTM databases

PhosphoSite

P10599.

2-D gel databases

SWISS-2DPAGE

P10599.

Aarhus/Ghent-2DPAGE

8006. IEF.

Cornea-2DPAGE

P10599.

DOSAC-COBS-2DPAGE

P10599.

PHCI-2DPAGE

P10599.

REPRODUCTION-2DPAGE

IPI00216298.

Siena-2DPAGE

P10599.

Proteomic databases

PeptideAtlas

P10599.

PRIDE

P10599.

Genome annotation databases

Ensembl

ENST00000374517; ENSP00000363641; ENSG00000136810; Homo sapiens. [Genome view]

GeneID

7295.

KEGG

hsa:7295.

UCSC

uc004bep.1. human.

Organism-specific databases

CTD

7295.

GeneCards

GC09M112045.

H-InvDB

HIX0008275.

HGNC

HGNC:12435. TXN.

HPA

CAB008678.

MIM

187700. gene.

PharmGKB

PA37091.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG493509.

HOVERGEN

P10599.

InParanoid

P10599.

OMA

IESKYAF.

OrthoDB

EOG969TD7.

PhylomeDB

P10599.

Enzyme and pathway databases

Pathway_Interaction_DB

p38_mkk3_6pathway. p38 MAPK signaling pathway.
ptp1bpathway. Signaling events mediated by PTP1B.
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_1698. Metabolism of nucleotides.

Gene expression databases

ArrayExpress

P10599.

Bgee

P10599.

CleanEx

HS_TXN.

Genevestigator

P10599.

GermOnline

ENSG00000136810. Homo sapiens.

Family and domain databases

InterPro

IPR017936. Thioredoxin-like.
IPR012336. Thioredoxin-like_fold.
IPR006662. Thioredoxin-like_subdom.
IPR015467. Thioredoxin_core.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR10438. Trx. 1 hit.

Pfam

PF00085. Thioredoxin. 1 hit.
[Graphical view]

PRINTS

PR00421. THIOREDOXIN.

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

28523.

SOURCE

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Entry information

Entry name

THIO_HUMAN

Accession

Primary (citable) accession number: P10599
Secondary accession number(s): Q53X69, Q96KI3, Q9UDG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.