Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Thioredoxin  

UniProtKB / Swiss-Prot ID :  THIO_HUMAN

Gene Name (Synonyms) : 
TXN, TRDX, TRX, TRX1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. Secreted. Note=Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus. 

Protein 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. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity. ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55). 

Protein Sequence MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECE...
Predicted Secondary Structure CEEECCCHHHHHHHHHCCCCCEEEEEEECCCCCHHHHHHHHHHHHHHHCCCCEEEEEECCCCHHHHHHCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
3N6-acetyllysine--MVKQIES
--CEEECCC
44.23HPRD
Link
3N6-acetyllysine--MVKQIES
--CEEECCC
44.23Phosphositeplus
Link
3N6-acetyllysine.--MVKQIES
--CEEECCC
44.23UniProtKB
Link
8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QIESKTAFQ
ECCCHHHHH
30.96Phosphositeplus
Link
39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)CKMIKPFFH
HHHHHHHHH
32.07Phosphositeplus
Link
39N6-acetyllysineCKMIKPFFH
HHHHHHHHH
32.07HPRD
Link
39N6-acetyllysineCKMIKPFFH
HHHHHHHHH
32.07Phosphositeplus
Link
39N6-acetyllysine.CKMIKPFFH
HHHHHHHHH
32.07UniProtKB
Link
62S-nitrosocysteineDVDDCQDVA
ECCCCHHHH
3.01dbSNO
Link
62S-nitrosocysteine.DVDDCQDVA
ECCCCHHHH
3.01UniProtKB
Link
69S-nitrosocysteineVASECEVKC
HHHHCCCCC
7.25dbSNO
Link
69S-nitrosocysteineVASECEVKC
HHHHCCCCC
7.25HPRD
Link
69S-nitrosocysteine.VASECEVKC
HHHHCCCCC
7.25UniProtKB
Link
73S-glutathionyl cysteineCEVKCMPTF
CCCCCCCEE
4.82HPRD
Link
73S-nitrosocysteineCEVKCMPTF
CCCCCCCEE
4.82dbSNO
Link
73S-nitrosocysteine; alternate.CEVKCMPTF
CCCCCCCEE
4.82UniProtKB
Link
94Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SGANKEKLE
ECCCHHHHH
56.54Phosphositeplus
Link
94N6-acetyllysineSGANKEKLE
ECCCHHHHH
56.54Phosphositeplus
Link
94N6-acetyllysine.SGANKEKLE
ECCCHHHHH
56.54UniProtKB
Link
96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ANKEKLEAT
CCHHHHHHH
53.92Phosphositeplus
Link
100PhosphothreonineKLEATINEL
HHHHHHHHH
18.24PhosphoELM
Link
100PhosphothreonineKLEATINEL
HHHHHHHHH
18.24Phosphositeplus
Link
100Phosphothreonine.KLEATINEL
HHHHHHHHH
18.24UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GCR_HUMANphysical interactionMINT-15482MINT9915858
APEX1_HUMANphysical interactionDIP:11002EDIP8736558
TXNIP_HUMANphysical interaction
physical interaction
EBI-1369231
EBI-1368856
intact10814541
10814541
CSN5_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
direct inter
EBI-594678
EBI-594810
EBI-594
intact15480426
15480426
15480426
15480426
15480426
15480426
15480426
15480426
APEX1_HUMANin vitro
in vivo
HPRD:01761HPRD11118054
10585464
9108029
CO1A1_HUMANin vitro
yeast 2-hybrid
HPRD:01761HPRD12099690
GCR_HUMANin vitroHPRD:01761HPRD9915858
NFKB1_HUMANin vitroHPRD:01761HPRD7788295
ALR_HUMANin vitro
in vivo
HPRD:01761HPRD15894171
CSN5_HUMANin vitro
in vivo
HPRD:01761HPRD15480426
DNJA1_HUMANin vivo
yeast 2-hybrid
HPRD:01761HPRD16458196
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya 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).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-39, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, AND MASSSPECTROMETRY.
S-nitrosylation
ReferencePubMed
"Thioredoxin catalyzes the S-nitrosation of the caspase-3 active sitecysteine.";
Mitchell D.A., Marletta M.A.;
Nat. Chem. Biol. 1:154-158(2005).
Cited for: FUNCTION, MUTAGENESIS OF CYS-73, AND S-NITROSYLATION AT CYS-73.
"Thioredoxin is required for S-nitrosation of procaspase-3 and theinhibition 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).
Cited for: FUNCTION, MUTAGENESIS OF CYS-69; GLU-70; LYS-72 AND CYS-73, ANDS-NITROSYLATION AT CYS-73 IN RESPONSE TO NITRIC OXIDE.
"Buried S-nitrosocysteine revealed in crystal structures of humanthioredoxin.";
Weichsel A., Brailey J.L., Montfort W.R.;
Biochemistry 46:1219-1227(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, DISULFIDE BONDS, ANDS-NITROSYLATION AT CYS-62 AND CYS-69.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures